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Database: UniProt
Entry: A0A672GKR7_SALFA
LinkDB: A0A672GKR7_SALFA
Original site: A0A672GKR7_SALFA 
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
//
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