ID A0A1Y4T6X8_9FIRM Unreviewed; 1168 AA.
AC A0A1Y4T6X8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=B5E66_09535 {ECO:0000313|EMBL:OUQ36981.1};
OS Faecalibacterium sp. An121.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=1965550 {ECO:0000313|EMBL:OUQ36981.1, ECO:0000313|Proteomes:UP000196164};
RN [1] {ECO:0000313|Proteomes:UP000196164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An121 {ECO:0000313|Proteomes:UP000196164};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria. This DNA
CC polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC is the DNA polymerase. {ECO:0000256|ARBA:ARBA00025611}.
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};
CC -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC and theta chains) that associates with a tau subunit. This core
CC dimerizes to form the POLIII' complex. PolIII' associates with the
CC gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC and with the beta chain to form the complete DNA polymerase III
CC complex. {ECO:0000256|ARBA:ARBA00026073}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000256|ARBA:ARBA00009496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUQ36981.1}.
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DR EMBL; NFLM01000017; OUQ36981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4T6X8; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000196164; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd12113; PHP_PolIIIA_DnaE3; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR NCBIfam; TIGR00594; polc; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 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; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000196164};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..79
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1168 AA; 131363 MW; D9BED2581679DEDC CRC64;
MSETQADGQG FVHLHVHTEY SLLDGACRID QLMDRVKECG QTAIACTDHG VMYGCVQFYK
AAKKAGIKPI IGCEVYVATR TRFDKVNKID GNNHLILLCK NETGYRNLIK MVSAAFTEGF
YSKPRVDKQL LEQYHEGLIC LSACLAGEVP QALLAGDYER AKAAALWYND LFGPGNYYIE
LQDHNLAEDE TVLPQLIRLS RDTGIPMAAT NDAHYLRRED ARVQEILLCI QTGKTIQDAD
RMEFQTDEFY LKTTQEMYDL FAVVPEACAN TVRIAQQCDF DFDFGHTKIP YYKAPDGMDN
QAYFEKLCWE GLERRYGPQV PQANKDRLSY EIGVIRSMGY TNYYLIVFDY INFAKSQNIP
VGPGRGSGAG SIAAYCVGIT DIDPIRYNLI FERFLNPERV SMPDFDVDFC YERRQEVIDY
VNRKYGSDHV AQIVTFGTMA ARNAIRDVGR VMGLPYQSVD TVAKLVPMEL KMTLKRALEV
SGELKKLYDI DPQVRELIDT AAKVEGMPRH ASTHAAGVVI TPEPVDHYLP LATNDGLPVT
QFNMTEIEEL GLLKMDFLGL RTLTVIRDAE TAAQKKDPGF CMSGLDYDDK ATYEMLGRGE
TEGVFQLEST GMRQVLMGLQ PQNLEDVIAL ISLYRPGPMD SIPTYLRNRH QPDKISYKTP
QLAHILDVTN GCIVYQEQVM QIFRELAGFS FGQADNVRRA MSKKKHDVME AEREHFVHGC
TEPGHECPGC VANGISEQVA NEIYDEMSSF ASYAFNKSHA ACYAYVAYQT AYLKCHYPAE
FMAALLTSVL DNTDKVIEYT AECARLGIKV LPPDINRSAG GFTADGEGKI RFGLNAVKNV
GRNLIEGVLK EREKEPFRSL YDFCRRMHGS ELNRRALECL IKAGAFDGMG ATRHSQVEAV
EGILKSVEND ARRNLEGQLD LFSVMVGGDG PAPQEGYEMK ALPEYTHSEL LRMEKEVSGL
YLSGHPLDAY REQSARFSSH SIKMLTGEDA HKLDNTRVKI VCTVVKNRMM TTKNNSMMAF
TSVEDLTGTM EVIVFPRVLD TYRDALQENA VVVIEGKLSV REDEPAKLMA ETVTPIDRYD
PARPDGYRPD PLREAPKRLY LRLPSRKGMV YQKVVNLLEI FDGDMPVVLY LEDEKKKLAA
PRRLYTSGHP LLMQELGRLL GAENVATK
//
