UniProt: W6TKI2

Database: UniProt
Entry: W6TKI2_9SPHI

LinkDB:  W6TKI2_9SPHI 
Original site:  W6TKI2_9SPHI

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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   W6TKI2_9SPHI            Unreviewed;       937 AA.
AC   W6TKI2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=N824_11845 {ECO:0000313|EMBL:ETZ19428.1};
OS   Pedobacter sp. V48.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=509635 {ECO:0000313|EMBL:ETZ19428.1, ECO:0000313|Proteomes:UP000019145};
RN   [1] {ECO:0000313|EMBL:ETZ19428.1, ECO:0000313|Proteomes:UP000019145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V48 {ECO:0000313|EMBL:ETZ19428.1,
RC   ECO:0000313|Proteomes:UP000019145};
RX   PubMed=24578271;
RA   Bitzer A.S., Garbeva P., Silby M.W.;
RT   "Draft Genome Sequence of Pedobacter sp. Strain V48, Isolated from a
RT   Coastal Sand Dune in the Netherlands.";
RL   Genome Announc. 2:e00094-e00014(2014).
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:ETZ19428.1}.
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DR   EMBL; AWRU01000034; ETZ19428.1; -; Genomic_DNA.
DR   RefSeq; WP_048908215.1; NZ_AWRU01000034.1.
DR   AlphaFoldDB; W6TKI2; -.
DR   STRING; 509635.N824_11845; -.
DR   PATRIC; fig|509635.5.peg.5821; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000019145; 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   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          344..525
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          694..901
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   937 AA;  104889 MW;  355E14DD8C97D9B7 CRC64;
     MKKLFLLDGM ALIYRAHFAL SKNPRFTSTG VNTSAVMGFT NTLLEVLKKE KPTHIAVVFD
     TEAPTERHTD FEAYKAHREA MPEDLSAALP YIFKLIEGFN IPVITKDGFE ADDIIGTLAK
     EAEKAGFQVY CMTPDKDFAQ LVSENIFIYK PARMGNEMEI LGVKEVLAKW EIENVEQVID
     ILGLWGDAVD NIPGIPGIGE KTAKLLIKQY GSVENIIANS HELKGKQREN VETYAEQGMI
     SKKLATIILD VPVPFDEKAL ELEEPSRELL EPLFAELEFR TIGKRVFGDG FNVTEGKTGG
     SQQIDLFGNV VDQVEIKTKT TIVISEVFEQ GVAAKTIENT EHNYKLIDTP ELRKELVDLL
     LKQESISFDT ETTGTDANLA DLVGISFSIT PGEGYYIPVP AERADAQVIV EEFRPVLESE
     NIAKIGQNIK YDMLVFKWYG VSVKGKLFDT MLAHYLIDPD TRHNMDVLAE NYLSYSPISI
     TKLIGAKGKG QGNMRDVPVE QVVDYAAEDA DITLQLANVF KPMLKQLNAE QLATDVENPL
     IYVLADIEKE GVRIDMDTLI NYSKELELDI RKFEQNVYDK CGIKFNLASP KQLGEVLFDK
     LQLDPKAKKT KTGQYQTGED VLLALAHKSD IVQDILDFRQ LQKLKSTYVD ALPLLVNPRT
     GRVHTSYNQA VAATGRLSSN NPNLQNIPIR TERGREVRKA FIARDADHVL LSADYSQIEL
     RIIAEISKEE NMLDAFSKGI DIHTATAAKV YGISIEEVDS TQRRNAKAVN FGIIYGQSAF
     GLSQNLGIPR KEAAAIIDQY FEQYPGIKKY MSDTMNFARE NGFVETILGR RRYLRDINSA
     NQTVRGFAER NAINAPIQGS AADLIKVAMI NIHKDIQDQN LQSKMTMQVH DELVFDVLRS
     EVEAMKKIIS HRMKTAIKTS VPIEVEIGEG DNWLAAH
//

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