ID W5MQJ3_LEPOC Unreviewed; 492 AA.
AC W5MQJ3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Tripartite motif-containing protein 35-like {ECO:0000313|Ensembl:ENSLOCP00000010652.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000010652.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000010652.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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DR EMBL; AHAT01007539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MQJ3; -.
DR STRING; 7918.ENSLOCP00000010652; -.
DR Ensembl; ENSLOCT00000010667.1; ENSLOCP00000010652.1; ENSLOCG00000008744.1.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00970000193390; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; W5MQJ3; -.
DR OMA; GFYESKY; -.
DR Proteomes; UP000018468; Linkage group LG6.
DR Bgee; ENSLOCG00000008744; Expressed in pharyngeal gill and 2 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd12893; SPRY_PRY_TRIM35; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF611; E3 UBIQUITIN-PROTEIN LIGASE TRIM39-RELATED; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 22..62
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 94..135
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 282..474
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT COILED 136..242
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 492 AA; 56394 MW; 296810D7CB067C58 CRC64;
SDCRSIKEMA ARSSGLEEDL SCSMCYDIFK DPVLLTCSHS FCKVCLEQHW KQKGSQECPA
CRRRSSRDLP PFNLALKNVC EKFLREQSQR PPAGSEELCS LHREKLKVFC MTDEEPVCLV
CQTAGKHKNH EFCPVEEAVM DRKEELKAAL EHLKKKLKEI DKVKQTSDQT AEFIKTQTQQ
TERQIKEELE KLHQFLRDEE EARIAALREE EKQKSQMMKE KFESLTREIS SLSETIRAIE
QEMRADNIFF LQNYKETKRR AQRTLQDPEE VSGALIDVAK YLGSLKYRVW EKMLGIVQYI
PLSLNTNTAS PQLSLSEDLT SVRYSGQRQQ LPDNPERFDS IVCVLGSEGF TSGTHCWDVD
VEDKTCWVLG VVKKSIKRKG SFTLRPEGGL WALWLSGDAY GALTSPVTQI TLKRKPKKIR
VQLDYDMGEV SFSDPSDGTI IYTFKHKFNE MMFPVFFPGS DLGPLRICPV KVSVTQCVED
EDQGRSGMKN HP
//
