ID   A0A0V0SCA5_9BILA        Unreviewed;       385 AA.
AC   A0A0V0SCA5;
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:KRX24321.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX24321.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX24321.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX24321.1};
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:KRX24321.1}.
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   EMBL; JYDL01000018; KRX24321.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0SCA5; -.
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   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"
SQ   SEQUENCE   385 AA;  42986 MW;  E493226E1392B84F 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 GKYNKVIILH
     MDEGDEADEL DQLSVEELWK RMKNL
//