PCNA_YEAST
ID PCNA_YEAST Reviewed; 258 AA.
AC P15873; D6VQ89;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Proliferating cell nuclear antigen;
DE Short=PCNA;
GN Name=POL30; OrderedLocusNames=YBR088C; ORFNames=YBR0811;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-41 AND
RP 231-240.
RX PubMed=1970160; DOI=10.1093/nar/18.2.261;
RA Bauer G.A., Burgess P.M.J.;
RT "Molecular cloning, structure and expression of the yeast proliferating
RT cell nuclear antigen gene.";
RL Nucleic Acids Res. 18:261-265(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, AND INTERACTION WITH RAD30.
RX PubMed=11545742; DOI=10.1016/s1097-2765(01)00319-7;
RA Haracska L., Kondratick C.M., Unk I., Prakash S., Prakash L.;
RT "Interaction with PCNA is essential for yeast DNA polymerase eta
RT function.";
RL Mol. Cell 8:407-415(2001).
RN [7]
RP FUNCTION, SUMOYLATION AT LYS-127 AND LYS-164, UBIQUITINATION AT LYS-164,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12226657; DOI=10.1038/nature00991;
RA Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.;
RT "RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin
RT and SUMO.";
RL Nature 419:135-141(2002).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-127 AND LYS-164, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15166219; DOI=10.1074/jbc.m404173200;
RA Zhou W., Ryan J.J., Zhou H.;
RT "Global analyses of sumoylated proteins in Saccharomyces cerevisiae.
RT Induction of protein sumoylation by cellular stresses.";
RL J. Biol. Chem. 279:32262-32268(2004).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=EJY251-11b;
RX PubMed=15542864; DOI=10.1074/mcp.m400154-mcp200;
RA Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D.,
RA Gygi S.P.;
RT "A proteomic strategy for gaining insights into protein sumoylation in
RT yeast.";
RL Mol. Cell. Proteomics 4:246-254(2005).
RN [10]
RP INTERACTION WITH MCM10.
RX PubMed=16782870; DOI=10.1128/mcb.02062-05;
RA Das-Bradoo S., Ricke R.M., Bielinsky A.-K.;
RT "Interaction between PCNA and diubiquitinated Mcm10 is essential for cell
RT growth in budding yeast.";
RL Mol. Cell. Biol. 26:4806-4817(2006).
RN [11]
RP DEUBIQUITINATION BY UBP10, AND INTERACTION WITH UBP10.
RX PubMed=22829782; DOI=10.1371/journal.pgen.1002826;
RA Gallego-Sanchez A., Andres S., Conde F., San-Segundo P.A., Bueno A.;
RT "Reversal of PCNA ubiquitylation by Ubp10 in Saccharomyces cerevisiae.";
RL PLoS Genet. 8:E1002826-E1002826(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=8001157; DOI=10.1016/0092-8674(94)90014-0;
RA Krishna T.S., Kong X.P., Gary S., Burgers P.M., Kuriyan J.;
RT "Crystal structure of the eukaryotic DNA polymerase processivity factor
RT PCNA.";
RL Cell 79:1233-1243(1994).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH RFC1; RCF2; RCF3;
RP RCF4 AND RCF5.
RX PubMed=15201901; DOI=10.1038/nature02585;
RA Bowman G.D., O'Donnell M., Kuriyan J.;
RT "Structural analysis of a eukaryotic sliding DNA clamp-clamp loader
RT complex.";
RL Nature 429:724-730(2004).
CC -!- FUNCTION: This protein is an auxiliary protein of DNA polymerase delta
CC and is involved in the control of eukaryotic DNA replication by
CC increasing the polymerase's processibility during elongation of the
CC leading strand. Involved in DNA repair. {ECO:0000269|PubMed:11545742,
CC ECO:0000269|PubMed:12226657}.
CC -!- SUBUNIT: Homotrimer (PubMed:15201901). Interacts with RAD30
CC (PubMed:11545742). Interacts with MCM10 (PubMed:16782870). Interacts
CC with UBP10 (PubMed:22829782). {ECO:0000269|PubMed:11545742,
CC ECO:0000269|PubMed:15201901, ECO:0000269|PubMed:16782870,
CC ECO:0000269|PubMed:22829782}.
