SAE2_DICDI
ID SAE2_DICDI Reviewed; 661 AA.
AC Q54L40;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=SUMO-activating enzyme subunit 2;
DE EC=2.3.2.-;
DE AltName: Full=Ubiquitin-like 1-activating enzyme E1B;
GN Name=uba2; Synonyms=sae2; ORFNames=DDB_G0286919;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: The dimeric enzyme acts as an E1 ligase for sumo. It mediates
CC ATP-dependent activation of sumo and formation of a thioester with a
CC conserved cysteine residue on sae2 (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Heterodimer of sae1 and sae2. The complex binds sumo via sae2
CC (By similarity). {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; AAFI02000092; EAL63957.1; -; Genomic_DNA.
DR RefSeq; XP_637463.1; XM_632371.1.
DR AlphaFoldDB; Q54L40; -.
DR SMR; Q54L40; -.
DR STRING; 44689.DDB0302360; -.
DR PaxDb; Q54L40; -.
DR PRIDE; Q54L40; -.
DR EnsemblProtists; EAL63957; EAL63957; DDB_G0286919.
DR GeneID; 8625862; -.
DR KEGG; ddi:DDB_G0286919; -.
DR dictyBase; DDB_G0286919; uba2.
DR eggNOG; KOG2013; Eukaryota.
DR HOGENOM; CLU_013325_7_3_1; -.
DR InParanoid; Q54L40; -.
DR OMA; VQWDTLL; -.
DR PhylomeDB; Q54L40; -.
DR Reactome; R-DDI-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-DDI-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR UniPathway; UPA00886; -.
DR PRO; PR:Q54L40; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031510; C:SUMO activating enzyme complex; ISS:dictyBase.
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:dictyBase.
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:dictyBase.
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; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
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; PF10585; UBA_e1_thiolCys; 1.
DR PIRSF; PIRSF039133; SUMO_E1B; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 3: Inferred from homology;
KW ATP-binding; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc.
FT CHAIN 1..661
FT /note="SUMO-activating enzyme subunit 2"
FT /id="PRO_0000328132"
FT REGION 545..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 29..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 61..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 122..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 436
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"
SQ SEQUENCE 661 AA; 74656 MW; CA7FB5EE3FBD9E1F CRC64;
MSERYSHIIQ ALGQSTFDKI QTCKILVVGA GGIGCELLKN LVLTGFKNID IIDLDTIDIS
NLNRQFLFRK QHIGMSKAKI AKESVMKYNE QVNITAHHGD VKSSEFGSEF FKQFDLVMNA
LDNISARRHV NRLCLSVDVP MIESGTAGYL GQVSVIRKGK TECFECQPIA VPKQFAVCTI
RTNPSAPIHC IVWAKMLFGK LFGPKDDDGG GDSSSLTDLD NNIIHGTEEL GNIKRDEQLL
IEKEKGFKRW VFHKIFHTDI ETLIHMPDLW KDKQPPTSLK LDEILSSKEV SQAEEEGDQL
IFKLPDQKQW TFKENVEVFL DCLEKLKQQF DQSNSKPMTW DKDDELALSF VCSASNIRSK
IFGIPMKSRF DVKSMAGNII PAIATTNAVI GGLIVMEAIK VVDGRFDQCL STYLYQLPSG
KRLLMPTQLE PQNPKCFVCN RSFIICRLNT EKTTISQFID HVLKKSLAVN EPILTVGNDI
IYEGGDQDLS KEEIEQRSKI EKKTLATHRL TNDTSLVVED YNQDFQITIT IQHTTDFDED
TKKLKKQQQK EKDQKEGKTT TIEKEEDDKF FEIIGKTSQT TTTTTTTTTT TESDNNSNNN
KNNNNNNDVE EDDGFMFIED QPSSTTTSSA TPSISKKRKE IDTNESEDLD SSKKLKSNLQ
D
