UniProt: A0A1M5QWC9

Database: UniProt
Entry: A0A1M5QWC9_9CLOT

LinkDB:  A0A1M5QWC9_9CLOT 
Original site:  A0A1M5QWC9_9CLOT

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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 (24)   
   InterPro (15)   
   Pfam (7)   
   SMART (2)   
All databases (32)   

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ID   A0A1M5QWC9_9CLOT        Unreviewed;      1451 AA.
AC   A0A1M5QWC9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=SAMN02745207_00336 {ECO:0000313|EMBL:SHH18435.1};
OS   Clostridium grantii DSM 8605.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121316 {ECO:0000313|EMBL:SHH18435.1, ECO:0000313|Proteomes:UP000184447};
RN   [1] {ECO:0000313|EMBL:SHH18435.1, ECO:0000313|Proteomes:UP000184447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8605 {ECO:0000313|EMBL:SHH18435.1,
RC   ECO:0000313|Proteomes:UP000184447};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQXM01000002; SHH18435.1; -; Genomic_DNA.
DR   RefSeq; WP_073336323.1; NZ_FQXM01000002.1.
DR   STRING; 1121316.SAMN02745207_00336; -.
DR   OrthoDB; 9804290at2; -.
DR   Proteomes; UP000184447; 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; 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; 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; 2.
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; 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; 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; 1.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000184447};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00356}.
FT   DOMAIN          353..420
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   DOMAIN          437..602
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
FT   REGION          193..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1451 AA;  163641 MW;  B4235B71A93B1EC5 CRC64;
     MNQNFVNSLL EDFNKNEILM NDKLRIEKVQ FLSKSCKMKV YIKSHNSLNG EKISVLKSII
     ASKLNGFENI ELIIAKDISN VDISEIVNKY WVDIVAKISE ETPLCKECLI AAEKKLDNNV
     LSLHLGEEFI YTFLKGKKIN NHIENSILEM FGAKIKVNIS YNNSIQTMGA DFFKERENKE
     REIITNIIKN KGTNESKSSD KKDSQKTFQK DFKGKSKDKQ FYNKEGKSSE NNPNVIVGRD
     FNGDTIEIST ITQTSGVVAI CGDIIKSEII ETKSGRKIFV FDVTDYTSSM TIKCFPRPKD
     TEKMEEEIKK GIRVKLRGEA TFDTFSREVV IMGRDIIKTT KIEKMDIYEE KRVELHLHTQ
     MSSMDAIAPA SKLIERAAKW GHKAIGITDH GVVQAFPEAM DAAKKYNIKV LYGVEAYFVD
     DGEPIAINCD EKTIKDSFTV FDIETTGFSS AYDKIIEIGA VKIINGEIVD RFSYFVNPET
     NIPFKIIELT GINNEMVKNS ETIEKILPKF VEFAKGTVLV AHNASFDVSF IRKNMSDLNM
     KFDFPVLDTI PLSKFLYPEL KRYKLNTVCK YLGISLENHH RAVDDAEATA LIVQESFKRL
     KEKAIVTIEE LNKEYLATID IKKMNTYHLI IYAKTQAGLK NLYKLISTSN LDYFFKRPRL
     SKSIINQYRD GLIIGSACEA GQVFSSVLQG KSSEEMQEIV KFYDFLEIQP TGNNEFMIKK
     GIVKNEDQLK ELNIKVVELG EKFNLPVVAT GDVHFLDEKD SIFREILMAG KGFSDAKDQP
     PLYFKTTNEM IKEFEYLGEE KAKEVVIYNT NMIANQIEDI LPIPKETFPP KIEGADDDIR
     NMTMQKAKSI YGDPLPDIVQ KRLDKELNSI ISNGYAVLYL IAHKLVAKSL EDGYLVGSRG
     SVGSSLVATM TDITEVNGLP AHYVCEKCKY SQFITDGSVS SGVDLPDKDC PNCGENLYKE
     GFDIPFETFL GFEGDKEPDI DLNFSGDNQA DIHRYTEVLF GKGHTFKAGT IGTIAEKTAY
     GFVKKYLDEN NSKVTTAEIN RLTAGCTGVK RTSGQHPGGI MVVPADNEIY NFCPIQHPAD
     DPNSDIITTH FDYHSISGRL LKLDILGHDD PTMLRMLKDI TGIDPTTVPI GDEKVLSLFT
     GTDALGITPE ELGCPVATYG LPEFGTKFVR GMLLDTMPQT FSDLVRISGL SHGTDVWLNN
     AQYFIKEGLT TLKDCISTRD DIMVYLIYKG LPPQDAFTIM EKVRKGKGLG EKDEELMRQN
     SVPDWYIESC KRIKYMFPKG HAVAYVMMAM RIAYYKVYYP EAYYSAFFTV RGLDDFDAEL
     ICKGEDAINL KINEINEMGN NISQKEKGLL TVLELSYEMY KRKINLLRVD LYKSEATRFV
     IEEKGIRPPL SALAGVGVNA AKAMVEARIH GEFISKEDLR LRTKVTKSVI ETLSIHGCIN
     GLPDTNQLCL F
//

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