ORC1B_ARATH
ID ORC1B_ARATH Reviewed; 813 AA.
AC Q9SU24;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Origin of replication complex subunit 1B {ECO:0000303|PubMed:16179646};
DE Short=AtORC1b {ECO:0000303|PubMed:16179646};
DE AltName: Full=Origin recognition complex 1b protein {ECO:0000303|PubMed:16179646};
DE AltName: Full=Protein UNFERTILIZED EMBRYO SAC 13 {ECO:0000303|PubMed:15634699};
GN Name=ORC1B {ECO:0000303|PubMed:16179646};
GN Synonyms=UNE13 {ECO:0000303|PubMed:15634699};
GN OrderedLocusNames=At4g12620 {ECO:0000312|Araport:AT4G12620};
GN ORFNames=T1P17.210 {ECO:0000312|EMBL:CAB53755.1};
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], SUBUNIT, INTERACTION WITH ORC2 AND ORC5, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY E2F AND SUCROSE, GENE
RP FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=16179646; DOI=10.1093/nar/gki854;
RA Diaz-Trivino S., Castellano M.M., Sanchez M.P., Ramirez-Parra E.,
RA Desvoyes B., Gutierrez C.;
RT "The genes encoding Arabidopsis ORC subunits are E2F targets and the two
RT ORC1 genes are differently expressed in proliferating and endoreplicating
RT cells.";
RL Nucleic Acids Res. 33:5404-5414(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 SUBUNIT, TISSUE SPECIFICITY, INDUCTION BY SUCROSE, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=15358564; DOI=10.1016/j.febslet.2004.07.088;
RA Masuda H.P., Ramos G.B.A., de Almeida-Engler J., Cabral L.M.,
RA Coqueiro V.M., Macrini C.M.T., Ferreira P.C.G., Hemerly A.S.;
RT "Genome based identification and analysis of the pre-replicative complex of
RT Arabidopsis thaliana.";
RL FEBS Lett. 574:192-202(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
RN [6]
RP INDUCTION BY E2F.
RX PubMed=16126853; DOI=10.1104/pp.105.066290;
RA Vandepoele K., Vlieghe K., Florquin K., Hennig L., Beemster G.T.S.,
RA Gruissem W., Van de Peer Y., Inze D., De Veylder L.;
RT "Genome-wide identification of potential plant E2F target genes.";
RL Plant Physiol. 139:316-328(2005).
RN [7]
RP REVIEW ON THE CORE DNA REPLICATION MACHINERY.
RX PubMed=17556508; DOI=10.1104/pp.107.101105;
RA Shultz R.W., Tatineni V.M., Hanley-Bowdoin L., Thompson W.F.;
RT "Genome-wide analysis of the core DNA replication machinery in the higher
RT plants Arabidopsis and rice.";
RL Plant Physiol. 144:1697-1714(2007).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH H3K4ME3, AND MUTAGENESIS
RP OF 183-CYS--CYS-186 AND PHE-190.
RX PubMed=19171893; DOI=10.1073/pnas.0811093106;
RA de la Paz Sanchez M., Gutierrez C.;
RT "Arabidopsis ORC1 is a PHD-containing H3K4me3 effector that regulates
RT transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:2065-2070(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 118-349 IN COMPLEX WITH ZINC AND
RP HISTONE H3 PEPTIDE, AND INTERACTION WITH H3.
RX PubMed=26876097; DOI=10.1016/j.str.2016.01.004;
RA Li S., Yang Z., Du X., Liu R., Wilkinson A.W., Gozani O., Jacobsen S.E.,
RA Patel D.J., Du J.;
RT "Structural basis for the unique multivalent readout of unmodified H3 tail
RT by Arabidopsis ORC1b BAH-PHD cassette.";
RL Structure 24:486-494(2016).
CC -!- FUNCTION: Essential protein required for ovules fertilization
CC (PubMed:15634699, PubMed:19171893). Component of the origin recognition
CC complex (ORC) that binds origins of replication. It has a role in both
CC chromosomal replication and mating type transcriptional silencing.
CC Binds to the ARS consensus sequence (ACS) of origins of replication (By
CC similarity). H3K4me3 effector that regulates positively the
CC transcription of a subset of genes (PubMed:19171893).
CC {ECO:0000250|UniProtKB:P54784, ECO:0000269|PubMed:15634699,
CC ECO:0000269|PubMed:19171893}.
