RN213_MOUSE
ID RN213_MOUSE Reviewed; 5148 AA.
AC E9Q555; F7A6H4; Q8BVK6;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 3.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=E3 ubiquitin-protein ligase RNF213;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q63HN8};
DE EC=3.6.4.- {ECO:0000269|PubMed:32573437};
DE AltName: Full=E3 ubiquitin-lipopolysaccharide ligase RNF213 {ECO:0000305};
DE EC=2.3.2.- {ECO:0000250|UniProtKB:Q63HN8};
DE AltName: Full=Mysterin {ECO:0000303|PubMed:26126547};
DE AltName: Full=RING finger protein 213 {ECO:0000305};
GN Name=Rnf213 {ECO:0000312|MGI:MGI:1289196};
GN Synonyms=Mystr {ECO:0000303|PubMed:26126547};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4807-5148.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=23410753; DOI=10.1016/j.bbrc.2013.02.015;
RA Kobayashi H., Yamazaki S., Takashima S., Liu W., Okuda H., Yan J.,
RA Fujii Y., Hitomi T., Harada K.H., Habu T., Koizumi A.;
RT "Ablation of Rnf213 retards progression of diabetes in the Akita mouse.";
RL Biochem. Biophys. Res. Commun. 432:519-525(2013).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=24440776; DOI=10.1016/j.brainres.2014.01.011;
RA Sonobe S., Fujimura M., Niizuma K., Nishijima Y., Ito A., Shimizu H.,
RA Kikuchi A., Arai-Ichinoi N., Kure S., Tominaga T.;
RT "Temporal profile of the vascular anatomy evaluated by 9.4-T magnetic
RT resonance angiography and histopathological analysis in mice lacking
RT RNF213: a susceptibility gene for moyamoya disease.";
RL Brain Res. 1552:64-71(2014).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=25383461; DOI=10.1097/wnr.0000000000000289;
RA Sonobe S., Fujimura M., Niizuma K., Fujimura T., Furudate S., Nishijima Y.,
RA Kure S., Tominaga T.;
RT "Increased vascular MMP-9 in mice lacking RNF213: moyamoya disease
RT susceptibility gene.";
RL NeuroReport 25:1442-1446(2014).
RN [7]
RP MUTAGENESIS OF ARG-4753.
RX PubMed=26315378; DOI=10.1016/j.brainres.2015.07.039;
RA Kanoke A., Fujimura M., Niizuma K., Ito A., Sakata H., Sato-Maeda M.,
RA Morita-Fujimura Y., Kure S., Tominaga T.;
RT "Temporal profile of the vascular anatomy evaluated by 9.4-tesla magnetic
RT resonance angiography and histological analysis in mice with the R4859K
RT mutation of RNF213, the susceptibility gene for moyamoya disease.";
RL Brain Res. 1624:497-505(2015).
RN [8]
RP MUTAGENESIS OF ARG-4753.
RX PubMed=26126547; DOI=10.1161/jaha.115.002146;
RA Kobayashi H., Matsuda Y., Hitomi T., Okuda H., Shioi H., Matsuda T.,
RA Imai H., Sone M., Taura D., Harada K.H., Habu T., Takagi Y., Miyamoto S.,
RA Koizumi A.;
RT "Biochemical and functional characterization of RNF213 (Mysterin) R4810K, a
RT susceptibility mutation of Moyamoya disease, in angiogenesis in vitro and
RT in vivo.";
RL J. Am. Heart Assoc. 4:0-0(2015).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=33420513; DOI=10.1007/s00335-020-09856-y;
RA Houzelstein D., Simon-Chazottes D., Batista L., Tokuda S., Langa Vives F.,
RA Flamand M., Montagutelli X., Panthier J.J.;
RT "The ring finger protein 213 gene (Rnf213) contributes to Rift Valley fever
RT resistance in mice.";
RL Mamm. Genome 32:30-37(2021).
RN [10]
RP FUNCTION.
RX PubMed=34012115; DOI=10.1038/s41586-021-03566-4;
RA Otten E.G., Werner E., Crespillo-Casado A., Boyle K.B., Dharamdasani V.,
RA Pathe C., Santhanam B., Randow F.;
RT "Ubiquitylation of lipopolysaccharide by RNF213 during bacterial
RT infection.";
RL Nature 594:111-116(2021).
