ID   SAE1_XENLA              Reviewed;         344 AA.
AC   Q8JGT5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=SUMO-activating enzyme subunit 1;
DE   AltName: Full=SUMO-activating enzyme E1 N subunit;
DE   AltName: Full=Ubiquitin-like 1-activating enzyme E1A;
GN   Name=sae1; Synonyms=uble1a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cavenagh M.M., Dasso M.;
RT   "Characterization of SUMO-1 E1 enzyme in Xenopus laevis.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The heterodimer acts as an E1 ligase for sumo1, sumo2, and
CC       sumo3. It mediates ATP-dependent activation of sumo proteins followed
CC       by formation of a thioester bond between a sumo protein and a conserved
CC       active site cysteine residue on uba2/sae2 (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC   -!- SUBUNIT: Heterodimer of sae1 and uba2/sae2. The heterodimer corresponds
CC       to the two domains that are encoded on a single polypeptide chain in
CC       ubiquitin-activating enzyme E1. Interacts with ube2i (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {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; AY099426; AAM47491.1; -; mRNA.
DR   EMBL; BC086263; AAH86263.1; -; mRNA.
DR   RefSeq; NP_001085258.1; NM_001091789.1.
DR   AlphaFoldDB; Q8JGT5; -.
DR   SMR; Q8JGT5; -.
DR   MaxQB; Q8JGT5; -.
DR   DNASU; 443558; -.
DR   GeneID; 443558; -.
DR   KEGG; xla:443558; -.
DR   CTD; 443558; -.
DR   Xenbase; XB-GENE-923367; sae1.L.
DR   OMA; TDVWGTF; -.
DR   OrthoDB; 1180926at2759; -.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 443558; Expressed in blastula and 19 other tissues.
DR   GO; GO:0031510; C:SUMO activating enzyme complex; ISS:UniProtKB.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   PANTHER; PTHR10953; PTHR10953; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SUPFAM; SSF69572; SSF69572; 1.
PE   2: Evidence at transcript level;
KW   Ligase; Nucleus; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..344
FT                   /note="SUMO-activating enzyme subunit 1"
FT                   /id="PRO_0000268870"
SQ   SEQUENCE   344 AA;  38247 MW;  029C153860C064D5 CRC64;
     MVEKEEAVIS EEEAAQYDRQ IRLWGLEAQK RLRTSRVLLV GMRGLGAEVA KNLILAGVKA
     LTLLDHEQVS SEDSRAQFLI PSGSLGQNRA EASLNRARNL NPMVSVEADT ENINQKSDDF
     FTQFDVVCLT SCPSDLLVRV NHICHKHNIK FFTGDVYGYH GSMFADLGEH EFVEEKAKVT
     KAKPLVEDGP EAKKAKIDPT ETILVKKKVQ FCPLKDALEI DWRSEKAKSA LKKTPTDYFL
     LQVLMKFRTD KGRDPQPSSY QEDSELLLQI CSDVLDSLGV SPDLLPKDFA SYCFSEMAPV
     CAVVGGVLGQ EIVKALSLRD APHNNFFFFD GKTSNGIVDC LGSK