ID A0A2U9BX34_SCOMX Unreviewed; 592 AA.
AC A0A2U9BX34;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 03-MAY-2023, entry version 22.
DE SubName: Full=Putative RING finger and SPRY domain-containing protein 1-like {ECO:0000313|EMBL:AWP08857.1};
GN ORFNames=SMAX5B_017812 {ECO:0000313|EMBL:AWP08857.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP08857.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP08857.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP026252; AWP08857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BX34; -.
DR STRING; 52904.ENSSMAP00000020360; -.
DR OMA; KYSHDSV; -.
DR Proteomes; UP000246464; Chromosome 10.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR CDD; cd16566; RING-HC_RSPRY1; 1.
DR CDD; cd12883; SPRY_RING; 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; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR045129; RNF123/RSPRY1-like.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035774; SPRY_RSPRY1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13363:SF6; RING FINGER AND SPRY DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR13363; RING FINGER AND SRY DOMAIN-CONTAINING; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF13920; zf-C3HC4_3; 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; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..592
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015976381"
FT DOMAIN 316..499
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT DOMAIN 543..578
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 53..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 65549 MW; FF4CEB1584003CDB CRC64;
MIVAAWITFC ACRSLARVLL FLSSSKSLPS FWETLASAVS ATGTMGNSCV CREDSDAEDH
HHGSSRATRG QARRADHAAG VGADTGEARS SRPRDPVRPP RRGRGPHEPR RKKQNVDGLV
LDTLAVIRTL VDNDQEPPYS MITLHEMAET DDGWLEVVQS LIRVIPLDDP LGPAVITLLL
DECPLPTKDA LQKLSDMLSL SSAVAQQDAL NPAKHRNTTA VLGCLAEKLA GPASIGLLSP
GTLEYLLESL SSEAHPTVML FALIALEKFS QTSENKLTVS ESCISNRLSV LESWAENPDY
LKRQVGFCSQ WSLDNLFLKD GRQFTYEKVN LTNINAMLNS NDVSEYLKIS PTGLEARCDA
SSFESVRCTF CVYSGVWYYE VTVVTSGVMQ IGWATKDSKF LNHEGYGIGD DEYSCAYDGC
RQLIWYNARS KPHSHSCWKE GDAIGFLLDL SKKQMIFYLN GHQLPPEKQV FSSATSGFFA
AASFMSYQQC EFNFGAKPFR HPPSVKFSTF NDFASLQPSE KIILPRHRRL ALLKQVSIRD
NCCTLCCDVM ADTELRPCGH GGMCMECALQ LETCPLCRQD IQNRVRLIAH VS
//