REV1_YEAST
ID REV1_YEAST Reviewed; 985 AA.
AC P12689; D6W341; Q12323;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=DNA repair protein REV1;
DE EC=2.7.7.-;
DE AltName: Full=Reversionless protein 1;
GN Name=REV1; OrderedLocusNames=YOR346W; ORFNames=O6339;
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 MUTAGENESIS OF GLY-193.
RX PubMed=2492497; DOI=10.1128/jb.171.1.230-237.1989;
RA Larimer F.W., Perry J.R., Hardigree A.A.;
RT "The REV1 gene of Saccharomyces cerevisiae: isolation, sequence, and
RT functional analysis.";
RL J. Bacteriol. 171:230-237(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90843 / S288c / FY73;
RX PubMed=8948102;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1475::aid-yea32>3.0.co;2-v;
RA Purnelle B., Goffeau A.;
RT "Nucleotide sequence analysis of a 40 kb segment on the right arm of yeast
RT chromosome XV reveals 18 open reading frames including a new pyruvate
RT kinase and three homologues to chromosome I genes.";
RL Yeast 12:1475-1481(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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.
RX PubMed=8751446; DOI=10.1038/382729a0;
RA Nelson J.R., Lawrence C.W., Hinkle D.C.;
RT "Deoxycytidyl transferase activity of yeast REV1 protein.";
RL Nature 382:729-731(1996).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF 467-ASP-GLU-468.
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 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 [8]
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 [9]
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 [10]
RP INTERACTION WITH REV7.
RX PubMed=18242152; DOI=10.1016/j.dnarep.2007.11.016;
RA Kosarek J.N., Woodruff R.V., Rivera-Begeman A., Guo C., D'Souza S.,
RA Koonin E.V., Walker G.C., Friedberg E.C.;
RT "Comparative analysis of in vivo interactions between Rev1 protein and
RT other Y-family DNA polymerases in animals and yeasts.";
RL DNA Repair 7:439-451(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 305-738 IN COMPLEX WITH MAGNESIUM
RP IONS; DNA AND DCTP, AND COFACTOR.
RX PubMed=16195463; DOI=10.1126/science.1116336;
RA Nair D.T., Johnson R.E., Prakash L., Prakash S., Aggarwal A.K.;
RT "Rev1 employs a novel mechanism of DNA synthesis using a protein
RT template.";
RL Science 309:2219-2222(2005).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 305-738 IN COMPLEX WITH
RP MAGNESIUM; DCTP AND TARGET DNA, AND COFACTOR.
RX PubMed=18275815; DOI=10.1016/j.str.2007.12.009;
RA Nair D.T., Johnson R.E., Prakash L., Prakash S., Aggarwal A.K.;
RT "Protein-template-directed synthesis across an acrolein-derived DNA adduct
RT by yeast Rev1 DNA polymerase.";
RL Structure 16:239-245(2008).
CC -!- FUNCTION: Deoxycytidyl transferase involved in DNA repair. Transfers a
CC dCMP residue from dCTP to the 3'-end of a DNA primer in a template-
CC dependent reaction. May assist in the first step in the bypass of
CC abasic lesions by the insertion of a nucleotide opposite the lesion.
CC Required for normal induction of mutations by physical and chemical
CC agents. Involved in mitochondrial DNA mutagenesis.
CC {ECO:0000269|PubMed:11316789, ECO:0000269|PubMed:16452144,
CC ECO:0000269|PubMed:8751446}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16195463, ECO:0000269|PubMed:18275815};
CC Note=Binds 2 magnesium ions. {ECO:0000269|PubMed:16195463,
CC ECO:0000269|PubMed:18275815};
CC -!- SUBUNIT: Interacts with REV7. {ECO:0000269|PubMed:18242152}.
CC -!- INTERACTION:
CC P12689; P47110: POL32; NbExp=4; IntAct=EBI-14951, EBI-6084;
CC P12689; P38927: REV7; NbExp=3; IntAct=EBI-14951, EBI-14960;
CC -!- SUBCELLULAR LOCATION: Nucleus. Mitochondrion.
CC -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR EMBL; M22222; AAA34967.1; -; Genomic_DNA.
DR EMBL; X95720; CAA65033.1; -; Genomic_DNA.
DR EMBL; Z75253; CAA99674.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11107.1; -; Genomic_DNA.
DR PIR; S67255; S67255.
DR RefSeq; NP_014991.1; NM_001183766.1.
DR PDB; 2AQ4; X-ray; 2.32 A; A=305-738.
DR PDB; 2M2I; NMR; -; A=158-251.
DR PDB; 3BJY; X-ray; 2.41 A; A=305-738.
DR PDB; 3OSP; X-ray; 2.50 A; A=305-738.
DR PDB; 4ID3; X-ray; 1.97 A; A/B=159-250.
DR PDB; 5UMV; X-ray; 1.75 A; A=162-251.
