DPOE_YEAST
ID DPOE_YEAST Reviewed; 2222 AA.
AC P21951; D6W0T1;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=DNA polymerase epsilon catalytic subunit A;
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:12124389};
DE AltName: Full=DNA polymerase II subunit A;
GN Name=POL2; Synonyms=DUN2; OrderedLocusNames=YNL262W; ORFNames=N0825;
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], PROTEIN SEQUENCE OF 1214-1221, AND
RP DOMAIN.
RX PubMed=2169349; DOI=10.1016/0092-8674(90)90391-q;
RA Morrison A., Araki H., Clark A.B., Hamatake R.K., Sugino A.;
RT "A third essential DNA polymerase in S. cerevisiae.";
RL Cell 62:1143-1151(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2221.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740425;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<505::aid-yea932>3.0.co;2-f;
RA Sen-Gupta M., Lyck R., Fleig U., Niedenthal R.K., Hegemann J.H.;
RT "The sequence of a 24,152 bp segment from the left arm of chromosome XIV
RT from Saccharomyces cerevisiae between the BNI1 and the POL2 genes.";
RL Yeast 12:505-514(1996).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF MET-644 AND PRO-710.
RX PubMed=1537345; DOI=10.1002/j.1460-2075.1992.tb05106.x;
RA Araki H., Ropp P.A., Johnson A.L., Johnston L.H., Morrison A., Sugino A.;
RT "DNA polymerase II, the probable homolog of mammalian DNA polymerase
RT epsilon, replicates chromosomal DNA in the yeast Saccharomyces
RT cerevisiae.";
RL EMBO J. 11:733-740(1992).
RN [6]
RP SUBUNIT.
RX PubMed=11024162; DOI=10.1093/nar/28.20.3846;
RA Ohya T., Maki S., Kawasaki Y., Sugino A.;
RT "Structure and function of the fourth subunit (Dpb4p) of DNA polymerase
RT epsilon in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 28:3846-3852(2000).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12124389; DOI=10.1074/jbc.m204476200;
RA Shimizu K., Hashimoto K., Kirchner J.M., Nakai W., Nishikawa H.,
RA Resnick M.A., Sugino A.;
RT "Fidelity of DNA polymerase epsilon holoenzyme from budding yeast
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 277:37422-37429(2002).
RN [8]
RP COMPOSITION OF THE DNA POLYMERASE EPSILON COMPLEX.
RX PubMed=12571237; DOI=10.1074/jbc.m211818200;
RA Chilkova O., Jonsson B.-H., Johansson E.;
RT "The quaternary structure of DNA polymerase epsilon from Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 278:14082-14086(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP CATALYTIC ACTIVITY, COFACTOR, AND IRON-SULFUR-BINDING.
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 [11]
RP FUNCTION, AND MUTAGENESIS OF MET-644.
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 the DNA polymerase epsilon complex
CC which participates in chromosomal DNA replication (PubMed:1537345).
CC Required during synthesis of the leading DNA strands at the replication
CC fork, binds at/or near replication origins and moves along DNA with the
CC replication fork (PubMed:31488849). Has 3'-5' proofreading exonuclease
CC activity that corrects errors arising during DNA replication
CC (PubMed:12124389). {ECO:0000269|PubMed:12124389,
CC ECO:0000269|PubMed:1537345, 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 epsilon is a heterotetramer consisting of POL2,
CC DPB2, DPB3 and DPB4. {ECO:0000269|PubMed:11024162}.
CC -!- INTERACTION:
CC P21951; P24482: DPB2; NbExp=7; IntAct=EBI-6140, EBI-6071;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The DNA polymerase activity domain resides in the N-terminal
CC half of the protein, while the C-terminus is necessary for complexing
CC subunits B and C. {ECO:0000269|PubMed:2169349}.
CC -!- DOMAIN: The CysA-type zinc finger is required for PCNA-binding.
CC {ECO:0000250|UniProtKB:P15436}.
