(data stored in SCRATCH zone)

SWISSPROT: A0A0H2Y481_YERPA

ID   A0A0H2Y481_YERPA        Unreviewed;      1171 AA.
AC   A0A0H2Y481;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 20.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|SAAS:SAAS01159143};
DE            EC=2.7.7.7 {ECO:0000256|SAAS:SAAS01144005};
GN   OrderedLocusNames=YPA_0535 {ECO:0000313|EMBL:ABG12503.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12503.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12503.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12503.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|SAAS:SAAS01143971};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS01143988}.
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DR   EMBL; CP000308; ABG12503.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABG12503; ABG12503; YPA_0535.
DR   KEGG; ypa:YPA_0535; -.
DR   KO; K02337; -.
DR   OMA; DFCMDGR; -.
DR   BioCyc; YPES360102:GHZU-558-MONOMER; -.
DR   Proteomes; UP000001971; 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   Gene3D; 1.10.10.1600; -; 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; 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   InterPro; IPR004805; PolC_alpha.
DR   PANTHER; PTHR32294; PTHR32294; 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; SSF89550; 1.
DR   TIGRFAMs; TIGR00594; polc; 1.
PE   4: Predicted;
DR   PRODOM; A0A0H2Y481.
DR   SWISS-2DPAGE; A0A0H2Y481.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS01144001};
KW   DNA replication {ECO:0000256|SAAS:SAAS01143938};
KW   DNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS01144000};
KW   Nucleotidyltransferase {ECO:0000256|SAAS:SAAS01143921,
KW   ECO:0000313|EMBL:ABG12503.1};
KW   Transferase {ECO:0000256|SAAS:SAAS01143903,
KW   ECO:0000313|EMBL:ABG12503.1}.
FT   DOMAIN       18     85       POLIIIAc. {ECO:0000259|SMART:SM00481}.
SQ   SEQUENCE   1171 AA;  131421 MW;  7D73FDB36C657E40 CRC64;
     MIQSTHFWYL DMAEPRFVHL RVHSDYSMID GLAKIGPLVK RAAALGMPAL AITDFTNLCG
     LVKFYGSAHG AGIKPIIGAD FYVQSEILGD ELAHLTVLAR NNEGYQNLTL LISEAYQRGY
     GAAGPIIDRD WLIKHKEGLI LLSGGRMGDV GKFLLRGNQV QVDQCLAFYQ EHFPDCYYLE
     LIRTGRPDEE NYLHAAVALA TERGLPVVAT NDVRFIDESD FDAHEIRVAI HDGFTLVDPK
     RPKNYSPQQF MRDEEQMCEL FADIPEALIN SVEIAKRCNV TIRLGEYFLP QFPTGEMSTE
     DFLVEKAKQG LEERLEFLFP DPEVRLQKRP EYDERLDIEL KVINQMGFPG YFLIVMEFIQ
     WSKDNGVPVG PGRGSGAGSL VAYALKITDI DPLEFDLLFE RFLNPERVSM PDFDVDFCME
     KRDLVIEHVA EMYGRDAVSQ IITFGTMAAK AVIRDVGRVL GHPYGFVDRI SKLIPLDPGM
     TLEKAFAAEP QLAEIYEADE EVRALIDMAR KLEGVTRNAG KHAGGVVIAP TKITDFAPLY
     CDAEGNNPVT QFDKNDVEYA GLVKFDFLGL RTLTIINWAL EMINARRAKT GLEPIDIASI
     PLEDKKSFDM LQRSETTAVF QLESRGMKDL IKRLKPDCFE DMIALVALFR PGPLQSGMVD
     NFIDRKHGRE AISYPDIEWQ HESLKPVLEP TYGIILYQEQ VMQIAQVLSG YSLGGADMLR
     RAMGKKNPAE MAKQRSVFED GAKNQGIDGE LAIKIFDLVE KFAGYGFNKS HSAAYALVSY
     QTLWLKAHYP AEFMAAVMTA DMDNTDKVVG LVDECWRMGL KILPPDINSG LYHFHVNDDG
     EIVYGIGAIK GVGEGPIEAI LEARKEGGYF KELFDLCARV DTKKLNKRIL EKLIMSGAFD
     RLGPHRAALM SSLGDALKAA DQHAKAEAIG QVDMFGVLAD APEQVEQSYA NVPPWQEQVV
     LDGERETLGL YLTGHPITQY LKEIERYAGG MRLKDMHPTD RGKMTTAVGL VIAARVMVTK
     RGNRIGICTL DDRSGRLEVM LFTDALEKYQ HLLEKDRILI ATGQVSFDDF SGGLKMTARE
     LMDISEAREK YASGLAISLT DRQIDDQLLN RLRQSLEPHR AGTIPVHLYY QREDARARLR
     FGATWRVTPT DRLLIDLRTL VGNEQVELEF D
//

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