ID A0A0P1AKC3_PLAHL Unreviewed; 1060 AA.
AC A0A0P1AKC3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
OS Plasmopara halstedii (Downy mildew of sunflower).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Plasmopara.
OX NCBI_TaxID=4781 {ECO:0000313|EMBL:CEG41288.1, ECO:0000313|Proteomes:UP000054928};
RN [1] {ECO:0000313|Proteomes:UP000054928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma Rahul, Thines Marco;
RL Submitted (SEP-2014) 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; CCYD01000553; CEG41288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1AKC3; -.
DR STRING; 4781.A0A0P1AKC3; -.
DR EnsemblProtists; CEG41288; CEG41288; CEG41288.
DR OMA; GANLHAF; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054928; 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; 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:SF4; UBA_E1_C DOMAIN-CONTAINING PROTEIN; 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|RuleBase:RU000519};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000054928};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 925..1055
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 1060 AA; 118072 MW; 8FE86912A3FED60F CRC64;
MSSHLVTAGD VSETADDVQK LVHVTDQAKD IDESGAMPID EGLYSRQLYV MGREAQLRMG
SSDVLIVGLD GLGVEIAKNV ILAGVKSVTV HDDTPASMLD LASQFYLTEA DIGIPRAAVS
VKKLAELNPY VPVRCHSGEI TEKFIHGFRA IVLVNQPLKD AKQIDAICHS KSIAFIATEA
RGVFGSVFCD FGDKFTVSDR DGVEPISCLI SSISNSVPLL VTVSDETRHN LDTGDLISFR
DVPGFSFLND SKPRKVTVTG PFTFLVDVVD DAEKKLIEEG QPSSGGYITQ VKQPLVTSFN
DLEHAIAAPG EFLISDFSKL GRSELLHIAF QALNAFRENH LGSYPKPGCM DDAEEVYALA
IEINKQYALK NQFSVKDLGT PDSKKIVQAL AAGATGVIAP MAAFLGGIVG QEILKACSGK
FTPIQQFFYF DAVECLPEAV HTGNSDEFLP IGSRYDGQIS VFGRKVQEKI KSLNIFLVGA
GAIGCEMLKN WAMMGVASDK DGIIHITDMD TIEKSNLNRQ FLFRSKDVQQ AKSLVVARAI
KQMNPDINVQ AYVSRVGAES ECQFTDDFFE SLSGVCTALD NVDARLYMDQ RCLFYGLPMF
ESGTLGTKGN TQIVVPHTTE NYGASRDPPE KSIPICTLKN FPHAIEHTLQ WARDWFEGEF
FQAPLDVNRY LKGPTFINEL NEQQNTKLEI LERLKSSLVD DLPMSFDDCI FWARSKFEEL
FSNQIKQLLY NFPLNQLTTS GTPFWSGPKR PPTPIQFDAK DPLHMNFIIS VANSRAKIYG
LKGHTDRDAF VRTLDGIFLP EFIPRKGVKI AASDAELREG SASQHDNMDS QCDYMLKNLP
KPDSLAGYRM QPIEFDKDDD SHMEVILSVS NLRARSYTIP EEDMHKSRFI AGNIIPAIAT
TTALVTGLVC FEFLKVFQNK PLDHYKNGFV NLALPLFTFA EPIEPKYTKT MIKGKELKWS
AWDRLEVDRG DMTLKEFLAF FEKEYDAEVS MLSYGVTILY AMYSAKSRSK ERMEMKISDL
IRTVTKKPID SKLKYLILEV CAMDADGEDV ELPYLRYRIK
//