CC -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC formation of polymerase complexes. {ECO:0000250|UniProtKB:P15436}.
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 -!- MISCELLANEOUS: Present with 1970 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M60416; AAA88711.1; -; Genomic_DNA.
DR EMBL; X92494; CAA63235.1; -; Genomic_DNA.
DR EMBL; Z71538; CAA96169.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10297.1; -; Genomic_DNA.
DR PIR; A36028; A36028.
DR RefSeq; NP_014137.1; NM_001183100.1.
DR PDB; 4M8O; X-ray; 2.20 A; A=1-1228.
DR PDB; 4PTF; X-ray; 2.81 A; A=1-1187.
DR PDB; 5OKI; X-ray; 4.50 A; A/B=1-524.
DR PDB; 6FWK; X-ray; 2.50 A; A/B=1-1186.
DR PDB; 6G0A; X-ray; 2.62 A; A=1-1186.
DR PDB; 6H1V; X-ray; 2.70 A; A=1-1187.
DR PDB; 6HV8; EM; 4.40 A; A=1308-2221.
DR PDB; 6HV9; EM; 4.98 A; A=1308-2221.
DR PDB; 6I8A; X-ray; 2.65 A; A/B=1-1185.
DR PDB; 6QIB; X-ray; 2.80 A; A=1-1187.
DR PDB; 6S1C; X-ray; 6.10 A; A/E=1-524.
DR PDB; 6S2E; EM; 4.20 A; A=1-1192.
DR PDB; 6S2F; EM; 5.80 A; A=1-1192.
DR PDB; 6WJV; EM; 3.50 A; A=1-2222.
DR PDB; 7PMK; EM; 3.20 A; Q=1-2222.
DR PDB; 7PMN; EM; 3.20 A; Q=1-2222.
DR PDBsum; 4M8O; -.
DR PDBsum; 4PTF; -.
DR PDBsum; 5OKI; -.
DR PDBsum; 6FWK; -.
DR PDBsum; 6G0A; -.
DR PDBsum; 6H1V; -.
DR PDBsum; 6HV8; -.
DR PDBsum; 6HV9; -.
DR PDBsum; 6I8A; -.
DR PDBsum; 6QIB; -.
DR PDBsum; 6S1C; -.
DR PDBsum; 6S2E; -.
DR PDBsum; 6S2F; -.
DR PDBsum; 6WJV; -.
DR PDBsum; 7PMK; -.
DR PDBsum; 7PMN; -.
DR AlphaFoldDB; P21951; -.
DR SMR; P21951; -.
DR BioGRID; 35577; 626.
DR ComplexPortal; CPX-2110; DNA polymerase epsilon complex.
DR DIP; DIP-2532N; -.
DR IntAct; P21951; 20.
DR MINT; P21951; -.
DR STRING; 4932.YNL262W; -.
DR iPTMnet; P21951; -.
DR MaxQB; P21951; -.
DR PaxDb; P21951; -.
DR PRIDE; P21951; -.
DR EnsemblFungi; YNL262W_mRNA; YNL262W; YNL262W.
DR GeneID; 855459; -.
DR KEGG; sce:YNL262W; -.
DR SGD; S000005206; POL2.
DR VEuPathDB; FungiDB:YNL262W; -.
DR eggNOG; KOG1798; Eukaryota.
DR GeneTree; ENSGT00390000010194; -.
DR HOGENOM; CLU_000556_0_1_1; -.
DR InParanoid; P21951; -.
DR OMA; MLDQCRY; -.
DR BioCyc; YEAST:G3O-33258-MON; -.
DR Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-68952; DNA replication initiation.
DR Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR PRO; PR:P21951; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P21951; protein.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IDA:SGD.
DR GO; GO:0043596; C:nuclear replication fork; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005657; C:replication fork; IDA:SGD.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IMP:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0032183; F:SUMO binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IMP:SGD.
DR GO; GO:0006287; P:base-excision repair, gap-filling; IBA:GO_Central.
