GenomeNet

Database: UniProt
Entry: A0A060X225_ONCMY
LinkDB: A0A060X225_ONCMY
Original site: A0A060X225_ONCMY 
ID   A0A060X225_ONCMY        Unreviewed;       526 AA.
AC   A0A060X225;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=E3 ubiquitin-protein ligase SH3RF1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GSONMT00016872001 {ECO:0000313|EMBL:CDQ73257.1};
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ73257.1, ECO:0000313|Proteomes:UP000193380};
RN   [1] {ECO:0000313|EMBL:CDQ73257.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24755649; DOI=10.1038/ncomms4657;
RA   Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA   Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA   Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA   Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA   Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA   Guiguen Y.;
RT   "The rainbow trout genome provides novel insights into evolution after
RT   whole-genome duplication in vertebrates.";
RL   Nat. Commun. 5:3657-3657(2014).
RN   [2] {ECO:0000313|EMBL:CDQ73257.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SH3RF family.
CC       {ECO:0000256|ARBA:ARBA00008649}.
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DR   EMBL; FR904889; CDQ73257.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A060X225; -.
DR   STRING; 8022.A0A060X225; -.
DR   PaxDb; 8022-A0A060X225; -.
DR   Proteomes; UP000193380; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd11927; SH3_SH3RF1_1; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 3.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR14167:SF44; E3 UBIQUITIN-PROTEIN LIGASE SH3RF1; 1.
DR   PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR   Pfam; PF00018; SH3_1; 3.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF50044; SH3-domain; 3.
DR   PROSITE; PS50002; SH3; 3.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193380};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          12..53
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          128..187
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          190..253
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          428..489
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          99..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..403
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   526 AA;  56962 MW;  82C617A5EA360478 CRC64;
     MDESVLLDLL ECPVCLERLD ATAKVLPCQH TFCRRCLQSI LGSRGELRCP ECRTLVECAV
     DELPSNILLV RLLDGIKQRP RRVGPVAGVC ANGTAGVRVQ GNGPRDPGVP GAQPQRAQAK
     TTPVRGVPQL PCAKALYNYD GKEPGDLKFN KGDIIILRRQ VDENWYHGEM GGVHGFFPTN
     FVQIIKPLPQ PPPQCKALYD FELKDNEADK DCLPFTKDDI LTVIRRVDEN WAEGMLGDKI
     GIFPISYVEF NTAARQLIEL DKPGDSSGDS GEGASSGPQS NGGPHRAGEK KNSKKRHSFT
     SLTMSHKPCL APPPQRHSME ISGPVLISSS NPTAAARIGE ISGGLSCSAP SQVHICTTGL
     LVTPPPSSPV TTATVFTFPP EASYTSIPVE ALPPPPPPPP QSSARGAASS LAAGQRPSPS
     TSDQSGRQRP TVYVALFPYP PRKEDELELR KGEMFLVLER CQDGWFKGTS MHTGKIGVFP
     GNYMSPVSRS VTHTDLTHAN TYTHDYMTKS MWAGLGLVEH LIPLLL
//
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