UniProt: A0A0D9QKG5

Database: UniProt
Entry: A0A0D9QKG5_PLAFR

LinkDB:  A0A0D9QKG5_PLAFR 
Original site:  A0A0D9QKG5_PLAFR

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (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)   
All databases (27)   

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ID   A0A0D9QKG5_PLAFR        Unreviewed;      1096 AA.
AC   A0A0D9QKG5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=AK88_04172 {ECO:0000313|EMBL:KJP86201.1};
OS   Plasmodium fragile.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP86201.1, ECO:0000313|Proteomes:UP000054561};
RN   [1] {ECO:0000313|EMBL:KJP86201.1, ECO:0000313|Proteomes:UP000054561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., Abouelleil A.,
RA   Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Plasmodium fragile nilgiri.";
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}.
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DR   EMBL; KQ001699; KJP86201.1; -; Genomic_DNA.
DR   RefSeq; XP_012337205.1; XM_012481782.1.
DR   AlphaFoldDB; A0A0D9QKG5; -.
DR   EnsemblProtists; KJP86201; KJP86201; AK88_04172.
DR   GeneID; 24269486; -.
DR   VEuPathDB; PlasmoDB:AK88_04172; -.
DR   OMA; CNNCRPR; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000054561; 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   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          172..473
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          538..969
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1005..1075
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
SQ   SEQUENCE   1096 AA;  126660 MW;  79F98738D0E6C09F CRC64;
     MERMKKCPFT SVIPYGTLYD KLKKEKMGQL PEDVMIEEFN QLLTTYERPS PYDANGLIHV
     SNEKDLILFQ IDIEYTVDSI FKSMVFTNDM TPNGRVLPDI YSPYRSMFQN NEKNYISVPV
     IRIYTVTNDG YSVLVNVHNF FPYFYVEMPS TFEQEDLLKL ECMMNENLNM NSQYKMYDQK
     ILNIEVVKTE SLMYYKRDGK KDFLKITVLL PKMVPTLKKL FENVINVNGK NIGGIVYEAN
     LPFILRYIID KKITGSSWLL CKKDKFHIRP RHKKISNCSF EIDISYEHVE PMPLENEYQQ
     IPKLRIVSFD IECIKLDGKG FPEAKNDPII QISSILYFQG DPIEKCAKFI FTLKECASIP
     GSNVIWFNDE KTLLDAWNEF IIKLDPDFLT GYNIINFDLP YILNRGTALN LKKLKMLGRI
     KNFSSVVKES TFASKQFGNH ETKEININGR IQFDVYDLIR RDYKLKSYTL NYVSFEFLKE
     QKEDVHYSIM NDLQNESPES RKRIATYCIK DGILPLRLID KLLFIYNYVE MARVTGTPFI
     YLLTRGQQIK VTSQLYRKCK ELNYVIPSTY MKSASNEKYE GATVLEPIKG YYTEPISTLD
     FASLYPSIMI AHNLCYSTLV KNTAQLEGLN EDEVTSIEGK NNIKFVKGSV KKGILPLIVE
     ELIDARKKVK LLIKNEKNKI TKMVLNGRQL ALKISANSVY GYTGAASGGQ LPCLEVAVSI
     TTLGRSMIDK TKEKVEQYYN KSNGFEHNAT VVYGDTDSVM IKFGTSSIEE AMALGKDAAQ
     RISKEFLHPI KLEFEKVYCP YLLLNKKRYA GLLYTTPEKH EKMDCKGIET VRRDFCILIQ
     QMMETVLNKL LIEKNLNSAI DYTKSKIKDL LTNNIDMSLL VVTKSLGKTD YETRLPHVEL
     AKKLKQRDSA TAPNVGDRVS YIIIKGVKGQ AQYERAEDPL YVLDNNLAID YNHYLDAIKN
     TLSRIFEVIM NNSDSLFCGE HTRHKTILTS SQTALSKFLQ KAVRCIGCNS SIKKPPLCNH
     CKTNKEFSIY MQKMNHFKHK QNEFFQLWTE CQRCQGNLHA EVICMNRDCP IFYRRAKIKK
     DMANVQEQIS ALRADW
//

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