ID   SAE1_XENTR              Reviewed;         347 AA.
AC   Q28DS0; A4QNJ2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=SUMO-activating enzyme subunit 1;
DE   AltName: Full=Ubiquitin-like 1-activating enzyme E1A;
GN   Name=sae1; Synonyms=uble1a; ORFNames=TGas081c19.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) 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}.
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DR   EMBL; CR848627; CAJ83949.1; -; mRNA.
DR   EMBL; BC135749; AAI35750.1; -; mRNA.
DR   RefSeq; NP_001016870.1; NM_001016870.2.
DR   AlphaFoldDB; Q28DS0; -.
DR   SMR; Q28DS0; -.
DR   STRING; 8364.ENSXETP00000000333; -.
DR   PaxDb; Q28DS0; -.
DR   DNASU; 549624; -.
DR   Ensembl; ENSXETT00000000333; ENSXETP00000000333; ENSXETG00000000161.
DR   GeneID; 549624; -.
DR   KEGG; xtr:549624; -.
DR   CTD; 10055; -.
DR   Xenbase; XB-GENE-923356; sae1.
DR   eggNOG; KOG2014; Eukaryota.
DR   HOGENOM; CLU_002556_4_0_1; -.
DR   InParanoid; Q28DS0; -.
DR   OrthoDB; 1180926at2759; -.
DR   Reactome; R-XTR-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR   Reactome; R-XTR-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000008143; Chromosome 8.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000000161; Expressed in egg cell and 14 other tissues.
DR   ExpressionAtlas; Q28DS0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031510; C:SUMO activating enzyme complex; ISS:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR   GO; GO:0019948; F:SUMO activating enzyme activity; IBA:GO_Central.
DR   GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
DR   GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
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..347
FT                   /note="SUMO-activating enzyme subunit 1"
FT                   /id="PRO_0000268871"
SQ   SEQUENCE   347 AA;  38776 MW;  FA2435E79E197875 CRC64;
     MVEKEEAVIS EEEAAQYDRQ IRLWGLEAQK RLRTSRVLLV GMRGLGAEVA KNLILAGVKA
     LTLLDHEQVS SEDSRAQFLI PSGSLGQNRA EASLNRARNL NPMVSVEADT ENINQKSDDF
     FTQFDVVCLT SCSRDLLVRV DHICHKHNIK FFTGDVFGYH GYMFADLGEH EFVEEKAKVA
     KVSKAKQEVE DGPEAKKAKI DPTESILVKK KVQFCPLKDA LEIDWHSEKA KSALKKTPTD
     FFLLQVLMKF RTDKKRDPQP SNYQEDSELL LQICSDVLDS LGVSPDLLPK DFASYCFSEM
     APVCAVVGGV LGQEIVKALS QRDAPHNNFF FFDGRSSNGI VDCLGSK