ID A0A5B1QAD1_9AGAM Unreviewed; 1009 AA.
AC A0A5B1QAD1;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=DENSPDRAFT_831101 {ECO:0000313|EMBL:KAA1466293.1};
OS Dentipellis sp. KUC8613.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Hericiaceae; Dentipellis.
OX NCBI_TaxID=1883078 {ECO:0000313|EMBL:KAA1466293.1, ECO:0000313|Proteomes:UP000322482};
RN [1] {ECO:0000313|EMBL:KAA1466293.1, ECO:0000313|Proteomes:UP000322482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUC8613 {ECO:0000313|EMBL:KAA1466293.1,
RC ECO:0000313|Proteomes:UP000322482};
RX PubMed=31482283; DOI=.1007/s00253-019-10089-6;
RA Park H., Min B., Jang Y., Kim J., Lipzen A., Sharma A., Andreopoulos B.,
RA Johnson J., Riley R., Spatafora J.W., Henrissat B., Kim K.H.,
RA Grigoriev I.V., Kim J.J., Choi I.G.;
RT "Comprehensive genomic and transcriptomic analysis of polycyclic aromatic
RT hydrocarbon degradation by a mycoremediation fungus, Dentipellis sp.
RT KUC8613.";
RL Appl. Microbiol. Biotechnol. 103:8145-8155(2019).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA1466293.1}.
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DR EMBL; NSJX01000001; KAA1466293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B1QAD1; -.
DR InParanoid; A0A5B1QAD1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000322482; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000322482}.
FT DOMAIN 880..1005
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
SQ SEQUENCE 1009 AA; 112195 MW; D485DF6C05D5B1EE CRC64;
MASTQLNVPM DIDEAQIDEG LYSRQLYVLG HEAMKRMAAS NVLIVGLEGL GVEIAKNLAL
AGVKSVTLYD PEPVQIQDLS TQFFLREDDI GKPRAAATIQ RLAELNAYVP VRNLGGVSGQ
PITVDLVKGF QVVVLVNQPL ERQLEINDWT HTNGVHFIAA ETRGLFGSAF NDFGPKFTCV
DPTGEQPLTG MIVSVDSDKD GLVTCLDETR HGLEDGDFVT FSEVKGMEEL NGCEPRKVSV
KGPYTFSIGD TSNLSEYKSG GIFTQVKMPK ILEFKSLRDS LKNPEFFITD FAKFDRPATL
HAGFQAVWQF FGKQQRLPRP RNAEDAASVV ALAKQIDADA DEKVLTELAY QSAGNVSPII
AVLGGFVAQE ALKACSAKFH PMLQHLYFDS LESLPTTLPT EQECQPTGHR YDGQIAVFGR
AFQEKIANHR QFLVGAGAIG CEMLKNWSMM GLGSGAKGVI HVTDLDTIEK SNLNRQFLFR
PKDLGKFKSE VAAAAVSDMN PDLKGHIESK QEPVGPDTEV IYDEKFFKDI DGVTNALDNI
KARLYMDQRC VFFEKPLLES GTLGTKGNTQ VIIPHLTESY ASSQDPPEKE TPSCTVKNFP
NAINHTIEWS RTEFDNLFVK PAQAVNSYLS DPTFLETTMK YSGQHKEQIE QIASYLVTNK
PLTFEECIVW ARLQFEDKYN NAIRQLLYSL PKDAVTSTGQ PFWSGPKRAP DPLTFDSNDP
THLGYIIAAA NLHAYNYGLR GETDPALFKK VADSVLVPEF TPKSGVKVQI TETDPVDNND
PTDPAELIKQ LPPPSSLAGY RLNPVDFEKD DDTNHHIDFI TAASNLRAMN YNITPADRHT
TKQIAGKIIP AIATTTSLVV GLVCLELYKI IDGKNKLEDY KNGFVNLALP FFGFSEPIAA
AKNKYGETEW TLWDRFEFKN DPSLKEIVDY FQKQHKLEVS MVSQGVSMLW SSFIGKKKSE
ERLPMRFSQL VEHVSKKPVP AHTTHFIVEV MVMDEEGEDV EVPFIVVRK
//
