ID A0A1H8PAX7_9EURY Unreviewed; 896 AA.
AC A0A1H8PAX7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=SAMN04487948_102187 {ECO:0000313|EMBL:SEO38917.1};
OS Halogranum amylolyticum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=660520 {ECO:0000313|EMBL:SEO38917.1, ECO:0000313|Proteomes:UP000199126};
RN [1] {ECO:0000313|EMBL:SEO38917.1, ECO:0000313|Proteomes:UP000199126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10121 {ECO:0000313|EMBL:SEO38917.1,
RC ECO:0000313|Proteomes:UP000199126};
RA de Groot N.N.;
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; FODV01000002; SEO38917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8PAX7; -.
DR OrthoDB; 323192at2157; -.
DR Proteomes; UP000199126; 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; cd05160; DEDDy_DNA_polB_exo; 1.
DR CDD; cd00145; POLBc; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 129..368
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 445..778
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 896 AA; 101747 MW; 9541E02A888398B1 CRC64;
MKQSGLVDFE GGDDDEDRPS AEAAAVAGNG GQDVSDVVDT ADMKFPDAEG SVDISVTQVD
YTIEGAGADE YPVVHLFGRT ADNETEHVRV LGFRPYFYAP TDSLADEKLD RDTITGTEEG
FESIRGDELT KIFGRTPRDV GQMRDEFDHY EADILFPNRF LIDKDVGSGV RVAERRLDDG
TLQVPHTEVE PVDADADLRV NVFDIEVDDR NGFPEEGEEP IVCLTSHDSY RDEYVAWHYV
APDGEGKRPD SLPDYDPLRD GPDVDVRTFD AEDEMLDAFI AYVEETDPDV LSGWNFEDFD
APYFLDRLDV LNPTSDYDLS AERLSRVDEV WRSGWGGPDI KGRVVFDLLY AYKRTQFTEL
ESYRLDAVGE LELDVGKERY SGDIGDLWEQ DPERLLEYNL RDVELCVEID RKQQVVPFWD
EVRTFVGCLL EDAPTPGDAV DIYVLHKVHG NFALPSKGQA ESEDYEGGAV FDPITGVKEN
VTVLDLKSLY PMCMVTTNAS PETKVDPETY DGETFRAPNG THFRKEPDGI IRSMVDELLT
EREEKKALRN EHDPSSAAYE QFDRQQSAVK VIMNSLYGVL GWDRFRLYDK EMGAAVTATG
REVINFTEKA ANEIGYEVAY GDTDSVMLEL GEGVSKEQAI EQSFEIEEHI NAAYDDFARE
ELGADEHRFQ IEFEKLYRRF FQAGKKKRYA GHIVWKEGKD VDDVDITGFE YKRSDIAPIT
KEVQKDVLEM IVHGEDTDVV KDYVHDVIND FREGNMAYDR IGIPGGIGKR LENYDTDTAQ
VRGAKYANLM LGTNFQRGSK PKRLYLEKVH PSFFRRMESE EGFDPQHDYL YAEFKRNPDV
ICFEYADQIP EEFEVDWDKM LDKTLKGPIE RVIEALGVSW DEVKSGQEQT GLGSFM
//
