DPOD_YEAST
ID DPOD_YEAST Reviewed; 1097 AA.
AC P15436; D6VRP8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=DNA polymerase delta catalytic subunit;
DE EC=2.7.7.7 {ECO:0000269|PubMed:22119860};
DE AltName: Full=3'-5' exodeoxyribonuclease {ECO:0000305};
DE EC=3.1.11.- {ECO:0000269|PubMed:1648480};
DE AltName: Full=DNA polymerase III;
GN Name=POL3; Synonyms=CDC2, TEX1; OrderedLocusNames=YDL102W; ORFNames=D2366;
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 FUNCTION.
RC STRAIN=YAB2;
RX PubMed=2670563; DOI=10.1002/j.1460-2075.1989.tb03580.x;
RA Boulet A., Simon M., Faye G., Bauer G.A., Burgers M.J.;
RT "Structure and function of the Saccharomyces cerevisiae CDC2 gene encoding
RT the large subunit of DNA polymerase III.";
RL EMBO J. 8:1849-1854(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX PubMed=1741270; DOI=10.1093/nar/20.2.375;
RA Morrison A., Sugino A.;
RT "Nucleotide sequence of the POL3 gene encoding DNA polymerase III (delta)
RT of Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 20:375-375(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896274;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1077::aid-yea8>3.0.co;2-z;
RA Saiz J.E., Buitrago M.J., Garcia R., Revuelta J.L., del Rey F.;
RT "The sequence of a 20.3 kb DNA fragment from the left arm of Saccharomyces
RT cerevisiae chromosome IV contains the KIN28, MSS2, PHO2, POL3 and DUN1
RT genes, and six new open reading frames.";
RL Yeast 12:1077-1084(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [5]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 78-79.
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 [6]
RP FUNCTION AS AN EXONUCLEASE.
RX PubMed=1648480; DOI=10.1002/j.1460-2075.1991.tb07751.x;
RA Simon M., Giot L., Faye G.;
RT "The 3' to 5' exonuclease activity located in the DNA polymerase delta
RT subunit of Saccharomyces cerevisiae is required for accurate replication.";
RL EMBO J. 10:2165-2170(1991).
RN [7]
RP COMPOSITION OF THE DNA POLYMERASE DELTA COMPLEX.
RX PubMed=11568188; DOI=10.1074/jbc.m108842200;
RA Johansson E., Majka J., Burgers P.M.;
RT "Structure of DNA polymerase delta from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 276:43824-43828(2001).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-37, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, IRON-SULFUR-BINDING, ZINC-BINDING,
RP INTERACTION WITH PCNA, AND MUTAGENESIS OF CYS-1009; CYS-1012; CYS-1024;
RP CYS-1027; CYS-1056; CYS-1069; CYS-1069 AND CYS-1074.
RX PubMed=22119860; DOI=10.1038/nchembio.721;
RA Netz D.J., Stith C.M., Stumpfig M., Kopf G., Vogel D., Genau H.M.,
RA Stodola J.L., Lill R., Burgers P.M., Pierik A.J.;
RT "Eukaryotic DNA polymerases require an iron-sulfur cluster for the
RT formation of active complexes.";
RL Nat. Chem. Biol. 8:125-132(2012).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF LEU-612.
RX PubMed=31488849; DOI=10.1038/s41467-019-11995-z;
RA Zhou Z.X., Lujan S.A., Burkholder A.B., Garbacz M.A., Kunkel T.A.;
RT "Roles for DNA polymerase delta in initiating and terminating leading
RT strand DNA replication.";
RL Nat. Commun. 10:3992-3992(2019).
CC -!- FUNCTION: Catalytic component of DNA polymerase delta (DNA polymerase
CC III) which participates in chromosomal DNA replication (PubMed:2670563,
CC PubMed:22119860, PubMed:31488849). Required during synthesis of the
CC lagging DNA strands at the replication fork, binds at/or near
CC replication origins and moves along DNA with the replication fork
CC (PubMed:31488849). Participates in leading strand synthesis during
CC replication initiation and termination (PubMed:31488849). Has 3'-5'
CC proofreading exonuclease activity that corrects errors arising during
CC DNA replication (PubMed:1648480). {ECO:0000269|PubMed:1648480,
CC ECO:0000269|PubMed:22119860, ECO:0000269|PubMed:2670563,
CC ECO:0000269|PubMed:31488849}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000269|PubMed:22119860};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:22119860};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:22119860};
CC -!- SUBUNIT: DNA polymerase delta is a heterotrimer of POL3, POL32 and
CC HYS2. Interacts with PCNA. {ECO:0000269|PubMed:22119860}.