RN [11] {ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 591-5152 IN COMPLEX
RP WITH ZINC AND ATP, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH
RP UBE2L3, DOMAIN, AND MUTAGENESIS OF ARG-4753.
RX PubMed=32573437; DOI=10.7554/elife.56185;
RA Ahel J., Lehner A., Vogel A., Schleiffer A., Meinhart A., Haselbach D.,
RA Clausen T.;
RT "Moyamoya disease factor RNF213 is a giant E3 ligase with a dynein-like
RT core and a distinct ubiquitin-transfer mechanism.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination
CC of both proteins and lipids, and which is involved in various
CC processes, such as lipid metabolism, angiogenesis and cell-autonomous
CC immunity (PubMed:32573437). Acts as a key immune sensor by catalyzing
CC ubiquitination of the lipid A moiety of bacterial lipopolysaccharide
CC (LPS) via its RZ-type zinc-finger: restricts the proliferation of
CC cytosolic bacteria, such as Salmonella, by generating the bacterial
CC ubiquitin coat through the ubiquitination of LPS (PubMed:34012115).
CC Also acts indirectly by mediating the recruitment of the LUBAC complex,
CC which conjugates linear polyubiquitin chains (By similarity).
CC Ubiquitination of LPS triggers cell-autonomous immunity, such as
CC antibacterial autophagy, leading to degradation of the microbial
CC invader (By similarity). Involved in lipid metabolism by regulating fat
CC storage and lipid droplet formation; act by inhibiting the lipolytic
CC process (By similarity). Also regulates lipotoxicity by inhibiting
CC desaturation of fatty acids (By similarity). Also acts as an E3
CC ubiquitin-protein ligase via its RING-type zinc finger: mediates 'Lys-
CC 63'-linked ubiquitination of target proteins (By similarity). Involved
CC in the non-canonical Wnt signaling pathway in vascular development:
CC acts by mediating ubiquitination and degradation of FLNA and NFATC2
CC downstream of RSPO3, leading to inhibit the non-canonical Wnt signaling
CC pathway and promoting vessel regression (By similarity). Also has
CC ATPase activity; ATPase activity is required for ubiquitination of LPS
CC (PubMed:32573437). {ECO:0000250|UniProtKB:Q63HN8,
CC ECO:0000269|PubMed:32573437, ECO:0000269|PubMed:34012115}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q63HN8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:32573437};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000269|PubMed:32573437};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q63HN8}.
CC -!- SUBUNIT: Monomer (PubMed:32573437). Interacts with UBE2L3/UBCH7;
CC UBE2L3/UBCH7 is the most efficient ubiquitin-conjugating enzyme E2 for
CC the ubiquitin ligase activity (PubMed:32573437). Interacts with
CC UBE2N/UBC13; promoting 'Lys-63'-linked ubiquitination of target
CC proteins (By similarity). {ECO:0000250|UniProtKB:Q63HN8,
CC ECO:0000269|PubMed:32573437}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q63HN8}.
CC -!- DOMAIN: Composed of an N-terminal stalk, a dynein-like core comprised
CC of two catalytically active and four inactive ATPase domains, and a C-
CC terminal E3 module (PubMed:32573437). The ATPase regions do not
CC generate movement but rather act like an intricate molecular 'switch'
CC (PubMed:32573437). {ECO:0000269|PubMed:32573437}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for the ubiquitin-
CC protein ligase activity. {ECO:0000250|UniProtKB:Q63HN8}.
