ID A4C5R8_9GAMM Unreviewed; 780 AA.
AC A4C5R8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=PTD2_10919 {ECO:0000313|EMBL:EAR29322.1};
OS Pseudoalteromonas tunicata D2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR29322.1, ECO:0000313|Proteomes:UP000006201};
RN [1] {ECO:0000313|EMBL:EAR29322.1, ECO:0000313|Proteomes:UP000006201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D2 {ECO:0000313|EMBL:EAR29322.1,
RC ECO:0000313|Proteomes:UP000006201};
RA Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., Ferriera S.,
RA Johnson J., Kravitz S., Halpern A., Remington K., Beeson K., Tran B.,
RA Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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 -!- 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:EAR29322.1}.
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DR EMBL; AAOH01000002; EAR29322.1; -; Genomic_DNA.
DR RefSeq; WP_009837197.1; NZ_AAOH01000002.1.
DR AlphaFoldDB; A4C5R8; -.
DR STRING; 87626.PTD2_10919; -.
DR eggNOG; COG0417; Bacteria.
DR HOGENOM; CLU_018487_0_0_6; -.
DR OrthoDB; 5807460at2; -.
DR Proteomes; UP000006201; Unassembled WGS sequence.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd05784; DNA_polB_II_exo; 1.
DR CDD; cd05537; POLBc_Pol_II; 1.
DR Gene3D; 2.40.50.590; -; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 2.
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 PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 2.
DR Pfam; PF03104; DNA_pol_B_exo1; 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 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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 64..296
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 375..430
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 473..749
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
SQ SEQUENCE 780 AA; 88863 MW; 5329FF48B4EE82DF CRC64;
MSELITVEGF VLTKQQLKTK YGFALCYWLT SDLGPIQVMV EQQEAVFFVL SSDLLQILAL
LKSENILLRT QALGLKSFDQ QAISGCYFST LHGFYQAKKI IQQAGFRLFE ADVRHCDRFL
MERFIRGSVL VQGQAIKKQG YLTLQQAKMK PSTYQPNFSV VSLDIECSGQ GILFSVGLYS
DDFDVVIMVG APQHSEQNIV WVSDEEQLLV QLQRYFVERD PDVIIGWNVI DFDMSLLYRR
AEQLGVPLYL GRAQQAMQLS ERAVGKLLLP GRVVLDGIDT LKNATYHFNS FSLASVAEQL
IGEKKLIESD DRLAEIEHQF KYDKLALAKY NLKDCQLVWD IFKQEKLIDF AILRTQLTGL
ELERQGGSVA AFVNLYLPLM HRSGYVAPNL GDHNHHFNSP GGYVMNSQPG LYQNVIVLDF
KSLYPSIIRT FLIDPIGMVE GLLAPTQSIA GFHDAYFSRT AHHLPNLIAT LWQARDVAKQ
QKNKMLSQAI KIIMNSFYGV LGSTGCRFYD PRLSSSITLR GHEIMLATRA EIERLGYQVI
YGDTDSTFVQ LASELSAEEC KKIGFLLQKK INNFWCDYCE KKYKIASYLE IEFETLYSPF
FMPTIRGSLE GSKKRYVGQV SDANGDHLVF KGMETVRSDW TELAREFQYN LFTLIFAGDS
VEVYIKQVIS DLMAGRLNHL LLYKKRLRQH LSEYVKNIPP HAQAAQKMSM KYPEKTPKRG
QWIEYVITLD GPVVATEKPL KLNLQHYLEK QLQPIADSIL PTLNMSFAQF LSGQVNLFEN
//
