ID   ULA1_DICDI              Reviewed;         520 AA.
AC   Q54JM3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=NEDD8-activating enzyme E1 regulatory subunit;
GN   Name=nae1; Synonyms=appbp1; ORFNames=DDB_G0287965;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Regulatory subunit of the dimeric uba3-nae1 E1 enzyme. E1
CC       activates nedd8 by first adenylating its C-terminal glycine residue
CC       with ATP, thereafter linking this residue to the side chain of the
CC       catalytic cysteine, yielding a nedd8-uba3 thioester and free AMP. E1
CC       finally transfers nedd8 to the catalytic cysteine of ube2m (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein neddylation.
CC   -!- SUBUNIT: Heterodimer of uba3 and nae1. The complex binds nedd8 and
CC       ube2m (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Nae1 and uba3 correspond to the N-terminal and the C-
CC       terminal part of yeast uba3. In yeast the two subunits form a single
CC       polypeptide chain.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000106; EAL63463.1; -; Genomic_DNA.
DR   RefSeq; XP_636963.1; XM_631871.1.
DR   AlphaFoldDB; Q54JM3; -.
DR   SMR; Q54JM3; -.
DR   STRING; 44689.DDB0237981; -.
DR   PaxDb; Q54JM3; -.
DR   EnsemblProtists; EAL63463; EAL63463; DDB_G0287965.
DR   GeneID; 8626383; -.
DR   KEGG; ddi:DDB_G0287965; -.
DR   dictyBase; DDB_G0287965; nae1.
DR   eggNOG; KOG2016; Eukaryota.
DR   HOGENOM; CLU_019618_2_1_1; -.
DR   InParanoid; Q54JM3; -.
DR   OMA; LHEICRY; -.
DR   PhylomeDB; Q54JM3; -.
DR   Reactome; R-DDI-8951664; Neddylation.
DR   UniPathway; UPA00885; -.
DR   PRO; PR:Q54JM3; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0019781; F:NEDD8 activating enzyme activity; ISS:dictyBase.
DR   GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
DR   GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR   GO; GO:0043326; P:chemotaxis to folate; IMP:dictyBase.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR   GO; GO:0045116; P:protein neddylation; ISS:dictyBase.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
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; PTHR10953; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   PIRSF; PIRSF039099; APP-BP1; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..520
FT                   /note="NEDD8-activating enzyme E1 regulatory subunit"
FT                   /id="PRO_0000330898"
FT   REGION          321..334
FT                   /note="Interaction with uba3"
FT                   /evidence="ECO:0000250"
FT   SITE            209
FT                   /note="Interaction with uba3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   520 AA;  59367 MW;  203A77240C506696 CRC64;
     MSTSTTDTDK YDRQLRLWGE DGQSKLERSH ILLLNGSATG TETLKNLVLP GIGSFTVVDN
     KKVTESDLGN NFFVERSSLG KPRATVVCEL LRELNDRVKG FSVEECPIHL INNNISFFKD
     FSLVVANRLS EEALLTLSQY LTEQNIPLLI TNSYGYIGYL RISTPEHQII ESKPDDPIDD
     LRIYNPFKQL VDMADALELD KLNTQQHSHV PYVLLLIKFL KEWRSTHNDK MPETRAEKDE
     FKKFFNSHSW SADEMNFVEG IQNLLKYIQP PRVPGDVQNL LKDPKTNITE NSDDFWVLVA
     ALKEFMTNND NTLPLHGNVP DMTSETHNFI QLQKGYQEKA LADLSEFSGY VDQILTKVGK
     SSISSDLVKK FCKNTRFLNI IRYRTISEEY NQPKTNLIKS ELEQADTVMV FYILLRGIDK
     FYKTYHKYPG SSDDFESDIP LLKTVITQYL AEINISNDLV KDDYIAEFVR FGGSELHNIA
     SLMGGVTSQE IIKLITHQYT PLNNTFIFNG INSTAGSYNL