ID A0A672GKR7_SALFA Unreviewed; 933 AA.
AC A0A672GKR7;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, 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 Name=uba1 {ECO:0000313|Ensembl:ENSSFAP00005019386.1};
OS Salarias fasciatus (Jewelled blenny) (Blennius fasciatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Blenniimorphae; Blenniiformes; Blennioidei; Blenniidae;
OC Salariinae; Salarias.
OX NCBI_TaxID=181472 {ECO:0000313|Ensembl:ENSSFAP00005019386.1, ECO:0000313|Proteomes:UP000472267};
RN [1] {ECO:0000313|Ensembl:ENSSFAP00005019386.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A672GKR7; -.
DR Ensembl; ENSSFAT00005020167.1; ENSSFAP00005019386.1; ENSSFAG00005005103.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000472267; Unplaced.
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; 2.
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; 2.
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; 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; 3.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
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:UP000472267};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 823..928
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 585
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 933 AA; 102601 MW; 4F93F715A7110343 CRC64;
MAKNGNDAEI DEGLYSRQLY VLGHEAMKRM QISNVLISGM RGLGVEIAKN VILGGVRSVT
VHDQGVAEWR DLSSQFYIRE EDLGKNRAEV SQPRLAELNN YVPVTAYTGA LTEDYLTKFQ
VVVLTNSTLD EQQHVGDFCH SKGIKLIVAD TRGLFGQLFC DFGDEMVVYD TNGEQPLSAM
ISMITKDSAG VVTCLDEARH GFESGDYVTF TEVQGMTELN GCQPVEIKVL GPYTFSICDT
SGFTDYVRGG IVSQVKMPKK VSFVSEQHIL QNFAKFERPG QLHLGFQAVH AFQKKHSRLP
TPWSQADGEE LVALTKELNA AQAGAAAVEQ LDEALLKKMS YVAAGDLAPV NAFIGGLAAQ
EVMKACTGKF MPIIQWLYFD ALECLAEEEG VMLTEEECAP RNSRYDGQIA VFGTKLQDLL
GKQRYFLVGA GAIGCELLKN FAMIGLASSE GEVIVTDMDT IEKSNLNRQF LFRPSDVTKM
KSDTAAAAVK LMNPSIRITG HQNRVGPDTE RIYDDDFFES LDGVANALDN VDARMYMDRR
CVYYRKPLLE SGTLGTKGNV QVVIPFLTES YSSSQDPPEK SIPICTLKNF PNAIEHTLQW
ARDEFEGLFK QPPENAIANT ATTSASSCTT SLQTRCSSSV TQYYCDHKTF IFCSCLGGFT
CCVFQLTSSG APFWSGPKRC PHPLEFSTSN ELHMDYVLAA ANLFAQTYGI QGSTDRAALV
KILQDVKVPV FTPRSGVKIH CLHLFPLQPD DDTNFHMDFI VAASNLRAEN YDIPPTDRHK
VGRSKLIAGK IIPAIATTTS AVVGLVCLEL IKIVQGHKKL DSFKNGFMNL ALPFFGFSEP
IAAPRHKVSL LFREAGPTVS ASVTPASAAC GAVCALRGLT LCVFLFPCRM TEIVTKVSKK
KLGKHVKALV FELCCNDLSD EDVEVPYVRY TIR
//