ID A0A2K5JAH5_COLAP Unreviewed; 1012 AA.
AC A0A2K5JAH5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ubiquitin-activating enzyme E1 C-terminal domain-containing protein {ECO:0000259|SMART:SM00985};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000025899.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000025899.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_011794454.1; XM_011939064.1.
DR AlphaFoldDB; A0A2K5JAH5; -.
DR STRING; 336983.ENSCANP00000025899; -.
DR Ensembl; ENSCANT00000048906.1; ENSCANP00000025899.1; ENSCANG00000036372.1.
DR GeneID; 105509689; -.
DR KEGG; cang:105509689; -.
DR CTD; 7318; -.
DR OMA; FWSGHRK; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233080; 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; 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 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:UP000233080};
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; 111801 MW; 7DAEF71F9F97E15E CRC64;
MDALDASKLL DEELYSRQLY VLGSPAMQRI QGARVLVSGL QGLGAEVAKN LVLMGVGSLT
LHDPHPTCWS DLAAQFLLSE QDLERSRAEA SQELLAQLNR AVQVVVHTGD ITEDLLLDFQ
VVVLTAAKLE EQLKVGTLCH KHGVCFLAAD TRGLVGQLFC DFGEDFTVQD PTEAEPLTAA
IQHISQGSPG ILTLRKGANT HYFRDGDLVT FSGIEGMVEL NDCDPRSIHV REDGSLEIGD
TTTFSRYLRG GAITEVKRPK TVRHKSLDTA LLQPHVVAQS SQEVHRAHCL HQAFCALHKF
QHLHGRPPQP WDPVDAETVV GLAQDLEPLK WTEEEPLEQP LDEALVRTVA LSSAGVLSPM
VAMLGAVAAQ EVLKAISKKF MPLDQWLYFD ALDCLPEDGE LLPSPEDCAP RGSRYDGQIA
VFGAGFQEKL SRQHYLLVGA GAIGCELLKV FALVGLGARN SRGLTVVDMD HIERSNLSRQ
FLFRSQDIGR PKAEVAAEAA RRLNPDLQVI PLTYPLDPTT EHIYGDNFFS HVDGVAAALD
SFQARRYVAA RCTHYLKPLL EAGTLGTRGS AKVFMPHVTE AYRAPASATA SEDAPYPVCT
VRHFPSTAEH TLQWARDEFE GLFRLSAETI NHHQQAHTSL ADMDGPQTLT LLKPALGVLR
VRPQNWQDCV AWALGHWKLC FHYGIKQLLR HFPPNKVLED GTPFWSGPKQ CPQPLEFDTN
QDMHLLYVLA AANLYAQMHG LPGSQDSTAL RKLLKLLPQP DPQQMAPIFA SNLELASASA
EFGPEQLKEL NKALEVWTVG PPLKPLMFEK DDDSNFHVDF VAAAASLRCQ NYGIPPVNRA
QSKRIVGQII PAIATSTAAV AGLLGLELYK VVGGPRPRSA FRHSYLHLAE NYLIRYMPFA
PAIQTFHHLK WTCWDRLKVP AGQPERTLEL LLAYLQEQHG LRVRMLLHGP AVLYSAGWSP
EKQAQRLPLR VTELVQQVTG QVLAPGLRVL VLKLSCEGEE EDTAFPPLHY EL
//