CC -!- DOMAIN: The RZ-type (RNF213-ZNFX1) zinc-finger is required for the
CC ubiquitination of the lipid A moiety of bacterial lipopolysaccharide
CC (LPS). {ECO:0000250|UniProtKB:Q63HN8}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:23410753,
CC PubMed:24440776). Males and female are fertile and produce normal-sized
CC litters (PubMed:23410753, PubMed:24440776). Mice do not spontaneously
CC develop Moyamoya disease, a chronic occlusive cerebrovascular disease
CC (PubMed:24440776). Mice are however more susceptible to Rift Valley
CC fever virus infection (PubMed:33420513). Mice show elevated expression
CC of MMP9 (PubMed:25383461). {ECO:0000269|PubMed:23410753,
CC ECO:0000269|PubMed:24440776, ECO:0000269|PubMed:25383461,
CC ECO:0000269|PubMed:33420513}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- CAUTION: The stoichiometry is unclear: was initially thought to form
CC homohexamers (By similarity). However, the electron microscopy
CC structure showed that it is monomeric and is composed of six ATPase
CC modules within a single polypeptide chain (PubMed:32573437).
CC {ECO:0000250|UniProtKB:Q63HN8, ECO:0000269|PubMed:32573437}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37048.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL645911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK077880; BAC37048.1; ALT_INIT; mRNA.
DR PDB; 6TAX; EM; 3.20 A; A=591-5148.
DR PDB; 6TAY; EM; 3.20 A; A=591-5148.
DR PDBsum; 6TAX; -.
DR PDBsum; 6TAY; -.
DR SMR; E9Q555; -.
DR IntAct; E9Q555; 1.
DR MINT; E9Q555; -.
DR STRING; 10090.ENSMUSP00000091429; -.
DR iPTMnet; E9Q555; -.
DR PhosphoSitePlus; E9Q555; -.
DR SwissPalm; E9Q555; -.
DR EPD; E9Q555; -.
DR jPOST; E9Q555; -.
DR PaxDb; E9Q555; -.
DR PeptideAtlas; E9Q555; -.
DR PRIDE; E9Q555; -.
DR ProteomicsDB; 300423; -.
DR Antibodypedia; 46314; 195 antibodies from 27 providers.
DR MGI; MGI:1289196; Rnf213.
DR VEuPathDB; HostDB:ENSMUSG00000070327; -.
DR eggNOG; ENOG502QQ65; Eukaryota.
DR HOGENOM; CLU_000066_0_0_1; -.
DR InParanoid; E9Q555; -.
DR OMA; NAYMKDM; -.
DR PhylomeDB; E9Q555; -.
DR TreeFam; TF329577; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR ChiTaRS; Rnf213; mouse.
DR PRO; PR:E9Q555; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; E9Q555; protein.
DR Bgee; ENSMUSG00000070327; Expressed in small intestine Peyer's patch and 216 other tissues.
DR ExpressionAtlas; E9Q555; baseline and differential.
DR Genevisible; E9Q555; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB.
DR GO; GO:0120323; P:lipid ubiquitination; IMP:UniProtKB.
DR GO; GO:2000051; P:negative regulation of non-canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0098792; P:xenophagy; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031248; RNF213.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22605; PTHR22605; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51981; ZF_RZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Angiogenesis; ATP-binding; Coiled coil; Cytoplasm; Hydrolase;
KW Immunity; Isopeptide bond; Lipid droplet; Lipid metabolism; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..5148
FT /note="E3 ubiquitin-protein ligase RNF213"
FT /id="PRO_0000415918"
FT ZN_FING 3947..3986
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 4429..4501
FT /note="RZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT REGION 38..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3435..3465
FT /evidence="ECO:0000255"
FT COMPBIAS 64..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4462
FT /note="Nucleophile; for E3 ubiquitin-lipopolysaccharide
FT ligase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 1957..1962
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY"
FT BINDING 2060
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY"
FT BINDING 2114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAY"
FT BINDING 2116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY"
FT BINDING 2177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAX"
FT BINDING 2460
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAY"
FT BINDING 2535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAX"
FT BINDING 3947
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY"
FT BINDING 3950
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY"
FT BINDING 3962
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY"
FT BINDING 3964
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY"
FT BINDING 3967
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY"
FT BINDING 3970
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY"
FT BINDING 3982
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY"
FT BINDING 3985
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32573437,
FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY"
FT BINDING 4451
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 4455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 4471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 4474
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63HN8"
FT MOD_RES 2234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63HN8"
FT CROSSLNK 1128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q63HN8"
FT MUTAGEN 4753
FT /note="R->K: Knockin mice grow normally and do not show any
FT visible phenotype. Slightly impaired angiogenesis. Does not
FT affect ATPase or E3 ubiquitin ligase activities."
