ID I1M0W3_SOYBN Unreviewed; 638 AA.
AC I1M0W3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=SUMO-activating enzyme subunit {ECO:0000256|PIRNR:PIRNR039133};
GN Name=100794304 {ECO:0000313|EnsemblPlants:KRH20803};
GN ORFNames=GLYMA_13G201500 {ECO:0000313|EMBL:KRH20803.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH20803};
RN [1] {ECO:0000313|EMBL:KRH20803.1, ECO:0000313|EnsemblPlants:KRH20803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH20803};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH20803.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH20803}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH20803};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH20803.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH20803.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718, ECO:0000256|PIRNR:PIRNR039133}.
CC -!- SUBUNIT: Heterodimer. {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 EMBL; CM000846; KRH20803.1; -; Genomic_DNA.
DR RefSeq; XP_003541605.1; XM_003541557.3.
DR AlphaFoldDB; I1M0W3; -.
DR SMR; I1M0W3; -.
DR STRING; 3847.I1M0W3; -.
DR PaxDb; 3847-GLYMA13G27140-1; -.
DR EnsemblPlants; KRH20803; KRH20803; GLYMA_13G201500.
DR GeneID; 100794304; -.
DR Gramene; KRH20803; KRH20803; GLYMA_13G201500.
DR KEGG; gmx:100794304; -.
DR eggNOG; KOG2013; Eukaryota.
DR HOGENOM; CLU_013325_7_4_1; -.
DR InParanoid; I1M0W3; -.
DR OMA; RFDIKQM; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000008827; Chromosome 13.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031510; C:SUMO activating enzyme complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
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; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
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; PF10585; UBA_E1_SCCH; 1.
DR PIRSF; PIRSF039133; SUMO_E1B; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
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 9..433
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 327..369
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT DOMAIN 442..533
FT /note="Ubiquitin/SUMO-activating enzyme ubiquitin-like"
FT /evidence="ECO:0000259|Pfam:PF14732"
FT REGION 592..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-1"
FT BINDING 20..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 52..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 113..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-2"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR039133-3"
SQ SEQUENCE 638 AA; 70979 MW; 74F5747C97B30486 CRC64;
MASSPPSSSA IKDAKVLMVG AGGIGCELLK TLALSGFPDI HIIDMDTIEV SNLNRQFLFR
QFHVGQSKAK VARDAVLKFR PHINITPYHA NVKDPEFNVD FFKQFNVVLN GLDNLDARRH
VNRLCLAANV PLVESGTTGF LGQVTVHVKG KTECYECQPK PAPKTYPVCT ITSTPSKFVH
CIVWAKDLLF AKLFGDKNQD NDLNVRSSDA ASSSKNVEDV FERRKDEDID QYGRKIFDHV
FGYNIELALS NEETWKNRNR PKPIYSKDVL SDEPAQQNGN LEKKYESDEL PVSAMASLGM
KNPQDIWSLK ENSRIFLEAF RLFFTKREKE IGNLSFDKDD QLAVEFVTAA ANIRAASFGI
PLQNLFEAKG IAGNIVHAVA TTNAVIAGLI VIEAIKVLNN DIKNYRMTYC LEHPARNMLL
MPVEPFEPNK SCYVCSETPL SLEINTNRSK LKDLVEKIVK AKLGMNLPLI MCASNLLYEA
GDVEDDMVAI YEANLEKALA ELPSPVTGGT MLTVEDMQQE FVCNINIKHR EEFDEEKEPD
GMVLSGWTQP VSAAENKDKS VGNGASTSDA LITAVESEKD DEITIVSTLK KRKLPDESDI
SNSAAESKNQ KQLEVIEDED DLVMLDGDSD SVKKRRLS
//
