ID K7MQ50_SOYBN Unreviewed; 841 AA.
AC K7MQ50;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=100811250 {ECO:0000313|EnsemblPlants:KRG98177};
GN ORFNames=GLYMA_18G055200 {ECO:0000313|EMBL:KRG98177.1};
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:KRG98177};
RN [1] {ECO:0000313|EMBL:KRG98177.1, ECO:0000313|EnsemblPlants:KRG98177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG98177};
RC TISSUE=Callus {ECO:0000313|EMBL:KRG98177.1};
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:KRG98177}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG98177};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRG98177.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRG98177.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; CM000851; KRG98177.1; -; Genomic_DNA.
DR RefSeq; XP_003551173.1; XM_003551125.3.
DR AlphaFoldDB; K7MQ50; -.
DR SMR; K7MQ50; -.
DR STRING; 3847.K7MQ50; -.
DR PaxDb; 3847-GLYMA18G06200-2; -.
DR EnsemblPlants; KRG98177; KRG98177; GLYMA_18G055200.
DR GeneID; 100811250; -.
DR Gramene; KRG98177; KRG98177; GLYMA_18G055200.
DR KEGG; gmx:100811250; -.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_006348_5_0_1; -.
DR InParanoid; K7MQ50; -.
DR OMA; NNKCSIA; -.
DR OrthoDB; 2721872at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008827; Chromosome 18.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23315; U BOX DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23315:SF7; U-BOX DOMAIN-CONTAINING PROTEIN 4; 1.
DR Pfam; PF00514; Arm; 3.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 6.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 238..312
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 598..640
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 680..722
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 721..762
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REGION 341..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 182..212
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 341..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 91180 MW; 32D8484D61F3748A CRC64;
MGVMEISLLK MIVNGMSSFL HLSFSGNMNS EPVSKYYQKA EEIHKLLKPI IDAIVNPELA
SDEVLNKILE EIGFAVNELK EHVENWHLLS SKVYFVMQVE PLISRIRTSG LNIFQQLKDS
QHCLPDELSS EYLQLCSQKL KLLGHEEISP VIKEAITEHL ENVGPSSELL TKIADSLGLR
SNQEVLIEAV ALERLKENAE QTEKTAEAEF IDQMIAVVTR MHERLVMLKQ AQSSSPVSIP
ADFCCPLSLE LMTDPVIVAS GQTYERAFIK NWIDLGLTVC PKTRQTLVHT HLIPNYTVKA
LIANWCESNN VQLVDPTKST NLNQASVLHG YMESGTTRES PVFAHSRSNQ PSSPESARSC
SFSSPANNLT SGGTQREGTS PLHPRSTSEG SFRGMVNGQY MDLARISPEG LDDRSASSDE
SSVDSASHPS MSPSRRESSS AFSSEQSQTH IRAVSDSSAL SNANFPQETQ DDDNNAPQLS
TSAGHSREAS GELNPGTETG GTTAVPSVHR EPEFPLRLET RSRSQAIWRR PSERHVPRIV
SSPVVETRAD LSAIETQVRN LVEGLRSSDV DTQREATAEL RLLAKHNMDN RIAIANCGAI
NLLVDLLQST DTTIQENAVT ALLNLSINDN NKTAIANAGA IEPLIHVLET GSPEAKENSA
ATLFSLSVIE ENKIFIGRSG AIGPLVELLG SGTPRGKRDA ATALFNLSIF HENKNRIVQA
GAVRHLVDLM DPAAGMVDKA VAVLANLATI PEGRNAIGDE GGIPVLVEVV ELGSARGKEN
AAAALLHLCL HSPKFSSKVL QQGAVPPLVA LSQSGTPRAK EKAQALLNQF KSQRHGSSGR
G
//
