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Database: UniProt
Entry: I1JP45_SOYBN
LinkDB: I1JP45_SOYBN
Original site: I1JP45_SOYBN 
ID   I1JP45_SOYBN            Unreviewed;       792 AA.
AC   I1JP45;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=100782215 {ECO:0000313|EnsemblPlants:KRH67392};
GN   ORFNames=GLYMA_03G163900 {ECO:0000313|EMBL:KRH67392.1};
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:KRH67392};
RN   [1] {ECO:0000313|EMBL:KRH67392.1, ECO:0000313|EnsemblPlants:KRH67392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH67392};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH67392.1};
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:KRH67392}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH67392};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH67392.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH67392.1};
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; CM000836; KRH67392.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1JP45; -.
DR   EnsemblPlants; KRH67392; KRH67392; GLYMA_03G163900.
DR   Gramene; KRH67392; KRH67392; GLYMA_03G163900.
DR   OMA; REYMENW; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008827; Chromosome 3.
DR   ExpressionAtlas; I1JP45; baseline and differential.
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:SF278; U-BOX DOMAIN-CONTAINING PROTEIN 3; 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; 4.
DR   PROSITE; PS51698; U_BOX; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          239..313
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REPEAT          547..589
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          588..630
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          629..671
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REPEAT          670..711
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REGION          360..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..384
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   792 AA;  87660 MW;  9961212AA7F9D062 CRC64;
     MHIGQINTSS VKCLVNSISR FIHLVSCQAV KPMPLQKNCN NMVCVLKHLK PVLDDIVDFK
     IPFDENLHRE CEELDMRVNE AREFIEKWGP KMSRIHSVLQ SGELLIKLQN SSYKICHMIV
     KSLKGPASVL VSGNLQQYMQ ELQCLKKEPA MIYIEDALRN QRDNIEPCYD SLKEIIRLLM
     ISNQELLIES IAVEKERSNA EVNKTKGDLD EINQIVNLVC SLRDYVMKFE RPEVKSGVSI
     PPYFRCPLSL ELMSDAVIVA SGQTYERQSI QKWLDHGLTV CPNTRQILVH TNLIPNYTVK
     AMIANWCEEN NVKLPSNSKQ SNSSHISSPS DHLLHQDLDR LCSFESSASS DSNSNQIANA
     FEKPKDDNSF RSSRESDRSW NGETEKFEQQ SPAPSCSNSR SESFSSSISS TDYVFPVLKE
     VSGISNKHQN VELSREITDG CPASPAYKES VIYPWLSGKQ FHSPGSKIGR MEDENKYNES
     NNISITSHSK VASHPVGSNE LITTSHVNEL IEDLQSQSNE TQTAAAEQLR LCTKHNMENR
     ISVGRCGAIM PLLSLLYSER KIIQEHAVTA LLNLSINEGN KALIMEAGAI EPLIHVLKTG
     NDGAKENSAA ALFSLSVIDN NKAKIGRSGA VKALVGLLAS GTLRGKKDSA TALFNLSIFH
     ENKARIVQAG AVKFLVLLLD PTDKMVDKAV ALLANLSTIA EGRIEIAREG GIPSLVEIVE
     SGSLRGKENA ASILLQLCLH NQKFCTLVLQ EGAVPPLVAL SQSGTPRAKE KAQQLLSHFR
     NQREGVKGKG KS
//
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