ID L5LVL0_MYODS Unreviewed; 263 AA.
AC L5LVL0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=RING finger protein 151 {ECO:0000313|EMBL:ELK30102.1};
GN ORFNames=MDA_GLEAN10007757 {ECO:0000313|EMBL:ELK30102.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK30102.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB107323; ELK30102.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LVL0; -.
DR eggNOG; KOG0297; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
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:InterPro.
DR CDD; cd16547; RING-HC_RNF151; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR013010; Znf_SIAH.
DR InterPro; IPR001293; Znf_TRAF.
DR PANTHER; PTHR10131:SF157; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10131; TNF RECEPTOR ASSOCIATED FACTOR; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
DR PROSITE; PS50145; ZF_TRAF; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00207}; Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00207};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00207}.
FT DOMAIN 27..65
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 85..143
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT DOMAIN 109..153
FT /note="TRAF-type"
FT /evidence="ECO:0000259|PROSITE:PS50145"
FT ZN_FING 109..153
FT /note="TRAF-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT REGION 224..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 263 AA; 29103 MW; 3429F330D86EFE4D CRC64;
MLLGGGRESG GYDLNLFTSP PNSNFLCSVC HGVLKKPVRL PCSHIFCKKC ILRWLARQKT
CPCCRKEVKR KKMIRVNKLR KTIGHLEVKC KNAEAGCSVT CPLAHRKGHQ NSCPFELMAC
PNEGCMVQIP RGTLVAHLQH CQHGTQQHCA LGCGANLGPT EHGPHNCHCE LREAWGQRQD
RSQTLVLCLL QHVRKVHRTT NLICWQLAQL GNFLENDALL LGAQQEDAPA QQEDAPAQQE
DAEATAEGSF GTEVWGAQDQ STL
//