CC -!- INTERACTION:
CC P15873; P43605: ECO1; NbExp=2; IntAct=EBI-12993, EBI-22988;
CC P15873; Q12050: ELG1; NbExp=9; IntAct=EBI-12993, EBI-32195;
CC P15873; P32354: MCM10; NbExp=4; IntAct=EBI-12993, EBI-5965;
CC P15873; Q03834: MSH6; NbExp=5; IntAct=EBI-12993, EBI-11383;
CC P15873; P15873: POL30; NbExp=10; IntAct=EBI-12993, EBI-12993;
CC P15873; P47110: POL32; NbExp=4; IntAct=EBI-12993, EBI-6084;
CC P15873; P26793: RAD27; NbExp=7; IntAct=EBI-12993, EBI-14693;
CC P15873; Q04049: RAD30; NbExp=7; IntAct=EBI-12993, EBI-36214;
CC P15873; Q12495: RLF2; NbExp=3; IntAct=EBI-12993, EBI-3913;
CC P15873; Q12306: SMT3; NbExp=6; IntAct=EBI-12993, EBI-17490;
CC P15873; P12954: SRS2; NbExp=10; IntAct=EBI-12993, EBI-18110;
CC P15873; P12887: UNG1; NbExp=4; IntAct=EBI-12993, EBI-2097931;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Sumoylated on Lys-164, and to a lesser extent on Lys-127 by the
CC UBC9/SIZ1 complex during S-phase; which impairs ubiquitination and
CC function in DNA repair. {ECO:0000269|PubMed:12226657,
CC ECO:0000269|PubMed:15166219, ECO:0000269|PubMed:15542864}.
CC -!- PTM: Monoubiquitinated on Lys-164 by the UBC2/RAD18 complex upon DNA
CC damage, and then polyubiquitinated through 'Lys-63'-linkage by
CC UBC13/MMS2. Ubiquitination is required for UBC2-mediated DNA repair.
CC {ECO:0000269|PubMed:12226657}.
CC -!- PTM: Lys-164 is deubiquitinated by UBP10 (PubMed:22829782).
CC {ECO:0000269|PubMed:22829782}.
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000305}.
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DR EMBL; X16676; CAA34664.1; -; Genomic_DNA.
DR EMBL; X78993; CAA55594.1; -; Genomic_DNA.
DR EMBL; Z35957; CAA85038.1; -; Genomic_DNA.
DR EMBL; AY557715; AAS56041.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07209.1; -; Genomic_DNA.
DR PIR; S22851; WMBYET.
DR RefSeq; NP_009645.1; NM_001178436.1.
DR PDB; 1PLQ; X-ray; 2.30 A; A=1-258.
DR PDB; 1PLR; X-ray; 3.00 A; A=1-258.
DR PDB; 1SXJ; X-ray; 2.85 A; F/G/H=1-258.
DR PDB; 2OD8; X-ray; 2.80 A; A=1-258.
DR PDB; 3F1W; X-ray; 2.90 A; A=1-258.
DR PDB; 3GPM; X-ray; 3.80 A; A=1-258.
DR PDB; 3GPN; X-ray; 2.50 A; A=1-258.
DR PDB; 3L0W; X-ray; 2.80 A; A=1-163.
DR PDB; 3L0X; X-ray; 3.00 A; A=1-163, B=165-258.
DR PDB; 3L10; X-ray; 2.80 A; A=1-163.
DR PDB; 3PGE; X-ray; 2.80 A; A=165-258, B=1-163.
DR PDB; 3V60; X-ray; 2.60 A; B=1-258.
DR PDB; 3V61; X-ray; 2.80 A; B=1-258.
DR PDB; 3V62; X-ray; 2.90 A; B/E=1-258.
DR PDB; 4L60; X-ray; 3.00 A; A=1-256.
DR PDB; 4L6P; X-ray; 2.68 A; A/B/C=1-258.
DR PDB; 4YHR; X-ray; 2.95 A; A=1-258.
DR PDB; 5JNE; X-ray; 2.85 A; D/H=1-258.
DR PDB; 5T9D; X-ray; 3.27 A; A/B/C=2-258.
DR PDB; 5V7K; X-ray; 3.05 A; A=1-258.