DR PDB; 5VX7; NMR; -; A=162-251.
DR PDB; 5WM1; X-ray; 1.85 A; A=305-738.
DR PDB; 5WM8; X-ray; 1.92 A; A=305-738.
DR PDB; 5WMB; X-ray; 2.25 A; A=305-738.
DR PDB; 5YRQ; X-ray; 2.00 A; A/B/D/E=876-985.
DR PDB; 6X6Z; X-ray; 1.40 A; A=305-746.
DR PDB; 6X70; X-ray; 2.05 A; A=305-746.
DR PDB; 6X71; X-ray; 1.78 A; A=305-746.
DR PDB; 6X72; X-ray; 2.19 A; A=305-746.
DR PDB; 6X73; X-ray; 2.05 A; A=305-746.
DR PDB; 6X74; X-ray; 1.69 A; A=305-746.
DR PDB; 6X75; X-ray; 1.95 A; A=305-746.
DR PDB; 6X76; X-ray; 2.53 A; A=305-746.
DR PDB; 6X77; X-ray; 1.64 A; A=305-746.
DR PDBsum; 2AQ4; -.
DR PDBsum; 2M2I; -.
DR PDBsum; 3BJY; -.
DR PDBsum; 3OSP; -.
DR PDBsum; 4ID3; -.
DR PDBsum; 5UMV; -.
DR PDBsum; 5VX7; -.
DR PDBsum; 5WM1; -.
DR PDBsum; 5WM8; -.
DR PDBsum; 5WMB; -.
DR PDBsum; 5YRQ; -.
DR PDBsum; 6X6Z; -.
DR PDBsum; 6X70; -.
DR PDBsum; 6X71; -.
DR PDBsum; 6X72; -.
DR PDBsum; 6X73; -.
DR PDBsum; 6X74; -.
DR PDBsum; 6X75; -.
DR PDBsum; 6X76; -.
DR PDBsum; 6X77; -.
DR AlphaFoldDB; P12689; -.
DR BMRB; P12689; -.
DR SMR; P12689; -.
DR BioGRID; 34731; 125.
DR DIP; DIP-1000N; -.
DR IntAct; P12689; 6.
DR MINT; P12689; -.
DR STRING; 4932.YOR346W; -.
DR iPTMnet; P12689; -.
DR MaxQB; P12689; -.
DR PaxDb; P12689; -.
DR PRIDE; P12689; -.
DR EnsemblFungi; YOR346W_mRNA; YOR346W; YOR346W.
DR GeneID; 854527; -.
DR KEGG; sce:YOR346W; -.
DR SGD; S000005873; REV1.
DR VEuPathDB; FungiDB:YOR346W; -.
DR eggNOG; KOG2093; Eukaryota.
DR GeneTree; ENSGT00940000156374; -.
DR HOGENOM; CLU_003901_1_0_1; -.
DR InParanoid; P12689; -.
DR OMA; YERSRLH; -.
DR BioCyc; YEAST:G3O-33819-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 EvolutionaryTrace; P12689; -.
DR PRO; PR:P12689; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P12689; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005657; C:replication fork; IPI:SGD.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0017125; F:deoxycytidyl transferase activity; IDA:SGD.
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:0070987; P:error-free translesion synthesis; IDA:SGD.
DR GO; GO:0042276; P:error-prone translesion synthesis; IDA:SGD.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR012112; REV1.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR PIRSF; PIRSF036573; REV1; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA synthesis; DNA-binding;
KW Magnesium; Metal-binding; Mitochondrion; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..985
FT /note="DNA repair protein REV1"
FT /id="PRO_0000173995"
FT DOMAIN 161..249
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 358..554
FT /note="UmuC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT REGION 319..329
FT /note="Interaction with target DNA"
FT REGION 395..397
FT /note="Interaction with target DNA"
FT REGION 554..557
FT /note="Interaction with target DNA"
FT REGION 620..628
FT /note="Interaction with target DNA"
FT BINDING 324
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000269|PubMed:16195463,
FT ECO:0000269|PubMed:18275815"
FT BINDING 362..366
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000269|PubMed:16195463,
FT ECO:0000269|PubMed:18275815"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216,
FT ECO:0000269|PubMed:18275815"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216,
FT ECO:0000269|PubMed:18275815"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216,
FT ECO:0000269|PubMed:18275815"
FT BINDING 402..408
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000269|PubMed:16195463,
FT ECO:0000269|PubMed:18275815"
FT BINDING 414
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000269|PubMed:16195463,
FT ECO:0000269|PubMed:18275815"
FT BINDING 467
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000269|PubMed:16195463,
FT ECO:0000269|PubMed:18275815"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216,
FT ECO:0000269|PubMed:18275815"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216,
FT ECO:0000269|PubMed:18275815"
FT SITE 681
FT /note="Interaction with target DNA"
FT SITE 692
FT /note="Interaction with target DNA"
FT SITE 694
FT /note="Interaction with target DNA"
FT MUTAGEN 193
FT /note="G->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:2492497"
FT MUTAGEN 467..468
FT /note="DE->AA: Loss of dCTP transferase activity."
