ID U3DCJ1_CALJA Unreviewed; 1012 AA.
AC U3DCJ1; F6YRN2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Ubiquitin-like modifier-activating enzyme 7 {ECO:0000313|EMBL:JAB36278.1};
GN Name=UBA7 {ECO:0000313|EMBL:JAB36278.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB36278.1};
RN [1] {ECO:0000313|EMBL:JAB36278.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum {ECO:0000313|EMBL:JAB50860.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB23664.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB12099.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB36278.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
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; GAMS01011037; JAB12099.1; -; mRNA.
DR EMBL; GAMR01010268; JAB23664.1; -; mRNA.
DR EMBL; GAMQ01005573; JAB36278.1; -; mRNA.
DR EMBL; GAMP01001895; JAB50860.1; -; mRNA.
DR AlphaFoldDB; U3DCJ1; -.
DR UniPathway; UPA00143; -.
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 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; 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:SF143; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 7; 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; 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 881..1008
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 599
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1012 AA; 111967 MW; 47282586A896C6F8 CRC64;
MDALNASKLL NEELYSRQLY VLGSPAMQKI RGARVLLSGL QGLGAEVAKN LVLMGVGSLT
LHDPHPTCWS DLAAQFLLSE QDLERSRAEA SQELLAQLNR DVKVVMHTGD ITEDLLLDFQ
VVVLTAAKLE EQLKVDTWCH KHGVCFLAAD TWGLVGQLFC DFGENFTVQD PTEAEPLTAA
IQHISQGSPG VLTLRKGANT HYFCDGDLVT FSGIEGMIEL NDCAPRSIHV REDGSLEIGD
TATFSRYLCG GAITEVKRPK TVRHKSLHTA LLQPHVVAQN PQEVHRAHCL HQAIRALHKF
EHLHGRPPQP WDPVDAETVV GLAQDLEPLK WTEEERLEQP LDEALVRTVA LSSAGVLSPM
VAMLGAVAAQ EVLKAVSRTF MPLDQWLYFD ALDCLPEDGE LLPSPEDCSP RGSRYDGQIA
VFGAGFQEKL GRQHYLLVGA GAIGCELLKG FALVGLGAGN SGGLTVADMD RIELSNLSRQ
FLFRSQDIGR PKAEVAAAAA QGLNPDLQVI PLTYPLDPTT ERIYGDNFFS HVDGVAAALD
SFQARRYVAA RCTHYLKPLL EAGTLGTRGS AQVFVPHVTE AYRAPASAAA SEDTSYPVCT
VRYFPSTAEH TLQWARNEFE GLFRLSAETI NHHQQAHTSL TDMDGTQTLT LLKSVFGVLR
ERPQNWQDCV AWALGHWELC FHYGIKQLLR HLPPNKVLED GTPFWSGPKR CPQPLEFDTN
QDTHLLYILA AANLYAQMHG LPDSRDWTAL RELLKLLPQP DPQQMVPIFP SNPELASASA
EFGPEQLKEL NKALEVWSMG PPLKPLMFEK DDDSNFHVDF VAAAASLRCQ NYGIPPVNRA
QSKLIVGQII PAIATTTAAV AGLVILELYK VVGGPRPRSA FRHSYLHLAE NYLIRYMPSA
PAIQTFHHLK WTCWDRLKIP AGQPERTLES LLAHLQEQHG LRVRMLLHHP ALLYSARWSP
EKQAQCLPLR VTELVQRVTG QVPAPGLRVL VLQLSCEDEE EDTAFPPLHY EL
//