FT /evidence="ECO:0000269|PubMed:26126547,
FT ECO:0000269|PubMed:26315378, ECO:0000269|PubMed:32573437"
FT HELIX 593..601
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 609..613
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 614..617
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 618..621
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 629..635
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 636..639
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 644..655
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 656..660
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 663..666
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 668..671
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 673..675
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 683..685
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 689..693
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 704..706
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 712..719
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 721..725
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 729..735
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 740..742
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 743..748
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 751..756
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 760..771
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 772..774
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 781..800
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 803..810
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 811..826
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 831..833
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 836..849
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 865..888
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:6TAY"
FT STRAND 897..900
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 904..908
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 909..917
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 924..927
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 930..938
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 943..950
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 952..955
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 963..981
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 995..1009
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1013..1015
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1022..1030
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1033..1043
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1045..1048
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1049..1051
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1054..1071
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1072..1076
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1080..1088
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1090..1101
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1114..1142
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 1143..1147
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1149..1151
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1155..1158
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1167..1170
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1191..1202
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1207..1217
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1231..1233
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1234..1240
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1242..1256
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 1257..1259
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1263..1269
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1271..1273
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1277..1288
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 1289..1292
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1296..1298
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1299..1328
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1339..1345
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1362..1367
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 1368..1370
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1375..1377
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1378..1386
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1389..1397
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1401..1403
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1404..1414
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1419..1439
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1448..1463
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1468..1476
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1479..1486
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1498..1506
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1508..1511
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1516..1518
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1522..1525
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1526..1530
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1541..1544
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1545..1556
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1564..1593
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1596..1600
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1602..1606
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1612..1616
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1620..1622
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1625..1627
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1631..1659
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1662..1665
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1668..1678
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1680..1682
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1687..1690
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 1691..1695
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1700..1708
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1714..1725
