ID A0A2U9BBM7_SCOMX Unreviewed; 359 AA.
AC A0A2U9BBM7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative E3 ubiquitin-protein ligase RNF128-like {ECO:0000313|EMBL:AWP01361.1};
GN ORFNames=SMAX5B_012588 {ECO:0000313|EMBL:AWP01361.1};
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:AWP01361.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP01361.1, 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; CP026247; AWP01361.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BBM7; -.
DR STRING; 52904.ENSSMAP00000034813; -.
DR OMA; CIESYKA; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000246464; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02122; PA_GRAIL_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16200:SF2; E3 UBIQUITIN-PROTEIN LIGASE RNF43; 1.
DR PANTHER; PTHR16200; RING ZINC FINGER; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..359
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015978428"
FT TRANSMEM 180..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 251..292
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 328..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 359 AA; 39939 MW; E9FA8A83B75128D5 CRC64;
MGETTQHFPL LLLCLSGLVR CSAAFVFWTA EMEIRYLNNN NETVDKICEC GVYGRNSAVE
TVSGIVTLPK EDTKGCGPGP VYNRNSSSPK WIALVKRGNC TFSEKINAAR RLGAVGVVVY
NVDGTGNSTT HMAHSDSVEA VAIMIGNNQG MEVVRLVKNG TNVHMTILVG SPHGPWMDTY
WLYFLSIAFF IVTAASIAYF VFISANRLYN LRQHRRSERR LKSDAKKAIG RLRVRTLKRD
DEETTSDSHM CAVCIESYRA GEVVTVLTCD HIFHKACIEP WLLEKRNCPM CKCDILKALG
IEDETKESDS PADVTVITVA GEETLYNVPL TDPASSDPGR HQNLYENRAF EDETEAARR
//
