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Database: UniProt
Entry: A0A2U4ARR8_TURTR
LinkDB: A0A2U4ARR8_TURTR
Original site: A0A2U4ARR8_TURTR 
ID   A0A2U4ARR8_TURTR        Unreviewed;       981 AA.
AC   A0A2U4ARR8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Ubiquitin-like modifier-activating enzyme 6 isoform X3 {ECO:0000313|RefSeq:XP_019783658.1};
GN   Name=UBA6 {ECO:0000313|RefSeq:XP_019783658.1};
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_019783658.1};
RN   [1] {ECO:0000313|RefSeq:XP_019783658.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019783658.1};
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_019783658.1; XM_019928099.2.
DR   AlphaFoldDB; A0A2U4ARR8; -.
DR   GeneID; 101333425; -.
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; 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          850..972
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
SQ   SEQUENCE   981 AA;  110880 MW;  E46EE4C125169550 CRC64;
     MMHYTAKNLV LAGIKALTIH DTEECQAWDL GTNFFLCEDD VVSMRNRAEA VLQRIAELNP
     YVHVTSSSIP LNETTDLSFL HRYQCVVLTE IKLSLQKKIN DFCRSQCPPV KFISADIHGI
     WSRLFCDFGD EFEVLDTTGE EPKEIFISNI TQANPGIVTC LENHPHKLET GQFLTFREIN
     GMTGLNGSTQ QITVVSPFSF SIGDTRELEP YLHGGIAVQV KTPKTFCFEP LEKQIKHPKC
     LIADFSKPEA PLEIHSAMLA LDQFQENYSR KPNTGCQQDS EELLKLATSI SETLEEQPEV
     NYDIVRWLSW TAQGFLPPLA AAVGGVASQE VLKAVTGKFS PLCQWLYIEA ADIVESLGKP
     EREEFLPRGD RYDALRACIG DTLCRKLQNL NIFLVGCGAI GCEMLKNFAL LGVGTGKEKG
     MVTVTDPDLI EKSNLNRQFL FRPHHIQKPK SYTAADATLK INPQLKIDAH LNKVCPATEV
     IYNDEFYTKQ DIIITALDNV EARRYVDSRC LANLRPLLDS GTMGTKGHTE VIVPHLTESY
     NSHRDPPEEE IPFCTLKSFP AAIEHTIQWA RDKFESSFSY KPSLFNKFWQ TYPSAEEVLK
     KIQTGQSLEG 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 IIVFTETSEV RKTEIRNGIS FTIWDRWIIH GKEEFTLLDF
     INAVKEKYGI EPTMVVQGVK MLYVPVMPGH AKRLKLTMHK LVKPSTEKKY VDLTVSFAPD
     TDGDEDLPGP PVRYYFSHDT D
//
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