ID   SAE1_CAEEL              Reviewed;         343 AA.
AC   Q17820;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=SUMO-activating enzyme subunit aos-1;
GN   Name=aos-1; ORFNames=C08B6.9;
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).
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   -!- PATHWAY: Protein modification; protein sumoylation.
CC   -!- SUBUNIT: Heterodimer of aos-1 and uba-2.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000305}.
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DR   EMBL; Z72502; CAA96591.1; -; Genomic_DNA.
DR   PIR; T19082; T19082.
DR   RefSeq; NP_505604.1; NM_073203.4.
DR   AlphaFoldDB; Q17820; -.
DR   SMR; Q17820; -.
DR   BioGRID; 44440; 6.
DR   IntAct; Q17820; 2.
DR   STRING; 6239.C08B6.9; -.
DR   EPD; Q17820; -.
DR   PaxDb; Q17820; -.
DR   PeptideAtlas; Q17820; -.
DR   EnsemblMetazoa; C08B6.9.1; C08B6.9.1; WBGene00000142.
DR   GeneID; 179409; -.
DR   KEGG; cel:CELE_C08B6.9; -.
DR   UCSC; C08B6.9; c. elegans.
DR   CTD; 179409; -.
DR   WormBase; C08B6.9; CE52896; WBGene00000142; aos-1.
DR   eggNOG; KOG2014; Eukaryota.
DR   GeneTree; ENSGT00550000075007; -.
DR   HOGENOM; CLU_002556_4_1_1; -.
DR   InParanoid; Q17820; -.
DR   OMA; TDVWGTF; -.
DR   OrthoDB; 1180926at2759; -.
DR   PhylomeDB; Q17820; -.
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:Q17820; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00000142; Expressed in germ line (C elegans) and 4 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:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR   GO; GO:0016925; P:protein sumoylation; IDA:WormBase.
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   SUPFAM; SSF69572; SSF69572; 1.
PE   3: Inferred from homology;
KW   Ligase; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..343
FT                   /note="SUMO-activating enzyme subunit aos-1"
FT                   /id="PRO_0000270189"
SQ   SEQUENCE   343 AA;  38738 MW;  2897C0F918E881B6 CRC64;
     MEVSKAEQAI YDRQIRLWGM EAQNKIRNSK VLIIGGKQLG AEVAKTLSLA GVDEMHLVDH
     RLVDTEEIGM NFLYDASVDN SKMTKWAASY NFLYNLNRNV KLFIVEEDVL SKNDSEIEEY
     LTKFTLVVVL DESYERTAKV NNICRKHHIR FISGAIYGWI GYAFFDFDGH AYLVKAKSPD
     CLNEEESETG KTSTVVTVDE EFVLETFSYP SFVETLNSDF TAKKIVRKCK RIVPTSYFLV
     KSMLRASSEN KLTGVTENDI EKLIPIWNEE VAAGNHTIDM QPVQPDRFDH LFGPNFGPTA
     ACVGGVIGQE AIKSISEGKN PLRNLFIYTG FESTGFMCNF PPV