ID Q7RSZ8_PLAYO Unreviewed; 1097 AA.
AC Q7RSZ8;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=PY00203 {ECO:0000313|EMBL:EAA21409.1};
OS Plasmodium yoelii yoelii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=73239 {ECO:0000313|EMBL:EAA21409.1, ECO:0000313|Proteomes:UP000008553};
RN [1] {ECO:0000313|EMBL:EAA21409.1, ECO:0000313|Proteomes:UP000008553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17XNL {ECO:0000313|EMBL:EAA21409.1,
RC ECO:0000313|Proteomes:UP000008553};
RX PubMed=12368865; DOI=10.1038/nature01099;
RA Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA Shoaibi A., Cummings L.M., Florens L., Yates J.R., Raine J.D., Sinden R.E.,
RA Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B.,
RA van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA Carucci D.J.;
RT "Genome sequence and comparative analysis of the model rodent malaria
RT parasite Plasmodium yoelii yoelii.";
RL Nature 419:512-519(2002).
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:EAA21409.1}.
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DR EMBL; AABL01000054; EAA21409.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7RSZ8; -.
DR STRING; 73239.Q7RSZ8; -.
DR PaxDb; 73239-Q7RSZ8; -.
DR EnsemblProtists; EAA21409; EAA21409; EAA21409.
DR VEuPathDB; PlasmoDB:Py17XNL_000504381; -.
DR InParanoid; Q7RSZ8; -.
DR OMA; CNNCRPR; -.
DR Proteomes; UP000008553; 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:UP000008553};
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..474
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 539..970
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1006..1076
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
SQ SEQUENCE 1097 AA; 126636 MW; 62F5D9558C061B8D CRC64;
MEQNIFSATN VIPYGPLYDK VKKVKNNDQD ENYPVVEEYE KLLKTYERPN PYDSNGSLKF
NNNDDLILFQ IDLDYTVENI FRNVIYNNEG STNNSDSKCN SIYEPYKIIL GKEKNFISVP
IIRIYSITNC GYSVVVNVHN FFPYFYVEKP NGFNNDDMIK LESMLNETLS LNNQFKMYEN
KILKIETVKT ESIMYFKKSG KTDFLKITVL LPKMVPSLKK FFESGINVNS KHFGGIVYEA
NLPFILRYII DKKITGSSWI KCEKNSYIIR SKNKQSSNCT FEIDIHYENI EPMALENEYQ
KIPKLRILSF DIECIKLDGK GFPEAKTDPI IQISSILYLQ GDPIENCAKF IFTLLECASI
PGSNVIWFND EKTMLEAWNE FVIRIDPDFL TGYNIINFDI PYILNRGTAL NLKKLKYIGR
IKNIPSLVKD ANFSSKQFGT HETKEINING RIQFDVYDLI KRDYRLKSYT LNYVSFEFLK
EQKEDVHYSI MNDLQNENSE SRKRIATYCI KDGLLPLRLI DKLLFIYNYV EMARVTGTPF
VYLLTRGQQI KVTSQLYRKC KELNYIIPST YIKVNNNDKF EGATVLEPIK GYYIEPISTL
DFASLYPSIM IAHNLCYSTL IKNNDEISDL NKNDITTVPG KNNFKFVKGN VKRGVLPLIV
EELIRARKNV KAMMKNEQNP ITKMVLNGRQ LALKISANSV YGYTGAAAGG QLPCLEIATS
ITTFGRSMIE KTKETVEAYY CKNNGFEHNA TVVYGDTDSV MVKFGTNDVG EAMRLGKDAA
ERISKEFLHP IKLEFEKVYC PYLLLNKKRY AGLLYTNPNK HDKMDCKGIE TVRRDFCILI
QQMMETVLNK LLIEKDLNSA IEYTKSKIKD LLTNNIDMSL LVVTKSLGKA EYETRLPHVE
LAKKLKQRDS ATAPNVGDRV SYIIIKGTKG QAQYERAEDP LYVLDNNLSI DHNHYLDAIK
NPLSRIFEVI MQNSDSLFCG EHTRHKTILT SSQTALSKFL KKTIRCIGCN SSIKKPPLCN
HCKTNKEFSI YMQKIKDLKL KQNEFFQLWT ECQRCQGNLH IDVICMNRDC PIFYRRAKIK
KDVANLQEQV TSLKIEW
//
