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Database: UniProt
Entry: W2J8A2_PHYPR
LinkDB: W2J8A2_PHYPR
Original site: W2J8A2_PHYPR 
ID   W2J8A2_PHYPR            Unreviewed;      1063 AA.
AC   W2J8A2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE            EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN   ORFNames=L916_06575 {ECO:0000313|EMBL:ETL42665.1}, L917_06446
GN   {ECO:0000313|EMBL:ETL95830.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL42665.1, ECO:0000313|Proteomes:UP000053864};
RN   [1] {ECO:0000313|EMBL:ETL95830.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL95830.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETL42665.1, ECO:0000313|Proteomes:UP000053864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ05E6 {ECO:0000313|EMBL:ETL42665.1,
RC   ECO:0000313|Proteomes:UP000053864};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CJ05E6.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC         = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC         L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000256|ARBA:ARBA00000488};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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DR   EMBL; KI672245; ETL42665.1; -; Genomic_DNA.
DR   EMBL; KI678959; ETL95830.1; -; Genomic_DNA.
DR   EnsemblProtists; ETL42665; ETL42665; L916_06575.
DR   EnsemblProtists; ETL95830; ETL95830; L917_06446.
DR   VEuPathDB; FungiDB:PPTG_02851; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053864; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
DR   CDD; cd01491; Ube1_repeat1; 1.
DR   CDD; cd01490; Ube1_repeat2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 2.40.30.180; Ubiquitin-activating enzyme E1, FCCH domain; 1.
DR   Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR   Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR   Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR   Gene3D; 3.10.290.60; Ubiquitin-activating enzyme E1, UFD domain; 1.
DR   InterPro; IPR032420; E1_4HB.
DR   InterPro; IPR032418; E1_FCCH.
DR   InterPro; IPR042302; E1_FCCH_sf.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR018965; Ub-activating_enz_E1_C.
DR   InterPro; IPR042449; Ub-E1_IAD_1.
DR   InterPro; IPR038252; UBA_E1_C_sf.
DR   InterPro; IPR019572; UBA_E1_SCCH.
DR   InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   InterPro; IPR018075; UBQ-activ_enz_E1.
DR   InterPro; IPR018074; UBQ-activ_enz_E1_CS.
DR   InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR   InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   NCBIfam; TIGR01408; Ube1; 1.
DR   PANTHER; PTHR10953:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF16191; E1_4HB; 1.
DR   Pfam; PF16190; E1_FCCH; 1.
DR   Pfam; PF09358; E1_UFD; 1.
DR   Pfam; PF00899; ThiF; 2.
DR   Pfam; PF10585; UBA_E1_SCCH; 1.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SMART; SM00985; UBA_e1_C; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR   PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR   PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000519};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000519};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU000519}.
FT   DOMAIN          926..1056
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
FT   ACT_SITE        636
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   1063 AA;  117800 MW;  A04F1980A2617451 CRC64;
     MSSHAVTAGD VNETADGVRN LVHVTDNAMD IDQSGAASID EGLYSRQLYV MGREAQLRMG
     TSNVLIVGLN GLGVEIAKNV ILAGVKSVTL HDDTPASKLD LASQFYLTEG DMGKPRAAVS
     VKKLAELNPY VPVRCYSGEI TEEFLLGFRA VVLVNAPLKE AKRINAICHA KSIAFITTEA
     RGVFGSVFCD FGDEFIVSDR DGVEPVSCLI SSISNSAPPL VTVNDDTRHG LETGDLVSFR
     EVAGFPFLND SKPRKVTVTG PFTFTLDIID EADKKLFEEG QSFTGGYVTQ VKQPLVTKFK
     SLENALAAPG EFLINDFAKL GRSELLHVAF QALDAFQEKH QGNYPKPGCM EDAEEVFTLS
     CEINKQFAAK KQFSVEGIDD ADSKKIIQAL AAGAVGVISP MAAFLGGIVG QEALKACSGK
     FTPIQQFFYF DAVECLPDAV YAGTPDEFAP TGSRYDGQIV VFGRKLQEKI NSLNMFLVGA
     GAIGCEMLKN WAMMGVASSK DGTIHITDMD TIEKSNLNRQ FLFRSKDVQQ AKSSVAARAI
     KEMNPDVNVQ SYVSRVGAES EDQFNDDFFE SLSGVCTALD NVEARLYMDQ RCLFYGLPMF
     ESGTLGTKGN TQIVVPHKTE NYGASRDPPE KSIPICTLKN FPNAIEHTLQ WARDWFEGEF
     FQAPSDVNRY LEGPAFMKEL NEQQNTKIET LERLKSSLVD DRPMSFEDCI SWARFKFEEL
     FSNQIKQLLY NFPLDQLTTS GTPFWSGPKR PPTPITFDAK DPLHMDFIVS VANSRAKNYG
     LKGHNDRDAF AQVLSGIHVP EFSPKKGVKI AASDAELKEG GAAPPLQDGD AQCDLILKEL
     PKPATLAGYR MQPIEFDKDD DSHMEVIVSV SNLRARSYKI PEEDMHKSRF IAGKIIPAIA
     TTTALVTGLV CFEFLKVFQD KPLDHYKNGF VNLALPLFTF AEPIAPKFTK TMLKGEEYKW
     TAWDRLEVDR GDMTLKEFLA YFEKEYDAEV SMLSYGVTIL YAMYSAKSRS KERMAMKISD
     LVRTVTKKPI DPKLKYLILE VCAMDAEGED VELPYLRYHY KQQ
//
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