ID A0A2S7UTE0_9GAMM Unreviewed; 939 AA.
AC A0A2S7UTE0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=BTO11_04595 {ECO:0000313|EMBL:PQJ53005.1};
OS Psychrosphaera saromensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Psychrosphaera.
OX NCBI_TaxID=716813 {ECO:0000313|EMBL:PQJ53005.1, ECO:0000313|Proteomes:UP000239007};
RN [1] {ECO:0000313|EMBL:PQJ53005.1, ECO:0000313|Proteomes:UP000239007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA4-48 {ECO:0000313|EMBL:PQJ53005.1,
RC ECO:0000313|Proteomes:UP000239007};
RA Yoshizawa S., Kogure K.;
RT "Diversity of luminous bacteria.";
RL Submitted (DEC-2016) 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 -!- SUBUNIT: Single-chain monomer with multiple functions.
CC {ECO:0000256|ARBA:ARBA00011541}.
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:PQJ53005.1}.
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DR EMBL; MSCH01000003; PQJ53005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7UTE0; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000239007; 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};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022839};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000239007};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 11..272
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 337..527
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 696..903
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 303..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 104306 MW; CDA0719AF94246F5 CRC64;
MSNDRISDPS SPLILVDGSS YLFRAYHSPP HLTNSRGEAT GAIYGVINML KSLVRQYSPE
QMIVIFDAKG PTFRNEMYSE YKANRPPMPD DLRTQIAPLH KIIEAMGLPI TAIEGVEADD
VIGTIADQQS KLGNKVLIST GDKDMAQLVN EHVTLINTMT NTILNPEGVE TKFGVKPEQI
IDYLALMGDK SDNIPGVPGV GEKTAVGLIQ GLGSIDNIYQ NLDDVAGLGF RGSKTMKAKL
VDNQDQLKLS YQLATIKLDV DHGITSDKMF IQSPDKEKLA ELYKECEFKR WLAEVLAGNS
NSEPPLVGST TKPANTSIDD QDEDSSIDAV SINKDLYQTI FTLEQWQSIL AEINNAKLIA
FDTETTSIDY MDAELVGFSI AYELNDDIKA IYVPLAHDYE DAPEQISLEQ ITPSLKALLE
DKNISKVGQN LKYDINVLAK YNLTIKGVVG DTMLQSYVFN STATKHNMDA LALKYLGHNC
ISFEDVAGKG AKQITFNQIS IETAAPYAAE DADITLRLYK YFDEKLQNIA PLNELMKNIE
LPLMPILSHI EHNGVLIDAD QMHALSSEFS IKLQELELKA HEIAGEEFNL ASPKQLQVIL
FEKLELPIVK KTPKGAPSTA EEVLLELSHD YDLPKVIMEF RGLSKLKSTY TDKLPLMIKP
ATGRVHTSYH QAIAATGRLS STDPNLQNIP IRNANGRRIR EAFVAPQGTK IVAIDYSQIE
LRIMAHLSDD KGLLTAFANN LDIHKKTASE VFSTPFEEVT KEQRRAAKAV NFGLIYGMSA
FGLARQLDIK RGEAQSYIDK YFERFPGVLT YMETTRVNAE KQGYVETLFG RRLYLPDITA
RNVPRRKAAE RAAINAPMQG TAADIIKMAM INVYQWLTSN DIQGVKIVMQ VHDELVFEID
ENLVDEYLPI LTDLMESAAS LKVPLIADSG TGDNWDQAH
//