ID A0A401PS29_SCYTO Unreviewed; 482 AA.
AC A0A401PS29;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM39-like {ECO:0008006|Google:ProtNLM};
GN ORFNames=scyTo_0018283 {ECO:0000313|EMBL:GCB75946.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB75946.1};
RN [1] {ECO:0000313|EMBL:GCB75946.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB75946.1}.
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DR EMBL; BFAA01012577; GCB75946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401PS29; -.
DR STRING; 75743.A0A401PS29; -.
DR OMA; RRNNDEY; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19800; Bbox2_xNF7-like; 1.
DR CDD; cd16594; RING-HC_TRIM7-like_C-IV; 1.
DR CDD; cd13733; SPRY_PRY_C-I_1; 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; 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; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF611; E3 UBIQUITIN-PROTEIN LIGASE TRIM7; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 16..56
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 86..127
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 276..481
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT COILED 70..97
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 185..241
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 482 AA; 55183 MW; EB37509EEFAD1200 CRC64;
MALRQQVQSL TEEAMCSICL DLFANPVTLD CGHNFCRSCI TQCWENNEIN SCPDCRAAFP
ERNLSTNWAL ANLTEKARKL NRKEKESKLH CEKHQEELKL LCETDKKLIC LICRDSREHR
EHRFLPIKEA VKKHKDQLKS SIDSLTAKTS AVLETELKQK RKISEVRKQS SSLQTYITSE
FSKMHQILTE KEQRLLRDLR KEEERILEPM EKNLREIQEN LNSMEENLSK LQKQMKQKDE
LIFLKEEACQ KRRNNDEYHL LSVSAAALSI GKFKDLLQYT AWREMITSIN PAPASLTLDL
NTANPRLILS EDRTSVRLGS SIFFHYQAMF QLLPDTPERF NPWPFVLGSE GFTSGRHYWE
VAVGEKTEWG LGVTRESVNR KGRKSPSPES GFWIVGLEPG SGYFAATLPS DTPLILSVNP
RKIGVFLDYE GGQVSFSNAD NMSHLHTFTH TFTEKIFPIF SPGWKVGGKN SAPLTICGTK
GH
//