ID A0A383S4J5_9ACTN Unreviewed; 1189 AA.
AC A0A383S4J5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-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=D7U36_01950 {ECO:0000313|EMBL:RLP12769.1}, PROPAUS_0071
GN {ECO:0000313|EMBL:SYZ32196.1};
OS Propionibacterium australiense.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=119981 {ECO:0000313|EMBL:SYZ32196.1, ECO:0000313|Proteomes:UP000263928};
RN [1] {ECO:0000313|EMBL:SYZ32196.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Propionibacterium_australiense1 {ECO:0000313|EMBL:SYZ32196.1};
RA Ferrada E.E., Latorre B.A.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000263928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hornung B.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RLP12769.1, ECO:0000313|Proteomes:UP000279336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML98A078 {ECO:0000313|EMBL:RLP12769.1,
RC ECO:0000313|Proteomes:UP000279336};
RA Bernier A.-M., Bernard K.;
RT "Propionibacterium australiense Genome Sequencing and Assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; RCIW01000002; RLP12769.1; -; Genomic_DNA.
DR EMBL; UNQJ01000001; SYZ32196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A383S4J5; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000263928; Unassembled WGS sequence.
DR Proteomes; UP000279336; 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 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000313|EMBL:SYZ32196.1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:SYZ32196.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000263928};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SYZ32196.1}.
FT DOMAIN 7..80
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 950..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1189 AA; 131664 MW; E80CC8EBBD44C3FC CRC64;
MSRSNFVHLH VHTEYSMLDG AASNVKLFAE VARQGMPAVA MTDHGNMFGA YEFFQTARKY
DGAENPAIKP IIGIEAYVAP SSRFSRKQEF WGGGRDSDAP EIEGGKDVSG GGRYTHMTMW
ARNPTGLHNL FKLSSLASYE GYYMKPRMDR ELIAEHAEGI IGATGCPSGE VQTRLRLGQF
EAACEAAAAY QEIFGKENYY CELMDHGVPI EHEVRDELLR LARRLKLPLL ATNDSHYVTE
DQADAHDNLL CVGVGRNKDD PNRFRFNGSG YYIKTNEEMR ALFPAEAADN TLRLAEMIEP
YDEVFAHVDR MPQFDVPAGE TQESWLRKKI QAGLKKHYGD NPSQQVLERV ETELATIEPL
GFSSYFLVVS DICDAARRMG VPVGPGRGSA AGSMIAYLTD IIAIDPLEHD LLFERFLNPE
RVNPPDIDLD FDDRQRDKVI EYVTDKYGAE YTSQVNTFST IKAKAAVKDA NRILGYPFSL
GDRITKAMPP DIMGKGVPLN DLFDPEHPRY AEGGEFRELY EADPDVHRVV DTGKGLEGLI
RGTGVHACAF ILSNEKLLDL VPMHKRDKDG MIIAGFAYPQ LEEMGLMKMD FLGLRNLGIM
DHCLKIIKQN RGEDVDLTSV PLDDKATYEL LSRGDTLGVF QLDGTAMRAL LRQMGPNVFD
DIIAVLALYR PGPMGANAHI EYADRKNGRR PIIPIHPELK EDLDEILAPT YHLIVYQEQI
MAIARKLAGY TLGGADLLRR AMGKKKKSIL DQNFTPFQAG MRANGYSDAS IQALWDVMVP
FAGYAFNKSH ATGYALVSYW TAYLKANYPA EYGAALLTSV GDDKDKMALY LADMRAQHIK
VLPPDVNASQ NEFTAVGEDI RFGLGAIRNV GESVVTGIAE SREEHGPAKD FYEFLDQVPL
SVCNKRCIES LIKAGSFDSM GHSRRALMDV FESAVDDVID LKRNQANGQD DLFGDLMGGD
EDSSGTGLRR TVPELPDWDK RTKLGFEREM LGLYVSDHPL QGLEHVLSAE SSIGVGALIE
SGPELDGRVE TICGMITQVQ RRQSKSGAFW ATVTVEDLDA SIQVLVFPKV YQTCLTQLVP
DTVVRITGRV ANKDESIEMQ ANELTVPDVR MSSDGPVTIQ LAATRCIPPV VQELRRVLTA
HPGGTEVRIK VLGSRRSTLM RLGDSLRVSN EQPLIADLKA LLGPSCIAV
//
