ID   A0A0V0SC86_9BILA        Unreviewed;       379 AA.
AC   A0A0V0SC86;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 5 {ECO:0000256|ARBA:ARBA00016279};
GN   ORFNames=T07_1100 {ECO:0000313|EMBL:KRX24323.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX24323.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX24323.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX24323.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC       subfamily. {ECO:0000256|ARBA:ARBA00005339}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX24323.1}.
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DR   EMBL; JYDL01000018; KRX24323.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0SC86; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   PANTHER; PTHR10953:SF9; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 5; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630}.
FT   DOMAIN          40..289
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   379 AA;  42279 MW;  3F70FA1B3D8AF641 CRC64;
     MASNEICRAD KSSHGTVGTK TARREKISEM SSEVTDSNPY SRLMALKRMG IVKNYENIRN
     FTIIIVGIGG VGSVVSEMLT RCGIGKLILI DYDKVEMANM NRLFFQPHQA GMSKVEAAKT
     TLQDINPDVE VDSYNCNIIT MENFNKLLHL IKCGSLHGGQ VDLVLSCVDN FEARMAINTA
     CNELNQRWFE SGVSENAVSG HMQFIIPGKT ACFACAPPLV VASKIDEKTL KKEGVCAASL
     PTTMGVIAGL LVQNVLKYLL KFGKVSYYLG YNSLEDFFPT YVIKPNPNCD DTICQMRQKE
     FVFMLDIVLS FEEEESAEPV EMEQKSTLKH SENPWGIEVL EGDLEKSESA GKYNKDEGDE
     ADELDQLSVE ELWKRMKNL
//