ID A0A1W1VL03_DESTI Unreviewed; 1241 AA.
AC A0A1W1VL03;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN00017405_0141 {ECO:0000313|EMBL:SMB94052.1};
OS Desulfonispora thiosulfatigenes DSM 11270.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfonispora.
OX NCBI_TaxID=656914 {ECO:0000313|EMBL:SMB94052.1, ECO:0000313|Proteomes:UP000192731};
RN [1] {ECO:0000313|EMBL:SMB94052.1, ECO:0000313|Proteomes:UP000192731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11270 {ECO:0000313|EMBL:SMB94052.1,
RC ECO:0000313|Proteomes:UP000192731};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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. {ECO:0000256|HAMAP-
CC 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|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; FWWT01000022; SMB94052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1VL03; -.
DR STRING; 656914.SAMN00017405_0141; -.
DR Proteomes; UP000192731; 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; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.150.700; PolC, middle finger domain; 2.
DR HAMAP; MF_00356; DNApol_PolC; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR006308; Pol_III_a_PolC-type_gram_pos.
DR InterPro; IPR044923; PolC_middle_finger_sf.
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; PF07733; DNA_pol3_alpha; 2.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {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:UP000192731};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 335..402
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1241 AA; 140067 MW; A0B8AAEF186C98ED CRC64;
MVMHVCSFPQ EFYKVPKIPE EVQTFLANMK ICKVSVSQVK STWEITFLCS KIPNIYILNE
CKKCLRYIFP GVMNFILSPK LEKNLSAREF IISNWDSLLE ILGDKFPSTK GWLGTSNYDL
KAENTIDIRF NSLLAIKYLQ KNGCKVYLEN FLANLIEEKF TINFKYDPSL KNEQSETQNI
DELVAKSVEV NHIEIKPNIS TRQGKINNTT KPTSKAVIMG KEIRQLERNI QEVTEEEPNI
VIAGRPFAIE VKELKTGRAI LSFSVTDLSD SLTCKVIQDG KLIAEIQEKL ANSKKVKVKG
TAQIDRYSQE LVIMARDINT LKLDEREDLA SEKRIELHLH TKFSSMDGIS SAKDLIKQAA
KWGHEAIAIT DHGVVQAFPE AHDVGKANNI KVIYGMEGYI FDDINPNNAN NQKKQNYHCI
ILVKTMEGLK NLYKLVTESH LNYFKRVPRI PKSLLNEMRT GLIIGSACEA GELIQSYLKD
DDPERLINIA QFYDFIEIQP RGNNYFLLRN GQLEDKEQLT KLNTDLYNLG KKLDIPVVAT
GDVHFLHPED ETFRKIIMTG KGFSDADDQP PLYLKTTEEM LAEFSYLGET ESKEVVIDNP
KNISDQIEEI IPIPDEFYPP EIEGAEDDIY EMVYKKAHEW YGEELPSIVE ARIKKEATAI
IDNGFAVLYL TAHKLVKKSN EDGYLVGSRG SVGSSFVATL CGITEVNPLE PHYRCPECKY
TEFITDGSVD SGADLPENKC PKCSSDFIKD GHNIPFEVFM GFKGDKVPDI DLNFSGEYQA
RAQKYTEELF GKDNVFRAGT ISTIASRTAF GFVKNYLDDK NIVSRTAEIG RLVDGCTGIK
RTTGQHPGGL MVIPKSVDVH MFTPLQRPAD DVKSDIITTH FDYHSISSRL VKLDNLGHDD
PTVIKILEDL TGVNAKTISL SEPKTMSLFC STKALGITEE ELGSPVGTYG IPEFGTKFVR
QMLVDTKPTT FSELVRISGF SHGTDVWINN AQDLIKSGTA QLSEAISARD DIMIYLIQRG
VESSTAFKIM EDVRKGRGVS PEFEQVLLEN NIPKWYIESC KRIKYMFPKA HAVAYVMMAF
RIAYFKVYYP LAFYTAFFTV RADEFDAELI CKGVNSIRNE IKNLTDKGHS VSQKESKLLT
IMEIALEMYL RGFDFQIVSL KKSDSKNFQI EGNTIIPPFA GLQGVGVQAS LNIANARAEK
YFTSIEDLRI RAKLSKTVID NLREHGCLNE LPETDQLSLF S
//
