ID A0A0K3CJM7_RHOTO Unreviewed; 1118 AA.
AC A0A0K3CJM7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN Name=FGENESH: predicted gene_9.345 {ECO:0000313|EMBL:CTR09138.1};
GN ORFNames=AAT19DRAFT_16658 {ECO:0000313|EMBL:PRQ72734.1},
GN BN2166_0049990 {ECO:0000313|EMBL:CTR09138.1};
OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR09138.1, ECO:0000313|Proteomes:UP000199069};
RN [1] {ECO:0000313|EMBL:CTR09138.1, ECO:0000313|Proteomes:UP000199069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Single colony {ECO:0000313|EMBL:CTR09138.1};
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PRQ72734.1, ECO:0000313|Proteomes:UP000239560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 0880 {ECO:0000313|EMBL:PRQ72734.1,
RC ECO:0000313|Proteomes:UP000239560};
RX PubMed=29521624;
RA Coradetti S.T., Pinel D., Geiselman G., Ito M., Mondo S., Reilly M.C.,
RA Cheng Y.F., Bauer S., Grigoriev I., Gladden J.M., Simmons B.A., Brem R.,
RA Arkin A.P., Skerker J.M.;
RT "Functional genomics of lipid metabolism in the oleaginous yeast
RT Rhodosporidium toruloides.";
RL Elife 7:0-0(2018).
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; CWKI01000009; CTR09138.1; -; Genomic_DNA.
DR EMBL; LCTV02000009; PRQ72734.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K3CJM7; -.
DR STRING; 5286.A0A0K3CJM7; -.
DR OMA; CNNCRPR; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000199069; Unassembled WGS sequence.
DR Proteomes; UP000239560; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
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 CDD; cd05777; DNA_polB_delta_exo; 1.
DR CDD; cd05533; POLBc_delta; 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; 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:UP000199069};
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 201..492
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 556..987
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1024..1097
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 125472 MW; 68B7F56544953DEB CRC64;
MDGEPVTKRR RTTPPVSQGE PATVAGEPTA DANLATQQDI PDEDHAAPPS SAAGAHAKPL
SALFQAKTPS PKKSKRTVDL RQAGRIGEED KENFTALLAR LNKETPQEEA EKWGRPDAPK
LNPQRDGLIF QQIDIEEFSA GGGAPTIRAF GVTKNGNSVL LHVKGFLPYF WVSAPRGFTN
SDCLPFMEHL NAAHFNGVRP VKAVSLANKR SLWGYKGDAV SPFIKITVMD TKQYPKVRNA
FERGEVQYKG FFDGTALMTY ESNIAYTLRF MIDHHIVGMN WLELKPGTYE RAKNPVSNCQ
YEIECQHDQL ISHPAEGEWS GIAPLRILSF DIECAGRKGI FPEPEIDPVI QIANMVTRQG
ESKPFIRNVF TLNTCAHIVG SDVLEFKKEA DLLSKWRKFV EEVDPDLIIG YNTSQFDFPY
LMDRAKALKV SDFPYFSRLK GVKTEVKDTH FSSKAYGTRD SKETSMDGRL QLDILQVMQR
DYKLRSYTLN SVCAHFLGEQ KEDVHHSVIT DLQNGTAESR RRLAVYCLKD AYLPQRLMDK
LMCFINYTEM ARVTGIPFNY LLSRGQQIKV ISQLYRQALK TGYVIPALKQ EGSDEQYEGA
TVLEPEQGYY DVPIATLDFA SLYPSIMQAH NLCYTTLLDV KIAQALNLKE GEDFVRTPNG
DLFVKAHKRK GLLPTILEDL LAARKRARAE LKQEKDPFKR AVLDGRQLAL KVSANSVYGF
TGATIGKLPC LPISMSVTAY GREMIDQTKE VVQSTYNTAN GYDYDAKVIY GDTDSVMVRF
GCPDLETAMK LGAEAAEFVT SKFIKPIKLE FEKVYYPYLL ISKKRYAGLY WTKPEKYDKM
DTKGIETVRR DNCRLVVTVI DTCLRKMLIE RDVRGAEDYA KQVISDLLQN KVDLSQLVIT
KALAKADYAA KQAHVELAER MKKRDAGSAP AMGDRVAYVI IKGTKDARAY EKSEDPLYVL
ENNIPIDTKY YLDNQLSKPL MRIFEPILGE KASSLLAGDH TRTVSIVAPT VGGLMKFAVK
TVTCLGCRTP LKPNSLNQAV CNNCRPRTAE LHAKQVSIAA QAETAYARLW TQCQRCQGSL
HQDVLCTSKD CPIFYMRKKA QKEAADAVGT LKRFDGEW
//
