ID A0A495IZX8_9SPHI Unreviewed; 955 AA.
AC A0A495IZX8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=BDD43_1535 {ECO:0000313|EMBL:RKR81389.1};
OS Mucilaginibacter gracilis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=423350 {ECO:0000313|EMBL:RKR81389.1, ECO:0000313|Proteomes:UP000268007};
RN [1] {ECO:0000313|EMBL:RKR81389.1, ECO:0000313|Proteomes:UP000268007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18602 {ECO:0000313|EMBL:RKR81389.1,
RC ECO:0000313|Proteomes:UP000268007};
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 (OCT-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:RKR81389.1}.
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DR EMBL; RBKU01000001; RKR81389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495IZX8; -.
DR Proteomes; UP000268007; 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:UP000268007};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 21..282
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 362..543
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 712..919
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 955 AA; 107392 MW; 9AD142B009F1D955 CRC64;
MYVGCLISDI KQIKTNQRSM KKLFLLDGMA LIYRAHFALS KTPRFTSGGL NTSAVMGFTN
TLLEVLRKEK PSHMAVVFDT EAPTERHTEF ADYKGHREAM PEDLSKALPY IFKVVLGFNI
PVITSDGFEA DDIIGTLAKK AEQKGYQVYC MTPDKDFAQL VSDNIFIYKP ARMGNDMEIL
GVKEVLAKWE IERVEQVIDI LGLWGDAVDN IPGIPGIGEK TAKSLIKTYG SMENIIAHSH
ELKGKQRENV EAFAEQGLLS KRLATINLNA PVELDEAGLE MCDPNRELLE PLFAELEFRT
LGRRVFGDGS SITEIKNVSI QHDLFSSPQS QEGTTTMTVD VTDIYEEPAG PLQNISNTEH
QYHLADTFEK RAELIKLLSA QKSICFDTET TGTDANQCDL VGLSFSIKKG QAWYVPVPKN
CDEIQPIVDE FKELFENPAI GKIGQNIKFD MLVLKYYNVT IQGELFDTML AHYIIDPDTR
HGMDVLAENY LGYSPVSITE LIGAKGKNQG TMRDVEIEKI KDYAAEDADI TLQLKEIFEP
KLEQVGGTVL ATDIENPLVY VLADIEFEGV RIDHDTLKEF SKELETEIGK LEKTVYEKAG
VRFNIASPKQ LGEVLFEKLK LDEKAKKTKT GQYQTGEDVL LALANKSDIV RDILDFRQMQ
KLKSTYVDAL PLMVNPKTGR VHTSYNQAVA ATGRLSSNNP NLQNIPIRTE RGREVRKAFI
PRNEDHVIMS ADYSQIELRI IAEISKDANM MEAFVQGVDI HTATAAKVYG KTLDEVDGTM
RRNAKAVNFG IIYGQSAFGL SQNLNIPRKE AADIIEQYFA QYPGIKNYMN DTMHFARQNG
YVQTLMGRRR YLRDINSANQ TVRGYAERNA INAPIQGSAA DMIKIAMINI HREFKAHKFD
SRMTMQVHDE LVFDVHKSEI EMVKPIILDN MRNAIKTVVP IVVEIGMGNN WLEAH
//