CC -!- INTERACTION:
CC P15436; P46957: POL31; NbExp=6; IntAct=EBI-6134, EBI-6080;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The CysA-type zinc finger is required for PCNA-binding.
CC {ECO:0000269|PubMed:22119860}.
CC -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC formation of polymerase complexes. {ECO:0000269|PubMed:22119860}.
CC -!- MISCELLANEOUS: In eukaryotes there are five DNA polymerases: alpha,
CC beta, gamma, delta, and epsilon which are responsible for different
CC reactions of DNA synthesis.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR EMBL; X15477; CAA33504.1; -; Genomic_DNA.
DR EMBL; X61920; CAA43922.1; -; Genomic_DNA.
DR EMBL; X95644; CAA64911.1; -; Genomic_DNA.
DR EMBL; Z74150; CAA98669.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11758.2; -; Genomic_DNA.
DR PIR; S67644; RNBYL3.
DR RefSeq; NP_010181.2; NM_001180161.2.
DR PDB; 3IAY; X-ray; 2.00 A; A=67-985.
DR PDB; 6P1H; EM; 3.20 A; A=1-1097.
DR PDB; 7KC0; EM; 3.20 A; A=1-1097.
DR PDBsum; 3IAY; -.
DR PDBsum; 6P1H; -.
DR PDBsum; 7KC0; -.
DR AlphaFoldDB; P15436; -.
DR SMR; P15436; -.
DR BioGRID; 31960; 683.
DR ComplexPortal; CPX-2101; DNA polymerase delta complex.
DR DIP; DIP-2524N; -.
DR IntAct; P15436; 4.
DR MINT; P15436; -.
DR STRING; 4932.YDL102W; -.
DR iPTMnet; P15436; -.
DR MaxQB; P15436; -.
DR PaxDb; P15436; -.
DR PRIDE; P15436; -.
DR TopDownProteomics; P15436; -.
DR EnsemblFungi; YDL102W_mRNA; YDL102W; YDL102W.
DR GeneID; 851456; -.
DR KEGG; sce:YDL102W; -.
DR SGD; S000002260; POL3.
DR VEuPathDB; FungiDB:YDL102W; -.
DR eggNOG; KOG0969; Eukaryota.
DR GeneTree; ENSGT00560000077365; -.
DR HOGENOM; CLU_000203_2_0_1; -.
DR InParanoid; P15436; -.
DR OMA; GNQKSPY; -.
DR BioCyc; YEAST:G3O-29505-MON; -.
DR Reactome; R-SCE-69166; Removal of the Flap Intermediate.
DR Reactome; R-SCE-69183; Processive synthesis on the lagging strand.
DR PRO; PR:P15436; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P15436; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043625; C:delta DNA polymerase complex; IPI:ComplexPortal.
DR GO; GO:0005657; C:replication fork; IDA:SGD.
DR GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IMP:SGD.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006287; P:base-excision repair, gap-filling; IBA:GO_Central.
DR GO; GO:0006259; P:DNA metabolic process; IDA:ComplexPortal.
DR GO; GO:0006260; P:DNA replication; IMP:SGD.
DR GO; GO:0045004; P:DNA replication proofreading; IMP:SGD.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IDA:SGD.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:0045005; P:DNA-templated DNA replication maintenance of fidelity; IGI:SGD.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR GO; GO:0006278; P:RNA-templated DNA biosynthetic process; IDA:SGD.
