ID A0A2U4ART0_TURTR Unreviewed; 1052 AA.
AC A0A2U4ART0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Ubiquitin-like modifier-activating enzyme 6 isoform X1 {ECO:0000313|RefSeq:XP_019783656.1};
GN Name=UBA6 {ECO:0000313|RefSeq:XP_019783656.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019783656.1};
RN [1] {ECO:0000313|RefSeq:XP_019783656.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019783656.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_019783656.1; XM_019928097.2.
DR AlphaFoldDB; A0A2U4ART0; -.
DR STRING; 9739.ENSTTRP00000007361; -.
DR GeneID; 101333425; -.
DR InParanoid; A0A2U4ART0; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000245320; Chromosome 5.
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:UP000245320}.
FT DOMAIN 921..1043
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1052 AA; 118262 MW; 5A4AD5E874D9F60D CRC64;
MEGSQPVAAR QGEEASCSSW GAGSVNTNLP NMPTESVEID DALYSRQRYV LGDTAMQKMA
KSHVFLSGMG GLGLEIAKNL VLAGIKALTI HDTEECQAWD LGTNFFLCED DVVSMRNRAE
AVLQRIAELN PYVHVTSSSI PLNETTDLSF LHRYQCVVLT EIKLSLQKKI NDFCRSQCPP
VKFISADIHG IWSRLFCDFG DEFEVLDTTG EEPKEIFISN ITQANPGIVT CLENHPHKLE
TGQFLTFREI NGMTGLNGST QQITVVSPFS FSIGDTRELE PYLHGGIAVQ VKTPKTFCFE
PLEKQIKHPK CLIADFSKPE APLEIHSAML ALDQFQENYS RKPNTGCQQD SEELLKLATS
ISETLEEQPE VNYDIVRWLS WTAQGFLPPL AAAVGGVASQ EVLKAVTGKF SPLCQWLYIE
AADIVESLGK PEREEFLPRG DRYDALRACI GDTLCRKLQN LNIFLVGCGA IGCEMLKNFA
LLGVGTGKEK GMVTVTDPDL IEKSNLNRQF LFRPHHIQKP KSYTAADATL KINPQLKIDA
HLNKVCPATE VIYNDEFYTK QDIIITALDN VEARRYVDSR CLANLRPLLD SGTMGTKGHT
EVIVPHLTES YNSHRDPPEE EIPFCTLKSF PAAIEHTIQW ARDKFESSFS YKPSLFNKFW
QTYPSAEEVL KKIQTGQSLE GCFQVIKLLS RRPRNWSHCV ELARLKFEKY FNHKALQLLH
CFPLDTRLKD GSLFWQSPKR PPSPLKFDLN EPLHFSFLLN AAKLYATVYC IPFTEEDLSA
DTLLNILSEV KIQEFRPSNK VVQTDETARK PDHVPVSSED ERNAVFQLEK AISSSEATTS
DLQMAVLSFE KDDDRNGHID FITAASNLRA KMYSIEPADR LKTKRIAGRI IPAIATSTAA
VTGLVALEMI KVAGDYPFEA YKNCFFNLAI PIIVFTETSE VRKTEIRNGI SFTIWDRWII
HGKEEFTLLD FINAVKEKYG IEPTMVVQGV KMLYVPVMPG HAKRLKLTMH KLVKPSTEKK
YVDLTVSFAP DTDGDEDLPG PPVRYYFSHD TD
//
