ID L0MIJ1_9GAMM Unreviewed; 1162 AA.
AC L0MIJ1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=D781_3513 {ECO:0000313|EMBL:AGB83723.1};
OS Serratia sp. FGI94.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=671990 {ECO:0000313|EMBL:AGB83723.1, ECO:0000313|Proteomes:UP000011001};
RN [1] {ECO:0000313|EMBL:AGB83723.1, ECO:0000313|Proteomes:UP000011001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI94 {ECO:0000313|EMBL:AGB83723.1,
RC ECO:0000313|Proteomes:UP000011001};
RX PubMed=23516234;
RA Aylward F.O., Tremmel D.M., Starrett G.J., Bruce D.C., Chain P., Chen A.,
RA Davenport K.W., Detter C., Han C.S., Han J., Huntemann M., Ivanova N.N.,
RA Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M., Pagani I., Pati A.,
RA Pitluck S., Teshima H., Deshpande S., Goodwin L., Woyke T., Currie C.R.;
RT "Complete Genome of Serratia sp. Strain FGI 94, a Strain Associated with
RT Leaf-Cutter Ant Fungus Gardens.";
RL Genome Announc. 1:E0023912-E0023912(2013).
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; CP003942; AGB83723.1; -; Genomic_DNA.
DR RefSeq; WP_015673549.1; NC_020064.1.
DR AlphaFoldDB; L0MIJ1; -.
DR KEGG; smaf:D781_3513; -.
DR PATRIC; fig|1249634.3.peg.3369; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_6; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000011001; Chromosome.
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; cd07433; PHP_PolIIIA_DnaE1; 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; IPR048472; DNA_pol_IIIA_C.
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 InterPro; IPR049821; PolIIIA_DnaE1_PHP.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000313|EMBL:AGB83723.1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
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 1162 AA; 130444 MW; 9DA62D239DF8A36F CRC64;
MAEPRFIHLR VHSDYSMIDG LAKTGPLVKR AAALAMPALA ITDFTNLCGL VKFYGTAHGA
GVKPIIGADF HVQSEVLGDE LAELTALAAN NAGYQNLTLL ISRAYQRGYG AAGPIIDRDW
LIEHREGLIL LSGARMGDVG KFMLRGNQAQ VDQCLEFYQQ YFPDSYYLEL IRTGRPDEEN
YLHAAVALAA ERGLPVVATN DVRFLVEDDF DAHEIRVAIH DGFTLDDPKR PRNYSVQQYM
RSEDEMCELF ADIPEALINS VEIAKRCNVT IRLGEYFLPQ FPTGEMTTED FLVAKSREGL
EERLEFLYPD PEERARRRPE YDERLDIELK VINQMGFPGY FLIVMEFIQW SKDNDVPVGP
GRGSGAGSLV AYALKITDLD PLEFDLLFER FLNPERVSMP DFDVDFCMEK RDRVIEHVAD
MYGREAVSQI ITFGTMAAKA VIRDVGRVLG HPYGFVDRIS KLVPPDPGMT LEKAFAAEPQ
LPEIYEADEE VKALIDMARK LEGVTRNAGK HAGGVVIAPT KITDFAPLYC DAEGHHPVTQ
FDKNDVEYAG LVKFDFLGLR TLTIIDWALE MINARRAKSG EPPIDIAAIP LDDKKSFDML
QRSETTAVFQ LESRGMKDLI KRLKPDCFED MIALVALFRP GPLQSGMVDN FIDRKHGREE
ISYPDIQWQH ESLKPVLEPT YGIILYQEQV MQIAQVLAGY TLGGADMLRR AMGKKKPEEM
AKQRSVFEEG AKSIGVDGEL SMKIFDLVEK FAGYGFNKSH SAAYALVSYQ TLWLKAHYPA
EFMAAVMTAD MDNTDKVVGL VDECWRMGLK ILPPDINSGL YHFHVNDDGE IVYGIGAIKG
VGEGPIEAII EARNSGEQGY FKDLFDLCAR SDIKKLNRRI LEKLIMSGAF DRLGPHRAAL
MNSLPDALKA ADQHAKAEAI GQVDMFGVLA EAPEQVEQSY ANVAPWQEQV VLDGERETLG
LYLTGHPITQ YLKEIERYAG GMRLKDMHPT DRGKMTTAVG LVVAARVMVT KRGNRIGICT
LDDRSGRLEV MLFTDALEKY QHLLEKDRIL IASGQVSFDD FSGGLKMTAR ELMDISEARE
KYARGLAISL TDRQIDDQLL NRLRQSLEPH RSGTIPVHLY YQRIDARAKL RFGATWRVTP
TDRLLIDLRT LVGNEQVELE FD
//