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1727..1730
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1736..1749
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1751..1753
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1761..1774
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1789..1796
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1799..1801
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1803..1809
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 1810..1812
FT /evidence="ECO:0007829|PDB:6TAY"
FT STRAND 1821..1826
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1833..1843
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1849..1851
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1853..1857
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1859..1861
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1864..1880
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1887..1892
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1894..1896
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 1901..1904
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1906..1908
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1918..1929
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1933..1935
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1938..1941
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1942..1945
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1947..1959
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1960..1973
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1974..1977
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1982..1987
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 1989..1991
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 1994..2001
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 2002..2004
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2005..2010
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2015..2020
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2028..2036
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2040..2042
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2048..2050
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2055..2062
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2081..2084
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2085..2087
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2090..2092
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 2096..2100
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2117..2120
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2123..2136
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2155..2165
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2173..2192
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2195..2202
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2203..2205
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2208..2223
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 2248..2250
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2251..2254
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2260..2262
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2266..2269
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2271..2273
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2276..2280
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2282..2285
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2289..2294
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2296..2298
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2301..2304
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 2309..2317
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2326..2329
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 2331..2341
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2352..2354
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2358..2373
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2377..2380
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2383..2387
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2388..2399
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2407..2411
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2418..2439
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2443..2449
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2456..2463
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2479..2485
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2493..2500
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2502..2504
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2510..2512
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2516..2521
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2522..2524
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2525..2527
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 2537..2539
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2540..2542
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 2551..2563
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2572..2588
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2589..2591
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 2598..2600
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2601..2614
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2618..2630
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2643..2653
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 2654..2657
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2661..2668
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 2669..2671
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2674..2676
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2679..2696
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2707..2721
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2726..2729
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2734..2737
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2738..2746
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2749..2751
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2753..2755
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 2756..2759
