ID A0A0Q8CET3_9MICO Unreviewed; 1156 AA.
AC A0A0Q8CET3;
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=ASD61_02480 {ECO:0000313|EMBL:KRA12666.1};
OS Leifsonia sp. Root60.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736567 {ECO:0000313|EMBL:KRA12666.1, ECO:0000313|Proteomes:UP000051073};
RN [1] {ECO:0000313|EMBL:KRA12666.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA12666.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA12666.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA12666.1,
RC ECO:0000313|Proteomes:UP000051073};
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:KRA12666.1}.
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DR EMBL; LMGR01000001; KRA12666.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8CET3; -.
DR STRING; 1736567.ASD61_02480; -.
DR Proteomes; UP000051073; 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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000051073};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..58
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1156 AA; 127396 MW; 278A5BC347207F43 CRC64;
MLDGAARVKP LIEAAVEQGM PAVAVTDHGN VFGAFDFWRT ATEAGIKPII GTEAYVTPGT
HRSDRTRVRW GNGGEDDVSG AGAYTHMTLL SATTEGMHNL FRLSSKASME GYYFKPRMDR
EILSEYSSGL IATTGCVSGE VQTRLRLGQY DEAVKAAGDF QDMFGKENYF AEIMDHGLPI
ERRTMNDLLR LAKQLDMPLV ATNDLHYTHA HDATSHAALL CVQSGSTLDD PNRFKFDADE
FYLKSADQMR SLFRDYPEAC DNTLLIAERC NVEFDTNANY MPRFPVPEGE TEDSWFTKEV
DAGLAERYPN GIPDDVRRQA DYEVGVILQM GFPGYFLVVA DFINWSKRNG IRVGPGRGSG
AGSMAAYAMK ITDLDPLRHG LIFERFLNPD RVSMPDFDVD FDDRRRGEVI KYVTEKYGSE
RVAQIVTYGT IKAKQALKDS SRVLGFPFGM GDKLTKAMPP PVMGKDIPLT GIFDKAHPRY
KEASDIRAVV ETDADARTVF DTALGIENLK RQWGVHAAGV IMSSDPLIDI IPIMKREQDG
QIVTQFDYPA AESLGLIKMD FLGLRNLTII SDALDNIEAN RGHRLDLESL ELDDQPSYDL
LARGDTLGVF QLDGGPMRGL LRLMKPDNFE DISAVLALYR PGPMGADSHT NYALRKNGLQ
PITPIHPELA EALEDVLGGT YGLIIYQEQV MSIAQKVAGF SLGQADILRR AMGKKKKSEL
DKQFEGFSAG MTANGYSAAA IKTLWDILLP FSDYAFNKAH SAAYGVVSYW TAYLKAHYPA
EYMAALLTSV GDSKDKMAIY LNECRRMGIR VLPPDVNESI GFFAAAGEDI RFGLGAVRNV
GMNVVDGIRA AREEKGRFES FHDYLRKVPI HATNKRTIES LIKAGAFDSL GNTRRSLVEI
HEQAVESAVK IKRDEDNGNV GFDFDSLFED AGAAPVSHVP DRPEWSKRDK LAFEREMLGL
YVSDHPLAGL EVPLAKHADV AIADLMANEN TQDGETVTIA GLVTSVQHRT AKNSGNQYGM
IQVEDFGGEI TVMFMGKAYQ EFAPALVGDS IVVVRGRVSL RDDGMNLHAY SIFSPDLGQG
DMDGAPVVIS VPESRATTDI MQSLGDVLIR HSGETEVRLK LVKGSTARVF EVPYPVRVTA
DLYGELKSLL GPNCLV
//
