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Database: UniProt
Entry: A0A401PCG5_SCYTO
LinkDB: A0A401PCG5_SCYTO
Original site: A0A401PCG5_SCYTO 
ID   A0A401PCG5_SCYTO        Unreviewed;       460 AA.
AC   A0A401PCG5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=scyTo_0010858 {ECO:0000313|EMBL:GCB70816.1};
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:GCB70816.1, ECO:0000313|Proteomes:UP000288216};
RN   [1] {ECO:0000313|EMBL:GCB70816.1, ECO:0000313|Proteomes:UP000288216}
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:GCB70816.1}.
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DR   EMBL; BFAA01004779; GCB70816.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401PCG5; -.
DR   STRING; 75743.A0A401PCG5; -.
DR   OMA; WSEVSIH; -.
DR   Proteomes; UP000288216; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd13733; SPRY_PRY_C-I_1; 1.
DR   Gene3D; 2.60.120.920; -; 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; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR   PANTHER; PTHR24103:SF639; E3 UBIQUITIN-PROTEIN LIGASE TRIM39; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288216};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          7..46
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          271..460
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
SQ   SEQUENCE   460 AA;  51501 MW;  8F54ED258736D6FC CRC64;
     MLDETLCPAC LQLYANPVSL PCGHCLCRRC ALPLPPCPLP PCPLCRQPFS RQSVRPNRSL
     GRKVARARQR LGRLAGEQAP CPGRQRGLAA AGELEALAQP LPRSVPVPAG CGTGRARPGR
     GSVKQVTELY KEMLRNKQDS LRKRKDYLHQ CQGIEEANRV EVKKYVEGLR ENITSEFAEL
     QQFIRSEETA LIARLEEKQK AVSQQIEGNM RKISKDLAAI DQTINNVENL LALQEAELLQ
     DMRSSIKWSG VDYQSPTRLP VALTLGEFSG PLQYVVWRRM LKEIRTVPVA LVLNAKTAHP
     HLSLSADCRS LRAGSGKQTS RRPASFGRCL CALSSEGFAS GRNYWEVRVR MNWEWAVGVA
     TASVIRKANT RPTPKAGIWA LRRSGEEYAA LTSPHTPLRL STKPQRIGVY LDYEMGQVSF
     YNADDLSHLF TFTDTFTEEL YPYFYTGCKM DSLKLVTLRV
//
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