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2762..2768
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2776..2790
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2797..2805
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 2807..2810
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2818..2820
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2821..2824
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2830..2832
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 2836..2838
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2841..2848
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2852..2855
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2857..2862
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2868..2879
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2886..2889
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2890..2892
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2893..2906
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 2908..2910
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 2914..2931
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2937..2947
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2956..2960
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 2975..2983
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3002..3009
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3011..3017
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3026..3028
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3038..3055
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3059..3062
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 3065..3067
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 3069..3071
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3072..3076
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3080..3082
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3085..3092
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3095..3100
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3107..3112
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3113..3119
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3122..3124
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3125..3127
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3130..3132
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 3136..3138
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3141..3158
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3164..3166
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3173..3176
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3184..3196
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3205..3218
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3223..3228
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3229..3231
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3232..3234
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3237..3248
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3255..3262
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3263..3265
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3271..3281
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3288..3294
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 3295..3299
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3304..3307
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3308..3310
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3314..3325
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3327..3344
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3349..3364
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3371..3378
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 3381..3386
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3397..3400
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3408..3410
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3414..3419
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3422..3425
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3477..3489
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3495..3498
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3502..3511
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3512..3517
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3518..3538
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3539..3542
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3544..3547
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3549..3554
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3557..3563
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3566..3589
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3591..3593
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3596..3599
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3600..3602
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3605..3614
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 3618..3620
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3654..3656
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3658..3675
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3678..3680
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3681..3691
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3693..3698
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3703..3721
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3725..3727
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 3728..3745
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3748..3750
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 3763..3783
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3788..3799
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3802..3805
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3808..3823
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3824..3827
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3829..3838
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3840..3846
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 3849..3851
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3857..3889
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3895..3909
