ID A0A672I919_SALFA Unreviewed; 993 AA.
AC A0A672I919;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
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};
GN Name=LOC115388776 {ECO:0000313|Ensembl:ENSSFAP00005037657.1};
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:ENSSFAP00005037657.1, ECO:0000313|Proteomes:UP000472267};
RN [1] {ECO:0000313|Ensembl:ENSSFAP00005037657.1}
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; A0A672I919; -.
DR Ensembl; ENSSFAT00005039056.1; ENSSFAP00005037657.1; ENSSFAG00005012625.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000472267; Unplaced.
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 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 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; IPR042449; Ub-E1_IAD_1.
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:SF198; E1 UBIQUITIN-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 2.
DR PRINTS; PR01849; UBIQUITINACT.
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:UP000472267};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 21..386
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 193..262
FT /note="Ubiquitin-activating enzyme E1 FCCH"
FT /evidence="ECO:0000259|Pfam:PF16190"
FT DOMAIN 263..333
FT /note="Ubiquitin-activating enzyme E1 four-helix bundle"
FT /evidence="ECO:0000259|Pfam:PF16191"
FT DOMAIN 414..864
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 601..789
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT DOMAIN 793..825
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT ACT_SITE 595
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 993 AA; 109487 MW; 7BF34196140A3C32 CRC64;
ITFSFFSPNM SGSEGIDEGF YSRQLYVLGH EAMHRMGSAS VLIAGMKGLG VETAKNVILS
GVKSVTVQDQ GVATWSDLSS QFFLKESHVG QNRALSSLQQ LIALNPHVHV SAHTGPLNKD
LILQFEVVVL TDSSLDDQKQ FGELCHSHGI KLIIADTKGL CGQLFCDFGE KFEVLDQDGE
APASVMIQHI SKDNPGVVIC TDDRKHGLTD GAKVVFSEVQ GMTELNNLKP VEVKVGGPYF
FSICDTSAFS EYERGGVATE VKQPVTLNFK PLHEALNDHE LLIWTDFGKI SRHQTLHLAF
QALHEFVKKE QRLPRSWCQS DADSLLAIVR ELNAAAQLEQ LDEAAVRNLS CTARGDLAPM
NAFIGSVAAQ EVIKACSGKF TPLQQWLYFD AFECLPEGKD QQTESAFLEK GTRYDGQVAV
FGSAFQEKLE RQKYFLVGAG AIGCELLKNF ALIGLGAGEE GLVTVTDMDF IEKSNLNRQF
LFRSQDIKKS KSAVAAKAVQ EMNPKMKITA HQNRLDPDSE GVYDYNFFMG LDGVAAALDN
VEARVYLDKR CVRHRRPMLE GGTLGSKGHT LAVVPHLTES YGPAKSSAGN DIPLCTLKNF
PHRIEHTLQW ARDQFEGLFK NAPENVNSYL RDSVFVTRTL EQGDAEALEI LGGVWSSLVD
VEAGGQRPQS WEDCVSWARC KWETLYNNDI RQLLHCFPPE EVTASGLPFW SGSKRCPHPL
TFDPSKTTHM DYVVAAANLY GQIYGIEGTK EHASIRKTLE GVRVPAFTPK SSVKIHVTDQ
EMEEDKKNDS GEDDDTNFHM DYIVAASNLR AENYDIPAAD RHQSKRIAGR IIPAIATTTA
AVAGLMCLEL YKLVQGHREI RSYRSAYINL AVQYFVMSQP SRPQHFEVSS SSLKPRSFLT
GRGHEGSPSG ETVSCGIRGC GDSTDLVSGL VTGKKFSICI KRWRDDRGSC DFLCSCGVPS
MLSSTDTKTR VFPQLLPVNS VVFAHTCAIS PAF
//
