DPOZ_YEAST
ID DPOZ_YEAST Reviewed; 1504 AA.
AC P14284; D6W3K1;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=DNA polymerase zeta catalytic subunit;
DE EC=2.7.7.7;
DE AltName: Full=Protein reversionless 3;
GN Name=REV3; Synonyms=PSO1; OrderedLocusNames=YPL167C; ORFNames=P2535;
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.
RX PubMed=2676986; DOI=10.1128/jb.171.10.5659-5667.1989;
RA Morrison A., Christensen R.B., Alley J., Beck A.K., Bernstine E.G.,
RA Lemontt J.F., Lawrence C.W.;
RT "REV3, a Saccharomyces cerevisiae gene whose function is required for
RT induced mutagenesis, is predicted to encode a nonessential DNA
RT polymerase.";
RL J. Bacteriol. 171:5659-5667(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 FUNCTION, AND INTERACTION WITH REV7.
RX PubMed=8658138; DOI=10.1126/science.272.5268.1646;
RA Nelson J.R., Lawrence C.W., Hinkle D.C.;
RT "Thymine-thymine dimer bypass by yeast DNA polymerase zeta.";
RL Science 272:1646-1649(1996).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11316789; DOI=10.1101/gad.882301;
RA Haracska L., Unk I., Johnson R.E., Johansson E., Burgers P.M.J.,
RA Prakash S., Prakash L.;
RT "Roles of yeast DNA polymerases delta and zeta and of Rev1 in the bypass of
RT abasic sites.";
RL Genes Dev. 15:945-954(2001).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16452144; DOI=10.1534/genetics.105.051029;
RA Zhang H., Chatterjee A., Singh K.K.;
RT "Saccharomyces cerevisiae polymerase zeta functions in mitochondria.";
RL Genetics 172:2683-2688(2006).
RN [8]
RP 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).
CC -!- FUNCTION: Nonessential DNA polymerase. Required for DNA damage induced
CC mutagenesis. Involved in DNA repair, mitochondrial DNA repair and
CC translesion synthesis. Translesion synthesis in S.cerevisiae may use a
CC specialized DNA polymerase that is not required for other DNA
CC replicative processes. Has a role in the bypass of abasic (AP) sites.
CC Highly inefficient in incorporating nucleotides opposite the AP site,
CC but efficiently extends from nucleotides, particularly an A, inserted
CC opposite the lesion. {ECO:0000269|PubMed:11316789,
CC ECO:0000269|PubMed:16452144, ECO:0000269|PubMed:2676986,
CC ECO:0000269|PubMed:8658138}.
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:11316789};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=543 uM for dGTP (insertion opposite abasic site)
CC {ECO:0000269|PubMed:11316789};
CC KM=81 uM for dATP (insertion opposite abasic site)
CC {ECO:0000269|PubMed:11316789};
CC KM=125 uM for dTTP (insertion opposite abasic site)
CC {ECO:0000269|PubMed:11316789};
CC KM=113 uM for dCTP (insertion opposite abasic site)
CC {ECO:0000269|PubMed:11316789};
CC KM=0.11 uM for dGTP (insertion opposite C)
CC {ECO:0000269|PubMed:11316789};
CC KM=267 uM for dATP (insertion opposite C)
CC {ECO:0000269|PubMed:11316789};
CC KM=552 uM for dTTP (insertion opposite C)
CC {ECO:0000269|PubMed:11316789};
CC KM=321 uM for dCTP (insertion opposite C)
CC {ECO:0000269|PubMed:11316789};
CC KM=344 uM for dGTP (insertion opposite G)
CC {ECO:0000269|PubMed:11316789};
CC KM=118 uM for dATP (insertion opposite G)
CC {ECO:0000269|PubMed:11316789};
CC KM=428 uM for dTTP (insertion opposite G)
CC {ECO:0000269|PubMed:11316789};
CC KM=0.14 uM for dCTP (insertion opposite G)
CC {ECO:0000269|PubMed:11316789};
CC KM=6.5 uM for dTTP (extension from G, A, T, or C opposite abasic
CC site) {ECO:0000269|PubMed:11316789};
CC KM=2.3 uM for dTTP (extension from G, A, T, or C opposite abasic
CC site) {ECO:0000269|PubMed:11316789};
CC KM=49 uM for dTTP (extension from G, A, T, or C opposite abasic site)
CC {ECO:0000269|PubMed:11316789};
CC KM=21 uM for dTTP (extension from G, A, T, or C opposite abasic site)
CC {ECO:0000269|PubMed:11316789};
CC KM=0.35 uM for dTTP (extension from G, A, T, or C opposite C)
CC {ECO:0000269|PubMed:11316789};
CC KM=2.3 uM for dTTP (extension from G, A, T, or C opposite C)
CC {ECO:0000269|PubMed:11316789};
CC KM=15 uM for dTTP (extension from G, A, T, or C opposite C)
CC {ECO:0000269|PubMed:11316789};
CC KM=26 uM for dTTP (extension from G, A, T, or C opposite C)
CC {ECO:0000269|PubMed:11316789};
CC KM=6.9 uM for dTTP (extension from G, A, T, or C opposite G)
CC {ECO:0000269|PubMed:11316789};
CC KM=2.1 uM for dTTP (extension from G, A, T, or C opposite G)
CC {ECO:0000269|PubMed:11316789};
CC KM=28.8 uM for dTTP (extension from G, A, T, or C opposite G)
CC {ECO:0000269|PubMed:11316789};
CC KM=0.23 uM for dTTP (extension from G, A, T, or C opposite G)
CC {ECO:0000269|PubMed:11316789};
CC -!- SUBUNIT: Forms DNA polymerase zeta with REV7.
