ID A0A3P9A175_ESOLU Unreviewed; 666 AA.
AC A0A3P9A175;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=E3 ubiquitin/ISG15 ligase TRIM25 {ECO:0000313|Ensembl:ENSELUP00000034767.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000034767.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000034767.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000034767.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_010887618.1; XM_010889316.2.
DR AlphaFoldDB; A0A3P9A175; -.
DR STRING; 8010.ENSELUP00000034767; -.
DR Ensembl; ENSELUT00000021813.2; ENSELUP00000034767.1; ENSELUG00000013450.2.
DR GeneID; 105021554; -.
DR KEGG; els:105021554; -.
DR GeneTree; ENSGT00940000164979; -.
DR InParanoid; A0A3P9A175; -.
DR OMA; KRGVHYW; -.
DR OrthoDB; 5359093at2759; -.
DR Proteomes; UP000265140; LG09.
DR Bgee; ENSELUG00000013450; Expressed in nose and 15 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR CDD; cd19776; Bbox2_TRIM25_C-IV; 1.
DR CDD; cd16597; RING-HC_TRIM25_C-IV; 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:SF40; E3 UBIQUITIN_ISG15 LIGASE TRIM25; 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; 2.
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:UP000265140};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 17..55
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 474..666
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 372..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 275..302
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 378..394
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 74943 MW; 9E3CF44DA6E613B0 CRC64;
MAEDMLSLMS LEDELTCSIC LCPFECPVTI PCGHNFCQDC LLKTWKENYS CPQCRTHFTT
KPELKKNTVL STVVETFKAK SNKDDLPIDM KDPSSWDADK KEPEEAVILC DTCMEVKAFK
TCLTCMASFC VDHVRPHQEN PVFAAHQLNE PLGDLLERIC PDHHKLMDFY CVQHGRCICS
VCLQQIHKGC TFSNPDEQRA LKESDLRGKL SLLDGKIDKN QTVISQMREQ QSKLKDSAAT
RKRDVANEYR LIRELLDGDE REALNMVDRE LESGHTKLQN LMKKFNKNIE QLTAAKDSVN
SLLSQTHSLG FLQASVDLPT VVGFDPYAPK TNLDSSKTMA AWTAYSAVLR EHLTHIIQKQ
PVEDRLQILK PERNMGMNSG PPPGPPPGPP RQPRSHSPGG ALKGRERKNY QDASTDRERK
SDKKPDQKKG QEHKAGKNQR KPPQYTTMGA TTPYENFRGA QESRTQENPC PPNVPMNITS
AAKRNDLLQY GSVLTFDPKT AHKRISLTDN QTTASVLNEP ANYPDGPARF SVCSQVLTSK
GFSRGRHYWE VKMNSNNFTG IGLAYNSIDR KGPSSRLGRN AQSWCVEWFN VKLSAWHASN
ETVLANPNPT RVGVLLDCDE GTATLYNVQD RAYPFHTFVF RFAEAVYPAF WLFSSGSSIN
LCKLQS
//