DR GO; GO:0045004; P:DNA replication proofreading; IMP:SGD.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
DR GO; GO:0042276; P:error-prone translesion synthesis; IDA:SGD.
DR GO; GO:0035822; P:gene conversion; IMP:SGD.
DR GO; GO:0006272; P:leading strand elongation; IMP:SGD.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:SGD.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IMP:SGD.
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; 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; IPR013697; DNA_pol_e_suA_C.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR029703; POL2.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10670; PTHR10670; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08490; DUF1744; 1.
DR SMART; SM01159; DUF1744; 1.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; DNA replication;
KW DNA-binding; DNA-directed DNA polymerase; Hydrolase; Iron; Iron-sulfur;
KW Metal-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..2222
FT /note="DNA polymerase epsilon catalytic subunit A"
FT /id="PRO_0000046467"
FT ZN_FING 2108..2133
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT REGION 90..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2164..2181
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2164
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2167
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2179
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2181
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MUTAGEN 644
FT /note="M->G: Increases rates of C-to-A transversion
FT substitutions."
FT /evidence="ECO:0000269|PubMed:31488849"
FT MUTAGEN 644
FT /note="M->I: In POL2-9; temperature-sensitive mutant."
FT /evidence="ECO:0000269|PubMed:1537345"
FT MUTAGEN 710
FT /note="P->S: In POL2-18; temperature-sensitive mutant."
FT /evidence="ECO:0000269|PubMed:1537345"
FT HELIX 33..49
FT /evidence="ECO:0007829|PDB:4M8O"
FT TURN 67..71
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 72..87
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6G0A"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:4M8O"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 196..215
FT /evidence="ECO:0007829|PDB:4M8O"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:4M8O"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:4M8O"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:6FWK"
FT STRAND 346..354
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 355..369
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:4M8O"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 383..393
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:6WJV"
FT HELIX 398..402
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:6FWK"
FT STRAND 415..421
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 422..429
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 439..447
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 459..465
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 467..487
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 489..497
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 504..509
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 512..526
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 546..553
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 564..567
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 572..575
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 578..597
FT /evidence="ECO:0007829|PDB:4M8O"
FT TURN 598..600
FT /evidence="ECO:0007829|PDB:6H1V"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 610..626
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 629..632
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 634..641
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 644..652
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 656..658
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 659..662
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 664..666
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:6QIB"
FT STRAND 678..689
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 694..705
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 708..710
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 714..717
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 720..722
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 728..747
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 752..766
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 769..797
FT /evidence="ECO:0007829|PDB:4M8O"
FT TURN 798..800
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 801..803
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 808..832
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 833..835
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 844..868
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 869..875
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 878..884
