ID A0A1Q3DX58_LENED Unreviewed; 1012 AA.
AC A0A1Q3DX58;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=LENED_000880 {ECO:0000313|EMBL:GAV99423.1};
OS Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Lentinula.
OX NCBI_TaxID=5353 {ECO:0000313|EMBL:GAV99423.1, ECO:0000313|Proteomes:UP000188533};
RN [1] {ECO:0000313|EMBL:GAV99423.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAV99423.1,
RC ECO:0000313|Proteomes:UP000188533};
RG Lentinula edodes genome sequencing consortium;
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAV99423.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAV99423.1,
RC ECO:0000313|Proteomes:UP000188533};
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RT "A genome survey and senescence transcriptome analysis in Lentinula
RT edodes.";
RL Submitted (FEB-2017) 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}.
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:GAV99423.1}.
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DR EMBL; BDGU01000014; GAV99423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3DX58; -.
DR STRING; 5353.A0A1Q3DX58; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000188533; 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}.
FT DOMAIN 883..1008
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
SQ SEQUENCE 1012 AA; 112344 MW; 101BBE83D3F0B323 CRC64;
MSNLPLSANM DVDETAIDEG LYSRQLYVLG HEAMKRMAVS NVLIIGMQGL GVEIAKDLVL
AGVKSVTVYD PEPVKIEDLS SQFFLREEDV GRPRAEVTVP RLAELNAYVP VRNLGGQAGQ
EITVDLVRGF QVVVVCNAPY AKQLEINDWT HQNNVPFIAT ETRGLFGYVF NDFGAKFTCV
DPTGEQPLSG MIVSIDKDQE GIVTCLDETR HGLEDGDFVT FSEVQGMTEL NGCEPRKISV
KGPYTFAIGD TTGLGDYVRG GVFTQVKMPK IIEFKSLRES LQSPEFFITD FAKFDRPSTL
HAGFQALSEF HAQHKRFPKP RNAHDADAVV AIAKKLNADA DENIVTQLAF QATGDLSPVI
AVIGAFVAQE ALKACSAKFH PMQQHMYFDS LESLPDVLPS EAECQPTGSR YDGQVAVFGK
TFQEKISNHR QFLVGSGAIG CEMLKNWSMM GLASGPKGAI QVTDLDTIEK SNLNRQFLFR
PKDLGRFKAE VAATVVSDMN KDLAGKITTR QDAVGPDTED IYNEDFFNNI DGVTNALDNV
KARLYMDQRC VFYEKPLIDS GTLGTKGNVQ VVVPHLTESY ASSQDPPEKE TPSCTIKNFP
NAIAHTIEWS RTAFDDLFVR PAQAVNSFLS EPDYLEKTLK YSGQQKEQIE QLVSFLVTNK
PLTFEECIVW ARLQFEEKYN NEIRQLLFSL PKDAVASNGQ PFWSGPKRAP DPIIFNSNDP
LHLSYIIAAA NLHAYNYGLK GETDSNVYRK VADSVIVPEF TPKSGVKVQI NDNDPVAQNE
TSESDHLAEL TAKLPVPSSL AGYRLNPVEF EKDDDTNHHI DFITAASNLR ATNYSINLAD
RHTTKQIAGK IIPAIATTTS LVTGLACLEL YKIIDGKRKL ESYKNGFVNI ALPFFGFSEP
IAAPKHKYGA TEWTLWDRFT FKSDPTLKEI IDWFHSEHKL DVAMVSSGVS MLWSSFVGKK
KSEERLPMKF SKLVEHVSRK PVSPHIKTLT VEVMVMDEEG EDVEVPFIIV GI
//
