ID A0A3Q2E553_CYPVA Unreviewed; 645 AA.
AC A0A3Q2E553;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=SUMO-activating enzyme subunit 2 {ECO:0000256|PIRNR:PIRNR039133};
DE EC=2.3.2.- {ECO:0000256|PIRNR:PIRNR039133};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000027373.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000027373.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3,
CC and probably SUMO4. It mediates ATP-dependent activation of SUMO
CC proteins followed by formation of a thioester bond between a SUMO
CC protein and a conserved active site cysteine residue on UBA2/SAE2.
CC {ECO:0000256|PIRNR:PIRNR039133}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718, ECO:0000256|PIRNR:PIRNR039133}.
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.
CC {ECO:0000256|ARBA:ARBA00026003}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR039133}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|PIRNR:PIRNR039133}.
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DR RefSeq; XP_015242732.1; XM_015387246.1.
DR AlphaFoldDB; A0A3Q2E553; -.
DR STRING; 28743.ENSCVAP00000027373; -.
DR Ensembl; ENSCVAT00000018526.1; ENSCVAP00000027373.1; ENSCVAG00000013687.1.
DR GeneID; 107092650; -.
DR KEGG; cvg:107092650; -.
DR CTD; 10054; -.
DR GeneTree; ENSGT00550000074924; -.
DR OMA; RFDIKQM; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000265020; Unplaced.
DR GO; GO:0031510; C:SUMO activating enzyme complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019948; F:SUMO activating enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0033334; P:fin morphogenesis; IEA:Ensembl.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniRule.
DR GO; GO:0061035; P:regulation of cartilage development; IEA:Ensembl.
DR GO; GO:0061074; P:regulation of neural retina development; IEA:Ensembl.
DR CDD; cd01489; Uba2_SUMO; 1.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 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:SF5; SUMO-ACTIVATING ENZYME SUBUNIT 2; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 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; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR039133};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR039133,
KW ECO:0000256|PIRSR:PIRSR039133-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR039133}; Nucleus {ECO:0000256|PIRNR:PIRNR039133};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW Ubl conjugation {ECO:0000256|PIRNR:PIRNR039133};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR039133};
KW Zinc {ECO:0000256|PIRNR:PIRNR039133, ECO:0000256|PIRSR:PIRSR039133-3}.
FT DOMAIN 8..419
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 449..536
FT /note="Ubiquitin/SUMO-activating enzyme ubiquitin-like"
FT /evidence="ECO:0000259|Pfam:PF14732"
FT DOMAIN 546..639
FT /note="SUMO-activating enzyme subunit 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16195"
FT REGION 203..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-1,
FT ECO:0000256|PROSITE-ProRule:PRU10132"
FT BINDING 25..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 57..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 96..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 118..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
SQ SEQUENCE 645 AA; 71120 MW; 171776B170D2F251 CRC64;
MVQLVGSLRK ELADSLSSCK VLVVGAGGIG CELLKNLVLT GFKNIDVIDL DTIDVSNLNR
QFLFQKKHVG KSKAEVAKES ALQFCPTANI TAYHDSIMNP DYNVEFFRKF SLVMNALDNR
AARNHVNRMC LAADIPLIES GTAGYLGQVT VIKKGMTECY ECVPKPAQKT FPGCTIRNTP
SEPIHCIVWA KYLFNQLFGE EDADQEVSPD TADPEAAWNP EETAARATAS EKDGDIRRVS
TKEWAKSTGY DPIKVFNKLF KDDIMYLLTM DKLWKKRKAP TPLDWQQLEN SARPQEESPA
SSGLKDQQVL DVWGYCQLFR HSVETLRSQL QEKGAGAELV WDKDDPPAMD FVTAAANLRM
NIFSMNMKSR FDVKSMAGNI IPAIATTNAV IAGLIVLEGL KILSGELESC RSIFLNKCPN
LRKKLLVPCI LDKPSPNCYV CASKPEVTVK VNVQKTTVLS LQDKILKERF GMVAPDVQIE
DGKGTILISS EEGETEANNN KFLSEFGIRN GSRLQADDFL QDYTLLINVL HTEELERDVE
FEVVGEAPDK APPPQSNKEE VNSITNGNKD SAQPSTSCKV TADDDDLMII DSDEEVGAPS
SSAAVASGTK RKHPDSETGE ASTKRPRTDQ SAATNYDDDD IIALD
//