DR DisProt; DP02848; -.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF14260; zf-C4pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Exonuclease; Hydrolase; Iron; Iron-sulfur;
KW Metal-binding; Nuclease; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1097
FT /note="DNA polymerase delta catalytic subunit"
FT /id="PRO_0000046454"
FT ZN_FING 1009..1027
FT /note="CysA-type"
FT /evidence="ECO:0000269|PubMed:22119860"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1056..1074
FT /note="CysB motif"
FT /evidence="ECO:0000269|PubMed:22119860"
FT BINDING 1009
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22119860"
FT BINDING 1012
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22119860"
FT BINDING 1024
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22119860"
FT BINDING 1027
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22119860"
FT BINDING 1056
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:22119860"
FT BINDING 1059
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:22119860"
FT BINDING 1069
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:22119860"
FT BINDING 1074
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:22119860"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 612
FT /note="L->G: Increases rates of C-to-A transversion
FT substitutions."
FT /evidence="ECO:0000269|PubMed:31488849"
FT MUTAGEN 1009
FT /note="C->A: Impairs iron-sulfur-binding."
FT /evidence="ECO:0000269|PubMed:22119860"
FT MUTAGEN 1012
FT /note="C->A: Impairs iron-sulfur-binding."
FT /evidence="ECO:0000269|PubMed:22119860"
FT MUTAGEN 1024
FT /note="C->A: Impairs iron-sulfur-binding."
FT /evidence="ECO:0000269|PubMed:22119860"
FT MUTAGEN 1027
FT /note="C->A: Impairs iron-sulfur-binding."
FT /evidence="ECO:0000269|PubMed:22119860"
FT MUTAGEN 1056
FT /note="C->A: Abolishes iron-sulfur-binding."
FT /evidence="ECO:0000269|PubMed:22119860"
FT MUTAGEN 1059
FT /note="C->A: Abolishes iron-sulfur-binding."
FT MUTAGEN 1069
FT /note="C->A: Abolishes iron-sulfur-binding."
FT /evidence="ECO:0000269|PubMed:22119860"
FT MUTAGEN 1074
FT /note="C->A: Abolishes iron-sulfur-binding."
FT /evidence="ECO:0000269|PubMed:22119860"
FT MUTAGEN 1074
FT /note="C->S: In pol3-13; synthetically lethal with
FT mutations of NBP35, DRE2 and TAH18."
FT /evidence="ECO:0000269|PubMed:22119860"
FT CONFLICT 78..79
FT /note="EL -> DV (in Ref. 1; CAA33504, 3; CAA64911 and 4;
FT CAA98669)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="H -> R (in Ref. 1; CAA33504)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="G -> D (in Ref. 1; CAA33504)"
FT /evidence="ECO:0000305"
FT CONFLICT 347..363
FT /note="SIAGAKKPFIRNVFTLN -> YLALRNHSFVMCYSD (in Ref. 1;
FT CAA33504)"
FT /evidence="ECO:0000305"
FT CONFLICT 647..649
FT /note="TPN -> HY (in Ref. 1; CAA33504)"
FT /evidence="ECO:0000305"
FT CONFLICT 870
FT /note="V -> D (in Ref. 1; CAA33504)"
FT /evidence="ECO:0000305"
FT CONFLICT 974
FT /note="Missing (in Ref. 1; CAA33504)"
FT /evidence="ECO:0000305"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6P1H"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 113..124
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:7KC0"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:3IAY"
FT TURN 185..189
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 191..203
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:6P1H"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:3IAY"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:7KC0"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:7KC0"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:3IAY"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 316..324
FT /evidence="ECO:0007829|PDB:3IAY"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 339..348
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 355..363
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 371..378
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 379..393
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:3IAY"
FT TURN 403..406
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 407..417
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:3IAY"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 464..471
