ID   A0A1V9Y4Z1_9STRA        Unreviewed;       523 AA.
AC   A0A1V9Y4Z1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=NEDD8-activating enzyme E1 regulatory subunit {ECO:0000256|PIRNR:PIRNR039099};
GN   ORFNames=ACHHYP_17155 {ECO:0000313|EMBL:OQR80791.1};
OS   Achlya hypogyna.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Achlya.
OX   NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR80791.1, ECO:0000313|Proteomes:UP000243579};
RN   [1] {ECO:0000313|EMBL:OQR80791.1, ECO:0000313|Proteomes:UP000243579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR80791.1,
RC   ECO:0000313|Proteomes:UP000243579};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
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:OQR80791.1}.
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DR   EMBL; JNBR01002870; OQR80791.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9Y4Z1; -.
DR   STRING; 1202772.A0A1V9Y4Z1; -.
DR   OrthoDB; 5488891at2759; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000243579; 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:UP000243579};
KW   Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR039099}.
FT   DOMAIN          7..515
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   523 AA;  57370 MW;  69A478A274BD424A CRC64;
     MATSDKYDRQ LRLWGAMGQR KLMSTKLLLL NAGPTGSEVL KNLVLPGIGN FEICDGNTVC
     EADLGNNFFV TDADLGRPRA QVVTELMLEM NPDVHGTFRH ESAAHVAEYE PSYIGQFNMV
     IATQLPEPAL SALAATCQTN DIPLLIVHSF GLLGHVRLQA PNHTIVDSKP DAPWHDLRIA
     EPFPELLSFA NEFNLEAMNS HEHGHVPYVV ILLQAINEWK AAHDGDLPKT FAAKSEFKAS
     VQAKARGSFG QEVNFLEAVD NAFKAYVLSK DAIPDDVRDV LAHASTLTLT PATSTFWFLA
     RALAGFVATH GTLPHSGHVP DMTAFTASYV ALQKLYMDKA KRDAAVVLAS VRQLLADVDP
     ARAVSEDEVA DYCKHASCTG MLQTRSLAEE TAAVHLDDVD MEEEDSVQSP LIWYFMLRAV
     HRFIAEFGKY PGVHDGPELE QDAKWLLEAA QAIAPEPFPV AWLTLDHARE VCRYAEAEVH
     NVAAVLGGIA AQEAVKIITN QFTPINNTYL FNGITGRACT YKL
//