UniProt: A0A3A5J151

Database: UniProt
Entry: A0A3A5J151_9GAMM

LinkDB:  A0A3A5J151_9GAMM 
Original site:  A0A3A5J151_9GAMM

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (23)   
   InterPro (14)   
   Pfam (4)   
   PROSITE (1)   
   SMART (4)   
All databases (30)   

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ID   A0A3A5J151_9GAMM        Unreviewed;       900 AA.
AC   A0A3A5J151;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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:RJS92545.1};
GN   ORFNames=D3260_11530 {ECO:0000313|EMBL:RJS92545.1};
OS   Salinisphaera sp. Q1T1-3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC   Salinisphaeraceae; Salinisphaera.
OX   NCBI_TaxID=2321229 {ECO:0000313|EMBL:RJS92545.1, ECO:0000313|Proteomes:UP000269039};
RN   [1] {ECO:0000313|EMBL:RJS92545.1, ECO:0000313|Proteomes:UP000269039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1T1-3 {ECO:0000313|EMBL:RJS92545.1,
RC   ECO:0000313|Proteomes:UP000269039};
RA   Zayas Rivera J., Montalvo Rodriguez R.;
RT   "Draft Genome of Salinisphaera endophytica, a Novel Species of the
RT   Salinisphaera Genus Isolated as an Endophyte of Avicennia germinans, at the
RT   Solar Salterns of Cabo Rojo.";
RL   Submitted (SEP-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   -!- 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:RJS92545.1}.
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DR   EMBL; QZWD01000011; RJS92545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A5J151; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000269039; 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:UP000269039};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          8..259
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          302..489
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          658..864
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   900 AA;  98511 MW;  9D949154345743A9 CRC64;
     MSETQAHGPL ILIDGSSWLY RAYHVLPPLT NGAGEPTGAI YGMTNMLRKF LREYDSNRIV
     VVFDPRGPTF RNELFADYKA NRPPVPPDLS DQFQGIQDVI AALGLPMLQV SGVEADDVIG
     TLAVAESGPV IIVTGDKDMA QLVDERVVLL DTMQDKRTDV ARVNDKFGVP PERITDYLAL
     VGDTSDNVPG VDKVGPKTAA KWIEKYGDLA GVIAHADEIG GKVAENLRAK LDELPLYQDL
     VTIRTVLDLG EAGSDLVRRE IDTEALVALY RRYEFYKFLD ELDAPATDTA ASAAPAPAET
     TYHTVLDEVA LDTLVARLEA AELICVDTET DALSAMQSGL VGLSFAVEPG EAWYVPVAHD
     YIGAPAQLSM DTVLARVKGV LTDADKPKLG QHIKYDLNVL ARHGIRIAGA DHDTMLESYV
     LDSTATRHDM DSLAQKYLER TTTKFEEVAG KGAKQVGFNQ VALDDAAPYA AEDADITLQL
     HHRLYGQLCE TPSLRALYEE IEMPLMPVLA RVEANGVLVD AELLARVSGE MKTRMDEIQA
     EAYIAAGTEF NLGSPNQLKT ILFDQLELPV IRKTPKGAPS TAEDVLRELA DAHELPALIV
     AWRELSKLRS TYAEKLPTLI NPGTGRIHTS YHQAVAATGR LSSSDPNLQN IPIRTEAGRR
     IREAFVARPG YRILAVDYSQ IELRIMAHLS GDPGLLAAFN EERDIHTATA SEVFDTPLDD
     VTADQRRAAK AINFGLMYGM SAYGLSKQLE TSREDAAAYI DKFFERFAGV ARFMEDTRKA
     AKAQGYVETL FGRRLYLPEI NARNGQRRQY AERTAINAPL QGTAADLIKK AMIAVDAWLG
     ETGTDATMIM QVHDELVFEV PVDTADAIGE QIVDRMNAIA TLDVPLRAEA GIADNWQAAH
//

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