UniProt: A0A1N6UPD5

Database: UniProt
Entry: A0A1N6UPD5_9BACI

LinkDB:  A0A1N6UPD5_9BACI 
Original site:  A0A1N6UPD5_9BACI

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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 (26)   
   InterPro (16)   
   Pfam (8)   
   SMART (2)   
All databases (34)   

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ID   A0A1N6UPD5_9BACI        Unreviewed;      1437 AA.
AC   A0A1N6UPD5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=DNA polymerase III PolC-type {ECO:0000256|HAMAP-Rule:MF_00356};
DE            Short=PolIII {ECO:0000256|HAMAP-Rule:MF_00356};
DE            EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_00356};
GN   Name=polC {ECO:0000256|HAMAP-Rule:MF_00356};
GN   ORFNames=SAMN05443094_103331 {ECO:0000313|EMBL:SIQ67515.1};
OS   Domibacillus enclensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX   NCBI_TaxID=1017273 {ECO:0000313|EMBL:SIQ67515.1, ECO:0000313|Proteomes:UP000186385};
RN   [1] {ECO:0000313|EMBL:SIQ67515.1, ECO:0000313|Proteomes:UP000186385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIO-1016 {ECO:0000313|EMBL:SIQ67515.1,
RC   ECO:0000313|Proteomes:UP000186385};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC       also exhibits 3' to 5' exonuclease activity.
CC       {ECO:0000256|ARBA:ARBA00003452, ECO:0000256|HAMAP-Rule:MF_00356}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00356};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00356}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00356}.
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DR   EMBL; FTLX01000003; SIQ67515.1; -; Genomic_DNA.
DR   RefSeq; WP_045850003.1; NZ_MWSK01000003.1.
DR   STRING; 1017273.SAMN05443094_103331; -.
DR   OrthoDB; 9804290at2; -.
DR   Proteomes; UP000186385; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
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:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd06127; DEDDh; 1.
DR   CDD; cd07435; PHP_PolIIIA_POLC; 1.
DR   CDD; cd04484; polC_OBF; 1.
DR   Gene3D; 1.10.150.870; -; 1.
DR   Gene3D; 3.30.1900.20; -; 2.
DR   Gene3D; 6.10.140.1510; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 1.10.150.700; PolC, middle finger domain; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   HAMAP; MF_00356; DNApol_PolC; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR024754; DNA_PolC-like_N_II.
DR   InterPro; IPR028112; DNA_PolC-type_N_I.
DR   InterPro; IPR004805; DnaE2/DnaE/PolC.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR006054; DnaQ.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR006308; Pol_III_a_PolC-type_gram_pos.
DR   InterPro; IPR044923; PolC_middle_finger_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   NCBIfam; TIGR00573; dnaq; 1.
DR   NCBIfam; TIGR01405; polC_Gram_pos; 1.
DR   PANTHER; PTHR32294:SF5; DNA POLYMERASE III POLC-TYPE; 1.
DR   PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR   Pfam; PF14480; DNA_pol3_a_NI; 1.
DR   Pfam; PF11490; DNA_pol3_a_NII; 1.
DR   Pfam; PF07733; DNA_pol3_alpha; 1.
DR   Pfam; PF17657; DNA_pol3_finger; 1.
DR   Pfam; PF14579; HHH_6; 1.
DR   Pfam; PF02811; PHP; 2.
DR   Pfam; PF00929; RNase_T; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00356};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00356};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|HAMAP-Rule:MF_00356};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_00356};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00356};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00356};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00356};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00356}.
FT   DOMAIN          336..403
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   DOMAIN          421..587
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
SQ   SEQUENCE   1437 AA;  162216 MW;  40BE04ECBEB7D2AE CRC64;
     MKEEGSSGRS RFLILLDQLR LKEDAVVRHF DQTEIKKLTV LKQEKKWHFV FSAPALIPCS
     VIVRFADALT STFSPFASVT FSIEIEDRTC TPDYITDYWS YCVRQLDGIA PPLLAALNNQ
     KPEVSGTKFV IRTQNEMEGM ALKNKYGRRI CDVYESLGFP PLTFDIQLSE KEQNDDYEKF
     LEEKRQEDAE RARQAVIDMQ NRAKDQDTAS EDSGPVTIGY TIKPDAEFKK LEEIMDEERR
     IASEGFIFDA ETKELRSGRT LLTFKITDYT DSLMVKMFSR DKEDAATFNR VKKGMWVRVR
     GSVQNDTFVR DLVMIANDIN EIRSPMREDT AEKKRVELHL HSPMSQMDAV SSVSALVSQA
     KKWGHSAIAI TDHAVAQSFP EAYSAGKKNG VKILYGMEAN LVDDGVPIAY EDADRELATE
     TYVVFDVETT GLSAVYDTII ELAAVKIKDG DIIDRFERFA NPHHPLSATT IELTGITDEM
     VRDAPDVDEA LRDFKEWAGD DILVAHNASF DMGFIQTGYE KYGIGRTASP VIDTLELARL
     LYPDMKNHRL NTLAKKFDVE LTQHHRAIYD AEATGYILLK LLKDAEEKGI KKHNEFNNYM
     GEGGAYKRAR PYHCTILAQN AEGLKNLFKL VSLSHINYFY RVPRIPRSVL QKHRTGLLIG
     SGCNKGEVFE AMMQKGMDEA RRAAEFYDYL EVQPKAVYAP LIDMELVRDE AGMEDIIGNI
     LKVGDEQKKL VVATGNVHYL NEEDKIYRHI LISSMGGANP LNRQTLPDVH FRSTDEMLDA
     FAFLGKEKAH EIVVENTNKI ADMIEDVKPI KDDLYTPKIE GADEEMREMS YGMARRIYGD
     ELPEIVEARL EKELKSIIGH GFAVIYLISH KLVKKSLDDG YLVGSRGSVG SSFVATMTEI
     TEVNPLPPHY VCPECKKSEF FDDGSVGSGF DLPDKDCPDC DIPFRKDGHD IPFETFLGFK
     GDKVPDIDLN FSGEYQPRAH NYTKELFGEE YVFRAGTIGT VAEKTAYGYV KKYAEEYTKQ
     YRSAEVDRLV SGCTGVKRTT GQHPGGIIVV PDYMDIFDFS PIQYPADSDK SEWKTTHFDF
     HSIHDNLLKL DILGHDDPTV IRMLQDLSGI DPKTIPTDDP EVMKIFSGTE SLGVTQEQIM
     CKTGTLGIPE FGTRFVRQML EETKPTTFSE LVQISGLSHG TDVWLGNAQE LIQKGICQLS
     DVIGCRDDIM VYLIYQGLDP AFAFKIMESV RKGKGLSDEM EDEMRKNEVP EWYIDSCKKI
     KYMFPKAHAA AYVLMAVRIA YFKVHLPLLY YAAYFTVRAE DFDIDVMSKG SSAIKALLQE
     INAKGLDASP KEKNLMTVLE LALEMVERGF TFKKVDLYRS SADEFVIDGD SLIPPFNALP
     GLGTNAAKNI VASRANGEFL SKEDLQQRGK VSKTIMEYLD KMGCLNELPD QNQLSLF
//

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