ID A0A0Q8DYX4_9ACTN Unreviewed; 1190 AA.
AC A0A0Q8DYX4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=ASD81_01065 {ECO:0000313|EMBL:KRA37357.1};
OS Nocardioides sp. Root614.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736571 {ECO:0000313|EMBL:KRA37357.1, ECO:0000313|Proteomes:UP000051699};
RN [1] {ECO:0000313|EMBL:KRA37357.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA37357.1,
RC ECO:0000313|Proteomes:UP000051699};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA37357.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA37357.1,
RC ECO:0000313|Proteomes:UP000051699};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KRA37357.1}.
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DR EMBL; LMGV01000001; KRA37357.1; -; Genomic_DNA.
DR RefSeq; WP_056705979.1; NZ_LMGV01000001.1.
DR AlphaFoldDB; A0A0Q8DYX4; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000051699; 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; IPR048472; DNA_pol_IIIA_C.
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; PF20914; DNA_pol_IIIA_C; 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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000051699};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..78
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1190 AA; 131507 MW; 7CA0D5647F52ED16 CRC64;
MAVGSGGSDF VHLHVHTEYS MLDGASLLDG LFTRVNDLGM TSIAMTDHGN LHGAYDFYNK
AKKYGVKPII GIEAYLTPQT HRTERRRVRW GKGNGGEGGE EGGNDVAGGG AYTHMTMWAE
TTEGMHNLFR LSSRSSLEGF YYKPRADREL LNEYGKGLIA TTGCPSGEIQ TRLRLGQYDE
AVRSASEFQD IFGKDSFFLE LMDHGIDIEK RVRDDLLRLG KQLNIPAIAT NDSHYNNPED
AEAHDALICV SSGKRLADPN RLKFDGGGYY IKSAAEMREL WSDRFGMPEA CDNTLLVAER
CNVEFTESTG GYMAAADIPA GETEESWFAK EVWRGIEARY PGDKLTQAVR DRVEMELGVV
ASKGYCGYYL VVADFIQWSK DNGIRVGPGR GSGAGSIAAY ALRITDLCPL EHGLIFERFL
NPERPSMPDF DIDFDERRRV EVIQYVSQKY GSDRVAYIAT FGRIKAKQAV KDAARVLDHG
FAISDKITKA LPPDIMGKGV PLKEIFNGDH KRYSDGGEFR SLYESDAEVR TIYQTGLGLE
GQIRQTGVHA AGVIMSSQPL IDIVPIMKRE QDGAIITQFD YPMCESLGLV KMDFLGLRNL
TVLDDALINI KRNRGEDVVL EDLPFDDQAT YDLLSRGDTL GVFQLDGGPM RALLRSMRPD
KFADISAVGA LYRPGPMGAD SHNKYARRKN GREPIDPIHP ELEAPLETVL GETYGLIVYQ
EQVMEIAQVL AGFSLGQADN LRRAMGKKKK EELDKQYAGF QAGMLGNGYS QKAISTLWEI
LLPFSDYAFN KAHSAAYGVI SYWTAYLKAN YPAEYMAALL TSTRVDKDKS AIYLNECRRM
KIQVLPPDVN ESVSNFTSVG TDIRFGMGAI RNVGEHVVDG VVAAREEKGR FADFNDFLSK
VPAQVCNKRV IDSLIRAGSF DDMKHKRRAL VAIHETAVDQ YVDIKRNEAI GQDSLFAGLG
DDDEDGGFGV SVAIPDLDEW DKMTLLGHER DMLGLYVSDH PLLGLEHVLS NGTDCTIGQL
LTDEDRPHNS TVTVAGLVTS VQRKITKNGD PWATVTLEDL EGAIDVLLFP SSYRLAAPYL
TDDAIIRVRG QLDKERDTAQ LRGQEVTLPD LERGSDGPVV ISLPSTRCTG PVVQSLRDVL
STYPGLTEVR LQLLSRDSTK LMRLGDNLRV TPSPSLFADL KQLLGPGCLS
//