DR PDB; 5V7L; X-ray; 3.20 A; A=1-258.
DR PDB; 5V7M; X-ray; 1.93 A; A=1-258.
DR PDB; 5ZUT; X-ray; 2.82 A; A=1-258.
DR PDB; 6CX2; X-ray; 3.10 A; A=1-258.
DR PDB; 6CX3; X-ray; 3.10 A; A=1-258.
DR PDB; 6CX4; X-ray; 3.08 A; A=1-258.
DR PDB; 6D0Q; X-ray; 2.80 A; A=1-258.
DR PDB; 6D0R; X-ray; 2.86 A; A=1-258.
DR PDB; 6E49; X-ray; 2.90 A; A/B/C=1-258.
DR PDB; 6W9W; X-ray; 2.65 A; A=1-254.
DR PDB; 6WAC; X-ray; 2.90 A; A=1-253.
DR PDB; 7KC0; EM; 3.20 A; E/F/G=1-258.
DR PDB; 7THJ; EM; 3.80 A; F/G/H=1-258.
DR PDB; 7THV; EM; 4.00 A; F/G/H=1-258.
DR PDB; 7TI8; EM; 3.50 A; F/G/H=1-258.
DR PDB; 7TIB; EM; 3.40 A; F/G/H=1-258.
DR PDB; 7TIC; EM; 3.90 A; F/G/H=1-258.
DR PDB; 7TID; EM; 3.30 A; F/G/H=1-258.
DR PDB; 7TKU; EM; 4.00 A; F/G/H=1-258.
DR PDBsum; 1PLQ; -.
DR PDBsum; 1PLR; -.
DR PDBsum; 1SXJ; -.
DR PDBsum; 2OD8; -.
DR PDBsum; 3F1W; -.
DR PDBsum; 3GPM; -.
DR PDBsum; 3GPN; -.
DR PDBsum; 3L0W; -.
DR PDBsum; 3L0X; -.
DR PDBsum; 3L10; -.
DR PDBsum; 3PGE; -.
DR PDBsum; 3V60; -.
DR PDBsum; 3V61; -.
DR PDBsum; 3V62; -.
DR PDBsum; 4L60; -.
DR PDBsum; 4L6P; -.
DR PDBsum; 4YHR; -.
DR PDBsum; 5JNE; -.
DR PDBsum; 5T9D; -.
DR PDBsum; 5V7K; -.
DR PDBsum; 5V7L; -.
DR PDBsum; 5V7M; -.
DR PDBsum; 5ZUT; -.
DR PDBsum; 6CX2; -.
DR PDBsum; 6CX3; -.
DR PDBsum; 6CX4; -.
DR PDBsum; 6D0Q; -.
DR PDBsum; 6D0R; -.
DR PDBsum; 6E49; -.
DR PDBsum; 6W9W; -.
DR PDBsum; 6WAC; -.
DR PDBsum; 7KC0; -.
DR PDBsum; 7THJ; -.
DR PDBsum; 7THV; -.
DR PDBsum; 7TI8; -.
DR PDBsum; 7TIB; -.
DR PDBsum; 7TIC; -.
DR PDBsum; 7TID; -.
DR PDBsum; 7TKU; -.
DR AlphaFoldDB; P15873; -.
DR SASBDB; P15873; -.
DR SMR; P15873; -.
DR BioGRID; 32794; 472.
DR ComplexPortal; CPX-544; PCNA homotrimer.
DR DIP; DIP-2417N; -.
DR IntAct; P15873; 36.
DR MINT; P15873; -.
DR STRING; 4932.YBR088C; -.
DR iPTMnet; P15873; -.
DR MaxQB; P15873; -.
DR PaxDb; P15873; -.
DR PRIDE; P15873; -.
DR TopDownProteomics; P15873; -.
DR EnsemblFungi; YBR088C_mRNA; YBR088C; YBR088C.
DR GeneID; 852385; -.
DR KEGG; sce:YBR088C; -.
DR SGD; S000000292; POL30.
DR VEuPathDB; FungiDB:YBR088C; -.
DR eggNOG; KOG1636; Eukaryota.
DR GeneTree; ENSGT00390000004965; -.
DR HOGENOM; CLU_043978_3_0_1; -.
