ID A0A0C3I7A7_9VIBR Unreviewed; 787 AA.
AC A0A0C3I7A7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=SU60_10430 {ECO:0000313|EMBL:KIN10905.1};
OS Vibrio mytili.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=50718 {ECO:0000313|EMBL:KIN10905.1, ECO:0000313|Proteomes:UP000031977};
RN [1] {ECO:0000313|EMBL:KIN10905.1, ECO:0000313|Proteomes:UP000031977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 528 {ECO:0000313|EMBL:KIN10905.1,
RC ECO:0000313|Proteomes:UP000031977};
RA Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra J.;
RT "Draft genome of Vibrio mytili type strain CAIM 528.";
RL Submitted (JAN-2015) 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:KIN10905.1}.
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DR EMBL; JXOK01000037; KIN10905.1; -; Genomic_DNA.
DR RefSeq; WP_041155453.1; NZ_JXOK01000037.1.
DR AlphaFoldDB; A0A0C3I7A7; -.
DR STRING; 50718.SU60_10430; -.
DR OrthoDB; 5807460at2; -.
DR Proteomes; UP000031977; 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; -; 2.
DR Gene3D; 6.10.140.1130; -; 1.
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 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; PF21474; DNApolII_N; 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 80..296
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 378..740
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
SQ SEQUENCE 787 AA; 90160 MW; C386CA8FDD02CA7D CRC64;
MNIQQGFLLT RQARDINGQT QIELWLSTAI GPTQLLIRGE RPVFFIAQEH VDQVNQIAHA
KSLALEVRTL DLTSFNHTPL AACYTQQSKD ATVIQQLLAQ KDIVTFEGDI RLADRYLMER
FIRGSLEFTG ERTTEQGFLR VQRAKCRAGD FEPQLQVVSL DLECSEKGIL YSIGLDSPMD
SRVIMIGTPE PAETAIQWVE NEKALLQALI AWFKQFDPDV IIGWNVIDFD FRLLHKRAEW
HNLKLRLGRA DQVSFFRNSS QTQQGFISIP GRVVMDGIDT LKTATYHFRS WSLESVSQEL
LGEGKEIHNV HDRMDEINRM FRRDKPSLAK YNLQDCVLVN KIFEHTHLLD FAIERSRLTG
VELDRVGGSV AAFTNLYLPQ IHRAGYVAPN LHPENWIASP GGYVMDSIPN LYDSVLVLDF
KSLYPSIIRS FLIDPIGLVE GLKLEIGKQK NQAVPGFRGG QFHRSKHFLP AMIENLWAAR
DLAKKNNEQA FSQAIKIIMN SFYGVLGSSG CRFFDTRLAS SITMRGHEIM KQTKLLIEEQ
GFQVIYGDTD STFVSLNGEY SQTDADKVGQ RLAEHINAWW CEHLRSEYNL TSMLEIEYET
HYRKFLMPTI RGSETGSKKR YAGLIGEGKQ ERLIFKGLES ARTDWTSLAQ KFQNTLYHMI
FHGEDPSEYV REIVEKTNNG EFDDQLIYQK RLRRKLHEYQ KNIPPQVRAA RLADEMNAKL
GRPLQYQNRG RIEYVITLNG PEPFEYLSSP IDYQHYIDKQ LKPVADAILP FIGTDFDALS
APQMGLF
//
