ID A0A061H0L0_9BASI Unreviewed; 1025 AA.
AC A0A061H0L0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=PFL1_06924 {ECO:0000313|EMBL:EPQ25827.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ25827.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ25827.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ25827.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
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; KE361650; EPQ25827.1; -; Genomic_DNA.
DR RefSeq; XP_007882431.1; XM_007884240.1.
DR AlphaFoldDB; A0A061H0L0; -.
DR GeneID; 19320990; -.
DR KEGG; pfp:PFL1_06924; -.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053664; 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: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:UP000053664};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 895..1020
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 604
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1025 AA; 112660 MW; EC124F61AE449F97 CRC64;
MSAPATDDMK VDQPETSQID EALYSRQLYV LGHDAMKRMA VSNVLVVGLK GLGAEIAKNI
ALAGVKSITI FDPTPVSISD LSTQFFLRPE DASSGARRDH ATQPRLAELN TYVPIRVLEE
AELTKDVLAR FQVVVMTDAS YDEQLRINDL THATGTHFIS AEVRGLFGSV FNDFGPDFVC
IDPTGEQPLS GMIVSVASDA EGLVTTLDET RHGLEDGDYV TFSEVQGMDG LNGCEPRKVT
VKGPYTFTIG DTTGLGEYKR GGTFTQVKMP KKIAFKSLRE SAKQPEFLVS DFAKFDRPAA
LHAGFQALSA FSQKQGRLPR PRNAEDADAV LELTKSIFQA SGQDAADLPE KVVRELAFQA
SGDLSPMVAF VGGFVAQEAL KACSGKFHPL VQHMYVDSLE SLPSSVPELP ESEFAPLGSR
YDGQIAVLGR TFQDKIANTR QFLVGSGAIG CEMLKNWSMM GLGSGPDGTI HVTDMDTIEK
SNLNRQFLFR SKDVGHFKAD TAAAAVAEMN PDLKGKIHSH QNRVGPETED IYGDAFFDQL
TGVTNALDNV QARQYMDRRC VYYEKPLLES GTLGTKANTQ VVIPHLTESY SSSQDPPEKS
IPVCTLKNFP NAIEHTIQWA REQFDDFFLK PAENVNQYLS NADYLETTLK SGSGQREQLE
QIKQYLVDQR PLSFEACIAW ARLRFEDNYS STIRQLLHSL PADSVTSTGQ PFWSGPKRAP
KPLVFDAEDP THLDYVVAAA NLHAANYGLK GETDPAYFKK VLASVPVPEF VPKSNVKVQI
NDNEPVQNAG ANDGGEADLT EITSSLPTPA SLAGFRLQPI EMEKDDDTNH HIDFITAASN
LRASNYGITP ADKHQTKGIA GKIIPAIATT TALATGLVNL ELYKVLDGKK ELEVYSNAFV
NLALPFLAFS DPIAAPRLRY NDTEWTLWSR FDIQEDMVLK DFIEHFKSQH GLEISMISSG
VSMLFSAFLP PKKRDERLKM RMSELIETVS KKPIPAHATR VIVEVMADDA EGEDVEVPFV
VVKVK
//
