ID   A0A2K5NFD6_CERAT        Unreviewed;      1015 AA.
AC   A0A2K5NFD6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Ubiquitin like modifier activating enzyme 6 {ECO:0000313|Ensembl:ENSCATP00000036035.1};
GN   Name=UBA6 {ECO:0000313|Ensembl:ENSCATP00000036035.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000036035.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000036035.1}
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}.
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DR   AlphaFoldDB; A0A2K5NFD6; -.
DR   Ensembl; ENSCATT00000060323.1; ENSCATP00000036035.1; ENSCATG00000040804.1.
DR   GeneTree; ENSGT00940000158826; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000040804; Expressed in pituitary gland and 12 other cell types or tissues.
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; 2.
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; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   NCBIfam; TIGR01408; Ube1; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   PANTHER; PTHR10953:SF186; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 6; 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; 2.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SMART; SM00985; UBA_e1_C; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT   DOMAIN          884..1006
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1015 AA;  113823 MW;  F2079C17EB0F072B CRC64;
     MEGSKPVAAP QGEEASCSSW GTGSTNKNLP IMSTASVEID DALYSRQRYV LGDTAMQKMA
     KSYVFLSGMG GLGLEIEKCQ AWDLGTNFFL SEDDVVNKRN RAEAVLKHIA ELNPYVHVTS
     SSVPFNETTD LSFLDKYQCV VLTEMKLPLQ KKINDFCRSQ CPPIKFISAD VHGIWSRLFC
     DFGDEFEVLD ATGEEPKEIF ISNITQANPG IVTCLENHPH KLETGQFLTF REINGMTGLN
     GSIQQITVIS PFSFSIGDTT ELEPYLHGGI AVQVKTPKTV FFEPLERQIK HPKCLIVDFS
     KPEAPLEIHT AMLALDQFQE KYSRKPNVGC QQDSEELLKL ATSVSETLEE KPDVNADIVH
     WLSWTAQGFL SPLAAAVGGV ASQEVLKAVT GKFSPLCQWL YLEAADIVES LGKPECEEFL
     PRGDRYDALR ACIGDTLCQK LQNLNIFLVG CGAIGCEMLK NFALLGVGTS KEKGMITVTD
     PDLIEKSNLN RQFLFRPHHI QKPKSYTAAD ATLKINSQIK IDAHLNKVCP ATETIYNDEF
     CTKQDIIITA LDNVEARRYV DSRCLANLRP LLDSGTMGTK GHTEVIVPHL TESYNSHRDP
     PEEEIPFCTL KSFPAAIEHT IQWARDKFES SFSHKPSLFN KFWQTYSSAE EVLQKIQSGH
     SLEGCFQVIK LLSRRPRNWS QCVELARLKF EKYFNHKALQ LLHCFPLDIR LKDGSKHLSF
     LQNAAKLYAT VYCIPFTEED LSADALLNIL SEVKIQEFKP SNKVVQTDET ARKPDHVPIS
     SEDERNAIFQ LEKAILSNEA TKSDLQMAVL SFEKDDDHNG HIDFITAASN LRAKMYSIEP
     ADRFKTKRVA GKIIPAIATT TATVSGLVAL EMIKVTGGYP FEAYKNCFLN LAIPIIVFTE
     TSEVRKTKIR NEISFTIWDR WTVHGKEDFT LLDFINAVKE KYGIEPTMVV QGVKMLYVPV
     MPGHAKRLKL TMHKLVKPST EKKYVDLTVS FAPDIDGDED LPGPPVRYYF SHDTD
//