ID A0A151JRW9_9HYME Unreviewed; 719 AA.
AC A0A151JRW9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=E3 ubiquitin-protein ligase TRIM9 {ECO:0000313|EMBL:KYN30119.1};
GN ORFNames=ALC57_00451 {ECO:0000313|EMBL:KYN30119.1};
OS Trachymyrmex cornetzi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN30119.1, ECO:0000313|Proteomes:UP000078492};
RN [1] {ECO:0000313|EMBL:KYN30119.1, ECO:0000313|Proteomes:UP000078492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN30119.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN30119.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex cornetzi WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ978566; KYN30119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151JRW9; -.
DR STRING; 471704.A0A151JRW9; -.
DR Proteomes; UP000078492; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19803; Bbox1_TRIM9-like_C-I; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd16576; RING-HC_TRIM9-like_C-I; 1.
DR CDD; cd12889; SPRY_PRY_TRIM67_9; 1.
DR Gene3D; 1.20.5.170; -; 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; 2.60.40.10; Immunoglobulins; 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; IPR003649; Bbox_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR PANTHER; PTHR24099:SF15; E3 UBIQUITIN-PROTEIN LIGASE TRIM9; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00060; FN3; 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; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000078492};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 140..189
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 204..247
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 355..415
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 430..534
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 519..704
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 38..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 248..296
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 38..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 78116 MW; 55756B4658AF6B33 CRC64;
MEDELRCPSC KELFVEPVLL PCWHALCLAC AVNLQAPPDS PPESTADSSN APGSDQEADK
LSILSETDSG VVCSSTSTSS RPGSYVGTPG NGGFPPSGGT LCLSCPVCQK TVYFDEGGAH
NLPKYRAMQH IVDKYQESRN SRLQCQMCEG EPRDATVACE QCEVLYCDAC RESCHPKRGP
LAAHNLGPPR GSWQSSGNKG SRPEGTPICN DHNGEAVTLY CALCKIAICA LCLRDRHAAH
PHDVLPLAAA CKAQKTELSQ NLQQLSERAR STTEFIQRLK GMTDKVHEEC VALEEEVEDR
VTNLVSLLQA RKSRLIEAAR QTREARVRSL RDQVARCATH LQATTALLTF CIEALKETDS
AAFLQIGGML SVRAATAAGS WGGAEGVQEI ARLPLLDLTL DDKPLRRAID QLTFVQLKRE
SAVIGECGLP PGAPLLIPEE CSAENNSVTV AWQPPPGHGI MGCAGQRGPA IEGYLLELDD
GCGGEFREVY CGRETICTVD GLHFNSLYNA RVRAFNSAGE GEYSELIGLQ TAEVAWFSWA
TGAAGIPQEV SISEDAMSAS CEGYEHRVVL SSVGFSRGVH YWELTIDRYH SDTDPAFGIA
RADVSRDQML GKDDKGWSMY IDRQRSWFMH GGGHAQRTEG GVQQGSTVGV LLDLDTTHTL
RFFVNDQPQG GIAFRDLYGV FYPAISLNRG VTVTLHTALD VPRHLLALHE EYISDMVQS
//
