ID A0A1H9HVA1_9LACT Unreviewed; 1112 AA.
AC A0A1H9HVA1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN05421767_10372 {ECO:0000313|EMBL:SEQ66152.1};
OS Granulicatella balaenopterae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Granulicatella.
OX NCBI_TaxID=137733 {ECO:0000313|EMBL:SEQ66152.1, ECO:0000313|Proteomes:UP000198556};
RN [1] {ECO:0000313|EMBL:SEQ66152.1, ECO:0000313|Proteomes:UP000198556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15827 {ECO:0000313|EMBL:SEQ66152.1,
RC ECO:0000313|Proteomes:UP000198556};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOGF01000003; SEQ66152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9HVA1; -.
DR STRING; 137733.SAMN05421767_10372; -.
DR Proteomes; UP000198556; 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; cd07431; PHP_PolIIIA; 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
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; SSF50249; Nucleic acid-binding proteins; 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:UP000198556};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1112 AA; 126733 MW; F024CCE45544E373 CRC64;
MNFVTLQVAS AYSLLKSTIA IDEYVKLGKK LGYDALALSD QGMMHGALEF YQTCQRHQIR
PIIGCEFAIP GVLHQEFLQP IMVYAKNKAG YHSLIKLSTI YQEKGCHAEF IEEINQQNSN
LKVLLAYKDS EWLRYIDQPE LLVQYFATIR EMFPTIELAL GIGIQQVDSK AYQVVAPIAK
QLAITPIAHQ VTFYLYTEDD FSWRVLEAID QGQQLQNYAS EITGPYYLHE THAMKRMFVE
RKAKELITNH LAFIEDLAVE IDMDKHLLPK YQVPNDAPSN SYLKEVCQKG LLQRGVANNS
VYQERLNYEL TVIEDMGFSD YFLIVWDIMA YAHKADIQTG PGRGSAAGSL VAYALDITQV
DPIEHGLIFE RFLNRERFTM PDIDLDFPDN KRELVLQYVL EKYGKAHVAQ IATFGTLAAK
QALRDVGRVM GLSVTEMAQW SKAVPNQLKI KLTTAYQQSR ALREIVERSP RNQLIYQTAL
KIEGLPRHMS THAAGVVISD RPLVDHIPLV YREGELPITQ YTMNDVEKIG LLKMDFLGLK
NLTILYDALQ FVKKINHEAI DIYQINPQDE KTLKLFGEAY TNGIFQFESD GIKQVLRRLK
PSSLEDIAAV NALYRPGPME QIDTFIKRKN HKETIRYINS DLAPILESTY GIMVYQEQVL
QVACKFAGFS LGEADILRRA IGKKKLAVIE QEKVHFIEGA KNLGYEEQTA IEVYRYIERF
ANYGFNKSHA YAYSLLAYQL AYLKANYPSA FFAALLKSMN ASSKKAQDYL TEAKRAGVRV
LPPSIQTSVM DFTVSDTGII TGLGAIKGLR KDVMMYIIQN RANYGEYRGF MDFCFRLGKK
YCREEVISAL VYVGALDSFG ETRASLIATI PGVVESVNLH GDNLVLDVND ELFPKMEVKP
EISLLEKLDK EIEFLGYPIS AHPTEEYQEA YDAGIVQTIN DIFEAKIVSV LGVITSVKRI
RTKKGEPMAF ATLQDATGTI DLVLFQRDYP KYYQLLEEKA LVQITGKVSK NRMNDWQIQI
QKVHPIEIIA EMLKESKKKC YLKIDENHYN QQTMDKISRI VQQHSGFTPV FIYLNREKKV
VKPNFIRGIK ISNNSTYELE KIVGQENVRI VE
//
