UniProt: C5MGA5

Database: UniProt
Entry: C5MGA5_CANTT

LinkDB:  C5MGA5_CANTT 
Original site:  C5MGA5_CANTT

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Ontology (11)   
   GO (11)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (32)   

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ID   C5MGA5_CANTT            Unreviewed;      1079 AA.
AC   C5MGA5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=CTRG_05098 {ECO:0000313|EMBL:EER31368.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER31368.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER31368.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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|ARBA:ARBA00024632,
CC         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; GG692401; EER31368.1; -; Genomic_DNA.
DR   RefSeq; XP_002550800.1; XM_002550754.1.
DR   AlphaFoldDB; C5MGA5; -.
DR   STRING; 294747.C5MGA5; -.
DR   EnsemblFungi; CTRG_05098-t43_1; CTRG_05098-t43_1-p1; CTRG_05098.
DR   GeneID; 8299254; -.
DR   KEGG; ctp:CTRG_05098; -.
DR   VEuPathDB; FungiDB:CTRG_05098; -.
DR   eggNOG; KOG0969; Eukaryota.
DR   HOGENOM; CLU_000203_2_0_1; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0043625; C:delta DNA polymerase complex; IEA:EnsemblFungi.
DR   GO; GO:0008296; F:3'-5'-DNA exonuclease activity; IEA:EnsemblFungi.
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; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0060090; F:molecular adaptor activity; IEA:EnsemblFungi.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0045004; P:DNA replication proofreading; IEA:EnsemblFungi.
DR   GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:EnsemblFungi.
DR   GO; GO:0006278; P:RNA-templated DNA biosynthetic process; IEA:EnsemblFungi.
DR   CDD; cd05777; DNA_polB_delta_exo; 1.
DR   CDD; cd05533; POLBc_delta; 1.
DR   Gene3D; 2.40.50.730; -; 2.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 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; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   NCBIfam; TIGR00592; pol2; 1.
DR   PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA 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 replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
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:UP000002037};
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          148..451
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          515..944
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          983..1057
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1079 AA;  123480 MW;  D0829EBE84698726 CRC64;
     MSAPKRALED THQDQAHSLP VASQSINGQL ELTPSQEQLL KKVKLPNGSE EPSEFERELL
     NMTQAARDLE NDDDQSWSRP PLPSDFNPDL EDISFQQLDA EEHSDDIDTY ARFFGITKEG
     RSVLCNVTGF VHYFYSPVPK GFLKDEHLND FVSYLQARHE GIEKVEIKLK ESIWGYNKNI
     KTPYFKIYVN GNRNITKVRG AFERGQIQFN DMFPSESVTY DNINYLLRLM IDCKITGMSW
     ITLPKTKYKL VTKKISTCQI ECSIDYRDLI SHPSEGEWLQ MAPLRILSFD IECAGRKGIF
     PEAKHDPVIQ IANVVQRSGE SKPFIRNVFT VGSCSPIIGS QIFSHEKEED MLMHWKEFIC
     EVDPDVIIGY NTANFDIPYV LRRAEALKLP KFPFFGRLKS VKQEIKDSVF SSRAYGTREN
     KVVNIDGRMQ LDLLQFINRE YKLRSYTLNS VSAHFLGEQK EDVQHSIITD LQNGNSETRR
     RLAVYCLKDA FLPLRLLDKL MCLVNYTEMA RVTGVPFSYL LSRGQQIKVI SQLFRKCLQE
     DVVIPNLRSE GTNEEYEGAT VIEPERGYYD VPIATLDFSS LYPSIMMAHN LCYTTLLNKK
     SIQAYGLTED DYTKTPNGDY FVKSSLRQGI LPTILNELLT ARKKAKADLK KETDPFKKDV
     LNGRQLALKI SANSVYGFTG ATIGKLPCLA ISSSVTAFGR EMIEKTKNVV QDYYSKKNGH
     PYDAKVIYGD TDSVMVCFGY EDLETCMKLG EEAANYVSTK FKDPIKLEFE KVYFPYLLIN
     KKRYAGLYWT RPEKFDKMDT KGIETVRRDN CRLVQNVVTK VLEFILEERD VGKAERFVKQ
     TIADLLQNRV DLSQLVITKA YSKHDYSAKQ AHVELAERMK ARDPGSAPQL GDRVAYVIIK
     TGSDKNYEKS EDPLYVLENS LPIDVKYYLE QQLTKPLERI FNPILGDAKT RELLNGDHTR
     TIKVAAPKKA GGLMRFTKTL EVCISCKNPL KPGNHGALCQ NCIVDGKGPD LYGAALSQMN
     YLENKFSRLW TECQRCQGSL HQEVLCSNKD CPIFYMRKKA EKDVHQKSIE LVKWDQTDW
//

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