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Database: UniProt
Entry: I1KCV7_SOYBN
LinkDB: I1KCV7_SOYBN
Original site: I1KCV7_SOYBN 
ID   I1KCV7_SOYBN            Unreviewed;       486 AA.
AC   I1KCV7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GLYMA_06G196600 {ECO:0000313|EMBL:KRH54592.1};
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:KRH54592};
RN   [1] {ECO:0000313|EMBL:KRH54592.1, ECO:0000313|EnsemblPlants:KRH54592}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH54592};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH54592.1};
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:KRH54592}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH54592};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH54592.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH54592.1};
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.
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DR   EMBL; CM000839; KRH54592.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1KCV7; -.
DR   SMR; I1KCV7; -.
DR   STRING; 3847.I1KCV7; -.
DR   PaxDb; 3847-GLYMA06G21160-1; -.
DR   EnsemblPlants; KRH54592; KRH54592; GLYMA_06G196600.
DR   Gramene; KRH54592; KRH54592; GLYMA_06G196600.
DR   eggNOG; KOG4159; Eukaryota.
DR   HOGENOM; CLU_025835_0_0_1; -.
DR   InParanoid; I1KCV7; -.
DR   Proteomes; UP000008827; Chromosome 6.
DR   ExpressionAtlas; I1KCV7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   CDD; cd16514; RING-HC_LONFs_rpt2; 1.
DR   Gene3D; 1.20.58.1480; -; 1.
DR   Gene3D; 2.30.130.40; LON domain-like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR003111; Lon_prtase_N.
DR   InterPro; IPR046336; Lon_prtase_N_sf.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23327:SF42; LON PEPTIDASE N-TERMINAL DOMAIN AND RING FINGER PROTEIN C14F5.10C; 1.
DR   PANTHER; PTHR23327; RING FINGER PROTEIN 127; 1.
DR   Pfam; PF02190; LON_substr_bdg; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00464; LON; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51787; LON_N; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          197..235
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          278..478
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51787"
SQ   SEQUENCE   486 AA;  55698 MW;  572FA125E2F08841 CRC64;
     MSSSLSPCPS SLDQILRDVD DYVLENGSED LSWDTLHYVY ELVKNGNAAF RENRMQEAIN
     LYSRANNIKS GDPIILSNRS AAYIRISEYF MRRTSSSSER RPLSGLEPTT IAELGLKDAE
     KLVELQSNSA KSYLLKASAL LLLEKYEKAR DVILSGLQVD PFSNSLRASL QNLERVSSSS
     TGMSTHGHPE RNDDFDCTLC LKLLYEPVTT PCGHSFCRSC LFQSMDRGNR CPLCRTVLFI
     SPRTCSISVT LKNIIQKNFP EEYAERKQEH DGLINAGVDL LPLFVMDVVI PCQRFALNIF
     EPRYRLMVRR IMEGNHRMGM AILDSTGSLA EFACEVEITE CEPLPDGRFY IEIESRRRFR
     IIRSRDQDGY RVAEVEWIQD IMPPEGTSER ETLQQQTYNA AEDARSWIAR AKEAAKHDPR
     KLERLASVEV MMPSPKDPER FSFWLATLSN RRPAERLDLL RIRDTAERIR RGLIFLRQEE
     QGCRIQ
//
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