ID   A0A137P917_CONC2        Unreviewed;       529 AA.
AC   A0A137P917;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=NEDD8-activating enzyme E1 regulatory subunit {ECO:0000256|PIRNR:PIRNR039099};
GN   ORFNames=CONCODRAFT_84636 {ECO:0000313|EMBL:KXN71507.1};
OS   Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS   (Delacroixia coronata).
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC   Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC   Ancylistaceae; Conidiobolus.
OX   NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN71507.1, ECO:0000313|Proteomes:UP000070444};
RN   [1] {ECO:0000313|EMBL:KXN71507.1, ECO:0000313|Proteomes:UP000070444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN71507.1,
RC   ECO:0000313|Proteomes:UP000070444};
RX   PubMed=25977457; DOI=10.1093/gbe/evv090;
RA   Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA   Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA   Spatafora J.W., Berbee M.L.;
RT   "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT   Walls of Algal Ancestors of Land Plants.";
RL   Genome Biol. Evol. 7:1590-1601(2015).
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}.
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DR   EMBL; KQ964473; KXN71507.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137P917; -.
DR   STRING; 796925.A0A137P917; -.
DR   EnsemblFungi; KXN71507; KXN71507; CONCODRAFT_84636.
DR   OMA; KLITHQY; -.
DR   OrthoDB; 5488891at2759; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000070444; 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:UP000070444};
KW   Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR039099}.
FT   DOMAIN          8..528
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   529 AA;  60399 MW;  44452D8156FE7676 CRC64;
     MDFKKQKYDR QLRLWNKSGQ SQLESSNIAL FNASATGTEA LKNLVLPGIK SFTIFDTKLV
     TQKDISKNFF IDVDKVNEST KRGALITELL GELNDMVTGT YEDIDLHNYL KTKPDQLTQF
     TLIILSKELD TSEEDLIQLS ELCEANNIPL ILTEAVGFVG YLKVAAQEHT IVETHPDSLV
     DLRLVDPFAE LIEFTESFGN IDEIQDADKF NQIPSVILLL HYLQKWKNSN EGRVPSNYKE
     KKQFKETLPV LKKEFVDLDN LSEALEYVNF HVKPYQVPRD ILALFDSHDL NLAQNSSNFW
     VLVKSLKQYY ENEGEGKYLP VTGAIPDIRT STDSYIKLKQ IYQQKAESDK VNFLNYLTKN
     LQELGRPEDF IEADDVTIFC KHSSYLKVQN YDKIHKEYNE TINVKQSLFN QNEDTWFYIA
     LLARHKFIKE HSRLPNHEVD TEAFNADIAT LESIITPIIN SWGISDTSAL KNYLVEVSRS
     GEFELTTTAS VIGGLIAQES IKLITRQYVP IEGVALFNGV KGSISTFKI
//