SAE2A_XENLA
ID SAE2A_XENLA Reviewed; 641 AA.
AC Q642Q1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=SUMO-activating enzyme subunit 2-A;
DE EC=2.3.2.-;
DE AltName: Full=Ubiquitin-like 1-activating enzyme E1B-A;
DE AltName: Full=Ubiquitin-like modifier-activating enzyme 2-A;
GN Name=uba2-a; Synonyms=sae2-a, uble1b-a;
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 [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-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}.
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DR EMBL; BC081199; AAH81199.1; -; mRNA.
DR RefSeq; NP_001083988.1; NM_001090519.1.
DR AlphaFoldDB; Q642Q1; -.
DR SMR; Q642Q1; -.
DR DNASU; 399235; -.
DR GeneID; 399235; -.
DR KEGG; xla:399235; -.
DR CTD; 399235; -.
DR Xenbase; XB-GENE-977715; uba2.L.
DR OMA; VQWDTLL; -.
DR OrthoDB; 686413at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 399235; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0031510; C:SUMO activating enzyme complex; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
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; IPR032426; UBA2_C.
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 Pfam; PF16195; UBA2_C; 1.
DR PIRSF; PIRSF039133; SUMO_E1B; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc.
FT CHAIN 1..641
FT /note="SUMO-activating enzyme subunit 2-A"
FT /id="PRO_0000268873"
FT REGION 546..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10132"
FT BINDING 24..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 56..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 95..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 117..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 641 AA; 70805 MW; 5A0DCF49447FAAC6 CRC64;
MAVIGALPKE VAEAVSASRL LVVGAGGIGC ELLKNLVLTG FTNLDVIDLD TIDVSNLNRQ
FLFQKKHVGR SKAQVAKESV LQFCPDANIT AYHDSIMNPD YNVEFFKQFT MAMNALDNNA
ARNHVNRMCL AAGIPLIESG TAGYLGQVSV IKKGVTECYE CQPKPTQKTF PGCTIRNTPS
EPIHCIVWAK YLFNQLFGEE DADQEVAPDI ADPEAAWDPT KAAERANASN VDGDIKRVST
KQWAKSTGYD PIKLFNKLFR DDIKYLLTMD RLWRKRKPPI PLEWASLHNK ENCSEIQNES
SLLGLKDQKV LNVASYAQLF SKSVETLREQ LREKGDGAEL VWDKDDVPAM DFVTAAANLR
MHIFSMNMKS KFDVKSMAGN IIPAIATTNA VISGLIVLEG LKILSGNTEQ CRTVFLNKQP
NPRKKLLVPC SLDPPNPSCY VCAIKPEVTV KLNVHKVTVQ MLQDKILKEK FAMVAPDVQI
EDGKGTILIS SEAGETDANN HRKISEFGIR NSSQLQADDF LQDYTLMMNI LHSDEMEKDV
DFEVVGDVPE KGPQKPPEES VKNITNGSDD GAQPSTSKAQ DQDDVLIVDS DEESPSSSNA
DVGMESASLK RKLPDEEAVS STKRKRIEPP VEEDDDIIAL D
