ID A0A1W1XR68_9CLOT Unreviewed; 1444 AA.
AC A0A1W1XR68;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN02745134_02803 {ECO:0000313|EMBL:SMC26377.1};
OS Clostridium acidisoli DSM 12555.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121291 {ECO:0000313|EMBL:SMC26377.1, ECO:0000313|Proteomes:UP000192468};
RN [1] {ECO:0000313|EMBL:SMC26377.1, ECO:0000313|Proteomes:UP000192468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12555 {ECO:0000313|EMBL:SMC26377.1,
RC ECO:0000313|Proteomes:UP000192468};
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.
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; FWXH01000012; SMC26377.1; -; Genomic_DNA.
DR STRING; 1121291.SAMN02745134_02803; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000192468; 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; 2.
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; 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:UP000192468};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 333..402
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 419..584
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1444 AA; 163037 MW; C50B1704C6F1D835 CRC64;
MKRINEIFSD YEANGNINAA IVESVVLRKK SKRLDMEISS DKYIEIREFE SFNRFIRKRF
ALEDSIIAVK YADGTDKKPI EEELKNIVLL VADKYPALKS VLNKSEYKVD ENTINFNFKI
AVSGFLKTMN YDKQLHKAIK NLYGTTYNIN FVDKVSSEEL ILQEEARDKE MLAISKEIKA
AMSNNIPKEV FTKKEEVKAD TDGKKANSSL ILGRNAKIKE PVIKITDLTP DEGRICLQGE
ISNIEAKELK SGKTLVSFDL YDGSSSMTCK SFLKPGDDTE VLPKLKKAKC IRLVGSAGYS
KFSGEVEMIA NTIIETEGVK RAKRQDNAEV KRVELHMHTQ MSQMDAMTSA TDLIKRAMSW
GMKSIAITDH GVVQAFPEAH KLLGRDNPDM KVIYGVEAYL APDKEPSVTN SKGQSIDTTY
CVLDLETTGF SPITEKITEI GIMKYKDGKV IDQFSCFVNP EKPIPSRVVE ITNITDDMVR
KAETIEQVFP KMLEFIRRSV LVAHNARFDV GFLKHNAKKL GYDFDFTYVD TLSLAQAVFP
KYKSYKLGRI AKNLGIKVEV AHRALDDVDT TVKVFKVMLE ELKERGAKTL EEIDFYGSDE
EAKKEEYKKL RTYHAIIFAK DYVGLKNLYK LVSYSHLDYF YKKPRILKSL YKKYSEGLIL
GSACSEGELF QAILLGKSDE EIEAIAKEYD YLEIQPLGND DYLIRLGQVP NGEYLKEINR
KIVALGEKLN KPVVATGDVH FMDPEDEIYR RILEAGQGFK DADNQAPLYL RTTEEMLQEF
SYLGKEKAYE VVVTNTNLIS DMCQQISPIS PEKCPPHIDG CEETIKNIAY EKAHELYGDP
LPEIVQSRLD KELESIIKNG FSVMYIIAQK LVWKSNEDGY LVGSRGSVGS SFVANMTGIT
EVNSLPPHYR CPKCKHSDFG DYGVKNGFDL PDKLCPVCGE NLTKDGIDIP FETFLGFNGD
KEPDIDLNFS GEYQAKAHRY TEVIFGKGTT FKAGTIGTIA EKTAFGYVRK YYEEKNIPVN
KAEITRIALG CTGIKRTTGQ HPGGIIVVPK GREIFEFCPV QHPANDSESD IITTHFDYHS
IDQNLLKLDI LGHDDPTVIR MLQDITGVNP HKIPLDDKET MSLFSSTQAL GVTPQQINSK
VGTFGIPEFG TKFVRGMLLD TMPKTFSDLI CISGLSHGTD VWLGNAKDLI DQGIVTLSEA
VCTRDDIMIY LIKKGLPPNT AFKIMELVRK GKALKDPQKW AEYEALMREH EVPEWYIDSC
RKIKYMFPKA HAAAYVMMAF RIAWFKVHIP KAYYAAYFSI RAKAFDSEFM IFGKEKVKEK
MKEIQTMGNE APPKDKDMYD DLELVLEMYE RGIKFLPIDL YKSHASKFLV EEDGIRPPIN
SISGMGNVAA EGIYNVVQEE KSISSIEDLK KRAKIGNSSI DSLRKFGCLQ GLPESDQLSF
FDAI
//
