ID W5D2V7_WHEAT Unreviewed; 388 AA.
AC W5D2V7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=RING-Gid-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRAES_3BF123200030CFD_c1 {ECO:0000313|EMBL:CDM84865.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EMBL:CDM84865.1};
RN [1] {ECO:0000313|EMBL:CDM84865.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25035497; DOI=10.1126/science.1249721;
RA Choulet F., Alberti A., Theil S., Glover N., Barbe V., Daron J.,
RA Pingault L., Sourdille P., Couloux A., Paux E., Leroy P., Mangenot S.,
RA Guilhot N., Le Gouis J., Balfourier F., Alaux M., Jamilloux V., Poulain J.,
RA Durand C., Bellec A., Gaspin C., Safar J., Dolezel J., Rogers J.,
RA Vandepoele K., Aury J.M., Mayer K., Berges H., Quesneville H., Wincker P.,
RA Feuillet C.;
RT "Structural and functional partitioning of bread wheat chromosome 3B.";
RL Science 345:1249721-1249721(2014).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG670306; CDM84865.1; -; Genomic_DNA.
DR AlphaFoldDB; W5D2V7; -.
DR Gramene; TraesKAR3B01G0403440.1; cds.TraesKAR3B01G0403440.1; TraesKAR3B01G0403440.
DR eggNOG; KOG2817; Eukaryota.
DR HOGENOM; CLU_020227_1_0_1; -.
DR OrthoDB; 208500at2759; -.
DR ExpressionAtlas; W5D2V7; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd16652; dRING_Rmd5p-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR037683; Rmd5_dRing.
DR InterPro; IPR044063; ZF_RING_GID.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12170; MACROPHAGE ERYTHROBLAST ATTACHER-RELATED; 1.
DR PANTHER; PTHR12170:SF12; RING-GID-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF10607; CTLH; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01215}.
FT DOMAIN 152..209
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT DOMAIN 331..374
FT /note="RING-Gid-type"
FT /evidence="ECO:0000259|PROSITE:PS51867"
FT ZN_FING 331..374
FT /note="RING-Gid-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 388 AA; 43954 MW; 719B0DB60DF0C5CC CRC64;
MTMEIDSLRE AFDRVVEKRV LSSAKVQEAI GQIVNEVEQA ISKMQMMNTD TMDSCDHSSI
LAELKAKLNE MVPLIQLEGC QKELNVALSK YLKLLEKSFS PDIAKAYRNV DYDACTVNNI
ITNHFYRQGL FDLGDSFVNE CGESDETHLK FSFQEMYGIL EAMQARNLEP ALSWAAKNHD
HLLQNSSMLE MKLHSLQFIE ILTKRSRDDA LQYARTHFVP FASLHTAEIQ KLMACLIWAD
RLDQSPYAEF VSSTHWEKLA EELIHQFCSL LGQSRESPLG VAISAGFQGL PTLLKLSTVM
AAKKQEWQTM KQLPVPIDIG PEFQYHSVFV CPVLREQSSE DNPPMLMPCG HAVSKQSIMK
LSKSSSRPFK CPYCPLEAVA SQCKQLQF
//
