SAE2_CAEEL
ID SAE2_CAEEL Reviewed; 582 AA.
AC Q9NAN1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=SUMO-activating enzyme subunit uba-2;
DE EC=2.3.2.-;
GN Name=uba-2; ORFNames=W02A11.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=11806825; DOI=10.1186/gb-2001-3-1-research0002;
RA Jones D., Crowe E., Stevens T.A., Candido E.P.M.;
RT "Functional and phylogenetic analysis of the ubiquitylation system in
RT Caenorhabditis elegans: ubiquitin-conjugating enzymes, ubiquitin-activating
RT enzymes, and ubiquitin-like proteins.";
RL Genome Biol. 3:RESEARCH0002.1-RESEARCH0002.15(2002).
RN [3]
RP FUNCTION.
RX PubMed=15107848; DOI=10.1038/ng1336;
RA Zhang H., Smolen G.A., Palmer R., Christoforou A., van den Heuvel S.,
RA Haber D.A.;
RT "SUMO modification is required for in vivo Hox gene regulation by the
RT Caenorhabditis elegans Polycomb group protein SOP-2.";
RL Nat. Genet. 36:507-511(2004).
RN [4]
RP FUNCTION.
RX PubMed=15990876; DOI=10.1038/sj.emboj.7600726;
RA Poulin G., Dong Y., Fraser A.G., Hopper N.A., Ahringer J.;
RT "Chromatin regulation and sumoylation in the inhibition of Ras-induced
RT vulval development in Caenorhabditis elegans.";
RL EMBO J. 24:2613-2623(2005).
CC -!- FUNCTION: The dimeric enzyme acts as an E1 ligase for smo-1. It
CC mediates ATP-dependent activation of smo-1 and formation of a thioester
CC with a conserved cysteine residue on uba-2 (Probable).
CC {ECO:0000305|PubMed:11806825, ECO:0000305|PubMed:15107848,
CC ECO:0000305|PubMed:15990876}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Heterodimer with aos-1.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; Z82062; CAB54319.4; -; Genomic_DNA.
DR PIR; T26072; T26072.
DR RefSeq; NP_001293154.1; NM_001306225.1.
DR AlphaFoldDB; Q9NAN1; -.
DR SMR; Q9NAN1; -.
DR STRING; 6239.W02A11.4; -.
DR iPTMnet; Q9NAN1; -.
DR EPD; Q9NAN1; -.
DR PaxDb; Q9NAN1; -.
DR PeptideAtlas; Q9NAN1; -.
DR PRIDE; Q9NAN1; -.
DR EnsemblMetazoa; W02A11.4.1; W02A11.4.1; WBGene00006700.
DR GeneID; 24104970; -.
DR KEGG; cel:CELE_W02A11.4; -.
DR UCSC; W02A11.4; c. elegans.
DR CTD; 24104970; -.
DR WormBase; W02A11.4; CE40719; WBGene00006700; uba-2.
DR eggNOG; KOG2013; Eukaryota.
DR GeneTree; ENSGT00550000074924; -.
DR HOGENOM; CLU_013325_7_4_1; -.
DR InParanoid; Q9NAN1; -.
DR OMA; VQWDTLL; -.
DR OrthoDB; 686413at2759; -.
DR PhylomeDB; Q9NAN1; -.
DR Reactome; R-CEL-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-CEL-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR UniPathway; UPA00886; -.
DR PRO; PR:Q9NAN1; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006700; Expressed in adult organism and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031510; C:SUMO activating enzyme complex; ISS:WormBase.
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:WormBase.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IGI:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IDA:WormBase.
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; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR PANTHER; PTHR10953:SF5; PTHR10953:SF5; 1.
DR Pfam; PF00899; ThiF; 1.
DR Pfam; PF14732; UAE_UbL; 1.
DR PIRSF; PIRSF039133; SUMO_E1B; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc.
FT CHAIN 1..582
FT /note="SUMO-activating enzyme subunit uba-2"
FT /id="PRO_0000270190"
FT REGION 204..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 20..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 52..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 91..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 113..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 582 AA; 64826 MW; 318CDD98FEA04BD1 CRC64;
MPSWREKHEK IVQSKILVIG AGGIGCELLK NLAVTGFRKV HVIDLDTIDI SNLNRQFLFR
KEHVSSSKAA TATQVVKQFC PQIELTFDHD SIFEKKYNME FFQAYDIVLN ALDNRAARNY
VNRMCHAANR PLIDSGSGGY FGQVSVIMRG KTECYECVDK PVQQTTYPGC TIRNTPSEHI
HCTVWAKHVF NQLFGEVDID DDVSPDMDAV DPDNTEAVTT EKEKEAMKEE PAPVGTRQWA
ESVDYDAAKV FDKLFLHDIE YLCKMEHLWK QRKRPSPLEF HTASSTGGEP QSLCDAQRDD
TSIWTLSTCA KVFSTCIQEL LEQIRAEPDV KLAFDKDHAI IMSFVAACAN IRAKIFGIPM
KSQFDIKAMA GNIIPAIAST NAIVAGIIVT EAVRVIEGST VICNSSIATT QSNPRGRIFG
GDATNPPNPR CFVCSEKREV FIYVNPDTMT VGGLCEKVLK QKLNMLAPDV MDSATSRIIV
SSDGDTDDLL PKKLAEVSIE DGAILSCDDF QQEMEIKLFI KKGDRLAGDD FEVARSEKEP
EPDDRKRKAD GSEEPEAKRQ KVEEKDDKNG NEAVAEITET MA