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 890..895
FT /evidence="ECO:0007829|PDB:4M8O"
FT TURN 896..898
FT /evidence="ECO:0007829|PDB:6H1V"
FT STRAND 900..904
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 905..918
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 920..928
FT /evidence="ECO:0007829|PDB:4M8O"
FT TURN 929..932
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 933..939
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 944..955
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 959..962
FT /evidence="ECO:0007829|PDB:6FWK"
FT STRAND 969..972
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 978..984
FT /evidence="ECO:0007829|PDB:4M8O"
FT TURN 985..987
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 988..992
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 993..1002
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 1003..1007
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 1009..1011
FT /evidence="ECO:0007829|PDB:6G0A"
FT HELIX 1012..1031
FT /evidence="ECO:0007829|PDB:4M8O"
FT TURN 1032..1036
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 1039..1046
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 1048..1051
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 1056..1059
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 1065..1077
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 1079..1082
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 1083..1086
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 1088..1095
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 1097..1099
FT /evidence="ECO:0007829|PDB:6QIB"
FT HELIX 1102..1104
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 1106..1108
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 1109..1113
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 1116..1127
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 1137..1140
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 1143..1157
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 1159..1164
FT /evidence="ECO:0007829|PDB:4M8O"
FT STRAND 1172..1174
FT /evidence="ECO:0007829|PDB:6WJV"
FT HELIX 1178..1183
FT /evidence="ECO:0007829|PDB:4M8O"
FT HELIX 1273..1293
FT /evidence="ECO:0007829|PDB:6WJV"
FT HELIX 1299..1301
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 1302..1305
FT /evidence="ECO:0007829|PDB:6WJV"
FT TURN 1308..1310
FT /evidence="ECO:0007829|PDB:6WJV"
FT HELIX 1311..1315
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 1319..1322
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 1324..1329
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1335..1342
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1345..1352
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1354..1363
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 1366..1370
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 1376..1379
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1397..1403
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1404..1411
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1419..1428
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1433..1440
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1444..1447
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 1452..1454
FT /evidence="ECO:0007829|PDB:6WJV"
FT HELIX 1455..1461
FT /evidence="ECO:0007829|PDB:6WJV"
FT HELIX 1465..1467
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1483..1486
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1493..1495
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 1498..1503
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 1504..1506
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 1507..1511
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1524..1538
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1540..1545
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 1546..1549
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1559..1561
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1571..1583
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1585..1591
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1595..1597
FT /evidence="ECO:0007829|PDB:6WJV"
FT HELIX 1599..1605
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1632..1656
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 1660..1662
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1668..1682
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1683..1686
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 1691..1695
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1700..1703
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1707..1714
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1725..1727
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1731..1735
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1739..1746
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1780..1782
