ID A0A2U0H3N7_9MICO Unreviewed; 1172 AA.
AC A0A2U0H3N7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=DEA06_12965 {ECO:0000313|EMBL:PVW03429.1};
OS Microbacterium sp. Gd 4-13.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=2173179 {ECO:0000313|EMBL:PVW03429.1, ECO:0000313|Proteomes:UP000245623};
RN [1] {ECO:0000313|EMBL:PVW03429.1, ECO:0000313|Proteomes:UP000245623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gd 4-13 {ECO:0000313|EMBL:PVW03429.1,
RC ECO:0000313|Proteomes:UP000245623};
RA Spirina E.V., Kuleshov K.V., Rivkina E.M.;
RT "Genome sequencing and assembly of Microbacterium sp. Gd 4-13.";
RL Submitted (APR-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}.
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:PVW03429.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QEIJ01000007; PVW03429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U0H3N7; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000245623; 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:UP000245623};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1172 AA; 129331 MW; E69AF16FC452C3D9 CRC64;
MAADSFVHLH VHSEYSMLDG AARIGPMVQE AARLDMPAIA VTDHGNTFAA YEFYKTAKDA
GIKPIIGIEA YVTPGTHRSD KARVRWGSPE QQSDDVSGSG AYTHMTLLSE TTQGMHNLFR
LSSKASMEGY YFKPRMDREL LQTYSKGLIA TTGCPSGEVQ TRLRLGQYDA AKAAAAEFQD
IFGRDNYFVE LMDHGLSIER RVMGDLLKIA KELSIPLVGT NDLHYTHQHD ATSHAALLCV
QSGSTLDDPK RFKFDGDGYY VKTAAEMRQV FRDHPEACDN TLLIAERCDV EFDTSANYMP
RFPVPAGETE ESWFVKEVEK GLEYRYPEGI SDEVRKQAEY ETGVIVQMGF PGYFLVVADF
INWAKENGIR VGPGRGSGAG SMAAYAMRIT DLDPLQHGLI FERFLNPDRV SMPDFDVDFD
DRRRGEVIQY VTEKYGSERV AQIVTYGTIK AKQALKDAGR VLGFPFSMGE RLTKAMPPAV
MGKDMPLGGM FDKNHPRYKE ASEFRTVIET DAEAKTVFDT AVGLENLKRQ WGVHAAGVIM
SSEPLIDIIP IMRREQDGQI VTQFDYPACE SLGLIKMDFL GLRNLTIIND ALDNIEANRG
HPLVLEDLPL DDRGAYDLLT RGDSLGVFQL DGGPLRSLMR LMRPDNFEDI SALIALYRPG
PMGANSHINY ALRKTGQQEI TPIHPELEEA LSDILDTSYG LIIYQEQVMA IAQRVAGFTL
GEADILRRAM GKKKKSELDK QYAGFEGGMK KNGFSEAAVK TLWDILLPFS DYAFNKAHSA
AYGMISYWTA YLKAHYPAEY MAALLTSVGD SKDKMAVYLN ECRRMGIKVL PPDVGQSIRY
FAAVGEDIRF GLGAVRNVGA NVVDGIVAAR ADGPFTSFHD YLARVPGPAA NKRTVESLIK
AGAFDSMGAT RRALHEIHED AAEAAVDVKR KEATGAIGFD FDSLYDEAEE AVPAKVPDRP
EWTKKDKLAF EREMLGLYVS DHPLAGLEVP LAKHASTSIH DLLASESIED GDQVTVAGLV
TSVQHRVAKA SGNPYGMITV EDFDGEVTVM FMGKTYQEFS PVLQQDSILV VRGRVSRRDD
GLNLHAQSAL SPDLGAVDAS GPLVLLMPEQ RATEVLVKDL AEVLERHRGE TEVSLRLHRG
GTAKVFEVPM PVRVTADLYG ELKGLLGPNC LG
//
