ID T1DHL9_CROHD Unreviewed; 1059 AA.
AC T1DHL9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
DE AltName: Full=Ubiquitin-activating enzyme E1 {ECO:0000256|ARBA:ARBA00030371};
OS Crotalus horridus (Timber rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=35024 {ECO:0000313|EMBL:JAA95090.1};
RN [1] {ECO:0000313|EMBL:JAA95090.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Venom gland {ECO:0000313|EMBL:JAA95090.1};
RX PubMed=23758969; DOI=10.1186/1471-2164-14-394;
RA Rokyta D.R., Wray K.P., Margres M.J.;
RT "The genesis of an exceptionally lethal venom in the timber rattlesnake
RT (Crotalus horridus) revealed through comparative venom-gland
RT transcriptomics.";
RL BMC Genomics 14:394-394(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; GAAZ01002853; JAA95090.1; -; mRNA.
DR AlphaFoldDB; T1DHL9; -.
DR UniPathway; UPA00143; -.
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 2: Evidence at transcript level;
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 Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 923..1054
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 633
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1059 AA; 118946 MW; 1E7703D2A675C43C CRC64;
MSSSPLSKKR RLGESESKTG SNCSSGKSIQ TDLREAPANG MAKNGSETDI DEGLYSRQLY
VLGHEAMKRM QNANILVSGL RGLGVEIAKN IILGGVKSVT IHDQGIAEWS DLSSQFYLRE
EDLGKNRAEV SQPRLAELNS YVPVTAYTGP LSEDFLNNFQ VVVLTNCPLE EQLRISDFCH
SQNIKLVVAD TKGLFGQLFC DFGENMVVTD TNGEQPLSAM VSMVTKGCPG EVTCLDEARH
GFESGDFVSF LEVEGMKELN SCEPMEIKVL GPYTFSIGDT SSFSDYVRGG IVTQVKMPKK
ISFKSLRASL PEPELVITDF GKFDRPGQLH LGFQALHEFH KKHGHFPRPR NQADATEVLS
LVKDLNEQAM PSLKQEQLNE DIIKEMAFQA SGDLAPVNAF IGGLAAQEVM KACSGKFMPV
IQWLYFDALE CLPEENKDTL TEENCSPKHC RYDGQIAVFG NELQIKLSQQ KYFLVGAGAI
GCELLKNFAM IGLGCGQGGD VAVTDMDTIE KSNLNRQFLF RPWDVTKMKS DTAAAAVKEM
NPSIHITSHQ DRVGPDTERI YDDDFFENLD GVANALDNVD ARMYMDRRCV YYRKPLLESG
TLGTKGNIQV VIPFLTESYS SSQDPPEKSI PICTLKNFPN AIEHTLQWAR DEFEGLFKQP
AENVNQYITD AKFMERTQKL PGTQPLEVLE AVYKSLVTDR PKSWADCVAW ACNHWHTQYS
NNIRQLLHNF PPNQKTNSGT LFWSGPKRCP HPLTFDVKNP LHMDYVVAAA NLCAQTYGIT
GTRDREAIVE LLCQVQVPEF TPKSGVRIHI SDQELQNANA SVDDSRLEEL KTSLPSPQQL
HDFRMFPVDF EKDDDTNFHM DFIVAASNLR AENYDIPPAD RHKSKLIAGK IIPAIATTTA
AVVGLVCLEL YKIIQGHKRL ESYKNGFLNL ALPFFGFSEP ISCPKNKYYN TEWTLWDRFE
VQGIQPDGQE MTLREFLAYF KKEYKLEITM LSQGVSMLYS FFMQPAKLKE RHDQPMTEIV
TRVSKKKIGR HVKALVFELC CNDDSGEDTE VPYVRYTIR
//
