UniProt: A0A0A8L7Q2

Database: UniProt
Entry: A0A0A8L7Q2_9SACH

LinkDB:  A0A0A8L7Q2_9SACH 
Original site:  A0A0A8L7Q2_9SACH

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (25)   

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ID   A0A0A8L7Q2_9SACH        Unreviewed;      1101 AA.
AC   A0A0A8L7Q2;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-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   ORFNames=KLDO_g2446 {ECO:0000313|EMBL:CDO94167.1};
OS   Kluyveromyces dobzhanskii CBS 2104.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO94167.1, ECO:0000313|Proteomes:UP000031516};
RN   [1] {ECO:0000313|EMBL:CDO94167.1, ECO:0000313|Proteomes:UP000031516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA   Nystedt B., Astrom S.;
RT   "The genome of Kluyveromyces dobzhanskii.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDO94167.1}.
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DR   EMBL; CCBQ010000037; CDO94167.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A8L7Q2; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000031516; 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; 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   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          176..480
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          544..971
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1013..1084
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
SQ   SEQUENCE   1101 AA;  124437 MW;  93780F8BB16BC6D3 CRC64;
     MTVGVTRTRD IETLEDAFQD IKKQRTQSFD RSSLSEPVST IEIIPTDKFK KQNVMGYKSS
     KVVDPTGKGN PTAFEQELSL MDHELVEKSE SGQTKLWSRT PIDADFDPKL SDISFQQLDA
     EQAQLSGQYD SNTNVVIRFF GVTDKGNSIL CNVTGFKHYL YVPAPLGFHQ ENILTLMQYL
     NEHYENNVDS IKVVPKQSIW GFSGDAKIPF LQIFVKNPNL LNKIRTGFEK GYIQPNDKWF
     VGGCTTYDNI AFPLRLMIDC GIVGMSWITL PASKYHIVPG AQRVSTCQFE VNINYKDLIA
     HPAEGEWSSN APLRIMSFDI ECAGRPGVFP EPEHDSVIQI ANVVSIAGAS KPFIRNVFTV
     NTCSPITGSQ IFEHEKEADM LKHWRDFIVE VDPDVIIGYN TTNFDFPYLL DRAAALGVQA
     FPYFGRLSNV KQEIKSSTFS SKAYGTRESK NINIDGRLQL DLLQFVQREY KLRSYTLNAV
     SAYFLGEQKE DVHHSIITSL QNGDSETRRR LAVYCLKDAY LPLRLLEKLM ALVNYTEMSR
     VTGVPFMYLL ARGQQIKVIS QLFRKCLQIQ TVIPNMNSQG SEEQYEGATV IEPKRGYYDV
     PIATLDFSSL YPSIMMAHNL CYTTLCDRAT IQRLKLKLDE DYIVTPNNDI FVTSKIRRGV
     LPEILDELIG ARKKAKFDLK NETDPFKRDV LNGRQLALKI SANSVYGFTG ATVGKLPCLA
     ISSSVTSFGR TMIETTKNAV ENKYCIKNGA SHDAVVVYGD TDSVMVKFGT TNLEESMKLG
     AEAAEFVSSL FKNPIKLEFE KVYFPYLLIN KKRYAGLYWT NPKKYDKLDQ KGLASVRRDS
     CPLVSIVMNK VLKKILIDRN VDGAMQFIRE TIDDILQNRC DISKLIISKT LAPNYTNPQP
     HAVLAERMRK RDGVGPNVGD RVDYVITGGS EKLFNRAEDP LYVLEQNIQL DSIYYLGNQL
     QNPIISIIAP IIGEKQANSM FIVKSIKRQS GPVGAASKQK GGLMSFVKKV DTCKSCKRVL
     RKNEGPLCAD CMSRSGELYM KALYDVRSLE ERFSRLWTQC QRCSGSLHNE VLCSNKNCDI
     FYMRVKAKKE LQEKVVELSK W
//

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