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
//