ID W9QQR2_9ROSA Unreviewed; 1093 AA.
AC W9QQR2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=L484_011695 {ECO:0000313|EMBL:EXB37970.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB37970.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Activates ubiquitin by first adenylating its C-terminal
CC glycine residue with ATP, and thereafter linking this residue to the
CC side chain of a cysteine residue in E1, yielding a ubiquitin-E1
CC thioester and free AMP. {ECO:0000256|ARBA:ARBA00002457}.
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; KE343674; EXB37970.1; -; Genomic_DNA.
DR RefSeq; XP_010089531.1; XM_010091229.1.
DR AlphaFoldDB; W9QQR2; -.
DR STRING; 981085.W9QQR2; -.
DR GeneID; 21394939; -.
DR KEGG; mnt:21394939; -.
DR eggNOG; KOG2012; Eukaryota.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000030645; 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; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF215; UBIQUITIN-ACTIVATING ENZYME E1 1; 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:UP000030645};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 966..1088
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 40..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 668
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1093 AA; 121274 MW; 748CF08A0F469AAE CRC64;
MLPRKRPCEG VVVEEGSGII NSSSDTSIIK KHRIGAAAGG TAESTVKNGN SSVSDGNVNG
SDSVASEGEE QEITMALGDS NTADIDEDLH SRQLAVYGRD TMRRLFASNV LVSGMQGLGA
EIAKNLILAG VKSVTLHDEG NVELWDLSSN FIFSENDVGK NRALASVQKL QELNNAVLVQ
TLTTKLTKEQ LSDFQAVVFT DISLEKAIEF NDYCHNHQPP IAFIKSEVRG LFGSVFCDFG
SEFTVVDVDG EEPHTGIIAS ISNDNPALVS CVDDERLEFQ DGDFVVFSEV RGMTELNDGK
PRKIKSARAY SFTLEDDTTN FGAYERGGIV TQVKQPKVLK FKPLREALND PGDFLLSDFS
KFDRPPLLHL AFQALDKFAS ELGRFPVAGS EEDAQKLITI AGNINESLGD GRLEDINPKL
LWHFSFGARA VLNPMAAMFG GIVGQEVVKA CSGKFHPLFQ FFYFDSVESL PTEPLDASDF
RPLNSRYDAQ ISVFGSRLQK KLEDAKVFIV GSGALGCEFL KNVALMGVSC GNQGKLTITD
DDVIEKSNLS RQFLFRDWNI GQAKSTVAAS AAASINPRLN IEALQNRVGP ETENVFDDAF
WENLSVVINA LDNVNARLYV DQRCLYFQKP LLESGTLGAK CNTQMVITHL TENYGASRDP
PEKQAPMCTV HSFPHNIDHC LTWARSEFEG LLEKTPTEVN TYLSNPSEYA MSMRNAGDAQ
ARDTLDRVLE CLDREKCESF QDCISWARLK FEDYFANRVK QLIFTFPEDA ATSTGAPFWS
APKRFPHPLQ FSAADPGHLH FVMAASILRA ETFGIPIPDW VKNPKKLAEA VDRVIVPEFQ
PKEGVKIETD EKATNVSSAA SVDDSLIINE LITKLEHSRA SLAPGFKMKP IQFEKDDDTN
YHMDMIAGLA NMRARNYSIP EVDKLKAKFI AGRIIPAIAT STAMATGLVC LELYKVLDGG
HKLEDYRNTF ANLALPLFSM AEPVPPKVIK HREMKWTVWD RWIVKDNPTL RELLEWLKNK
GLNAYSISCG SCLLYNSMFT RHKDRMDKKV VDLARDVAKV ELPAYRRHLD VVVACEDDDD
NDIDIPLVSI YFR
//
