ID   W5NKN9_LEPOC            Unreviewed;       566 AA.
AC   W5NKN9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Tripartite motif-containing protein 16-like {ECO:0008006|Google:ProtNLM};
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:ENSLOCP00000021198.1, 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:ENSLOCP00000021198.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AHAT01037805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5NKN9; -.
DR   STRING; 7918.ENSLOCP00000021198; -.
DR   Ensembl; ENSLOCT00000021234.1; ENSLOCP00000021198.1; ENSLOCG00000017145.1.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT01090000260029; -.
DR   HOGENOM; CLU_013137_0_2_1; -.
DR   InParanoid; W5NKN9; -.
DR   OMA; VEWTERQ; -.
DR   Proteomes; UP000018468; Linkage group LG8.
DR   Bgee; ENSLOCG00000017145; Expressed in zone of skin and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   CDD; cd19769; Bbox2_TRIM16-like; 1.
DR   CDD; cd16040; SPRY_PRY_SNTX; 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; 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:SF36; E3 UBIQUITIN-PROTEIN LIGASE TRIML1-RELATED; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF15227; zf-C3HC4_4; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
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; 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   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:PRU00175}.
FT   DOMAIN          15..58
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          369..562
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   COILED          206..298
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   566 AA;  64042 MW;  BF8CE0DE68CA21E4 CRC64;
     LKMAAGQWTE DELDCPICLD ILKDPATLPC GHSYCMGCIK NYWDQNNRTG VYSCPQCRET
     FTPRPALRRN TMLAEVVEKL RRRGTSTPLP PPAPSPSGPG DVLCDFCTGR QVRAVKSCLV
     CLASYCQTHL QPHCEAAPLK RHQLVEATGE LQEKTCSSHD RFLEVSSRTD QKGAFYACLM
     DEHRGHNTVS AEAERMKKQK QLGATQTQTQ QRLQEREKEL QELRQAVDSL RSSAHTAVQD
     TDRIFTELIR SIERTRSELT QLIRAQERAA VSQAEGLLER LEQEIAELRR RDAELSQLSH
     TEDHIHFLQN FQSVCVLPGA GDSPSIPVRP HFSPEAVRRA VSGLKEQLED VCREESVKIS
     RTVKETLVCS LKTSEPRTRT ELLHYACQLA LDPNTANRHL CLSEGNRRVS TTKEPLQYPD
     HPERFDNWRQ VLCREGLSGT RAYWEVEWSG VRSDIGVAYK GINRKGKGVD CRLGRNRKSW
     SLYWSGTSYS IWHNNQETEI AAPPSSRIGV YVDHRAGTLS FYSVSGDTAT LLHRVQASFT
     EPLYPGFGFG LKFFIFFLDS SLTLCR
//