ID A0A3B4TCQ0_SERDU Unreviewed; 607 AA.
AC A0A3B4TCQ0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=E3 ubiquitin-protein ligase MSL2-like {ECO:0000313|Ensembl:ENSSDUP00000003732.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000003732.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000003732.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3B4TCQ0; -.
DR STRING; 41447.ENSSDUP00000003732; -.
DR Ensembl; ENSSDUT00000003815.1; ENSSDUP00000003732.1; ENSSDUG00000002830.1.
DR GeneTree; ENSGT00390000016814; -.
DR OrthoDB; 4153116at2759; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0072487; C:MSL complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR CDD; cd13122; MSL2_CXC; 1.
DR CDD; cd16522; RING-HC_MSL2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR037922; MSL2.
DR InterPro; IPR032049; Msl2-CXC.
DR InterPro; IPR032043; Msl2_Znf-RING.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16048:SF3; E3 UBIQUITIN-PROTEIN LIGASE MSL2; 1.
DR PANTHER; PTHR16048; MSL2-RELATED; 1.
DR Pfam; PF16682; MSL2-CXC; 1.
DR Pfam; PF16685; zf-RING_10; 1.
DR SMART; SM01114; CXC; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
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:PRU00175}.
FT DOMAIN 44..85
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 141..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..283
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..335
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 64749 MW; E7FF49A554B473F9 CRC64;
MNPVNATSLY VSASRSVLQC DPRDPRALAE LCKLLPFFRQ SLSCLVCGNL LQDPIAPTDS
SCQHYVCRGC KGQRMQLKPS CSWCKDYSRF EENRQLSLLV HCYRKLCLYI TQSPLAPHIA
SAASDSPDLQ AILNEGLTLA ESEPEAEDIS DSVGPSQTAS TSDVVQPSEA PPTKELKGEE
PSPVSINGLH DCNGLVSSDT LQPITIETGG GVAKQESFSG EIPVCVSVTG TGEAGLCDIS
TFGDELKHGG GPLLLSVEEV LRTLETDPDP TPEPNPQPDC PPSVPQSSLN GSHCPSGPDS
SRLIPSLPPE NSTRPLQPHP QPSLQPPPQP STVVPRVPPR CHRKRSRSES DSEKVQPLPI
SSLLRGPPLG ANSSPHHPNP GATTKQEPKF PAAPPHPHLA PVPNGGPPKV GKAVLVSNKA
LKKTVEHHGA TKKAYTKARQ GVPKPRAQPR DRVPPHPHAH PLTHPPSPSK PLYKKPVEKK
GCKCGRATQN PSVLTCRGQR CPCYSNRKAC LDCICRGCQN SYMANGEKKL EAFAVPEKAL
EQTRLTLGIN LTSITAAALR SPATSSPGNT LLNVTAATGA PVTATFLSGA GHDNRGFDDS
LEMRFDC
//