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 3918..3940
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 3948..3950
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 3955..3959
FT /evidence="ECO:0007829|PDB:6TAY"
FT STRAND 3965..3967
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 3968..3975
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 3976..3978
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 3983..3985
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4000..4025
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 4026..4028
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4030..4032
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4036..4044
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4069..4072
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4075..4077
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 4083..4088
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4093..4095
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4097..4110
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4113..4115
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4117..4137
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4143..4155
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 4161..4163
FT /evidence="ECO:0007829|PDB:6TAY"
FT STRAND 4166..4168
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4172..4197
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 4202..4204
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4205..4218
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4223..4235
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4238..4244
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4246..4248
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4252..4254
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4257..4261
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4272..4275
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4280..4292
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4297..4303
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4310..4330
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4331..4334
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 4338..4342
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4343..4352
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 4354..4356
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4359..4369
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 4374..4377
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4381..4384
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 4385..4402
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4406..4408
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4409..4416
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4418..4421
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4422..4425
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 4523..4543
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4545..4551
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4560..4577
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4578..4580
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4582..4595
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4614..4632
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 4636..4638
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4639..4647
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 4650..4654
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4656..4659
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 4660..4663
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4666..4668
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4669..4672
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4677..4680
FT /evidence="ECO:0007829|PDB:6TAY"
FT TURN 4681..4684
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4692..4701
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 4702..4706
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4709..4716
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4718..4721
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4722..4726
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4727..4740
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4743..4745
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4752..4756
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4762..4782
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 4783..4785
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4786..4789
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4798..4801
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4807..4809
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4816..4819
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4821..4844
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4855..4857
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 4860..4862
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4868..4871
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4873..4877
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4880..4884
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4891..4894
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4896..4904
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 4905..4907
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4908..4910
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4916..4918
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4931..4940
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4948..4956
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4961..4979
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 4985..4988
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 4989..4993
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 4994..4996
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 5004..5010
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 5015..5017
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 5018..5035
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 5046..5048
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 5054..5065
