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Database: UniProt
Entry: A0A1H7SRF3_9GAMM
LinkDB: A0A1H7SRF3_9GAMM
Original site: A0A1H7SRF3_9GAMM 
ID   A0A1H7SRF3_9GAMM        Unreviewed;       819 AA.
AC   A0A1H7SRF3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=SAMN05216262_12038 {ECO:0000313|EMBL:SEL75200.1};
OS   Colwellia chukchiensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=641665 {ECO:0000313|EMBL:SEL75200.1, ECO:0000313|Proteomes:UP000199297};
RN   [1] {ECO:0000313|Proteomes:UP000199297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9127 {ECO:0000313|Proteomes:UP000199297};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOBI01000020; SEL75200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7SRF3; -.
DR   STRING; 641665.GCA_002104455_01548; -.
DR   OrthoDB; 5807460at2; -.
DR   Proteomes; UP000199297; 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; 3.30.70.2250; -; 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; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000199297};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          91..330
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          411..791
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
SQ   SEQUENCE   819 AA;  92913 MW;  979227CC826B0031 CRC64;
     MQFSPEKVTT HAAPLIANRG FLLTRSARDR NDRLEISLWL KTPQGPAQLL INNERAVFFV
     EQTSLAHAKS VLAQQQVNLD EIKALPLKTF KQRPVFALYF LSLREFYQAR AALHKQGIKC
     YEDDIRPDDR YLMERFITAD ITFAGQQAWL TPKFAGTFTR FEHVKCKRLD KSQQTDIKLS
     TVSLDIECAM SGELYSVGLY SENCQQVLMI ASATDIAREQ QANPDADIDI VWQADEKQLL
     LSLLAWFQAH DPDIIIGWNV INFDFSLLQK RFDLYGLTFA IGRDAQAPYW RKNKASEQQF
     IDINGRVVLD GIDLLKTATY NFPSFSLDNV ANTLLGLGKK VTDVDNRIAE INHNFHHDKT
     ALARYNLEDC RLVLLIFQHT QLLEFAMLRA QLTGLAIDRI GGSVAAFTNL YLPKLHRSGY
     VAPNMGDGEQ GFESPGGFVM DSIPGLYKNV LVLDFKSLYP SIIRSFNIDP MGLIEGLKSP
     DTAIAGYDGA LFSRTAHFLP AIITALWQER DKAKVENNAA LSQAIKIIMN SFYGILGSAG
     CRFFDPRLSG SITKRSHSIL KTTKVWIEAK GYRVIYGDTD SIFVHIGDQH NGASSRALGK
     VLQDDINHKW QQLLKTDYGI ESALEIEFET RFSKFLMPTI RGQDIGTKKR YAGLVEKGGE
     QQLIFKGLES VRTDWTELAK QFQRTLYLKI FNDEPVADYI KAVVADTLAG KHDQLLYYRK
     RLRRKLSDYV KNVPPHVRAA RLADEIYQQQ GKPQRYQNKG WIEYVMTTNG PQAKGCQSAA
     LDYQFYIDRQ LMAVADAILP FINSSFDEIT NSQMTLFDR
//
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