ID A0A553IJ12_ACHLA Unreviewed; 880 AA. AC A0A553IJ12; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 02-OCT-2024, entry version 24. DE RecName: Full=DNA polymerase I {ECO:0000256|ARBA:ARBA00020311, ECO:0000256|NCBIfam:TIGR00593}; DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|NCBIfam:TIGR00593}; GN Name=polA {ECO:0000256|RuleBase:RU004460, GN ECO:0000313|EMBL:TRY00197.1}; GN ORFNames=FNV44_03890 {ECO:0000313|EMBL:TRY00197.1}; OS Acholeplasma laidlawii. OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales; OC Acholeplasmataceae; Acholeplasma. OX NCBI_TaxID=2148 {ECO:0000313|EMBL:TRY00197.1, ECO:0000313|Proteomes:UP000315938}; RN [1] {ECO:0000313|EMBL:TRY00197.1, ECO:0000313|Proteomes:UP000315938} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PG8REry {ECO:0000313|EMBL:TRY00197.1, RC ECO:0000313|Proteomes:UP000315938}; RA Medvedeva E.S., Baranova N.B., Siniagina M.N., Mouzykantov A., RA Chernova O.A., Chernov V.M.; RT "Genome sequence of Acholeplasma laidlawii strain with increased resistance RT to erythromycin."; RL Submitted (JUL-2019) 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:RU004460}; 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:TRY00197.1}. 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; VKID01000001; TRY00197.1; -; Genomic_DNA. DR RefSeq; WP_012242303.1; NZ_VKID01000001.1. DR AlphaFoldDB; A0A553IJ12; -. DR GeneID; 66293346; -. DR OMA; NRPPMPD; -. DR Proteomes; UP000315938; Unassembled WGS sequence. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro. DR GO; GO:0008409; F:5'-3' 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:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule. DR GO; GO:0006302; P:double-strand break repair; IEA:TreeGrafter. DR CDD; cd08637; DNA_pol_A_pol_I_C; 1. DR CDD; cd06140; DNA_polA_I_Bacillus_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; PF22619; DNA_polI_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 Coiled coil {ECO:0000256|SAM:Coils}; KW DNA damage {ECO:0000256|RuleBase:RU004460}; KW DNA repair {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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, KW ECO:0000256|RuleBase:RU004460}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}. FT DOMAIN 2..264 FT /note="5'-3' exonuclease" FT /evidence="ECO:0000259|SMART:SM00475" FT DOMAIN 306..474 FT /note="3'-5' exonuclease" FT /evidence="ECO:0000259|SMART:SM00474" FT DOMAIN 640..844 FT /note="DNA-directed DNA polymerase family A palm" FT /evidence="ECO:0000259|SMART:SM00482" FT COILED 498..525 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 880 AA; 100085 MW; 34FB7052DEFE9298 CRC64; MKKITLVDGN SILFRAYNAT AYPGAKVLQT STGIYTNAVF AFSGMIDKII EISNSHMLIA FDTGEPTHRH KSYDDYKAGR KEMPEELGSQ IPLIHELIKY LGIKEYSMAG YEADDIIGTL AKMAEKAGYK VDVFSSDYDL LQLVTEHITV HMLKKGMRVV ETYTPETLKE TYGFSHELFI DFKALVGDKS DNIPGVPGVG EVTAKKLIAE YGTLENILNN AEHIKGKLGE NIRTNKEQAV FSKELSTILT DMPLPFDLED TKVGEVDEES LINFYKRLEL KQLVISYNKK NPEVAATTAE TSEFQYKAID SENALKSLLN QDLAIYFEFS DFNYHKAELW GVGLSNGKIN YFVDSETFLN SASFKAYLES SKYKKYTYHY KGTKVFLKKL GTEFNHVTYD LLLAAYLIQS SIGKQDFTFI AQQFQITDIQ YDEEVYGKGA KKALPLIPSD YEGHIAKKAY IIHKLMQQTL DVLTERNQLS LLNDVELPLS DVLADMEYQG LTVDLKELEN QTKDMSLRID KLRTEILLLA GVDFNVDSPK QLGDVLFDTL GLPNGKKTKT GYSTGIEVLN NLIDHHPIIN LIIEYRQLTK LYSTYLIGIK ESVFEDNRVH TIYNQALTLT GRLSSLEPNL QNIPIRTEEG RQIRKLFIPE PDSYFVGADY SQIELRVLAA MADVKNLKQA FEEDQDIHTV TAQKVFHVDT VDSEQRRRAK AVNFGIIYGI GPWSLSEDIG VTVKEAENFI SRYLEVYPEI KDYMTNIVEF AKTHGYVETL LNRRRYIPEL SSKVFNLREF GKRTSLNAPI QGTAADIIKL AMIDLHNYLK DNKKKSKLIL QVHDELIVEV VKEELDEMKE VIPNIMEKAF NLGVRLKTSC DVGNNWYELK //