ID A0A0C1JST0_9BACT Unreviewed; 894 AA.
AC A0A0C1JST0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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:KIC73546.1};
GN ORFNames=DB41_JH00070 {ECO:0000313|EMBL:KIC73546.1};
OS Neochlamydia sp. TUME1.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Neochlamydia.
OX NCBI_TaxID=1478174 {ECO:0000313|EMBL:KIC73546.1, ECO:0000313|Proteomes:UP000031320};
RN [1] {ECO:0000313|EMBL:KIC73546.1, ECO:0000313|Proteomes:UP000031320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUME1 {ECO:0000313|EMBL:KIC73546.1,
RC ECO:0000313|Proteomes:UP000031320};
RX PubMed=25069652; DOI=10.1093/molbev/msu227;
RA Domman D., Collingro A., Lagkouvardos I., Gehre L., Weinmaier T.,
RA Rattei T., Subtil A., Horn M.;
RT "Massive expansion of Ubiquitination-related gene families within the
RT Chlamydiae.";
RL Mol. Biol. Evol. 31:2890-2904(2014).
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 -!- 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:KIC73546.1}.
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DR EMBL; JRXI01000164; KIC73546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1JST0; -.
DR PATRIC; fig|1478174.3.peg.1749; -.
DR Proteomes; UP000031320; 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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 2..261
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 305..485
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 652..859
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 894 AA; 101615 MW; 7663D87995E61D25 CRC64;
MMNDIYIIDA SGYIYRSYFA IRNITNHQGE STNALFGFIR SVSKLIIDFQ PYHLVAVFDG
PRSINARTSI YADYKAHRPD MPPDLLYQIQ WAREYCALRG IPILNIPEVE ADDTMGSIAV
WASQQQQAKA YICTSDKDMC QLVNDQVFIL NTFKDNLIMG AQEIEAVYGV PPHKIIDFLA
ITGDASDNIP GLSGFGPKTA SALLQQFGSL EYILAHPEEI PGKKKQETLI QEAEKALLSK
QLVTINTHVS IPREESFYRL IPCQKEQLKS FYISKNFNSL LKELEKEIPS SNPLGLSASD
EQVAYQCVDD EESLSALVGE LMLQKEICFD TETTSIHALK AELIGIGLCY QPSQAWYVPV
NGQLGLEKVV QTLKPLFENS SIGFYGHNVK YDLHVLSLYG IQVANITFDT ILASYLLNSH
RRQHSLDTLS LEYFGKVKIS IHSLIGKGKK AITMHEVPLE QVMAYCCEDV DFTCRLKKIL
KKQLQERKLY SLLNNVELPL LKVLLEMERQ GIYLDKEFLK NFSIKVTAQI RVLEKEIYLM
AGEEFNLNSP KQMSDILFNK LGIQPPKKTA TGNSTSAEVL EFLQHQYPIA SKLMEYRMLE
KLRSTYVETL PLEVNPKTHR IHCTFNQSVA ATGRLSCQDP NLQNIPVRTE WGIQIRQAFR
PEKLGWSFLA ADYSQIELRL LAHLSEDPTL LEAFQSNQDI HLRTAAAIFN VPLEHVTKEM
RYQAKTVNFG VIYGQGPFGL SQTLGIDVKD AKLFIEMYFK QYSKVKEYLE SVKESVRKLG
KAVTLTGRER LIPEINSKNM QIRAAAERLA VNAPIQGTAA DLIKLAMIQI NERLHKERKL
GYMVIQIHDE LIFELPDFEI LSIEPMVREI MQNVFKLKVP LIVDISIGKN WKEC
//
