ID A0A4Z0A3E1_9AGAM Unreviewed; 1626 AA.
AC A0A4Z0A3E1;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-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=EWM64_g3261 {ECO:0000313|EMBL:TFY80751.1};
OS Hericium alpestre.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Hericiaceae; Hericium.
OX NCBI_TaxID=135208 {ECO:0000313|EMBL:TFY80751.1, ECO:0000313|Proteomes:UP000298061};
RN [1] {ECO:0000313|EMBL:TFY80751.1, ECO:0000313|Proteomes:UP000298061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 108284 {ECO:0000313|EMBL:TFY80751.1,
RC ECO:0000313|Proteomes:UP000298061};
RA Buettner E., Kellner H.;
RT "Genome sequencing of the rare red list fungi Hericium alpestre (H.
RT flagellum).";
RL Submitted (FEB-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}.
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:TFY80751.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SFCI01000293; TFY80751.1; -; Genomic_DNA.
DR STRING; 135208.A0A4Z0A3E1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000298061; 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 CDD; cd22249; UDM1_RNF168_RNF169-like; 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; IPR019134; Cactin_C.
DR InterPro; IPR018816; Cactin_central.
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; PF10312; Cactin_mid; 1.
DR Pfam; PF09732; CactinC_cactus; 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; SM01050; CactinC_cactus; 1.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000298061}.
FT DOMAIN 1497..1622
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 154..198
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1626 AA; 185073 MW; 820CA34F7AB42BE4 CRC64;
MAGRDSRSIS PRREDRHRRG DTTDRYDRYD RYDRSSTHRD PDDDRRKRRR SRSRDVDDNR
SRRRTDRSRS RSRSKDRSER KEKKQKRDKS EERKARKAEK RRVQEEEEAR QIAELSVYSA
TDNPFHDVNL GQQFRWHKKT EKEKKSGLTL AEAQHRDAIR RQEAKEELEK LNKRRAEREA
EQRLREEEEV RMQRLQESAQ MSEWIAKDGD FQLEQERRRA AIRIREKRAK AIDFLALNLR
YINPDEEEEE ELGDDAGLEI DIDEPYNIFR SLSPDQVEEL HDDIERYLSL EQSDVNIDFW
TNMMVVCKDR LDRIKADQRL GVEAAAAVEA DITALLEGKS YEHLVALQRQ IQAKLSSGEP
LDTDYWEGLL KKLLAKLKTL HEVVVRNRLE QLRKKQRDEA LQAQEELLEG VASDAVKGKA
HVIEPAAQQE RTVAEDIEPY NRAMSPALVD ITKLPYEERQ IDIVLEADDT RALFEQRRAV
AGSRFIPKAA QPIIEEPDEE APSGADLASE ALYRAEAERD MDEEEELFNL EENIQTPTSY
NWEDKYRPRK PRYFNRVHTG YEWNKYNQTH YDTDNPPPKV VQGYKFNIFY PDLIDKSKAP
TYKMVKEAGN DETVLLHFSA GPPYEDIAFR IVNREWEYSH KRYVLGHEAM KRMAASNVLI
VGLEGLGVEI AKNIVLAGVK SVTLFDPEPV RIQDLSSQFF LREDDVGKPR AEATHKRLAE
LNAYVPVRNL GGVAGTPVNV GLIKDFQVVV LVNQSLEKQL EINDWTHKNG VYFIATETRG
LFGSAFNDFG PKFTCVDPTG EQPLTGMIVS VDKDKEGLVT CLDETRHGLE DGDYVTFSEV
QGMEELNGCE PRKVTVKGPY TFSIGDTTGF GDYKSGGIFT QVKMPKILEF HSLRESLKSP
ECFITDFAKF DRPATLHAGF QALWQFKAQN QRAPRPRNAE DATAVVSLAK KIDADADEKV
LTELSYQAVG NLSPMVAVLG GFVAQEVLKA CSAKFHPTIQ HLYFDSLESL PSELPSEQDC
QPTGSRYDGQ IAVFGKKFQE KIANHRQFLV GAGAIGCEML KSWSMMGLGA GPKGVIHVTD
LDTIEKSNLN RQFLFRPKDL GKFKAEVAAA AVSEMNPDLK GHIQSKQEPV GPDTENVYGE
EFFKDIDGVT NALDNIKARL YMDQRCVFFE KPLLESGTLG TKGNTQVIIP HLTESYASSQ
DPPEKETPSC TVKNFPNAIA HTIEWSRQEF DNLFVKPAQS VNSYLTDPSF LENTMKYSGQ
HKEQIEQIVS YLVTNKPITF EECIVWARLQ FEEKYNNAIR QLLFSLPKDA TTSTGQPFWS
GPKRAPEPLT FDSNDPTHLG YIIAAANLHA FNYGLRGETD PAVFRKVADS VLVPEFTPKS
GVKVQISDTD PTESNPDPTD PMELVKQLPP PSSLAGYRLN PVEFEKDDDS NHHIDFITAA
SNLRAMNYSI NPADRHTTKQ IAGKIIPAIA TTTSLVVGLV CLELYKIIDG KNKLENYKNG
FVNLALPFFG FSEPIAAAKN KYGTTEWTLW DRFVFSNDPT LKDIVDHFSK VHKLEVTMVS
QGVSMLWSSF LGKKKSEERL PMKFSQLVEY ISKKPVAPHV TQFIVEVMVM DEEGEDVEVP
FLVVRK
//
