UBA3_SCHPO
ID UBA3_SCHPO Reviewed; 444 AA.
AC Q09765;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=NEDD8-activating enzyme E1 catalytic subunit;
DE EC=6.2.1.64;
DE AltName: Full=Ubiquitin-activating enzyme E1 3;
GN Name=uba3; ORFNames=SPAC24H6.12c;
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 INTERACTION WITH BUT1 AND BUT2.
RX PubMed=14623327; DOI=10.1016/j.bbrc.2003.10.058;
RA Yashiroda H., Tanaka K.;
RT "But1 and But2 proteins bind to Uba3, a catalytic subunit of E1 for
RT neddylation, in fission yeast.";
RL Biochem. Biophys. Res. Commun. 311:691-695(2003).
CC -!- FUNCTION: Catalytic 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-
CC cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8
CC protein]-yl-L-cysteine.; EC=6.2.1.64;
CC -!- PATHWAY: Protein modification; protein neddylation.
CC -!- SUBUNIT: Heterodimer of uba3 and ula1. Interacts with NEDD8 and ubc12
CC (By similarity). Interacts with but1 and but2. {ECO:0000250,
CC ECO:0000269|PubMed:14623327}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAA90856.1; -; Genomic_DNA.
DR PIR; T38368; S62414.
DR RefSeq; NP_592940.1; NM_001018341.2.
DR AlphaFoldDB; Q09765; -.
DR SMR; Q09765; -.
DR BioGRID; 278575; 5.
DR STRING; 4896.SPAC24H6.12c.1; -.
DR MaxQB; Q09765; -.
DR PaxDb; Q09765; -.
DR EnsemblFungi; SPAC24H6.12c.1; SPAC24H6.12c.1:pep; SPAC24H6.12c.
DR GeneID; 2542099; -.
DR KEGG; spo:SPAC24H6.12c; -.
DR PomBase; SPAC24H6.12c; uba3.
DR VEuPathDB; FungiDB:SPAC24H6.12c; -.
DR eggNOG; KOG2015; Eukaryota.
DR HOGENOM; CLU_013325_13_1_1; -.
DR InParanoid; Q09765; -.
DR OMA; LENYMMY; -.
DR PhylomeDB; Q09765; -.
DR Reactome; R-SPO-8951664; Neddylation.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00885; -.
DR PRO; PR:Q09765; -.
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; IBA:GO_Central.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
DR Gene3D; 1.10.10.520; -; 1.
DR InterPro; IPR014929; E2-binding.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR030468; Uba3.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR PANTHER; PTHR10953:SF6; PTHR10953:SF6; 1.
DR Pfam; PF08825; E2_bind; 1.
DR Pfam; PF00899; ThiF; 1.
DR SMART; SM01181; E2_bind; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..444
FT /note="NEDD8-activating enzyme E1 catalytic subunit"
FT /id="PRO_0000194949"
FT ACT_SITE 205
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 54..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 444 AA; 48942 MW; D1734FE0DA61117D CRC64;
MPSSDVCKAG SHRHSGWIQS LKKPGPFNLD APENPEETLK SAFSSKILII GAGGLGCEIL
KDLALSGFRD LSVIDMDTID ITNLNRQFLF NESNIDEPKA NVAASMIMKR IPSTVVTPFY
GKIQDKTIEF YKEFKLIICG LDSVEARRWI NSTLVAIAKT GDLIPLVDGG SEGLKGQARV
IIPTITSCYE CSLDMLTPKI SYPICTLANT PRLPEHCVEW AYLLEWPRVF LNASVDSFSK
QEVFEPLDGK NSNFEPDNIR HIDWLVKRSI ERANKFQIPS SSINRFFVQG IVKRIIPAVA
STNAIIAASC CNEALKILTE SNPFLDNYMM YVGEDGAYTY TFNLEKRSDC PVCGVLSEVY
DISASSTVTL KDILNHYSKS YNLQNPSVST AAGTPLYLAS PPALQVATSK NLSQPILSIT
SVDVNLVITD KNLSTSLSVQ LREC
