ID   A0A4X2LHU7_VOMUR        Unreviewed;      1011 AA.
AC   A0A4X2LHU7;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Ubiquitin like modifier activating enzyme 7 {ECO:0000313|Ensembl:ENSVURP00010023523.1};
GN   Name=UBA7 {ECO:0000313|Ensembl:ENSVURP00010023523.1};
OS   Vombatus ursinus (Common wombat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Vombatidae; Vombatus.
OX   NCBI_TaxID=29139 {ECO:0000313|Ensembl:ENSVURP00010023523.1, ECO:0000313|Proteomes:UP000314987};
RN   [1] {ECO:0000313|Proteomes:UP000314987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Yazar S.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSVURP00010023523.1}
RP   IDENTIFICATION.
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, ECO:0000256|RuleBase:RU000519}.
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DR   AlphaFoldDB; A0A4X2LHU7; -.
DR   STRING; 29139.ENSVURP00010023523; -.
DR   Ensembl; ENSVURT00010026774.1; ENSVURP00010023523.1; ENSVURG00010018001.1.
DR   GeneTree; ENSGT00940000161447; -.
DR   OMA; FWSGHRK; -.
DR   OrthoDB; 20494at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000314987; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019782; F:ISG15 activating enzyme activity; IEA:Ensembl.
DR   GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR   GO; GO:0032020; P:ISG15-protein conjugation; IEA:Ensembl.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd01491; Ube1_repeat1; 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; IPR033127; UBQ-activ_enz_E1_Cys_AS.
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:SF143; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 7; 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.
DR   PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU000519};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW   Reference proteome {ECO:0000313|Proteomes:UP000314987};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU000519}.
FT   DOMAIN          878..1006
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
FT   ACT_SITE        595
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   1011 AA;  113395 MW;  4AF2D9B5A0CB9E30 CRC64;
     MGDLKTYLDI NEQLYSRQLY VLGTEAMRRL RGSSMLVSGM KGLGVEIAKN LVLAGVGRLT
     LRDPSPTCWM DLASQFFLSE KDIGQNRAKA SLPHLAQLNS DVYISTYDGP LTETVLRGFQ
     VVVLTDSTLK EQLQVGSLCH EHGVHFLVAS TRGLVGQLFC DFGEKFIIHD PSEAEPLQSN
     IGHISQGSPG ILTVLEENGH RFQDGDWVTF SDIEGMTELN DCGPLPIRVR DKWTLEIGDT
     TAFSPYLRSG AITQVKRSQT RSYEALPLSL HQPRIMAANL QEAERARCLH QAFRALHKYQ
     AETGHLPRPW CLEDANELVI LAQGLEPLQG DNGKKVNEPL DEALVRKFAM TSTGDLSPIN
     SVFGGMAAQE MLKAASGKFI PLDQWLYFDA LECLPEDGKP PLRPEACAPR NCRYDGQIAV
     FGDDFQKNLG KQCYFLVGAG AIGCELLKTF AMLGLGAGQG GGITVTDMDT VELSNLSRQF
     LFHSWDLNKP KSEAAALAVR SMNPALSVTA HTKELGPDTE HVFGDDFFSS LDGVASALDS
     FQARKYVSER CIHYMKPMLE SGTQGTQGSA AIFVPCLTQP YSTSSEDAET AYPVCTLRHF
     PSTIEHTLQW AWNEFEGLFR LPAEMINRYL QEPDFLERME GPQALDYLKT ASLSFLSPPQ
     GWQECVAWAW GRWQHCFHDS ITHLLQYFPH DKVNEEGVPF WSGTKRCPQP LEFDISRDTH
     LDYILAAANL YAKTHKLPGS QDRDELRVIL QELPAPAFHL HTHTPIFAND QELEQSSEKW
     GPTYVQELRL ALAKWPGTSL EPQLFEKDDD SNFHMDFIVA ASNLRAENYG IPPADRSKSK
     RIVGAIIPAI ATTTAVVAGL VGLELYKIVM GHRCLSSYRH SYLQLAVPHL SRWIPKAPCV
     QQYHDMRWTC WDRLTVPAPA PGQPEMTLRD LLAYLQEKYD LPVTMLLLDT YLLYSRRWPE
     AQQNLQLRVT ELAHRVTGKE PKMGQKELVF EISCEDEEED TTFPPLHYRL C
//