CD48A_ARATH
ID CD48A_ARATH Reviewed; 809 AA.
AC P54609;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Cell division control protein 48 homolog A;
DE Short=AtCDC48a;
GN Name=CDC48A; Synonyms=CDC48; OrderedLocusNames=At3g09840;
GN ORFNames=F8A24.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8521820; DOI=10.1002/j.1460-2075.1995.tb00250.x;
RA Feiler H.S., Desprez T., Santoni V., Kronenberger J., Caboche M., Traas J.;
RT "The higher plant Arabidopsis thaliana encodes a functional CDC48 homologue
RT which is highly expressed in dividing and expanding cells.";
RL EMBO J. 14:5626-5637(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH SYP31 AND KNOLLE, AND SUBUNIT.
RX PubMed=12427991; DOI=10.1104/pp.011742;
RA Rancour D.M., Dickey C.E., Park S., Bednarek S.Y.;
RT "Characterization of AtCDC48. Evidence for multiple membrane fusion
RT mechanisms at the plane of cell division in plants.";
RL Plant Physiol. 130:1241-1253(2002).
RN [6]
RP INTERACTION WITH PUX1, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=15498773; DOI=10.1074/jbc.m405498200;
RA Rancour D.M., Park S., Knight S.D., Bednarek S.Y.;
RT "Plant UBX domain-containing protein 1, PUX1, regulates the oligomeric
RT structure and activity of arabidopsis CDC48.";
RL J. Biol. Chem. 279:54264-54274(2004).
RN [7]
RP INTERACTION WITH PUX1; PUX2; PUX3; PUX4 AND PUX11.
RA Posthuma R., Rancour D., Park S., Bates B., Bednarek S.;
RT "The plant UBX-domain containing (PUX) protein family regulates the
RT function of Arabidopsis CDC48, a conserved essential AAA-ATPase.";
RL (In) Proceedings of the 16th international conference on Arabidopsis
RL research, abstract#116, Madison (2005).
RN [8]
RP INTERACTION WITH SERK1; GRF6 AND KAPP, SUBUNIT, AND IDENTIFICATION IN THE
RP SERK1 COMPLEX.
RX PubMed=15592873; DOI=10.1007/s00425-004-1447-7;
RA Rienties I.M., Vink J., Borst J.W., Russinova E., de Vries S.C.;
RT "The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the
RT 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP.";
RL Planta 221:394-405(2005).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SERK1.
RX PubMed=16621602; DOI=10.1016/j.jsb.2006.03.004;
RA Aker J., Borst J.W., Karlova R., de Vries S.C.;
RT "The Arabidopsis thaliana AAA protein CDC48A interacts in vivo with the
RT somatic embryogenesis receptor-like kinase 1 receptor at the plasma
RT membrane.";
RL J. Struct. Biol. 156:62-71(2006).
RN [10]
RP INTERACTION WITH PUX1; PUX4 AND PUX5, MUTAGENESIS OF LYS-254; GLU-308;
RP LYS-527 AND GLU-581, AND SUBUNIT.
RX PubMed=17190830; DOI=10.1074/jbc.m609042200;
RA Park S., Rancour D.M., Bednarek S.Y.;
RT "Protein domain-domain interactions and requirements for the negative
RT regulation of Arabidopsis CDC48/p97 by the plant ubiquitin regulatory X
RT (UBX) domain-containing protein, PUX1.";
RL J. Biol. Chem. 282:5217-5224(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [12]
RP SUBUNIT, INTERACTION WITH SERK1, AND PHOSPHORYLATION AT SER-41.
RX PubMed=17693538; DOI=10.1104/pp.107.103986;
RA Aker J., Hesselink R., Engel R., Karlova R., Borst J.W., Visser A.J.W.G.,
RA de Vries S.C.;
RT "In vivo hexamerization and characterization of the Arabidopsis AAA ATPase
RT CDC48A complex using forster resonance energy transfer-fluorescence
RT lifetime imaging microscopy and fluorescence correlation spectroscopy.";
RL Plant Physiol. 145:339-350(2007).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP INTERACTION WITH PUX7.