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1785..1803
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1807..1819
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1825..1827
FT /evidence="ECO:0007829|PDB:6WJV"
FT HELIX 1830..1853
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1857..1862
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1865..1869
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1875..1890
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1893..1895
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1901..1913
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1916..1922
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 1935..1939
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1940..1943
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 1947..1949
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 1950..1973
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 1999..2002
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 2003..2006
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 2008..2025
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 2029..2031
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 2032..2035
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 2046..2048
FT /evidence="ECO:0007829|PDB:6WJV"
FT HELIX 2050..2063
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 2069..2080
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 2081..2083
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 2090..2092
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 2102..2108
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 2109..2112
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 2113..2118
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 2119..2121
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 2124..2128
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 2131..2133
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 2139..2158
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 2162..2164
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 2165..2167
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 2173..2175
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 2180..2182
FT /evidence="ECO:0007829|PDB:6WJV"
FT STRAND 2185..2189
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 2191..2208
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 2211..2221
FT /evidence="ECO:0007829|PDB:7PMK"
SQ SEQUENCE 2222 AA; 255671 MW; CBCDDE2AB147D65B CRC64;
MMFGKKKNNG GSSTARYSAG NKYNTLSNNY ALSAQQLLNA SKIDDIDSMM GFERYVPPQY
NGRFDAKDID QIPGRVGWLT NMHATLVSQE TLSSGSNGGG NSNDGERVTT NQGISGVDFY
FLDEEGGSFK STVVYDPYFF IACNDESRVN DVEELVKKYL ESCLKSLQII RKEDLTMDNH
LLGLQKTLIK LSFVNSNQLF EARKLLRPIL QDNANNNVQR NIYNVAANGS EKVDAKHLIE
DIREYDVPYH VRVSIDKDIR VGKWYKVTQQ GFIEDTRKIA FADPVVMAFD IETTKPPLKF
PDSAVDQIMM ISYMIDGEGF LITNREIISE DIEDFEYTPK PEYPGFFTIF NENDEVALLQ
RFFEHIRDVR PTVISTFNGD FFDWPFIHNR SKIHGLDMFD EIGFAPDAEG EYKSSYCSHM
DCFRWVKRDS YLPQGSQGLK AVTQSKLGYN PIELDPELMT PYAFEKPQHL SEYSVSDAVA
TYYLYMKYVH PFIFSLCTII PLNPDETLRK GTGTLCEMLL MVQAYQHNIL LPNKHTDPIE
RFYDGHLLES ETYVGGHVES LEAGVFRSDL KNEFKIDPSA IDELLQELPE ALKFSVEVEN
KSSVDKVTNF EEIKNQITQK LLELKENNIR NELPLIYHVD VASMYPNIMT TNRLQPDSIK
AERDCASCDF NRPGKTCARK LKWAWRGEFF PSKMDEYNMI KRALQNETFP NKNKFSKKKV
LTFDELSYAD QVIHIKKRLT EYSRKVYHRV KVSEIVEREA IVCQRENPFY VDTVKSFRDR
RYEFKGLAKT WKGNLSKIDP SDKHARDEAK KMIVLYDSLQ LAHKVILNSF YGYVMRKGSR
WYSMEMAGIT CLTGATIIQM ARALVERVGR PLELDTDGIW CILPKSFPET YFFTLENGKK
LYLSYPCSML NYRVHQKFTN HQYQELKDPL NYIYETHSEN TIFFEVDGPY KAMILPSSKE
EGKGIKKRYA VFNEDGSLAE LKGFELKRRG ELQLIKNFQS DIFKVFLEGD TLEGCYSAVA
SVCNRWLDVL DSHGLMLEDE DLVSLICENR SMSKTLKEYE GQKSTSITTA RRLGDFLGED
MVKDKGLQCK YIISSKPFNA PVTERAIPVA IFSADIPIKR SFLRRWTLDP SLEDLDIRTI
IDWGYYRERL GSAIQKIITI PAALQGVSNP VPRVEHPDWL KRKIATKEDK FKQTSLTKFF
SKTKNVPTMG KIKDIEDLFE PTVEEDNAKI KIARTTKKKA VSKRKRNQLT NEEDPLVLPS
EIPSMDEDYV GWLNYQKIKW KIQARDRKRR DQLFGNTNSS RERSALGSMI RKQAESYANS
TWEVLQYKDS GEPGVLEVFV TINGKVQNIT FHIPKTIYMK FKSQTMPLQK IKNCLIEKSS
ASLPNNPKTS NPAGGQLFKI TLPESVFLEE KENCTSIFND ENVLGVFEGT ITPHQRAIMD
LGASVTFRSK AMGALGKGIQ QGFEMKDLSM AENERYLSGF SMDIGYLLHF PTSIGYEFFS
LFKSWGDTIT ILVLKPSNQA QEINASSLGQ IYKQMFEKKK GKIETYSYLV DIKEDINFEF
VYFTDISKLY RRLSQETTKL KEERGLQFLL LLQSPFITKL LGTIRLLNQM PIVKLSLNEV
LLPQLNWQPT LLKKLVNHVL SSGSWISHLI KLSQYSNIPI CNLRLDSMDY IIDVLYARKL
KKENIVLWWN EKAPLPDHGG IQNDFDLNTS WIMNDSEFPK INNSGVYDNV VLDVGVDNLT
VNTILTSALI NDAEGSDLVN NNMGIDDKDA VINSPSEFVH DAFSNDALNV LRGMLKEWWD
EALKENSTAD LLVNSLASWV QNPNAKLFDG LLRYHVHNLT KKALLQLVNE FSALGSTIVY
ADRNQILIKT NKYSPENCYA YSQYMMKAVR TNPMFSYLDL NIKRYWDLLI WMDKFNFSGL
ACIEIEEKEN QDYTAVSQWQ LKKFLSPIYQ PEFEDWMMII LDSMLKTKQS YLKLNSGTQR
PTQIVNVKKQ DKEDSVENSL NGFSHLFSKP LMKRVKKLFK NQQEFILDPQ YEADYVIPVL
PGSHLNVKNP LLELVKSLCH VMLLSKSTIL EIRTLRKELL KIFELREFAK VAEFKDPSLS
LVVPDFLCEY CFFISDIDFC KAAPESIFSC VRCHKAFNQV LLQEHLIQKL RSDIESYLIQ
DLRCSRCHKV KRDYMSAHCP CAGAWEGTLP RESIVQKLNV FKQVAKYYGF DILLSCIADL
TI
