ID A0A1F2P4K3_9EURY Unreviewed; 800 AA.
AC A0A1F2P4K3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=SBU_001104 {ECO:0000313|EMBL:OFV65922.1};
OS Candidatus Syntrophoarchaeum butanivorans.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinales incertae sedis; ANME-2 cluster;
OC Syntrophoarchaeum.
OX NCBI_TaxID=1839936 {ECO:0000313|EMBL:OFV65922.1, ECO:0000313|Proteomes:UP000185779};
RN [1] {ECO:0000313|EMBL:OFV65922.1, ECO:0000313|Proteomes:UP000185779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BOX1 {ECO:0000313|EMBL:OFV65922.1};
RA Laso-Perez R., Richter M., Wegener G., Musat F.;
RT "Microbial consortia oxidize butane by reversing methanogenesis.";
RL Submitted (MAY-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}.
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:OFV65922.1}.
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DR EMBL; LYOR01000005; OFV65922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F2P4K3; -.
DR STRING; 1839936.SBU_001104; -.
DR PATRIC; fig|1839936.3.peg.1116; -.
DR Proteomes; UP000185779; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000185779};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 92..298
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 375..704
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
SQ SEQUENCE 800 AA; 92332 MW; 289ADEDD5F9C0E17 CRC64;
MYTTLDMYFP DEMPDADHSG RIELGITQIS YTLDESGYPI INLYCRDTAG RFRRVDVQGF
QPYFYIEADP DEVLELMKDP RVVDIKEGYR TIDNREVYKV VTRTPSDVKD LRENYRHYEA
DILFTTRFMV DTGIKSGIMV PDKEMVQVEE IKPIELDVPT RICIIDIECD DRNGFPQPER
DAVICITAWD SFDDEYTTFI WPYRQRDEKE MLEMLLAYIQ TKDPDILTGW NFTNFDVPYL
IDRMRALGID PSPLSRDGMV KNKAGHFSPA MIKGRVLFDL LYGYKKMQPT QKESYRLDWI
AEDELGETKH HYTGSLGNLW ENDPDELIRY NRKDVELCVE IERKNDIIGF SKEVANFVGC
SIEDTLNASR VIDTYVLRKS LGRFVLPSKH GEFKGEFEGA VVLSPIKGVR ENVIVLDLAS
LYPMSMMTLN ASPETKSPDG ELVAPNGVRF KKSPDGLTRM ILKELIESRL EKKRLRDRYP
LGSDEYRKYD LQQAAIKVIT NSYYGVSGYP RFRLYDRDIA AATTSVGRAI IRHTKSVIES
MGYEVVYGDT DSCMVTVGGG KDLDEVIEIG KEIERRVNES YDDFAKTLNA DKHYFSIKFE
KVYSRFFQAG TKKRYAGRLV WKEGKYTDQL DITGFEFRRS DFPKITKEVQ REVIRRIIDG
EGFNEIGEYL RGVISKFEKG ELSLDEIGIP GGIQKRLDRY ETDDAQIRGA IYANKYFGTN
FGKGSKPKRV YISKTPEGYP PTDVICFEYE DQVPDGFIPN WDVMLEKTIK NPIERILEAM
GWSWTEIKSG KKQMGLDGFF
//
