ID A0A4P6XGV0_9ASCO Unreviewed; 1017 AA.
AC A0A4P6XGV0;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN Name=MPUL0A03200 {ECO:0000313|EMBL:QBM85695.1};
GN ORFNames=METSCH_A03200 {ECO:0000313|EMBL:QBM85695.1};
OS Metschnikowia aff. pulcherrima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX NCBI_TaxID=2163413 {ECO:0000313|EMBL:QBM85695.1, ECO:0000313|Proteomes:UP000292447};
RN [1] {ECO:0000313|Proteomes:UP000292447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APC 1.2 {ECO:0000313|Proteomes:UP000292447};
RA Gore-Lloyd D., Sumann I., Brachmann A.O., Schneeberger K.,
RA Ortiz-Merino R.A., Moreno-Beltran M., Schlaefli M., Kirner P.,
RA Santos Kron A., Wolfe K.H., Piel J., Ahrens C.H., Henk D., Freimoser F.M.;
RT "Snf2 controls pulcherriminic acid biosynthesis and connects pigmentation
RT and antifungal activity of the yeast Metschnikowia pulcherrima.";
RL Submitted (MAR-2019) 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; CP034456; QBM85695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P6XGV0; -.
DR STRING; 2163413.A0A4P6XGV0; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000292447; Chromosome i.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; 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; 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:UP000292447};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 887..1013
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 594
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1017 AA; 112786 MW; 39FE9C6F5C0BEE03 CRC64;
MADSMQIDSP VIDESLYLRQ LYVLGKEAML KMQNANVLII GLKGLGVEIA KNVALAGVKA
LALYDPLPVA VQDLSTQFFL RADDVGKPTA EACAERLLEL NSYVPISVVD NISEATLRQY
KCVVATNLSL EEQVQINEFT HANGIGFIAA DVRGLFASLF VDLGAEFPVI DQNGEEPLTG
IVSDIEKNGT VTMLDDSRHG LQDGDYVKFS EVVGMPKLNE GNPHKVEVLG PYAFKIQLDE
SYGTYVKGGL YQQVKMPVKI SFESLKQQLA APEYLFSDFA KFDRPPQLHI GFQALHAFKT
RNSRLPRPYD DADANEFLRY AEEISAQNPS ILGDTDLDVK LLEELAFQAT GDLPGMVAFL
GGLVAQEVLK CCSSKFNPVK QFMYFDSLES LPAHDKFPRT AENTKPVGSR YDPQIAVFGA
DYQQAIANLK VFLVGSGAIG CEMLKNWALM GLGSGPAGGI IVTDNDSIEK SNLNRQFLFR
PKDVGGNKSE IAARAVQAMN PDLTGKIFPK LDKVGPETED IFGDEFWEPL DFVTNALDNV
DARTYVDRRC IFYKKPLLES GTLGTKGNTQ VVIPNLTESY SSSQDPPEKS IPLCTLRSFP
NKIDHTIAWA KSLFQGYFAD SPETVNLYLS QPNYVEQTLK QNPDIKGTLA NIADLLNKRP
YSFADCIRWA RQEFETKYNH DIKQLLYNFP ADAKTSNGAP FWSGPKRAPK PLDFDVNNPD
HFNFIVGGAN LLAFIYGLND KNVSNDEYKK VLDSFEPEPF VPKTGVKIAA SDAEAEEEAK
KLSGGFDESE IQKIVATMPE PSTLAGYRLT PIEFEKDDDT NHHIEFITAA SNCRALNYGI
ETADASKTKF IAGKIIPAIA TTTALVTGLV CLELYKVVAK HDDVELFKNG FVNLALPFFG
FSEPVKSAKG KYNDKEFDQI WDRFEVHGDI KLKDLLEKFQ ENEGLDISML SHGVTLLYAS
FFPPKKVKER LEMKITELIE AVSKKPVPAH MKNLILEICC DDKEGEDVEV PYINVKI
//