CC -!- SUBUNIT: Component of the origin recognition complex (ORC) composed of
CC at least ORC1 (ORC1A or ORC1B), ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is
CC regulated in a cell-cycle and development dependent manner. It is
CC sequentially assembled at the exit from anaphase of mitosis and
CC disassembled as cells enter S phase. Interacts directly with ORC2 and
CC ORC5 (PubMed:15358564, PubMed:16179646). Binds mostly unmodified
CC histone H3, and, with lower efficiency, H3K4me1 H3K4me2 and H3K4me3
CC (PubMed:19171893, PubMed:26876097). {ECO:0000269|PubMed:15358564,
CC ECO:0000269|PubMed:16179646, ECO:0000269|PubMed:19171893,
CC ECO:0000269|PubMed:26876097}.
CC -!- INTERACTION:
CC Q9SU24; B7U179: ABAP1; NbExp=2; IntAct=EBI-2114228, EBI-541722;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P54789,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- TISSUE SPECIFICITY: Follow a cell-cycle regulation with a peak at the
CC G1/S-phase (PubMed:16179646). Mostly expressed in flower buds, and, to
CC a lower exent, in roots, leaves and stems (PubMed:16179646,
CC PubMed:15358564). {ECO:0000269|PubMed:15358564,
CC ECO:0000269|PubMed:16179646}.
CC -!- DEVELOPMENTAL STAGE: Restricted to proliferating cells. First active
CC during embryogenesis, but inactive in mature embryos. Expressed in
CC shoot and root apical meristems. Later observed in lateral root
CC primordia and meristems. Detected in young flower buds, developing
CC anthers and mature pollen. {ECO:0000269|PubMed:16179646}.
CC -!- INDUCTION: Regulated by E2F (PubMed:16179646, PubMed:16126853).
CC Accumulates rapidly after cell cycle reactivation by sucrose addition
CC following cell cycle arrest mediated by sucrose deprivation
CC (PubMed:16179646, PubMed:15358564). {ECO:0000269|PubMed:15358564,
CC ECO:0000269|PubMed:16126853, ECO:0000269|PubMed:16179646}.
CC -!- DISRUPTION PHENOTYPE: Lethal (PubMed:19171893). Unfertilized ovules but
CC normal pollen tube attraction (PubMed:15634699).
CC {ECO:0000269|PubMed:15634699, ECO:0000303|PubMed:19171893}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000305}.
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DR EMBL; AJ426477; CAD20132.1; -; mRNA.
DR EMBL; AL049730; CAB53755.1; -; Genomic_DNA.
DR EMBL; AL161534; CAB78305.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83158.1; -; Genomic_DNA.
DR PIR; E85135; E85135.
DR RefSeq; NP_192999.1; NM_117332.3.
DR PDB; 5HH7; X-ray; 1.90 A; A=118-349.
DR PDBsum; 5HH7; -.
DR AlphaFoldDB; Q9SU24; -.
DR SMR; Q9SU24; -.
DR DIP; DIP-46671N; -.
DR IntAct; Q9SU24; 9.
DR MINT; Q9SU24; -.
DR STRING; 3702.AT4G12620.1; -.
DR iPTMnet; Q9SU24; -.
DR PaxDb; Q9SU24; -.
DR PRIDE; Q9SU24; -.
DR ProteomicsDB; 248904; -.
DR EnsemblPlants; AT4G12620.1; AT4G12620.1; AT4G12620.
DR GeneID; 826875; -.
DR Gramene; AT4G12620.1; AT4G12620.1; AT4G12620.
DR KEGG; ath:AT4G12620; -.
DR Araport; AT4G12620; -.
DR TAIR; locus:2135575; AT4G12620.
DR eggNOG; KOG1514; Eukaryota.
DR HOGENOM; CLU_010923_0_0_1; -.
DR InParanoid; Q9SU24; -.
DR OMA; DSKELPW; -.
DR OrthoDB; 935804at2759; -.
DR PhylomeDB; Q9SU24; -.
DR PRO; PR:Q9SU24; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SU24; baseline and differential.
DR Genevisible; Q9SU24; AT.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IBA:GO_Central.