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 479..487
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 499..503
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 507..530
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 533..544
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 550..553
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 556..570
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 604..609
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 612..619
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 624..626
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 630..635
FT /evidence="ECO:0007829|PDB:3IAY"
FT TURN 641..643
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:3IAY"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 662..682
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 687..711
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 714..717
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 721..745
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 748..750
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 757..760
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 762..769
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 775..790
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 799..812
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 815..826
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 829..835
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 836..838
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 840..842
FT /evidence="ECO:0007829|PDB:6P1H"
FT HELIX 844..858
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 863..878
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 884..887
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 889..892
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 902..914
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 922..929
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 931..933
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 935..937
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 942..947
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 954..960
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 963..974
FT /evidence="ECO:0007829|PDB:3IAY"
FT HELIX 976..982
FT /evidence="ECO:0007829|PDB:3IAY"
FT STRAND 997..1005
FT /evidence="ECO:0007829|PDB:7KC0"
FT TURN 1010..1012
FT /evidence="ECO:0007829|PDB:7KC0"
FT STRAND 1019..1023
FT /evidence="ECO:0007829|PDB:7KC0"
FT HELIX 1028..1030
FT /evidence="ECO:0007829|PDB:7KC0"
FT HELIX 1031..1036
FT /evidence="ECO:0007829|PDB:6P1H"
FT TURN 1037..1041
FT /evidence="ECO:0007829|PDB:6P1H"
FT HELIX 1042..1060
FT /evidence="ECO:0007829|PDB:6P1H"
FT STRAND 1063..1065
FT /evidence="ECO:0007829|PDB:6P1H"
FT STRAND 1074..1076
FT /evidence="ECO:0007829|PDB:6P1H"
FT TURN 1077..1079
FT /evidence="ECO:0007829|PDB:6P1H"
FT HELIX 1080..1094
FT /evidence="ECO:0007829|PDB:6P1H"
SQ SEQUENCE 1097 AA; 124619 MW; 16E4245C5DCC66DB CRC64;
MSEKRSLPMV DVKIDDEDTP QLEKKIKRQS IDHGVGSEPV STIEIIPSDS FRKYNSQGFK
AKDTDLMGTQ LESTFEQELS QMEHDMADQE EHDLSSFERK KLPTDFDPSL YDISFQQIDA
EQSVLNGIKD ENTSTVVRFF GVTSEGHSVL CNVTGFKNYL YVPAPNSSDA NDQEQINKFV
HYLNETFDHA IDSIEVVSKQ SIWGYSGDTK LPFWKIYVTY PHMVNKLRTA FERGHLSFNS
WFSNGTTTYD NIAYTLRLMV DCGIVGMSWI TLPKGKYSMI EPNNRVSSCQ LEVSINYRNL
IAHPAEGDWS HTAPLRIMSF DIECAGRIGV FPEPEYDPVI QIANVVSIAG AKKPFIRNVF
TLNTCSPITG SMIFSHATEE EMLSNWRNFI IKVDPDVIIG YNTTNFDIPY LLNRAKALKV
NDFPYFGRLK TVKQEIKESV FSSKAYGTRE TKNVNIDGRL QLDLLQFIQR EYKLRSYTLN
AVSAHFLGEQ KEDVHYSIIS DLQNGDSETR RRLAVYCLKD AYLPLRLMEK LMALVNYTEM
ARVTGVPFSY LLARGQQIKV VSQLFRKCLE IDTVIPNMQS QASDDQYEGA TVIEPIRGYY
DVPIATLDFN SLYPSIMMAH NLCYTTLCNK ATVERLNLKI DEDYVITPNG DYFVTTKRRR
GILPIILDEL ISARKRAKKD LRDEKDPFKR DVLNGRQLAL KISANSVYGF TGATVGKLPC
LAISSSVTAY GRTMILKTKT AVQEKYCIKN GYKHDAVVVY GDTDSVMVKF GTTDLKEAMD
LGTEAAKYVS TLFKHPINLE FEKAYFPYLL INKKRYAGLF WTNPDKFDKL DQKGLASVRR
DSCSLVSIVM NKVLKKILIE RNVDGALAFV RETINDILHN RVDISKLIIS KTLAPNYTNP
QPHAVLAERM KRREGVGPNV GDRVDYVIIG GNDKLYNRAE DPLFVLENNI QVDSRYYLTN
QLQNPIISIV APIIGDKQAN GMFVVKSIKI NTGSQKGGLM SFIKKVEACK SCKGPLRKGE
GPLCSNCLAR SGELYIKALY DVRDLEEKYS RLWTQCQRCA GNLHSEVLCS NKNCDIFYMR
VKVKKELQEK VEQLSKW
