ID M3W5E9_FELCA Unreviewed; 1052 AA.
AC M3W5E9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 3.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Ubiquitin like modifier activating enzyme 6 {ECO:0000313|Ensembl:ENSFCAP00000005728.5};
GN Name=UBA6 {ECO:0000313|Ensembl:ENSFCAP00000005728.5,
GN ECO:0000313|VGNC:VGNC:66750};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000005728.5, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000005728.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000005728.5,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000005728.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000005728.5,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000005728.5}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000005728.5};
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 EMBL; AANG04001605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3W5E9; -.
DR PaxDb; 9685-ENSFCAP00000005728; -.
DR Ensembl; ENSFCAT00000006164.6; ENSFCAP00000005728.5; ENSFCAG00000006160.6.
DR VGNC; VGNC:66750; UBA6.
DR eggNOG; KOG2012; Eukaryota.
DR GeneTree; ENSGT00940000158826; -.
DR HOGENOM; CLU_002556_0_0_1; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000011712; Chromosome B1.
DR Bgee; ENSFCAG00000006160; Expressed in embryonic head and 10 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; 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; 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; 1.
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:UP000011712}.
FT DOMAIN 921..1043
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
SQ SEQUENCE 1052 AA; 118067 MW; 659C485EA7210FEA CRC64;
MEASEPVVAA REEEASCSSW VAGSTNTNLP IMSAESVEID DALYSRQRYV LGDTAMQKMA
KSHVFLSGMG GLGLEIAKNL VLAGIKALTI HDTEKCQAWD LGANFFLCED DVVNMRNRAE
AVLQHIAELN PYVHVTSSSI PLNETTDLSF LDKYQCVILT EIKLPLQKKI NNFCRSRCPP
IKFISADVHG IWSRLFCDFG DEFEVSDATG EEPKEIFISN ITQANPGIVT CLENHPHKLE
TGQFLMFREI NGMTGLNGST QQITVVSPFS FSIGDTTELD PYLHGGIAVQ VKTPKTFCFE
PLERQIKHPK CLIVDFGKPE APLQIHTAML ALDQFQESYS RKPNIGCQQD SEELLKLATS
ISETLEEKPE VNADIVHWLS WTAQGFLPPL AAAVGGVASQ EVLKAVTGKF SPLCQWLYIE
AADIVQSLDK PEREEFLPRG DRYDALRACI GDTLCQKLQK LNIFLVGCGA IGCEMLKNFA
LLGVGTGKEK GMVTVTDPDL IEKSNLNRQF LFRPHHIQKP KSYTAADATL KINPQFKIDA
HLNKVCPATE AIYNDEFYTK QDIIITALDN VEARRYVDSR CLANLRPLLD SGTMGTKGHT
EVIVPHLTES YNSHRDPPEE EIPFCTLKSF PAAIEHTIQW ARDKFESSFS HKPSLFNKFW
QTYPSAEEVL QKIQTGHSLE GCFQVIKLLS RRPRNWSQCV ELARLKFEKY FNHKALQLLH
CFPLDTRLKD GSLFWQSPKR PPSPIKFDLN EPLHFSFLLN AAKLYAAVYC IPFTEEDLSA
DALLNILSEV KIQEFKPSNK VVQTDETARK PEQVPISSED ERNAIFQLEK AISSNKATTS
DLQMAVLSFE KDDDHNGHID FITAASNLRA KMYNIEPADR FKTKRIAGKI IPAIATSTAA
VSGLVALEMI KVAGDYPFEA YKNCFLNLAI PIIVFTETSE VRRTEIRNGI SFTIWDRWTV
HGKEDFTLLD FINAVKEKYG IEPTMVVQGV KMLYVPVMPG HAKRLKLTMH KLVKPSTEKK
YVDLTVSFAP DTDGDEDLPG PPVRYYFSHD TD
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