FT /evidence="ECO:0000269|PubMed:11316789"
FT CONFLICT 646
FT /note="G -> S (in Ref. 1; AAA34967)"
FT /evidence="ECO:0000305"
FT CONFLICT 816
FT /note="Q -> H (in Ref. 1; AAA34967)"
FT /evidence="ECO:0000305"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:5UMV"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:5UMV"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:5UMV"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:5UMV"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5UMV"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:5UMV"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:5UMV"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:5UMV"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:2M2I"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:5UMV"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:5UMV"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 324..342
FT /evidence="ECO:0007829|PDB:6X6Z"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 366..373
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:6X6Z"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:6X6Z"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 418..422
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 438..454
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 459..465
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 468..474
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:6X72"
FT HELIX 483..500
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 506..513
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 514..524
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 539..542
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 555..564
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 571..577
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 580..587
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 589..598
FT /evidence="ECO:0007829|PDB:6X6Z"
FT TURN 599..601
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 605..612
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 614..618
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 623..627
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 636..656
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 659..671
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 687..701
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 704..718
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 722..724
FT /evidence="ECO:0007829|PDB:6X6Z"
FT STRAND 725..737
FT /evidence="ECO:0007829|PDB:6X6Z"
FT HELIX 883..898
FT /evidence="ECO:0007829|PDB:5YRQ"
FT TURN 899..901
FT /evidence="ECO:0007829|PDB:5YRQ"
FT HELIX 905..919
FT /evidence="ECO:0007829|PDB:5YRQ"
FT TURN 920..922
FT /evidence="ECO:0007829|PDB:5YRQ"
FT HELIX 924..937
FT /evidence="ECO:0007829|PDB:5YRQ"
FT TURN 941..943
FT /evidence="ECO:0007829|PDB:5YRQ"
FT HELIX 950..961
FT /evidence="ECO:0007829|PDB:5YRQ"
FT HELIX 963..967
FT /evidence="ECO:0007829|PDB:5YRQ"
FT HELIX 974..984
FT /evidence="ECO:0007829|PDB:5YRQ"
SQ SEQUENCE 985 AA; 112227 MW; 330E30A27F8300BE CRC64;
MGEHGGLVDL LDSDLEYSIN RETPDKNNCL SQQSVNDSHL TAKTGGLNAR SFLSTLSDDS
LIEYVNQLSQ TNKNNSNPTA GTLRFTTKNI SCDELHADLG GGEDSPIARS VIEIQESDSN
GDDVKKNTVY TREAYFHEKA HGQTLQDQIL KDQYKDQISS QSSKIFKNCV IYINGYTKPG
RLQLHEMIVL HGGKFLHYLS SKKTVTHIVA SNLPLKKRIE FANYKVVSPD WIVDSVKEAR
LLPWQNYSLT SKLDEQQKKL DNCKTVNSIP LPSETSLHKG SKCVGSALLP VEQQSPVNLN
NLEAKRIVAC DDPDFLTSYF AHSRLHHLSA WKANLKDKFL NENIHKYTKI TDKDTYIIFH
IDFDCFFATV AYLCRSSSFS ACDFKRDPIV VCHGTKNSDI ASCNYVARSY GIKNGMWVSQ
AEKMLPNGIK LISLPYTFEQ FQLKSEAFYS TLKRLNIFNL ILPISIDEAV CVRIIPDNIH
NTNTLNARLC EEIRQEIFQG TNGCTVSIGC SDSLVLARLA LKMAKPNGYN ITFKSNLSEE
FWSSFKLDDL PGVGHSTLSR LESTFDSPHS LNDLRKRYTL DALKASVGSK LGMKIHLALQ
GQDDEESLKI LYDPKEVLQR KSLSIDINWG IRFKNITQVD LFIERGCQYL LEKLNEINKT
TSQITLKLMR RCKDAPIEPP KYMGMGRCDS FSRSSRLGIP TNEFGIIATE MKSLYRTLGC
PPMELRGLAL QFNKLVDVGP DNNQLKLRLP FKTIVTNRAF EALPEDVKND INNEFEKRNY
KRKESGLTSN SLSSKKKGFA ISRLEVNDLP STMEEQFMNE LPTQIRAEVR HDLRIQKKIQ
QTKLGNLQEK IKRREESLQN EKNHFMGQNS IFQPIKFQNL TRFKKICQLV KQWVAETLGD
GGPHEKDVKL FVKYLIKLCD SNRVHLVLHL SNLISRELNL CAFLNQDHSG FQTWERILLN
DIIPLLNRNK HTYQTVRKLD MDFEV
