UBA2_SCHPO
ID UBA2_SCHPO Reviewed; 628 AA.
AC O42939;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Ubiquitin-activating enzyme E1-like;
DE AltName: Full=Pmt3-activating enzyme subunit 2;
GN Name=uba2; ORFNames=SPBC16H5.03c;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559 AND SER-563, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: The dimeric enzyme acts as a SUMO/pmt3 E1 ligase. It mediates
CC ATP-dependent activation of pmt3 and formation of a thioester with a
CC conserved cysteine residue on aos1 (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Heterodimer of uba2 and aos1. The complex binds pmt3 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA17901.1; -; Genomic_DNA.
DR PIR; T39623; T39623.
DR RefSeq; NP_595945.1; NM_001021853.2.
DR AlphaFoldDB; O42939; -.
DR SMR; O42939; -.
DR BioGRID; 276511; 3.
DR DIP; DIP-35490N; -.
DR IntAct; O42939; 3.
DR STRING; 4896.SPBC16H5.03c.1; -.
DR iPTMnet; O42939; -.
DR MaxQB; O42939; -.
DR PaxDb; O42939; -.
DR PRIDE; O42939; -.
DR EnsemblFungi; SPBC16H5.03c.1; SPBC16H5.03c.1:pep; SPBC16H5.03c.
DR GeneID; 2539967; -.
DR KEGG; spo:SPBC16H5.03c; -.
DR PomBase; SPBC16H5.03c; uba2.
DR VEuPathDB; FungiDB:SPBC16H5.03c; -.
DR eggNOG; KOG2013; Eukaryota.
DR HOGENOM; CLU_013325_7_3_1; -.
DR InParanoid; O42939; -.
DR OMA; VQWDTLL; -.
DR PhylomeDB; O42939; -.
DR Reactome; R-SPO-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-SPO-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR UniPathway; UPA00886; -.
DR PRO; PR:O42939; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0031510; C:SUMO activating enzyme complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019948; F:SUMO activating enzyme activity; IDA:PomBase.
DR GO; GO:0061656; F:SUMO conjugating enzyme activity; EXP:PomBase.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IDA:PomBase.
DR Gene3D; 1.10.10.520; -; 1.
DR Gene3D; 3.50.50.80; -; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR028077; UAE_UbL_dom.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR030661; Uba2.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR PANTHER; PTHR10953:SF5; PTHR10953:SF5; 1.
DR Pfam; PF00899; ThiF; 1.
DR Pfam; PF14732; UAE_UbL; 1.
DR Pfam; PF10585; UBA_e1_thiolCys; 1.
DR PIRSF; PIRSF039133; SUMO_E1B; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SUPFAM; SSF69572; SSF69572; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1..628
FT /note="Ubiquitin-activating enzyme E1-like"
FT /id="PRO_0000248628"
FT REGION 597..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 35..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 64..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 125..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 628 AA; 70614 MW; AAC9247BB8D2F634 CRC64;
MPTLMQLSND MKPLTFVEAL RNFKSAKVLL VGAGGIGCEL LKNLLMSGVK EVHIIDLDTI
DLSNLNRQFL FRKKHVKQPK AIVAAKTASS FNPNVKLEAY HANIKEDRFN VAWFRQFDLV
FNALDNLDAR RHVNKQCLLA SVPLIESGTT GFLGQVQVII HGKTECYDCN PKEPPKTYPV
CTIRSTPSQP IHCVVWAKSY FFPQLFSNDQ ESDGIIDNVS ANEMERREIA ELARETTELN
ELRSSIGQSD NGFEKIFTKM FTKDIVRLRE VPDAWTYRSP PKELSYSELL ENAEKATSPW
LNEQNVWNVA ESFAVLRDSI RRLALRSKSS KDDLSFDKDD KDTLDFVAAA ANLRAHVFGI
QQLSEFDIKQ MAGNIIPAIA TTNAVIAGLC ITQAIKVLQG DLNDLKNIYL AKRPTRVLHC
EKTCKPNPYC PTCSFVLLQL GVNDKNMTLR VLVDDILKSR LHYSEEVSVL NDKLIYDPDF
DDNLDKTFDD LGINPAKNTI LTVLGDSAVE KDDDGEEATR VPLLIEVTFI DSNSTEGLPY
QILSNATSIP LKQQPPSNSP EDSQVLTDEI NEVNDFSSSE RIVINLDEYD IIVDSKTSSH
NKQLKRRPSN DTLTQEAKSK KQAKIHTM
