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Database: UniProt
Entry: A0A2K5JAH5_COLAP
LinkDB: A0A2K5JAH5_COLAP
Original site: A0A2K5JAH5_COLAP 
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
//
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