RX PubMed=23747397; DOI=10.1016/j.gene.2013.05.056;
RA Gallois J.L., Drouaud J., Lecureuil A., Guyon-Debast A., Bonhomme S.,
RA Guerche P.;
RT "Functional characterization of the plant ubiquitin regulatory X (UBX)
RT domain-containing protein AtPUX7 in Arabidopsis thaliana.";
RL Gene 526:299-308(2013).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-481 IN COMPLEX WITH ADP.
RA Heinemann U., Roske Y., Banchenko S., Arumughan A., Wanker E., Petrovic S.;
RT "Common mode of remodeling AAA ATPases p97/CDC48 by their disassembly
RT cofactors ASPL/PUX1.";
RL Submitted (AUG-2018) to the PDB data bank.
CC -!- FUNCTION: Probably functions in cell division and growth processes.
CC Interacts with certain SNAREs as part of specialized membrane fusion
CC events where vesicles from the same organelle fuse (homotypic fusion)
CC (By similarity). {ECO:0000250}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40.5 uM for ATP (at 22 degrees Celsius)
CC {ECO:0000269|PubMed:15498773};
CC Vmax=3.47 umol/min/ug enzyme with ATP as substrate (at 22 degrees
CC Celsius) {ECO:0000269|PubMed:15498773};
CC -!- SUBUNIT: Homohexamer (PubMed:15498773, PubMed:17190830). Interacts with
CC SERK1, GRF6, KAPP and SYP31, but not with KNOLLE. Component of the
CC SERK1 signaling complex, composed of KAPP, CDC48A, GRF6 or GRF7, SERK1,
CC SERK2, SERK3/BAK1 and BRI1 (PubMed:12427991, PubMed:15592873,
CC PubMed:16621602, PubMed:17693538, PubMed:23747397). Interacts with
CC PUX1, PUX2, PUX3, PUX4, PUX5, PUX7 and PUX11 via its N-terminus
CC (PubMed:15498773, Ref.7, PubMed:17190830).
CC {ECO:0000269|PubMed:12427991, ECO:0000269|PubMed:15498773,
CC ECO:0000269|PubMed:15592873, ECO:0000269|PubMed:16621602,
CC ECO:0000269|PubMed:17190830, ECO:0000269|PubMed:17693538,
CC ECO:0000269|PubMed:23747397, ECO:0000269|Ref.7}.
CC -!- INTERACTION:
CC P54609; P54609: CDC48A; NbExp=5; IntAct=EBI-1563238, EBI-1563238;
CC P54609; Q94JZ8: PUX7; NbExp=3; IntAct=EBI-1563238, EBI-10684297;
CC P54609; Q94AG2: SERK1; NbExp=12; IntAct=EBI-1563238, EBI-1555537;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, phragmoplast.
CC Cell membrane; Peripheral membrane protein. Note=Primarily localized to
CC the nucleus and, during cytokinesis, to the phragmoplast, a site where
CC membrane vesicles are targeted in the deposition of new cell wall
CC materials.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the proliferating cells of the
CC vegetative shoot, root, floral inflorescence and flowers, and in
CC rapidly growing cells.
CC -!- PTM: Phosphorylated on at least one threonine residue and on Ser-41 by
CC SERK1. {ECO:0000269|PubMed:17693538}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; U37587; AAC49120.1; -; mRNA.
DR EMBL; AC015985; AAF23260.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74820.1; -; Genomic_DNA.
DR EMBL; AY065076; AAL38252.1; -; mRNA.
DR EMBL; AY094434; AAM19807.1; -; mRNA.
DR PIR; S60112; S60112.
DR RefSeq; NP_187595.1; NM_111819.5.
DR PDB; 6HD3; X-ray; 2.80 A; A/C=1-481.
DR PDBsum; 6HD3; -.
DR AlphaFoldDB; P54609; -.
DR SMR; P54609; -.
DR BioGRID; 5476; 79.
DR IntAct; P54609; 4.
DR STRING; 3702.AT3G09840.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR iPTMnet; P54609; -.
DR MetOSite; P54609; -.
DR SwissPalm; P54609; -.
DR PaxDb; P54609; -.
DR PRIDE; P54609; -.
DR ProteomicsDB; 223907; -.
DR EnsemblPlants; AT3G09840.1; AT3G09840.1; AT3G09840.
DR GeneID; 820142; -.
DR Gramene; AT3G09840.1; AT3G09840.1; AT3G09840.
