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Database: UniProt
Entry: K7MVL5_SOYBN
LinkDB: K7MVL5_SOYBN
Original site: K7MVL5_SOYBN 
ID   K7MVL5_SOYBN            Unreviewed;      1088 AA.
AC   K7MVL5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=100820501 {ECO:0000313|EnsemblPlants:KRH01819};
GN   ORFNames=GLYMA_18G300300 {ECO:0000313|EMBL:KRH01819.1};
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|EMBL:KRH01819.1};
RN   [1] {ECO:0000313|EMBL:KRH01819.1, ECO:0000313|EnsemblPlants:KRH01819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH01819};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH01819.1};
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:KRH01819}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH01819};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH01819.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH01819.1};
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; KRH01819.1; -; Genomic_DNA.
DR   RefSeq; XP_006603073.1; XM_006603010.2.
DR   AlphaFoldDB; K7MVL5; -.
DR   EnsemblPlants; KRH01819; KRH01819; GLYMA_18G300300.
DR   GeneID; 100820501; -.
DR   Gramene; KRH01819; KRH01819; GLYMA_18G300300.
DR   HOGENOM; CLU_008502_0_0_1; -.
DR   OMA; DSGTYQF; -.
DR   OrthoDB; 1219578at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008827; Chromosome 18.
DR   ExpressionAtlas; K7MVL5; baseline and differential.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; 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; IPR045210; RING-Ubox_PUB.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR007527; Znf_SWIM.
DR   PANTHER; PTHR35549; OS04G0584500 PROTEIN; 1.
DR   PANTHER; PTHR35549:SF1; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51698; U_BOX; 1.
DR   PROSITE; PS50966; ZF_SWIM; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT   DOMAIN          298..336
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50966"
FT   DOMAIN          611..686
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          47..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1088 AA;  122308 MW;  86FFBA14C06D657A CRC64;
     MASSLEELLA KEGFKGIRRV TRSRSSFHYG ASSEPLHSLD GRFSVSSERI RTQRTKSDAS
     RYQISSGQLK TDNDTAMNRR SRDNLFLRDK MDQRLKNSSI DTDSGRGVDT NSSEYMPRNE
     ITEVTEQEAN IVKDNCSTEV SSKRGKEKNF NELVEEENPV KDAKARSRSS SIHMLGHSSE
     TRNNIKPQKD SYTRSNSSRN KDSNHAIQAA SSLALDEVAV QAVVSILNGY IKSFPKDADF
     RSTLRHKCFS SLNFIELEEE NITGTKVIRS LEQAIEAIEQ TAEEPISTMY LKRTMMQLSI
     ITGLSLNDLK YECTCGIPNF KLSACAHLYL SVVYMMQKKN KVSAKHLLQV FCDSPFQART
     VLLPELWEHL FSSQFSHLKA WYSKQAEFLV DAPSKTRKLK LLQKVYNEHL DSGTHIFAVY
     YKDWLTEGVE SPPTPSIGIP SASVMGSQEG SSLGYSFESA SSIDPLSPQP MVSKKLYDSM
     FGSLSKPRVY QVKDIKDDDN IDNCMKDSYG STIVRQTLTY ESETVKFTDQ DIENFSQGVA
     IDTIKPKGNS MTASEEWQKR NLSNDINNSF SMETNLNSHS IDALSHEKAS EPVLIKPNKT
     CSSLEGPYFP SIPHEFICPL TGNLFEEPVT LETGQTFERE AIKAWFEKGN RTCPVTGNTL
     ECVTMPFTNL ILKRLIDTWK SELFDYLIDL PSQTVENPEE LKLKKRDEAA VFKLESLFSS
     LKEEDKSTYA KHLISLGFLP FLFRRFEQGN VEEKSHVMSL LLNCIQVDSG CIYQIATSVN
     KKCLLELLHS KKATPTTNAI LFLTEILSMK RRKDVTSFIS GLAGEKVFNI MHILLMYLKK
     SSPFEKPLIA VLLLHFDLLV EPQKFSIYRE VAVNAIAEAL DASLNDEKGR EKCCRALVIL
     CSHFSSTGKI PTKTSILKQA GYNNDSLEVK PPGHEEEGQR LYVAISSEGE EKRGEELLKK
     LLESLIGDGE SPFLKNISRC LDSKHLDLVR ACLITVTWLS SSLSMLFSAG LHLPAFLSII
     SQLKGILENG ELELKTLASL SLLNFSKISE CKTLLKTMAE DIGPLLHELD DVTWTAKQLH
     AIVSRENL
//
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