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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
 
 
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