ID   A0A091PLM4_HALAL        Unreviewed;      1029 AA.
AC   A0A091PLM4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Ubiquitin-like modifier-activating enzyme 6 {ECO:0000313|EMBL:KFQ08515.1};
DE   Flags: Fragment;
GN   ORFNames=N329_03167 {ECO:0000313|EMBL:KFQ08515.1};
OS   Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Haliaeetus.
OX   NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ08515.1, ECO:0000313|Proteomes:UP000054379};
RN   [1] {ECO:0000313|EMBL:KFQ08515.1, ECO:0000313|Proteomes:UP000054379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ08515.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK661519; KFQ08515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091PLM4; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000054379; Unassembled WGS sequence.
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:UP000054379}.
FT   DOMAIN          898..1020
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ08515.1"
FT   NON_TER         1029
FT                   /evidence="ECO:0000313|EMBL:KFQ08515.1"
SQ   SEQUENCE   1029 AA;  115647 MW;  64A00CFB5068518E CRC64;
     SVNKSPCIMA ADSMEIDDAL YSRQRYVLGD TAMQKMAQSH VFLSGIGGLG VEIAKNIILA
     GVKALTVHDT KQCTKWDLGI NFFIHEDDIT SQRNRAEATL HRIAELNPYV HVAASVVPLD
     ETTDLSFLKQ YQCVILTEVS LLLQKKINDF CHAQQPPIKF ISADVYGICS RLFCDFGDEF
     EVLDTTGEEP KEIFISNITQ SNPGIVTCLE NHPHRLETGQ FLTFREVNGM SCLNGSTHQI
     TVVSPYSFSI GDTSDMEPYL HGGIAVQVKT PKMFYFERLE KQITNPLCLV ADFSKSEAPL
     QIHVAMLALN HFQENFGRGP NIGCLQDAEE MLKIAMSVSE TLENKPQVNG DVVKWLSRTA
     QGFLAPLAAA VGGVASQEVL KAVTGKFSPL QQWLYIDMLD IVTPLEKMSC EEFLPRGDRY
     DALRACIGDS LCQKLHDLNV FLVGCGAIGC EMLKNFALLG VGTGQDKGLV TITDPDLIEK
     SNLNRQFLFR PHHIQKPKSY TAAEATLNIN PYLKIDSYIN KVCPATENTY SDEFYTKQDV
     IVTALDNVEA RRYIDSRCVA NLRPLIDSGT MGTKGHTEVI VPHLTESYNS HRDPPEEEIP
     FCTLKSFPAA IEHTIQWARD KFESSFSHKP SLFNKFWQTY PSAEEVLQRI KSGESLEGCF
     HVIKTLSRRP RSWTQCVELA RVKFEKYFSH KALQLLHSFP LDTRLKDGSL FWQSPKRPPF
     PVKFEFNDPL HYGFIVSAAK LFATVYCVPF TEKDLSEETI LKIISAVKVP EFRPSNKVVQ
     TDETARKPDH IPVSSEDERH AIFQLEKSIV SNEALENDLQ MKPISFEKDD DSNGHIDFIT
     AASNLRAKMY NIEPADRFKT KRIAGKIIPA IATATAAVSG LVALELIKVV GGYPADAYKN
     CFLNLAIPIM VFTETAEVRR TEIRNGISFT IWDRWTIYGK EDFTLLDFIN AVREKYGIEP
     TMVVQGVKML YVPVMPGHIK RLKLTMQKLV KPSADKKYVD LTVSFAPETD GEEDLPGPPV
     RYYFVQEDN
//