ID   ULA1_SCHPO              Reviewed;         517 AA.
AC   Q9UT93;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=NEDD8-activating enzyme E1 regulatory subunit;
DE   AltName: Full=Ubiquitin-activating enzyme E1-like 1;
DE   AltName: Full=Ubiquitin-like activation protein 1;
GN   Name=uba5; Synonyms=ula1; ORFNames=SPAC323.06c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Regulatory subunit of the dimeric uba3-ula1 E1 enzyme. E1
CC       activates NEDD8/ubl1 by first adenylating its C-terminal glycine
CC       residue with ATP, thereafter linking this residue to the side chain of
CC       the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP.
CC       E1 finally transfers NEDD8 to the catalytic cysteine of ubc12 (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein neddylation.
CC   -!- SUBUNIT: Heterodimer of uba3 and ula1. The complex binds NEDD8/ubl1 and
CC       ubc12 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1
CC       subfamily. {ECO:0000305}.
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; CU329670; CAB53409.3; -; Genomic_DNA.
DR   PIR; T38643; T38643.
DR   RefSeq; NP_594376.2; NM_001019797.2.
DR   AlphaFoldDB; Q9UT93; -.
DR   SMR; Q9UT93; -.
DR   BioGRID; 279508; 2.
DR   STRING; 4896.SPAC323.06c.1; -.
DR   MaxQB; Q9UT93; -.
DR   PaxDb; Q9UT93; -.
DR   EnsemblFungi; SPAC323.06c.1; SPAC323.06c.1:pep; SPAC323.06c.
DR   GeneID; 2543075; -.
DR   KEGG; spo:SPAC323.06c; -.
DR   PomBase; SPAC323.06c; uba5.
DR   VEuPathDB; FungiDB:SPAC323.06c; -.
DR   eggNOG; KOG2016; Eukaryota.
DR   HOGENOM; CLU_019618_2_1_1; -.
DR   InParanoid; Q9UT93; -.
DR   OMA; LHEICRY; -.
DR   Reactome; R-SPO-8951664; Neddylation.
DR   UniPathway; UPA00885; -.
DR   PRO; PR:Q9UT93; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019781; F:NEDD8 activating enzyme activity; ISO:PomBase.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR   GO; GO:0045116; P:protein neddylation; ISO:PomBase.
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   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..517
FT                   /note="NEDD8-activating enzyme E1 regulatory subunit"
FT                   /id="PRO_0000194961"
SQ   SEQUENCE   517 AA;  59569 MW;  801C0473A8CF19E3 CRC64;
     MGTSAKMQKY DRQVRLWKAE GQNAIEKSHV CLLYANTVGC EALKNLILPG IGSFAVVDDT
     SVDFSMDGMN FFIQYDQEGK SRARCTASLL QQLNPNVEME YLEMSPEALI DKNIEYFSKF
     SVVLSSNLKE KPLFRLEEYL RSHKIPLLHF NSVGFAGILR ISTHEYTTTQ SQPELPQDLR
     LKNPWPELIN YVKSMDLDNM DSSSLSEIPY IVLIIHVLLK VSPAHAQNSQ EADDCAMFRK
     IMEEYKGKCD SENIEEASSN SWKAFKEYKL PSNVYEVLHD TRCVKIQEDS ESFWIMAHCL
     KMFYDETEFL PLSGLLPDMN CSTQQYVKLQ VIYKEKSEND ILKFKKYVQQ TLKRLNRSVE
     EITDLEIKHF SRNCLNIKVM DFKTMKEEYQ PTSNSVLESS SIDSNSLLPW YLAFRIYDTI
     LEKHGKNYKE AFSDTTKTIS VAQSFLSQIG LEKFFDVVYT AIQELERADG HELHSISSFI
     GGIVAQETIK LLAQQYLPLN NTFVFDGVHS RTETFKL