ID A0A3N2N7K0_9BACT Unreviewed; 930 AA.
AC A0A3N2N7K0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN Name=polA {ECO:0000256|RuleBase:RU004460,
GN ECO:0000313|EMBL:ROT18413.1};
GN ORFNames=EEL51_09925 {ECO:0000313|EMBL:ROT18413.1};
OS Muribaculaceae bacterium Isolate-110 (HZI).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2486473 {ECO:0000313|EMBL:ROT18413.1, ECO:0000313|Proteomes:UP000275373};
RN [1] {ECO:0000313|EMBL:ROT18413.1, ECO:0000313|Proteomes:UP000275373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate-110 (HZI) {ECO:0000313|Proteomes:UP000275373};
RA Clavel T., Strowig T.;
RT "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT host preference, and functional potential of this yet undescribed family.";
RL Submitted (NOV-2018) 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 -!- 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:ROT18413.1}.
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; RIBL01000017; ROT18413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2N7K0; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000275373; Unassembled WGS sequence.
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:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
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; 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; 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 PRINTS; PR00868; DNAPOLI.
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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000275373};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 3..266
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 688..894
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 930 AA; 103433 MW; B5D364EB2BEF05E6 CRC64;
MEKRLFLLDA YALIYRAYYA LIHSPRFATT AGFNTSAIFG FCNTLDDLLR KENPSHIAVC
FDPPHGRTFR HEQFEAYKAQ RDKQPEDITL AIPYIKRVLE GYRIPVIEVP GYEADDVIGT
LATRAAAKGY DTYMMTPDKD YGQLVAPHIY MYRPALKGEG FEVRDVAKVC ERYGIAEPRQ
VIDLLALEGD ASDNIPGCPG VGEKTARKLI DEWGSVENLL ENTDKLKGAL QRRVIENADQ
IRMSKWLATI CTDAPIDIEV DDLVRRPIDA DSLMEVFREL DFKSLMGRLK AQIASGEAVD
KASQTAPAQA APADDGSGMG SLFDTPADGP TALEVCEERH YETVSTPARA AEIVRLASAQ
PMIGIAAYAP GEEAMTGRLE GLALSWEPCG GYFIPFPKDD TAARAEIRAI VSPLFSGKAP
LMVSFDVKRT LLLMRHEGIS LDMPYFDVSV AHYVIDPEMK HDVATISLKY LDMPLQGVPA
DSRPGHPKSS LEPEAAVTRY CEEADLALRL RPRLQAEVAE RDMTRLLEEV EFPLIRVLAD
MEWTGVRIDP SVLTDLSAKL KEQVSALELE AYEMAGGPFN IASPAQVGMV LFDRLAIDPK
AKRTAKGSYS TTEQVLEKYA HKVPLVGLIL KIRRLRKLIT TYLDALPALI NPETGKIHTS
FNQTVTATGR ISSTNPNLQN IPIRTDDGRE IRRAFIPDNG DLMMSADYSQ IELRLIADLS
NDKDMIEAFL SGDDIHRITA SKVYKKPLEE VTDDERRHAK TANFGIIYGI SAFGLSERLG
IARPDAKKLI DGYFATYPHV REYLDKAVAD ARERGYVTTR MGRRRYLPDI NSRNAVVRGY
AERNAVNAPI QGSAADIIKV AMVRIYAEMQ RRSLRSRMIM QVHDELIFNV VPEELDELKR
IVFEGMEGAY AGAVPLEVAA GVAANWLEAH
//