DR GO; GO:0000808; C:origin recognition complex; ISS:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:TAIR.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; ISS:TAIR.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IMP:TAIR.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR DisProt; DP02966; -.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041083; AAA_lid_10.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR020793; ORC1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10763:SF23; PTHR10763:SF23; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17872; AAA_lid_10; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ATP-binding; DNA replication; DNA-binding;
KW Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..813
FT /note="Origin of replication complex subunit 1B"
FT /id="PRO_0000431427"
FT DOMAIN 226..344
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT ZN_FING 166..215
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..187
FT /note="Histone H3 binding"
FT /evidence="ECO:0000269|PubMed:26876097,
FT ECO:0007744|PDB:5HH7"
FT REGION 203..207
FT /note="Histone H3 binding"
FT /evidence="ECO:0000269|PubMed:26876097,
FT ECO:0007744|PDB:5HH7"
FT REGION 319..324
FT /note="Histone H3 binding"
FT /evidence="ECO:0000269|PubMed:26876097,
FT ECO:0007744|PDB:5HH7"
FT REGION 349..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..803
FT /note="Necessary and sufficient for ORC complex assembly"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MOTIF 83..90
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26876097,
FT ECO:0007744|PDB:5HH7"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26876097,
FT ECO:0007744|PDB:5HH7"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26876097,
FT ECO:0007744|PDB:5HH7"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26876097,
FT ECO:0007744|PDB:5HH7"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26876097,
FT ECO:0007744|PDB:5HH7"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26876097,
FT ECO:0007744|PDB:5HH7"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26876097,
FT ECO:0007744|PDB:5HH7"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26876097,
FT ECO:0007744|PDB:5HH7"
FT BINDING 471..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 561
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 562
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT BINDING 660
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13415"
FT MUTAGEN 183..186
FT /note="CDDC->ADDA: In ORC1b-PHD(C/A); reduced H3K4me3
FT interaction."
FT /evidence="ECO:0000269|PubMed:19171893"
FT MUTAGEN 190
FT /note="F->A: In ORC1b-PHD(F/A); reduced H3K4me3
FT interaction."
FT /evidence="ECO:0000269|PubMed:19171893"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:5HH7"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:5HH7"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:5HH7"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:5HH7"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:5HH7"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:5HH7"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:5HH7"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:5HH7"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:5HH7"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:5HH7"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:5HH7"
FT STRAND 246..258
FT /evidence="ECO:0007829|PDB:5HH7"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:5HH7"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:5HH7"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:5HH7"
FT STRAND 291..300
FT /evidence="ECO:0007829|PDB:5HH7"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:5HH7"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:5HH7"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:5HH7"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:5HH7"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:5HH7"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:5HH7"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:5HH7"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:5HH7"
SQ SEQUENCE 813 AA; 92170 MW; 5F732C91B00944A8 CRC64;
MASTPRAKTF KSPTKTPSNI YRKSYLSPSS TSHTPQTPET HTPLRRSARH VSRKIDLGND
PIDAPGNDPI EGMNLIRKRE RAPRKPTTDV VPSKSKKTET PKKKKKIDSF TPVSPIRSET
IKKTKKKKRV YYNKVEFDET EFEIGDDVYV KRREDSNSDE EEDPEIEDCQ ICFKSDTNIM
IECDDCLGGF HLKCLKPPLK EVPEGDWICQ FCEVKKSGQS QTLDLPKPPE GKKLARTMRE
KLLSGDLWAA RIDKLWKEVD DGVYWIRARW YMIPEETVSG RQPHNLKREL YLTNDFADIE
MECILRHCSV KCPKEFSKAS NDGDDVFLCE YEYDVHWRSF KRLAELADGD SDSDQEWNGR
KEEEVDDSDE EMELDDEVLK SKRGGLTSAR GGANSRKGRF FGVEKVGMKL IPEHVRCHKQ
SELEKAKATL LLATRPKSLP CRSKEMEEIT SFIKGSISDD QCLGRCMYIH GVPGTGKTIS
VLSVMKNLKA EVEEGSVSPY CFVEINGLKL ASPENIYSVI YEALSGHRVG WKKALQCLNE
RFAEGKRIGK EDEKPCILLI DELDLLVTRN QSVLYNILDW PTKPNSKLVV LGIANTMDLP
EKLLPRISSR MGIQRLCFGP YNHTQLQEII STRLNGIDAF EKTAIEFASR KVAAISGDAR
RALEICRRAA EVADHRLNTN KSAKNQLVIM ADVEAAIQEM FQAPHIQVMK SVSKLSKIFL
TAMVHELYKT GMAETTFDRV ATTVSSICLT NGEAFPGWDI LLKIGCDLGE CRIILCEPGE
KHRLQKLQLN FPSDDVAFAL KDNKDLPWLA NYL
