ID A0A1D8PKE9_CANAL Unreviewed; 1630 AA.
AC A0A1D8PKE9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN Name=REV3 {ECO:0000313|CGD:CAL0000176488,
GN ECO:0000313|EMBL:AOW28616.1};
GN OrderedLocusNames=CAALFM_C306080WA {ECO:0000313|EMBL:AOW28616.1},
GN orf19.7390 {ECO:0000313|CGD:CAL0000176488};
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561 {ECO:0000313|EMBL:AOW28616.1, ECO:0000313|Proteomes:UP000000559};
RN [1] {ECO:0000313|EMBL:AOW28616.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2] {ECO:0000313|EMBL:AOW28616.1, ECO:0000313|Proteomes:UP000000559}
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=17419877; DOI=.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3] {ECO:0000313|EMBL:AOW28616.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=24025428; DOI=.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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:0000256|RuleBase:RU000442};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR EMBL; CP017625; AOW28616.1; -; Genomic_DNA.
DR RefSeq; XP_716630.2; XM_711537.2.
DR AlphaFoldDB; A0A1D8PKE9; -.
DR SMR; A0A1D8PKE9; -.
DR STRING; 237561.A0A1D8PKE9; -.
DR EnsemblFungi; C3_06080W_A-T; C3_06080W_A-T-p1; C3_06080W_A.
DR GeneID; 3641749; -.
DR KEGG; cal:CAALFM_C306080WA; -.
DR CGD; CAL0000176488; REV3.
DR VEuPathDB; FungiDB:C3_06080W_A; -.
DR eggNOG; KOG0968; Eukaryota.
DR InParanoid; A0A1D8PKE9; -.
DR OMA; GRNKMGF; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IBA:GO_Central.
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; IBA:GO_Central.
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; IEA:EnsemblFungi.
DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR CDD; cd05778; DNA_polB_zeta_exo; 1.
DR CDD; cd05534; POLBc_zeta; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
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; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU000442};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000000559};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 771..979
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1045..1500
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1527..1607
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 541..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1630 AA; 188925 MW; 34AD753B5A08092C CRC64;
MNTTNESTNY TTINASSVNW SNNQINSSFS SLRVQINDYD TYQTLPTRLD QLCTQVTQVP
IIRIYGSLSV QNSLSNTDSP NKKKRKIDET TSPAVFNVVI HVHNFYPYIY VDCHETDFTK
LENDDFIKLI TDYLETVLEE SFKYRKSSKN LDDDEQNHVE NLKRSGQRKY IANVSVCKGV
PIYGFQLGYR FFYKISLLSP LYKSRLAKLF QENTISLFRI GMEKKKNVTY NPEPAYVYEA
HIPYLLQFLT DYNLFGCGWV NIDKDFVSQE DAKTRGLYFR SPIFTNIHKS FHSPNDLLAL
RQCLSNYITA DNVLYNGQLD NGNPCPFNRI GKSTLEMDIT TNSIVNRTWL SPRELHDDFI
EKAEFLEYKR AIESGSHKYG YKYDQDGQPR IYLSSLKQIY NDLKYQCRSR DSSFNVAADV
LETENSSYFG TGSTNWSNQE QLNELFDYLK KLNGDVKLDS SKYSKKYLQA RKLKQPAVFS
RIPTAFQLVD IEKSIVQHKL KMRFDSDLLN WTNYVKLFDS QNSQVLNNDE PVAINILPEE
NLSDNEISDN NGRETMNENT NSDADENLVI DNQLEVEPTE NIPKEDNKEP DDYELTQLHQ
FDESLMRNLT QIQATKTANF LGVEDLSYLD DFSFTSSQSQ SDFKNFQITD NTYEVPIPDQ
LKPENIDQTF QSAGLLKVNY SDPFYDNQND VPAKPLVFAN QKIVVPLKNE SSIPSLEMSQ
LIKQNTHITK PISQIFSTWQ YVPEPPSKRE VSKWLKHDEA YTLKKNTKYQ FQIEPGVTQS
YDYKYSYNSM KISRRPDEFN CLTNFHMELH ANPPNSKLTV DPLRDPISLI FYSFDDANNM
FRHLNFASGI LIFNNTNIDM NLIQRLSHTL NKHIEIFDDE LKMITKLVTL VELFDPDILS
GYEVNSMSWG YIVERLRDVF GINIMSDLSR GSFKSNGKFG DRWGYTHTSN IEISGRHMLN
VWRPLRSELS LTSYSLENVT YHLLHKSLPR YSNYRLSEWL KEGTFSSIFA VLSYYINRID
IVLKIINVQE LITRNVEHSR LIGIEFNSNF YRGSQYKVES ILARICKPES LLLNSPSKQQ
VHEMRPIECI PLILEPKSNF YKSPLVVLDF QSLYPSIMIA YNYCYSTLVG KLHNYRPTKN
NIGYLRNLKI PYGLVNLLQR EDGFNISPNG FVFVKSHIRK SVLAKMLEEI LSIRIKIKQV
MKLFKEDAEL TKLYNSRQLA LKLIANVTYG YTSATFSGRM PNSDIADAIV STGREILNKS
IELIEAGNYG AKVVYGDTDS LFVYFPGKPK TEAFKLGKQI AKTITNYFPD PVKLKFEKVY
HPCVLLAKKR YVGFSYEYED QKTPKFDAKG IETVRRDGIP AQSKMTEKTL RILFETKNLS
KVKQYTIDQF YKIIFNKVPI RDFCFAKEVR YGTYKNEKYL PPGAIIAKNM AEEDPRKEPQ
YRERVPYVVI RDSSKPRIKD RCVTPEDFIK SYETNSPVSL DYEYYITRVL IPPLERIFNL
IGIDITGWYR QMPIVMRGSH VAYAEGCLVC GNRLDDSANI CSKCLANEQE VIADIISTSR
DTEKKLVEVE RVCQKCVDNN TSSSMGRFID QCTDDCVNGD CIVYYNKFKL NYESKQIFTK
KDKILQELDW
//
