ID A0A1G7MSR9_CHIFI Unreviewed; 1214 AA.
AC A0A1G7MSR9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=SAMN04488121_102530 {ECO:0000313|EMBL:SDF64169.1};
OS Chitinophaga filiformis (Myxococcus filiformis) (Flexibacter filiformis).
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=104663 {ECO:0000313|EMBL:SDF64169.1, ECO:0000313|Proteomes:UP000199045};
RN [1] {ECO:0000313|EMBL:SDF64169.1, ECO:0000313|Proteomes:UP000199045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 527 {ECO:0000313|EMBL:SDF64169.1,
RC ECO:0000313|Proteomes:UP000199045};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNBN01000002; SDF64169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7MSR9; -.
DR STRING; 104663.SAMN04488121_102530; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000199045; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..83
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1214 AA; 137962 MW; 424E4BC956720616 CRC64;
MIFSHLHVHT QYSLLDGAAD IKSLYKKAMA SNQPALAITD HGNMFGVFQF VAEAYNNKLN
PEDPKDKRLK VKPIVGCEFY VVENRFKRAF TREEKDIRNH QVLLAKNDEG YRNLIKLCSL
GYMEGLYGKY PRIDKELILQ YHKGLIATTC CLGASVPRAI LKKGEEAGEE EFKWWLDIFG
EDYYVELQRH GIPEQEKVNE SLIKFAAKHN VKIIASNDSH YVDQADANAH DILLCINTGE
KKSTPTMKDF SDDDVSMKNK RFAFYNDQFY FKTTEEMSTL FHDLPQAIDN TNEIVDKVEL
LDLKRDILLP NFPIPAPFIT QDQYLRHLTM EGARQKYAEV TAEVEERLNF ELQVIENMGF
AGYFLIVSDF IKAGRDLGVF IGPGRGSAAG SAVAYCIGIT NIDPIKYNLL FERFLNPERK
SMPDIDTDFD DEGRQKVIDY VVQKYGKNQV AQIITYGTMA AKMSIKDVAR VMDLPLAESN
MLAKMVPDKP GIQLDRIFNA PIDEGEKSLA EKEGLGPEDL ENVRRLRELI KGQDLQGEVL
REACVLEGSV RNTGIHAAGI IIAPKDLYDL IPVSTAKDSD LLVTQFEGSI IESAGVIKMD
FLGLKTLTII KGALELIKAN HGIDISIDDI PLDDAKTYEL YQKGETNATF QFESAGMQKY
LRELKPDRFD DLIAMNALYR PGPLEYIPLF IRRKHGLEET VYDLPEMEEY LNDTYGITVY
QEQVMLLSQK LANFSKGDAD VLRKAMGKKQ KAVLDKMKKQ FMEGCAANGH DLKVCDKVWT
DWEAFASYAF NKSHSTCYAF VAYQTAYLKA HYPAEYMAAV LNNASNIEKI TFFMEEAKRM
GIDVLPPDVN ESFKGFAVNK QGQIRFGLAG LKGVGEAAVE NILEERRKEG AYKNIFEMIR
RVNQRAVNKK SLEALAMSGA FDCFPELHRA QYFHKPENDT TTGLDKIVKF GQQVSAGVAT
AMGSLFGEES MPDIEPPKIP PCDPWPLILK LNNEREVTGI YISGHPLDDY RFESRYYNMN
TVQELVEYQA DLTTPGNARA GRERNFRLAV YVTGAQERIS RNNRQFGIMT IEDYSGKFEF
ALWSEDFIRF APYLKTGLCL FINGGFKAKR FNDAEYEFKV NGIQLLQEVK KTHTKKVTLV
TMPKFITREL VDFLVDNIAK YPGASELFLQ LIDRDDQMTV KLHTFNKHIE MNDELAHFLS
KQPDVDVYID TINK
//