DR InParanoid; P15873; -.
DR OMA; EMKLINM; -.
DR BioCyc; YEAST:G3O-29055-MON; -.
DR Reactome; R-SCE-110312; Translesion synthesis by REV1.
DR Reactome; R-SCE-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SCE-110320; Translesion Synthesis by POLH.
DR Reactome; R-SCE-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-SCE-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-SCE-5655862; Translesion synthesis by POLK.
DR Reactome; R-SCE-5656121; Translesion synthesis by POLI.
DR Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-69091; Polymerase switching.
DR Reactome; R-SCE-69166; Removal of the Flap Intermediate.
DR Reactome; R-SCE-69183; Processive synthesis on the lagging strand.
DR EvolutionaryTrace; P15873; -.
DR PRO; PR:P15873; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P15873; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0043626; C:PCNA complex; IPI:SGD.
DR GO; GO:0005657; C:replication fork; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0070987; P:error-free translesion synthesis; IGI:SGD.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IGI:SGD.
DR GO; GO:0006273; P:lagging strand elongation; IDA:SGD.
DR GO; GO:0006272; P:leading strand elongation; IDA:SGD.
DR GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IMP:SGD.
DR GO; GO:0000710; P:meiotic mismatch repair; IMP:SGD.
DR GO; GO:0006298; P:mismatch repair; IMP:SGD.
DR GO; GO:0000278; P:mitotic cell cycle; IGI:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IGI:SGD.
DR GO; GO:0006289; P:nucleotide-excision repair; IMP:SGD.
DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:ComplexPortal.
DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:ComplexPortal.
DR GO; GO:1902394; P:positive regulation of exodeoxyribonuclease activity; IDA:SGD.
DR GO; GO:1905779; P:positive regulation of exonuclease activity; IDA:SGD.
DR GO; GO:1903022; P:positive regulation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands; IDA:SGD.
DR GO; GO:0006301; P:postreplication repair; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0019985; P:translesion synthesis; IBA:GO_Central.
DR HAMAP; MF_00317; DNApol_clamp_arch; 1.
DR InterPro; IPR000730; Pr_cel_nuc_antig.
DR InterPro; IPR022649; Pr_cel_nuc_antig_C.
DR InterPro; IPR022659; Pr_cel_nuc_antig_CS.
DR InterPro; IPR022648; Pr_cel_nuc_antig_N.
DR PANTHER; PTHR11352:SF0; PTHR11352:SF0; 1.
DR Pfam; PF02747; PCNA_C; 1.
DR Pfam; PF00705; PCNA_N; 1.
DR PRINTS; PR00339; PCNACYCLIN.
DR TIGRFAMs; TIGR00590; pcna; 1.
DR PROSITE; PS01251; PCNA_1; 1.
DR PROSITE; PS00293; PCNA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair;
KW DNA replication; DNA-binding; Isopeptide bond; Nucleus; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..258
FT /note="Proliferating cell nuclear antigen"
FT /id="PRO_0000149176"
FT DNA_BIND 61..80
FT /evidence="ECO:0000255"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15166219"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000269|PubMed:15166219,
FT ECO:0000269|PubMed:15542864"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:12226657"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:5V7M"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:5V7M"
FT TURN 18..22
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:5ZUT"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:5V7M"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:5V7M"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5V7K"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:5V7M"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3V62"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:7KC0"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:5V7M"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:3V60"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:5V7M"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:5V7M"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:5V7M"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1PLQ"
SQ SEQUENCE 258 AA; 28916 MW; 9B56C5851621DDDC CRC64;
MLEAKFEEAS LFKRIIDGFK DCVQLVNFQC KEDGIIAQAV DDSRVLLVSL EIGVEAFQEY
RCDHPVTLGM DLTSLSKILR CGNNTDTLTL IADNTPDSII LLFEDTKKDR IAEYSLKLMD
IDADFLKIEE LQYDSTLSLP SSEFSKIVRD LSQLSDSINI MITKETIKFV ADGDIGSGSV
IIKPFVDMEH PETSIKLEMD QPVDLTFGAK YLLDIIKGSS LSDRVGIRLS SEAPALFQFD
LKSGFLQFFL APKFNDEE
