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Database: UniProt
Entry: W5M4X3_LEPOC
LinkDB: W5M4X3_LEPOC
Original site: W5M4X3_LEPOC 
ID   W5M4X3_LEPOC            Unreviewed;       596 AA.
AC   W5M4X3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=E3 ubiquitin-protein ligase TRIM39-like {ECO:0000313|Ensembl:ENSLOCP00000003431.1};
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:ENSLOCP00000003431.1, 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:ENSLOCP00000003431.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AHAT01038764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015201614.1; XM_015346128.1.
DR   AlphaFoldDB; W5M4X3; -.
DR   STRING; 7918.ENSLOCP00000003431; -.
DR   Ensembl; ENSLOCT00000003438.1; ENSLOCP00000003431.1; ENSLOCG00000002915.1.
DR   GeneID; 102683306; -.
DR   KEGG; loc:102683306; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT01040000240385; -.
DR   InParanoid; W5M4X3; -.
DR   OMA; LVEETIM; -.
DR   OrthoDB; 1116590at2759; -.
DR   Proteomes; UP000018468; Linkage group LG5.
DR   Bgee; ENSLOCG00000002915; Expressed in pharyngeal gill and 3 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   CDD; cd19769; Bbox2_TRIM16-like; 1.
DR   CDD; cd13733; SPRY_PRY_C-I_1; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 4.10.830.40; -; 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; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR25465; B-BOX DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR25465:SF34; TRIPARTITE MOTIF-CONTAINING 80; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 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   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   TRANSMEM        370..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..55
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          144..184
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          396..592
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   COILED          253..294
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   596 AA;  67197 MW;  BF1B61A924049562 CRC64;
     MISPGSLLSE EQLLCSICLD VFASPVSLPC GHNFCQACIG GYWDSGGACQ CPLCKEAFGR
     RPSLQINRTL NEIAEQFKAT RSSRADGGAA GPGEVPCDVC AAEKLRAVKS CLVCLASYCD
     EHVQPHREVG RLSRHRLVDP ARSLRDKLCR KHGRQLELFC RRDQAFICRL CTKKDHRTHS
     TVPIEAQRLE LQNNMRKTQA HLQQMAQDRL KKVEDVKKSV KLHKRWVQKE MKDSVKLCTA
     LAHCVERSQA EVIKALEDKQ RAAEVQAEGL IKELEQEMAA IKRRNAELEQ LARTEDHLLF
     LQCFPSLCSP PQTKEWSSIT LPTEPSADSS WEALTHLEER FLEELRKLKN KGPQDNPARR
     RSSCSWRTMV LSYMWTVILT AVLLGFYAHT HMQKQTPQDE MRNAQISSTS VRMVNVTLDS
     STAHPSLILS EDGKQVRLGD APQDLPDNPE RFDQDFCVLG AEGFTSGRHY WEVEVGDKTE
     WDLGVARESV DRKGEITLSP EDGYWSIWLK NGKEYQALTD NAVALPLSTR PRKVGVYVDY
     EGGQVSFYNV EASSHIYTFM ASFTEKLYPY FSPGLNSDGK NSAPLIISSP AHIKNK
//
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