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Database: UniProt
Entry: A0A1S8VU12_9FUNG
LinkDB: A0A1S8VU12_9FUNG
Original site: A0A1S8VU12_9FUNG 
ID   A0A1S8VU12_9FUNG        Unreviewed;       518 AA.
AC   A0A1S8VU12;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=NEDD8-activating enzyme E1 regulatory subunit {ECO:0000256|PIRNR:PIRNR039099};
GN   ORFNames=BSLG_04529 {ECO:0000313|EMBL:OON05636.1};
OS   Batrachochytrium salamandrivorans.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=1357716 {ECO:0000313|EMBL:OON05636.1, ECO:0000313|Proteomes:UP000189906};
RN   [1] {ECO:0000313|EMBL:OON05636.1, ECO:0000313|Proteomes:UP000189906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS {ECO:0000313|EMBL:OON05636.1,
RC   ECO:0000313|Proteomes:UP000189906};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme.
CC       {ECO:0000256|PIRNR:PIRNR039099}.
CC   -!- PATHWAY: Protein modification; protein neddylation.
CC       {ECO:0000256|ARBA:ARBA00005032, ECO:0000256|PIRNR:PIRNR039099}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006868,
CC       ECO:0000256|PIRNR:PIRNR039099}.
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:OON05636.1}.
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DR   EMBL; LYON01000738; OON05636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8VU12; -.
DR   STRING; 1357716.A0A1S8VU12; -.
DR   VEuPathDB; FungiDB:BSLG_04529; -.
DR   OrthoDB; 5488891at2759; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000189906; Unassembled WGS sequence.
DR   GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR030667; APP-BP1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953:SF29; NEDD8-ACTIVATING ENZYME E1 REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   PIRSF; PIRSF039099; APP-BP1; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000189906};
KW   Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR039099}.
FT   DOMAIN          8..516
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   518 AA;  57474 MW;  A0AEE299D2B02516 CRC64;
     MDGHSQKYDR QLRLWQAHGQ SILQKSHICL LNGSAVGAET LKNLILPGVG SFTVVDQGLV
     TGEQAGRNFF LDTVSIGKSR SESLVYFLGE LNDDVIGKAV VRCPSEIISS SPEFFNQFSL
     VIATEICEKD MRKLSEICWS RSIALIIIKS HGFFGYCRLV KPEHTIIERH DAPGSDFRFD
     CPFPALVSHV NDINIDTMDS MGASHVPYVA LILKALLNWK SKNDGALPSN SLEKAAFRHE
     ITLLKHPSAM DDENIVEALS MAYKAYSETK IPSEVVAILG DPKTTNLSAT SSDFWLLVAA
     LKRFTELEGN GLLPVSGVVP DMKADTDSFI KLQRIYRTKA HEDRVCIRRH LDTLLNSVGR
     DLSSINDDQV EIFSKNASTL RLIRFRSIES EYANSLAGTY VDDENIAYYW LLRAVDRFRD
     VYERYPGSCI QDIDTDTQSL GVLVSQLHQE NNVSGVTINL DQTSEIVRAG GCELHNIASI
     IGGIASQEAI KLLTGQYTPV DNTVIFNGIR SAFSVFKL
//
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