ID A0A318UJF0_9SPHI Unreviewed; 938 AA.
AC A0A318UJF0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=B0O44_102254 {ECO:0000313|EMBL:PYF75700.1};
OS Pedobacter nutrimenti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1241337 {ECO:0000313|EMBL:PYF75700.1, ECO:0000313|Proteomes:UP000248198};
RN [1] {ECO:0000313|EMBL:PYF75700.1, ECO:0000313|Proteomes:UP000248198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27372 {ECO:0000313|EMBL:PYF75700.1,
RC ECO:0000313|Proteomes:UP000248198};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-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:PYF75700.1}.
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DR EMBL; QKLU01000002; PYF75700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318UJF0; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000248198; 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 Reference proteome {ECO:0000313|Proteomes:UP000248198};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 2..263
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 345..526
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 695..902
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 938 AA; 104935 MW; 1F0AF44A003A19E6 CRC64;
MKKLFLLDGM ALIYRAHFAL SKNPRFTSTG INTSAVMGFA NTLMEVLKKE KPSHLAVVFD
TEAPTERHTD FEAYKAHRQA MPEDLSAALP YVIKLIEGFN IPVITKDGYE ADDIIGTLAK
EGEKRGFTVY CMTPDKDFAQ LVSENIFIYK PARMGNEMEI LGVREVLAKW EIEDVRQVID
ILGLWGDAVD NIPGIPGIGE KTAKQLIKQY GSVENIIANA HELKGKQREN VENFAEQGLI
SKKLATIILD VPVDFDEDAL EMGAPNRELL EPLFAELEFR TLGKRVFGEG FSVGASSATL
VAQQTDLFGN VTGASYASQT VVAEPEIEPA EQTTLKTIAD VPHTYLLTDT AEKRKALIST
LLSQENISFD TETTGTDANQ ADLVGLSFCV KAGEAYYIPL SANREEVLLI LEEFKPVLEN
EKIAKTGQNL KYDILVMKWY DVQVKGKLFD TMLAHYLIDP DTRHNMDILS ENYLGYQPIS
ITALIGPKGK NQGTMRDVPV EKVVDYAAED ADVTLQLANV FEPMLKKQNA FELAANVENP
LVYVLADIEK EGVRIDMDTL QNYSKELELD IRRFEQNVYD KCGVQFNLAS PKQLGEVLFD
KLQLDPKAKK TKTGQYQTGE DVLLALAHKS DVVQDILDFR QLQKLKSTYV DALPLMVNPK
TGRVHTSYNQ AVAATGRLSS NNPNLQNIPI RTERGREVRK AFIARDDDHV LLSADYSQIE
LRIIAEISKE ENMLDAFNKG IDIHTATAAK VYGVGIQEVD ATQRRNAKAV NFGIIYGQSA
FGLSQNLGIP RKEAAQIIEQ YFEQYPGIKR YMSDTMNFAR ENGFVETILG RRRYLRDINS
ANQTVRGFAE RNAINAPIQG SAADMIKVAM IRIHKDIQEQ GLQSKMTMQV HDELVFDVLK
SEVAQMKEII RHRMKTAIAT TVPIEVEIGE GKNWLEAH
//