CC -!- INTERACTION:
CC P14284; P38927: REV7; NbExp=3; IntAct=EBI-6155, EBI-14960;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16452144}.
CC Nucleus {ECO:0000305}.
CC -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC formation of polymerase complexes. {ECO:0000250}.
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; M29683; AAA34968.1; -; Genomic_DNA.
DR EMBL; X96770; CAA65554.1; -; Genomic_DNA.
DR EMBL; Z73523; CAA97873.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11267.1; -; Genomic_DNA.
DR PIR; A33602; A33602.
DR RefSeq; NP_015158.1; NM_001183981.1.
DR PDB; 6V8P; EM; 4.10 A; A=1-1504.
DR PDB; 6V93; EM; 3.10 A; A=1-1504.
DR PDB; 7LXD; EM; 4.11 A; A=1-1504.
DR PDB; 7S0T; EM; 3.05 A; A=1-1504.
DR PDBsum; 6V8P; -.
DR PDBsum; 6V93; -.
DR PDBsum; 7LXD; -.
DR PDBsum; 7S0T; -.
DR AlphaFoldDB; P14284; -.
DR SMR; P14284; -.
DR BioGRID; 36016; 145.
DR ComplexPortal; CPX-1091; DNA polymerase zeta complex.
DR DIP; DIP-8024N; -.
DR IntAct; P14284; 3.
DR MINT; P14284; -.
DR STRING; 4932.YPL167C; -.
DR PaxDb; P14284; -.
DR PRIDE; P14284; -.
DR EnsemblFungi; YPL167C_mRNA; YPL167C; YPL167C.
DR GeneID; 855936; -.
DR KEGG; sce:YPL167C; -.
DR SGD; S000006088; REV3.
DR VEuPathDB; FungiDB:YPL167C; -.
DR eggNOG; KOG0968; Eukaryota.
DR GeneTree; ENSGT00940000169521; -.
DR HOGENOM; CLU_000203_3_1_1; -.
DR InParanoid; P14284; -.
DR OMA; WIHEEEF; -.
DR BioCyc; YEAST:G3O-34063-MON; -.
DR Reactome; R-SCE-110312; Translesion synthesis by REV1.
DR Reactome; R-SCE-5655862; Translesion synthesis by POLK.
DR Reactome; R-SCE-5656121; Translesion synthesis by POLI.
DR SABIO-RK; P14284; -.
DR PRO; PR:P14284; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P14284; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IDA: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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0070987; P:error-free translesion synthesis; IDA:SGD.
DR GO; GO:0042276; P:error-prone translesion synthesis; IDA: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; 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; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR PANTHER; PTHR45812; PTHR45812; 2.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 2.
