ID W1N9B0_9GAMM Unreviewed; 928 AA.
AC W1N9B0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=DNA polymerase I {ECO:0000256|ARBA:ARBA00020311, ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU004460};
GN Name=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=BJB45_08965 {ECO:0000313|EMBL:ERL52084.1};
OS Halomonas huangheensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL52084.1, ECO:0000313|Proteomes:UP000019113};
RN [1] {ECO:0000313|EMBL:ERL52084.1, ECO:0000313|Proteomes:UP000019113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL52084.1,
RC ECO:0000313|Proteomes:UP000019113};
RA Miao C., Wan Y., Jin W.;
RT "draft genome of Halomonas huanghegensis, strain BJGMM-B45T.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
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:RU004460};
CC -!- SUBUNIT: Single-chain monomer with multiple functions.
CC {ECO:0000256|ARBA:ARBA00011541}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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:ERL52084.1}.
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DR EMBL; AVBC01000019; ERL52084.1; -; Genomic_DNA.
DR RefSeq; WP_021817916.1; NZ_CP013106.1.
DR AlphaFoldDB; W1N9B0; -.
DR STRING; 1178482.AR456_18035; -.
DR KEGG; hhu:AR456_18035; -.
DR PATRIC; fig|1178482.3.peg.954; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000019113; Unassembled WGS sequence.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR CDD; cd06139; DNA_polA_I_Ecoli_like_exo; 1.
DR CDD; cd09898; H3TH_53EXO; 1.
DR CDD; cd09859; PIN_53EXO; 1.
DR Gene3D; 3.30.70.370; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR020045; DNA_polI_H3TH.
DR InterPro; IPR018320; DNA_polymerase_1.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00593; pola; 1.
DR PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00475; 53EXOc; 1.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU004460};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU004460};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022839};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000019113};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 4..266
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 329..516
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 685..892
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 296..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 928 AA; 102756 MW; 2EB3209B53DCB0CF CRC64;
MAASPIVLVD GSSYLYRAFH ALPPLTTSEG KPTGAIKGVI NMLKRLLRDY PGSPMAVVFD
ASGKTFRDDL YAEYKAQRPP MPDDLRAQVE PLHACIKALG LPLLCIKGVE ADDVIGTLAR
LATEQGRDAV ISTGDKDMAQ LVNQHITLVN TMKDETLDVA GVNDKFGLPP ELIIDYLALM
GDKVDNIPGV PGVGEKTAIG LLQGMEGGLD TIYADLDKVT TLSFRGAKTL PKKLEENREL
AYLSYQLATI KTDCELDVGL DDLAIAEPDR EALKELYKRL EFRNWLEELL KGQDKGVDDV
AGGTPTPSAE GDAEEGNNQQ GSSSSERRDC VILEQTEFDE WLTRLGKADA FCFDLETTSL
DYMEADIVGV GLAIEPGEAA YIPLGHDYLD APDQLDRKTT LAALSEVLGD ASITKIGQNL
KYDISVLARH DITVAGPLVD TMLESYVLDS TATRHDMDSL ALKYLGESTV KFEDIAGKGA
KQLTFNQIAL EQAVPYACED VDITLRLHHE LRPRLERIGR LAEVLDEIER PLIRVLSHME
RNGVALDAEL LHTQSRELDT RIRELEARAY ELAGREFNLG SPKQLGQILF EEQGIPVIKK
TPKGAPSTAE AVLEELALDF PLPKVIMEHR GLSKLRSTYT EKLPKLVNKS TRRLHTSYHQ
AVASTGRLSS SDPNLQNIPI RTEEGRRIRQ AFIARPGYRI VAADYSQIEL RIMAHLSGDK
GLLTAFAEGR DIHSATAAEV FGVALDKVSS DQRRSAKAIN FGLIYGMSAW GLGRQLHIEQ
SQAKTYIERY FDRYPGVARY MERIRSQAAE DGFVETVYGR RLYLPEIHSQ NRARRQGAER
TAINAPMQGT AADIIKRAMI DVDAWLTDND EFDAWMVMQV HDELVFEVRE EQAEPFMAAV
SERMQNAASL DVSLIVEANH GANWDEAH
//
