UniProt: K2Q1M5

Database: UniProt
Entry: K2Q1M5_9FLAO

LinkDB:  K2Q1M5_9FLAO 
Original site:  K2Q1M5_9FLAO

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (23)   
   InterPro (14)   
   Pfam (4)   
   PROSITE (1)   
   SMART (4)   
Literature (1)   
   PubMed (1)   
All databases (32)   

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ID   K2Q1M5_9FLAO            Unreviewed;       942 AA.
AC   K2Q1M5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
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=I215_11105 {ECO:0000313|EMBL:EKF54731.1};
OS   Galbibacter marinus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Galbibacter.
OX   NCBI_TaxID=555500 {ECO:0000313|EMBL:EKF54731.1, ECO:0000313|Proteomes:UP000007364};
RN   [1] {ECO:0000313|EMBL:EKF54731.1, ECO:0000313|Proteomes:UP000007364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ck-I2-15 {ECO:0000313|Proteomes:UP000007364};
RX   PubMed=23209227; DOI=10.1128/JB.01852-12;
RA   Lai Q., Li C., Shao Z.;
RT   "Genome Sequence of Galbibacter marinum Type Strain ck-I2-15.";
RL   J. Bacteriol. 194:6973-6973(2012).
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:EKF54731.1}.
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DR   EMBL; AMSG01000016; EKF54731.1; -; Genomic_DNA.
DR   RefSeq; WP_008992061.1; NZ_AMSG01000016.1.
DR   AlphaFoldDB; K2Q1M5; -.
DR   STRING; 555500.I215_11105; -.
DR   PATRIC; fig|555500.3.peg.2290; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000007364; 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:UP000007364};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          5..266
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          349..530
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          699..906
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   942 AA;  106260 MW;  06EDE978E6896D36 CRC64;
     MSEKKKLFLL DAYALIFRGY YAFIKNPRIN SKGMDTSAVL GFMNSLLDVI KREQPHHLAV
     AFDKDGSKDR LEMFESYKAN RDETPEAIKI AVPIIQQILQ AMHIPCIVKP GYEADDIIGT
     LAKQAEKANY QVYMVTPDKD FAQLVSENIF MYRPARMGNG IEIWGIPEVQ KKFEVERPEQ
     VIDFLGMMGD AVDNIPGLPG VGEKTAKKFL KEFGSMENLL ANTSQLKGKM KEKVEANAEL
     GLLSKDLARI MLDVPVEFNE KDFELNTPDL PKVQEIFQEL EFRRLADNLM KTFSPQTTAP
     NDPSPTKATT VSKAVDQQLD LFSDPVSSQA SGGSMESGFK TIDQTTHLYQ HVDSDMSRKL
     LLEMLLKQKR VCFDTETTSL KSLEAQLVGC AFSWETGSGY YMSFPEDQQQ TKQLLEPFKA
     FFENPNITKV GQNLKYDIKV LSNYDIKVEG PIFDTMIAHY LINPDMRHQL DILAETYLNY
     KPIPIEDLIG KKGKNQGTMR STPPELQTKY AVEDADITLQ LAAIFETQLK QNNTGRVFSE
     IESPLVKVLS AMEIEGIGLD TAFLNSLTKD LNNDLLQLEQ DIYSQAGEEF NIASPKQLGP
     ILFDKLKLAD KPKKTKTGQY STAEDVLSYL AKENKIVSDI LQWRQLNKLK STYIEALPTV
     VNPKTGRVHT VYSQAVAATG RLSSNNPNLQ NIPIRTERGR QVRKAFVPRS EEYLLLAADY
     SQIELRIIAA LSDEDTMINA FKNGEDIHAS TAAKVFKVDL DKVTREQRSN AKTVNFGIIY
     GVSAFGLSNQ TNLNRSEAKE LIDTYYETYP KLKAYMSKQV HFAQDNGYVE TILGRRRYLK
     DINSRNQVVR GAAERNAVNA PIQGSAADII KIAMIRIQEK LKAGNYKTKM LLQVHDELVF
     DAHKEEINEV TQLIKTEMEN AFQLKVPLDV EIGVGENWLE AH
//

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