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 damage; DNA repair; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1504
FT /note="DNA polymerase zeta catalytic subunit"
FT /id="PRO_0000046470"
FT ZN_FING 1398..1417
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MOTIF 1446..1473
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1446
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1449
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1468
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 1473
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 96..115
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 133..150
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 286..290
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 308..321
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 346..359
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 390..393
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 532..539
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 559..562
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 577..579
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 584..589
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 600..606
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 613..621
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 669..672
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 686..688
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 691..693
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 696..698
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 700..702
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 712..717
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 726..734
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 739..744
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 745..759
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 762..768
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 770..772
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 773..783
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 790..793
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 794..796
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 807..812
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 819..825
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 826..833
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 841..848
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 858..865
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 871..894
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 897..908
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 913..915
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 921..933
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 934..936
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 944..948
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 965..967
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 971..978
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 979..986
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 991..993
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 994..1000
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1017..1019
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1020..1023
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1024..1029
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1033..1037
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 1039..1041
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1045..1064
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1068..1070
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1072..1094
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1099..1101
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1107..1128
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1132..1134
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1137..1140
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1142..1144
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1146..1149
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 1155..1157
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1158..1170
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1184..1192
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1195..1200
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1210..1216
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 1217..1219
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1221..1223
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1225..1241
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1244..1260
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1270..1273
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1287..1298
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1309..1313
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1318..1320
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1323..1326
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1330..1335
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1343..1360
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 1361..1363
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1367..1371
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1424..1449
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1451..1454
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1461..1465
FT /evidence="ECO:0007829|PDB:6V93"
FT HELIX 1474..1486
FT /evidence="ECO:0007829|PDB:6V93"
FT TURN 1490..1492
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1493..1495
FT /evidence="ECO:0007829|PDB:6V93"
FT STRAND 1497..1499
FT /evidence="ECO:0007829|PDB:6V93"
SQ SEQUENCE 1504 AA; 172957 MW; 54C2C6B664F734F5 CRC64;
MSRESNDTIQ SDTVRSSSKS DYFRIQLNNQ DYYMSKPTFL DPSHGESLPL NQFSQVPNIR
VFGALPTGHQ VLCHVHGILP YMFIKYDGQI TDTSTLRHQR CAQVHKTLEV KIRASFKRKK
DDKHDLAGDK LGNLNFVADV SVVKGIPFYG YHVGWNLFYK ISLLNPSCLS RISELIRDGK
IFGKKFEIYE SHIPYLLQWT ADFNLFGCSW INVDRCYFRS PVLNSILDID KLTINDDLQL
LLDRFCDFKC NVLSRRDFPR VGNGLIEIDI LPQFIKNREK LQHRDIHHDF LEKLGDISDI
PVKPYVSSAR DMINELTMQR EELSLKEYKE PPETKRHVSG HQWQSSGEFE AFYKKAQHKT
STFDGQIPNF ENFIDKNQKF SAINTPYEAL PQLWPRLPQI EINNNSMQDK KNDDQVNASF
TEYEICGVDN ENEGVKGSNI KSRSYSWLPE SIASPKDSTI LLDHQTKYHN TINFSMDCAM
TQNMASKRKL RSSVSANKTS LLSRKRKKVM AAGLRYGKRA FVYGEPPFGY QDILNKLEDE
GFPKIDYKDP FFSNPVDLEN KPYAYAGKRF EISSTHVSTR IPVQFGGETV SVYNKPTFDM
FSSWKYALKP PTYDAVQKWY NKVPSMGNKK TESQISMHTP HSKFLYKFAS DVSGKQKRKK
SSVHDSLTHL TLEIHANTRS DKIPDPAIDE VSMIIWCLEE ETFPLDLDIA YEGIMIVHKA
SEDSTFPTKI QHCINEIPVM FYESEFEMFE ALTDLVLLLD PDILSGFEIH NFSWGYIIER
CQKIHQFDIV RELARVKCQI KTKLSDTWGY AHSSGIMITG RHMINIWRAL RSDVNLTQYT
IESAAFNILH KRLPHFSFES LTNMWNAKKS TTELKTVLNY WLSRAQINIQ LLRKQDYIAR
NIEQARLIGI DFHSVYYRGS QFKVESFLIR ICKSESFILL SPGKKDVRKQ KALECVPLVM
EPESAFYKSP LIVLDFQSLY PSIMIGYNYC YSTMIGRVRE INLTENNLGV SKFSLPRNIL
ALLKNDVTIA PNGVVYAKTS VRKSTLSKML TDILDVRVMI KKTMNEIGDD NTTLKRLLNN
KQLALKLLAN VTYGYTSASF SGRMPCSDLA DSIVQTGRET LEKAIDIIEK DETWNAKVVY
GDTDSLFVYL PGKTAIEAFS IGHAMAERVT QNNPKPIFLK FEKVYHPSIL ISKKRYVGFS
YESPSQTLPI FDAKGIETVR RDGIPAQQKI IEKCIRLLFQ TKDLSKIKKY LQNEFFKIQI
GKVSAQDFCF AKEVKLGAYK SEKTAPAGAV VVKRRINEDH RAEPQYKERI PYLVVKGKQG
QLLRERCVSP EEFLEGENLE LDSEYYINKI LIPPLDRLFN LIGINVGNWA QEIVKSKRAS
TTTTKVENIT RVGTSATCCN CGEELTKICS LQLCDDCLEK RSTTTLSFLI KKLKRQKEYQ
TLKTVCRTCS YRYTSDAGIE NDHIASKCNS YDCPVFYSRV KAERYLRDNQ SVQREEALIS
LNDW