DR KEGG; ath:AT3G09840; -.
DR Araport; AT3G09840; -.
DR TAIR; locus:2085064; AT3G09840.
DR eggNOG; KOG0730; Eukaryota.
DR HOGENOM; CLU_000688_12_0_1; -.
DR InParanoid; P54609; -.
DR OMA; VEMRHFR; -.
DR OrthoDB; 194195at2759; -.
DR PhylomeDB; P54609; -.
DR PRO; PR:P54609; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P54609; baseline and differential.
DR Genevisible; P54609; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005811; C:lipid droplet; IDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005819; C:spindle; IDA:TAIR.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0051228; P:mitotic spindle disassembly; IBA:GO_Central.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0031648; P:protein destabilization; IMP:TAIR.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005938; AAA_ATPase_CDC48.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR TIGRFAMs; TIGR01243; CDC48; 1.
DR PROSITE; PS00674; AAA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
KW Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..809
FT /note="Cell division control protein 48 homolog A"
FT /id="PRO_0000084579"
FT REGION 782..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|Ref.15, ECO:0007744|PDB:6HD3"
FT BINDING 248..256
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|Ref.15, ECO:0007744|PDB:6HD3"
FT BINDING 387
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|Ref.15, ECO:0007744|PDB:6HD3"
FT BINDING 521..529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17693538"
FT MUTAGEN 254
FT /note="K->A: Decreases ATPase activity."
FT /evidence="ECO:0000269|PubMed:17190830"
FT MUTAGEN 308
FT /note="E->Q: Decreases ATPase activity."
FT /evidence="ECO:0000269|PubMed:17190830"
FT MUTAGEN 527
FT /note="K->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:17190830"
FT MUTAGEN 581
FT /note="E->Q: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:17190830"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:6HD3"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:6HD3"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 163..180
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 213..228
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 274..278
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 284..298
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:6HD3"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:6HD3"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 322..337
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 344..351
FT /evidence="ECO:0007829|PDB:6HD3"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:6HD3"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 377..386
FT /evidence="ECO:0007829|PDB:6HD3"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 399..405
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 411..429
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:6HD3"
FT HELIX 452..460
FT /evidence="ECO:0007829|PDB:6HD3"
SQ SEQUENCE 809 AA; 89393 MW; 93222D637EA193B0 CRC64;
MSTPAESSDS KSKKDFSTAI LERKKSPNRL VVDEAINDDN SVVSLHPATM EKLQLFRGDT
ILIKGKKRKD TVCIALADET CEEPKIRMNK VVRSNLRVRL GDVISVHQCP DVKYGKRVHI
LPVDDTVEGV TGNLFDAYLK PYFLEAYRPV RKGDLFLVRG GMRSVEFKVI ETDPAEYCVV
APDTEIFCEG EPVKREDEER LDDVGYDDVG GVRKQMAQIR ELVELPLRHP QLFKSIGVKP
PKGILLYGPP GSGKTLIARA VANETGAFFF CINGPEIMSK LAGESESNLR KAFEEAEKNA
PSIIFIDEID SIAPKREKTN GEVERRIVSQ LLTLMDGLKS RAHVIVMGAT NRPNSIDPAL
RRFGRFDREI DIGVPDEIGR LEVLRIHTKN MKLAEDVDLE RISKDTHGYV GADLAALCTE
AALQCIREKM DVIDLEDDSI DAEILNSMAV TNEHFHTALG NSNPSALRET VVEVPNVSWN
DIGGLENVKR ELQETVQYPV EHPEKFEKFG MSPSKGVLFY GPPGCGKTLL AKAIANECQA
NFISVKGPEL LTMWFGESEA NVREIFDKAR QSAPCVLFFD ELDSIATQRG GGSGGDGGGA
ADRVLNQLLT EMDGMNAKKT VFIIGATNRP DIIDSALLRP GRLDQLIYIP LPDEDSRLNI
FKAALRKSPI AKDVDIGALA KYTQGFSGAD ITEICQRACK YAIRENIEKD IEKEKRRSEN
PEAMEEDGVD EVSEIKAAHF EESMKYARRS VSDADIRKYQ AFAQTLQQSR GFGSEFRFEN
SAGSGATTGV ADPFATSAAA AGDDDDLYN
