ID A0A341BL22_NEOAA Unreviewed; 1051 AA.
AC A0A341BL22;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Ubiquitin-like modifier-activating enzyme 6 isoform X2 {ECO:0000313|RefSeq:XP_024603445.1};
GN Name=UBA6 {ECO:0000313|RefSeq:XP_024603445.1};
OS Neophocaena asiaeorientalis asiaeorientalis (Yangtze finless porpoise)
OS (Neophocaena phocaenoides subsp. asiaeorientalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Phocoenidae; Neophocaena.
OX NCBI_TaxID=1706337 {ECO:0000313|Proteomes:UP000252040, ECO:0000313|RefSeq:XP_024603445.1};
RN [1] {ECO:0000313|RefSeq:XP_024603445.1}
RP IDENTIFICATION.
RC TISSUE=Meat {ECO:0000313|RefSeq:XP_024603445.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_024603445.1; XM_024747677.1.
DR AlphaFoldDB; A0A341BL22; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000252040; 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; 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:UP000252040}.
FT DOMAIN 920..1042
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 1051 AA; 118165 MW; 7293EC00735224D1 CRC64;
MEGSQPVAAR QGEEASCSSW GAGSVNTNLP NMPTESVEID DALYSRQRYV LGDTAMQKMA
KSHVFLSGMG GLGLEIAKNL VLAGIKALTI HDTEECQAWD LGTNFFLCED DVVSMRNRAE
AVLHRIAELN PYVHVTSSSI PLNETTDLSF LHKYQCVVLT EIKLSFQKKI NDFCRSQCPP
IKFISADIHG IWSRLFCDFG DEFEVLDTTG EEPKEIFISN ITQANPGIVT CLENRPHKLE
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
QTYTSAEEVL KIQTGHSLEG CFQVIKLLSR RPRNWSHCVE LARLKFEKYF NHKALQLLHC
FPLDTRLKDG SLFWQSPKRP PSPLKFDLNE PLHFSFLLNA AKLYATVYCI PFTEEDLSAD
TLLNILSEVK IQEFRPSNKV VQTDETARKP DHVPVSSEDE RNAVFQLEKA ISSSEATTSD
LQMAVLSFEK DDDRNGHIDF ITAASNLRAK MYSIEPADRL KTKRIAGRII PAIATSTAAV
TGLVALEMIK VAGDYPFEAY KNCFFNLAIP IIVFTEASEV RKTEIRNGIS FTIWDRWIIH
GKEEFTLLDF INAVKEKYGI EPTMVVQGVK MLYVPVMPGH AKRLKLTMHK LVKPSTEKKY
VDLTVSFAPD TDGDEDLPGP PVRYYFSHDT D
//
