UniProt: A0A0E4HBA6

Database: UniProt
Entry: A0A0E4HBA6_9BACL

LinkDB:  A0A0E4HBA6_9BACL 
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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (26)   
   InterPro (16)   
   Pfam (8)   
   SMART (2)   
All databases (35)   

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ID   A0A0E4HBA6_9BACL        Unreviewed;      1441 AA.
AC   A0A0E4HBA6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
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   ECO:0000313|EMBL:CQR56437.1};
GN   ORFNames=PRIO_4034 {ECO:0000313|EMBL:CQR56437.1};
OS   Paenibacillus riograndensis SBR5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus;
OC   Paenibacillus sonchi group.
OX   NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR56437.1, ECO:0000313|Proteomes:UP000033163};
RN   [1] {ECO:0000313|Proteomes:UP000033163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wibberg D.;
RL   Submitted (MAR-2015) 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; LN831776; CQR56437.1; -; Genomic_DNA.
DR   RefSeq; WP_046504301.1; NZ_LN831776.1.
DR   STRING; 483937.AMQ84_25010; -.
DR   KEGG; pri:PRIO_4034; -.
DR   PATRIC; fig|1073571.4.peg.4315; -.
DR   HOGENOM; CLU_003297_0_0_9; -.
DR   Proteomes; UP000033163; Chromosome I.
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; 2.
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; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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          338..405
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   DOMAIN          423..589
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
FT   COILED          171..198
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1441 AA;  162292 MW;  9A7FBF29C7E3A171 CRC64;
     MEQNEERRKR FELLMKQGEI PPAIIDPYFL DGHIERVEIS RGNHDWHIVI VKESLVPAQT
     YRTFVLRMRE KLQHIAKVSF LFLYDEKISR AELVQEYWGL FLEWVQREIP SVNGWLTRST
     QELQDGTLVL SLNDSMSLEL ARKKGIEGAI VKFYDKFFGL SLKVKLQITE NESKADAYEE
     FQQKLQQEQR ELVEMMMMAS EPDEPEDEGD PNEVIKLQVG YEIKEQAVPI IEIQDEEKKI
     TIQGTIFGLE SKELRNGNTL FTFCITDFTD SLQIKMFAKT KEDLKIMGQL ANGKWVRARG
     KVEYDRFMQI PELVMIPSDL CEVQAPPARK DLAPVKRVEF HLHTTMSTMD AVTPIDAYVK
     TAAKWGHPAI AVSDHGVVQS FPDADHAAHK HKIKMLYGVE ANVVNDSVNI VENPQPLDLK
     KATYVVFDIE TTGLSITRNN ITELAAVKMC EGKELDRYTT FVNPHEKIPY HIQQLTNITD
     EMVKDAPDLE PVLEEFVEFV GDSVLVAHNA RFDMGFIQAS LTKLGKPVLP NPSLDTLELA
     RLLFPSMKNH RLNTLADKYK VLLESHHRAV DDTVALGGIL NGLLADAEKL KNITRLERLN
     DYVGNDLSNV RPFHCGIYAL NPAGKKNLYK LISMSHTEYY KRVPCIPKSK LEEHRDGLLV
     ISGCERGEFF EAVLNKTTEE AMEVAQFYDV LEIQPLTMYM HLVDKGFVAS PEDLRDVVRK
     ICEIGEQMNK PVIATGNVHY LEPRDKLFRD ITIHGITGFS PLKDQRKPDA HFRTTDEMLA
     EFEFLGAEKA LEVVVTNTVA LAERFEEYPL FPSELFTPII EGADEEIRNT CYNTAKSIYG
     EELPEVVVAR LEKELAPIIK YGFSANYLIS ERLVKKSNQD GYLVGSRGSV GSSVVATFLG
     ISEVNPLPAH YICVNPECRH SEWFLDGSVP SGFDLPDKDC PNCGGKLRGE GQDIPFETFL
     GFKGDKVPDI DLNFSGEYQP NAHNFTKTMF GPDNVFRAGT IGTVAEKTAF GFTKKYEEHH
     QKRWRGAEVG RLAAGCTGVK RSTGQHPGGI VVLPDYMEIE DITPVQYPAD DVTAEWKTTH
     FDYHAFDANL LKLDILGHDD PTMMRMLQDL TGVDPTTIPM NDPKVMSMFN STEALGVSPE
     QIRTPVATYG VPEMGTKFVR QMLVESKPSS FADLLQISGL SHGTGVWLGN AQELIKNNTC
     NIKTVIGCRD DIMLYLIYKA GMDAGLAFKI TESVRKGKGL SAEWIEEMKK CKVPGWYIDS
     CLKIQYMFPK AHAAAYVISA VRTAYFKLYH PIEYYATYFS VRAADFDIEL CCKGYEAIGR
     QIVEIEQKGF QALPKEKAML PVLEMALEMT ARGFTFKNID LYRSDATKFT VDGTSLIPPF
     SSLAGIGENA AINIAAAKEA GEFLSIEDFQ QKSKASKTVV ELLNGMGCFR GLPESNQLSL
     F
//

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