SAE2_XENTR
ID SAE2_XENTR Reviewed; 641 AA.
AC Q28GH3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=SUMO-activating enzyme subunit 2;
DE EC=2.3.2.-;
DE AltName: Full=Ubiquitin-like 1-activating enzyme E1B;
DE AltName: Full=Ubiquitin-like modifier-activating enzyme 2;
GN Name=uba2; Synonyms=sae2, uble1b; ORFNames=TEgg032e11.1;
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=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2006) 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: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Shuttles between the cytoplasm and the nucleus, sumoylation is
CC required either for nuclear translocation or nuclear retention.
CC {ECO:0000250}.
CC -!- PTM: Sumoylated with SUMO1 and SUMO2/3 and by UBC9. Sumoylation at Lys-
CC 236 inhibits enzymatic activity. Sumoylation at the C-terminal lysine
CC cluster plays an essential role in nuclear trafficking (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000305}.
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DR EMBL; CR761388; CAJ82171.1; -; mRNA.
DR EMBL; BC123969; AAI23970.1; -; mRNA.
DR RefSeq; NP_001017091.1; NM_001017091.2.
DR AlphaFoldDB; Q28GH3; -.
DR SMR; Q28GH3; -.
DR STRING; 8364.ENSXETP00000058805; -.
DR DNASU; 549845; -.
DR GeneID; 549845; -.
DR KEGG; xtr:549845; -.
DR CTD; 10054; -.
DR Xenbase; XB-GENE-977709; uba2.
DR eggNOG; KOG2013; Eukaryota.
DR InParanoid; Q28GH3; -.
DR OrthoDB; 686413at2759; -.
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 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000002374; Expressed in egg cell and 17 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
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; IPR019572; UBA_E1_SCCH.
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 Pfam; PF10585; UBA_e1_thiolCys; 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; Cytoplasm; Isopeptide bond; Metal-binding; Nucleotide-binding;
KW Nucleus; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..641
FT /note="SUMO-activating enzyme subunit 2"
FT /id="PRO_0000268875"
FT REGION 546..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..605
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"
FT CROSSLNK 190
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 236
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250"
FT CROSSLNK 257
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 610
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 612
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 623
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 641 AA; 70999 MW; 11180F7C8B486A41 CRC64;
MAMIGALPKE LAEAVSTSRL LVVGAGGIGC ELLKNLVLTG FINLDVIDLD TIDVSNLNRQ
FLFQKKHVGR SKAQVAKESV LQFCPEANIT AYHDSIMNPD YNVEFFKQFT MVMNALDNNA
ARNHVNRMCL AAGIPLIESG TAGYLGQVTV VKKGVTECYE CQPKPTQKTF PGCTIRNTPS
EPIHCIVWAK YLFNQLFGEE DADQEVAPDI ADPEAAWDPT QAAERANASN VDGDIKRVST
KQWAKSTGYD PIKLFNKLFR DDIKYLLTMD RLWRKRKPPV PLEWSSLHNK ENCSETQNES
SLQGLKDQKV LDVTSCAQLF SKSVETLREQ LREKGNGAEL VWDKDDPPAM DFVTAAANLR
MHIFSMNMKS RFDVKSMAGN IIPAIATTNA VISGLIVLEG LKILSGNTEQ CRTVFLNKQP
NPRKKLLVPC SLDPPNPSCY VCAIKPEVTV KLNVHKVTVQ MLQDKILKEK FAMVAPDVQI
EDGKGTILIS SEAGETDANN NRKISEFGIR NSSQLQADDF LQDYTLMINI LHSDEMEKDV
DFEVVGDVPE KGPQKPSEQS VKNITNGSDD GAQPSTSKAQ DQDDVLIVDS DEESPSSSNA
DINMDSASLK RKLPEEETIS STKRKRLEPP VEEDDDIIAL D