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 5069..5083
FT /evidence="ECO:0007829|PDB:6TAX"
FT STRAND 5090..5092
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 5099..5106
FT /evidence="ECO:0007829|PDB:6TAX"
FT TURN 5109..5111
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 5115..5120
FT /evidence="ECO:0007829|PDB:6TAX"
FT HELIX 5128..5130
FT /evidence="ECO:0007829|PDB:6TAY"
FT HELIX 5132..5148
FT /evidence="ECO:0007829|PDB:6TAX"
SQ SEQUENCE 5148 AA; 584258 MW; 668FFE0AB2C2F8CE CRC64;
MECPQCGHVS SEKAPKFCSE CGQKLPSAAT VQGDLKNDNT LVVSSTPEGK TEQGAVLREE
EVLLSSTDPG KELEKPEESD SNASWTTQMS KKEKRRRKRQ GTISSSEAPS SGLWSLDMPP
SPGSHNSALP QNQAQQGGAA SQPGHPLDTE NMPMEDGFVH TEGSGSPLQG QAAERTDAQS
NLAPSDLAEV KDLNTSKPSV DKGLPLDGGP ALSAFKGHPK MTDASQKAPL PESKGETSGQ
EKKVPPIDAA ASPVKTAGKE TGEDVRKPKP SPVSPVASKH GDQEAELKGK LATPVRKSNE
GGNTQPEDQR KPGEGRNFAA AVKTQQAAAP QQAAAPEPTS AFNPRDTVTV YFHAIVSRHF
GFNPEEHKVY VRGGEGLGQK GWTDACEMYC TQDLHDLGSL VEGKMDIPRQ SLDKPIPYKY
VIHRGGSSKD TVEYEFIYEQ AQKKGEHVNR CLRVVSTSLG NGDWHQYDDI ICMRSTGFFQ
QAKNRILDST RKELLKGKKQ AAVVMLDRIF SVLQPWSDIN LQSFMTQFLQ FYSVVREPMI
HDGRARKWTS LQYEEKEVWT NLWEHVKKQM APFLEGKSGE SLPADCPVRS KLTLGLSILF
MVEAAEFTVP KKDLDSLCYL LIPSAGSPEA LHSDLSPVLR IRQRWRIYLT NLCLRCIDER
CDRWLGILPL LHTCMQKSPP KKNSKSQPED TWAGLEGISF SEFRDKAPTR SQPLQFMQSK
MALLRVDEYL FRSWLSVVPL ESLSSYLENS IDYLSDVPVR VLDCLQGISY RLPGLRKISN
QNMKKDVENV FKMLMHLVDI YQHRIFGENL LQIYLTECLT LHETVCNITA NHQFFEIPAL
SAELICKLLE LSPPGHTDEG LPEKSYEDLV TSTLQEALAT TRNWLRSLFK SRMLSISSAY
VRLTYSEEMA VWRRLVEIGF PEKHGWKGSL LGDMEGRLKQ EPPRLQISFF CSSQCRDGGL
HDSVSRSFEK CVIEAVSSAC QSQTSVLEGL SCQDLQKFGT LLSAVITKSW PVHNGEPVFD
VDEIFKYLLK WPDVRQLFEL CGTNEKIIDN ITEEGRQLMA TAESVFQKVA GELENGTIVV
GQLELILEHQ SQFLDIWNLN RRRLPSQEKA CDVRSLLKRR RDDLLFLKQE KRYVESLLRQ
LGRVKHLVQV DFGNIEIIHS QDLSNKKLNE AVIKLPNSSS YKRETHYCLS PDIREMASKL
DSLKDSHIFQ DFWQETAESL NTLDKDPREL KVSLPEVLEY LYNPCYDNFY TLYENLKSGK
ITFAEVDAIF KDFVDKYDEL KNDLKFMCTM NPQDQKGWIS ERVGQIKEYH TLHQAVSSAK
VILQVRRALG VTGDFSVLNP LLNFADSFED FGNEKLDQIS PQFIKAKQLL QDISEPRQRC
LEELARQTEL VAWLHKALED INELKVFVDL ASISAGENDI DVDRVACFHD AVQGYASLLY
KMDERTNFSD FMNHLQELWR ALDNDQHLPD KLKDSARNLE WLKTVKESHG SVELSSLSLA
TAINSRGVYV IEAPKDGQKI SPDTVLRLLL PDGHGYPEAL RTYSTEELKE LLNKLMLMSG
KKDHNSNTEV EKFSEVFSNM QRLVHVFIKL HCAGNMLFRT WTAKVYCCPD GGIFMNFGLE
LLSQLTEKGD VIQLLGALCR QMEDFLDNWK TVVAQKRAEH FYLNFYTAEQ LVYLSSELRK
PRPSEAALMM LSFIKGKCTV QDLVQATSAC ESKADRYCLR EVMKKLPQQL LSEPSLMGKL
QVIMMQSLVY MSAFLPHCLD LDALGRCLAH LATMGGTPVE RPLPKGLQAG QPNLILCGHS
EVLPAALAIY MQAPRQPLPT FDEVLLCTPA TTIEEVELLL RRCLTSGSQG HKVYSLLFAD
QLSYEVGCQA EEFFQSLCTR AHREDYQLVI LCDAAREHCY IPSTFSQYKV PLVPQAPLPN
IQAYLQSHYQ VPKRLLSAAT VFRDGLCVGI VTSERAGVGK SLYVNTLHTK LKAKLRDETV
PLKIIRLTEP HLDENQVLSA LLPFLKEKYQ KMPVIFHIDI STSVQTGIPI FLFKLLILQY
LMDINGKIWR RSPGHLYLVE IPQGLSVQPK RSSKLNARAP LFKFLDLFPK VTCRPPKEVI
DMELTPERSH TDPAMDPVEF CSEAFQRPYQ YLKRFHQQQN LDTFQYEKGS VEGSPEECLQ
HFLIYCGLIN PSWSELRNFA WFLNCQLKDC EASIFCKSAF TGDTLRGFKN FVVTFMILMA
RDFATPTLHT SDQSPGRQSV TIGEVVEEDL APFSLRKRWE SEPHPYVFFN GDHMTMTFIG
FHLETNNNGY VDAINPSNGK VIKKDVMTKE LFDGLRLQRV PFNIDFDNLP RYEKLERLCL
ALGIEWPIDP DETYELTTDN MLKILAIEMR FRCGIPVIIM GETGCGKTRL IKFLSDLKRG
SVEAETMKLV KVHGGTTPSM IYSKVKEAER TAFSNKAQHK LDTILFFDEA NTTEAVSCIK
EILCDRTVDG EHLHEDSGLH IIAACNPYRK HSQEMILRLE SAGLGYRVSA EETADRLGSI
PLRQLVYRVH ALPPSLIPLV WDFGQLNDSA EKLYIQQIVQ RLVDSVSVNP SETCVIADVL
SASQMFMRKR ENECGFVSLR DVERCVKVFR WFHDHSDMLL KELDKFLHES SDSTHTFERD
PVLWSLVMAI GVCYHASLEE KASYRTAIAR CFPKPYNSSR AILDEVTHVQ DLFLRGAPIR
TNIARNLALK ENVFMMVICI ELKIPLFLVG KPGSSKSLAK IIVADAMQGQ AAFSELFRCL
KQVHLVSFQC SPHSTPQGII STFKQCARFQ QGKDLGQYVS VVVLDEVGLA EDSPKMPLKT
LHPLLEDGCI EDDPAPYKKV GFVGISNWAL DPAKMNRGIF VSRGSPNEKE LIESAEGICS
SDRLVQDKIR GYFAPFAKAY ETVCQKQDKE FFGLRDYYSL IKMVFAKAKA SKRGLSPQDI
THAVLRNFSG KDNIQALSIF TASLPEARYK EEVSTVELIK QNIYPGPQAS SRGLDGAESR
YLLVLTRNYV ALQILQQTFF EGQQPEIIFG SSFPQDQEYT QICRNINRVK ICMETGKMVV
LLNLQNLYES LYDALNQYYV YLGGQKYVDL GLGTHRVKCR VHTAFRLIVI EEKDVVYKQF
PVPLINRLEK HYLDMNTVLQ PWQKSIVQEL QQWAHEFADV KADQFIARHK YSPADVFIGY
HSDACASVVL QAVERQGCRD LTEELYRKVS EEARSILLDC ATPDAVVRLS GSSLGSFTAK
QLSQEYYYAQ QHNSFVDFLQ AHLRMTHHEC RAVFTEITTF SRLLTGNDCD VLASELRGLA
SKPVVLSLQQ YDTEYSFLKD VRSWLTNPGK RKVLVIQADF DDGTRSAQLV ASAKYTAINE
INKTQGTKDF VFVYFVTKLS RMGSGTSYVG FHGGLWRSVH IDDLRRSTIM ASDVTKLQNV
TISQLFKPED KPEQEEMEIE TSQSKELAEE QMEVEDSEEM KKASDPRSCD CSQFLDTTRL
VQSCVQGAVG MLRDQNESCA RNMRRVTILL DLLNEDNTRN ASFLRESKMR LHVLLNKQEE
NQVRSLKEWV TREAANQDAL QEAGTFRHTL WKRVQDVVTP ILASMIAHID RDGNLELLAQ
PDSPAWVQDL WMFIYSDIKF LNISLVLNNT RSNSEMSFIL VQSHMNLLKD AYNAVPFSWR
IRDYLEELWV QAQYITDTEG LSKKFVEIFQ KTPLGVFLAQ FPVAQQQKLL QSYLKDFLLL
TMKVSSREEL MFLQMALWSC LRELQEASGT PDETYKFPLS LPWVHLAFQH FRTRLQNFSR
ILTIHPQVLS SLSQAAEKHS LAGCEMTLDA FAAMACAEML KGDLLKPSPK AWLQLVKNLS
TPLELVCSEG YLCDSGSMTR SVIQEVRALW NRIFSIALFV EHVLLGTESH IPELSPLVTT
YVSLLDKCLE EDSNLKTCRP FVAVMTTLCD CKDKASKKFS RFGIQPCFIC HGDAQDPVCL
PCDHVYCLRC IQTWLIPGQM MCPYCLTDLP DKFSPTVSQD HRKAIEKHAQ FRHMCNSFFV
DLVSTMCFKD NTPPEKSVID TLLSLLFVQK ELLRDASQKH REHTKSLSPF DDVVDQTPVI
RSVLLKLLLK YSFHEVKDYI QNYLTQLEKK AFLTEDKTEL YLLFISCLED SVHQKTSAGC
RNLEQVLREE GHFLRTYSPG LQGQEPVRIA SVEYLQEVAR VRLCLDLAAD FLSELQEGSE
LAEDKRRFLK HVEEFCTRVN NDWHRVYLVR KLSSQRGMEF VQSFSKQGHP CQWVFPRKVI
AQQKDHVSLM DRYLVHGNEY KAVRDATAKA VLECKTLDIG NALMACRSPK PQQTAYLLLA
LYTEVAALYR SPNGSLHPEA KQLEAVNKFI KESKILSDPN IRCFARSLVD NTLPLLKIRS
ANSILKGTVT EMAVHVATIL LCGHNQILKP LRNLAFYPVN MANAFLPTMP EDLLVHARTW
RGLENVTWYT CPRGHPCSVG ECGRPMQEST CLDCGLPVGG LNHTPHEGFS AIRNNEDRTQ
TGHVLGSPQS SGVAEVSDRG QSPVVFILTR LLTHLAMLVG ATHNPQALTV IIKPWVQDPQ
GFLQQHIQRD LEQLTKMLGR SADETIHVVH LILSSLLRVQ SHGVLNFNAE LSTKGCRNNW
EKHFETLLLR ELKHLDKNLP AINALISQDE RISSNPVTKI IYGDPATFLP HLPQKSIIHC
SKIWSCRRKI TVEYLQHIVE QKNGKETVPV LWHFLQKEAE LRLVKFLPEI LALQRDLVKQ
FQNVSRVEYS SIRGFIHSHS SDGLRKLLHD RITIFLSTWN ALRRSLETNG EIKLPKDYCC
SDLDLDAEFE VILPRRQGLG LCGTALVSYL ISLHNNMVYT VQKFSNEDNS YSVDISEVAD
LHVISYEVER DLNPLILSNC QYQVQQGGET SQEFDLEKIQ RQISSRFLQG KPRLTLKGIP
TLVYRRDWNY EHLFMDIKNK MAQSSLPNLA ISTISGQLQS YSDACEALSI IEITLGFLST
AGGDPGMDLN VYIEEVLRMC DQTAQVLKAF SRCQLRHIIA LWQFLSAHKS EQRLRLNKEL
FREIDVQYKE ELSTQHQRLL GTFLNEAGLD AFLLELHEMI VLKLKGPRAA NSFNPNWSLK
DTLVSYMETK DSDILSEVES QFPEEILMSS CISVWKIAAT RKWDRQSR
