ID A0A132BYZ9_9RHOB Unreviewed; 945 AA.
AC A0A132BYZ9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ECO:0000313|EMBL:KUP92980.1};
GN ORFNames=TRIHO_21030 {ECO:0000313|EMBL:KUP92980.1};
OS Tritonibacter horizontis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP92980.1, ECO:0000313|Proteomes:UP000068382};
RN [1] {ECO:0000313|EMBL:KUP92980.1, ECO:0000313|Proteomes:UP000068382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O3.65 {ECO:0000313|EMBL:KUP92980.1,
RC ECO:0000313|Proteomes:UP000068382};
RA Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT Tritonibacter horizontis.";
RL Submitted (DEC-2015) 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:KUP92980.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LPUY01000063; KUP92980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132BYZ9; -.
DR PATRIC; fig|1768241.3.peg.2212; -.
DR Proteomes; UP000068382; 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:UP000068382};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 17..280
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 338..534
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 702..905
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 945 AA; 103615 MW; 3940EE71214A422B CRC64;
MGNNRLGSNT MSTSNFGKGC HLHLIDGSAF IFRAYHALPP LTRKSDGLPI GAVAGFCNML
FKQVEDNKGP DAPTHVAVIF DHSGKSFRND LYDLYKANRP PAPEDLVPQF PLTREATRAF
NIACKEIEGF EADDIIATLA CQAREAGGRV TIISSDKDLM QLVGNGVEML DAMKNKRIDS
DGVREKFGVG PERVVDVQAL AGDSVDNVPG APGIGIKTAA LLINEFGSLE DLLDRAEEIK
QPKRRQTLVE NRAQIEMSKT LVQLDCEMEL GFGLDELEIR DPDPEVLLGF LSSMEFRTLT
KRFADQLGLE APTIPETTPQ AAAALETPEA PRFDTAEYTT VRDAEGLQSW IDLIREHGYV
AVDTETTGLD EMVADLVGIS LCVLPGQACY IPLTHKAGSS DDLFGSDALA EGQMDLETAL
AMLKPVLEDS AILKIGQNMK YDAKIFVRNG IEVAPIDDTM LLSYALNGGL HGHGMDTLSE
RYLDHQPIPI KSLLGTGKSA ITFDRVPIDD ATPYAAEDAD ITLRLWSQFK PQLHQKQVTT
VYETLERPLV PVLAQMERHG IKVDRDTLSR MSNAFSQKMA GLEAEIHELA GESFNVGSPK
QLGEILFDKM SLPGGKKGKT GAYATGADIL EDLATEHVLP ARVLDWRQLS KLKSTYTDAL
QDHINPETGR VHTSYLQTGA NTGRMASSDP NLQNIPVRSE EGRRIREAFV ADEGNVLLSL
DYSQIELRIL AHVADIDALK QAFADGHDIH AMTASEIFDV PLAEMTSDIR RKAKAINFGV
IYGISGFGLA RNLRIPRGEA QGFIDRYFER FPGIRQYMDD TVAFAKEHGY VQTLFGRKIH
TPEIAAKGPR ASFAKRAAIN APIQGTAADV IRRAMVRMPE AIAHLPARML LQVHDELLFE
VPESHVEETI ETARRIMEGA ADPAVHMTVP LVVEAGRGAN WAEAH
//
