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Database: UniProt
Entry: A0A1S3LIY2_SALSA
LinkDB: A0A1S3LIY2_SALSA
Original site: A0A1S3LIY2_SALSA 
ID   A0A1S3LIY2_SALSA        Unreviewed;      1305 AA.
AC   A0A1S3LIY2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=E3 ubiquitin-protein ligase TRIM33-like isoform X5 {ECO:0000313|RefSeq:XP_013990790.1};
GN   Name=LOC106566845 {ECO:0000313|RefSeq:XP_013990790.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013990790.1};
RN   [1] {ECO:0000313|RefSeq:XP_013990790.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013990790.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_013990790.1; XM_014135315.1.
DR   OrthoDB; 4204111at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa13.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05502; Bromo_tif1_like; 1.
DR   CDD; cd15541; PHD_TIF1_like; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45915:SF3; E3 UBIQUITIN-PROTEIN LIGASE TRIM33; 1.
DR   PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50119; ZF_BBOX; 2.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
PE   4: Predicted;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          295..342
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          355..396
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          1054..1101
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          1157..1213
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..796
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          856..971
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          987..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1026..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1106..1128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1249..1305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..689
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..760
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..789
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..897
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        927..971
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        992..1010
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1033..1047
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1284..1305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1305 AA;  142723 MW;  97D72CE3F4EA3967 CRC64;
     MADNKGEEDM ESSSKLDSEP QGEDSGDPEL KDVNPPISIE TNLKEGEDSQ SQENVSQMPK
     PANDVVSGGG DASSNSAGTG EEDSISSNVS PVGNTNGGTT ELKNVNAVIV IESNSKEGED
     SQSQENISQV PTPANVSEGG DASSNSAGAV EEGSTSSSPV GNTNGGTTES SAAGDTAGTS
     PTLTTDMSPP PTVPPANPVI PINLMDTCAV CKQSLQTRDC EPKLLPCLHS FCLKCIPLPE
     RQVTVQVPGP NGQPDTHIVN VMRCVVCCQD CKQSDIIDNY FVKDTTEASK TSDEKSAQMC
     TSCEDNADTI GFCAECGEWL CKTCIEAHQR VKITKDHKIR KKEDVSEESV GVSEQRPVFC
     PIHKQEPLKL FCETCDTLTC RDCQLLEHKE HRYQFLEEAF QNQKGIIETH MVKLQEKKTY
     VHYSHSQVTS RIKEVTDTHK KVEHDIKIAV FTLINEINKK GKYLLQQLES VTKERSMKLL
     TQQTDIANLA RQILHVLNFT HSAINSGSST ALLYSKRLII YQLRKVLKAG LEPVPQANGA
     VRFFCDPTFW AKNVVNLGNL VIEKMPQAQH PPNIMVGPIS PGHGHPGHGK SPGQINLAQL
     RQQHMQQQAF AQQKQQQQHQ HQQHQQQQQQ HQQQHQQQHQ QQHQQQHQQQ QQQQQQQQHQ
     QQQQHQQRIQ EQMRIASQIS QQHPRQAVPQ MVQQQPPRLI SMQAQQRGPM NGGPNMYPPH
     HLRLPPGQGR MPSSSAQPRM PNGQQYSPMM QPQLQRQHSN PGHAGPFPVA SLHNVSAANP
     TSPTSASMAS AHAHRGPASP IVGAIDLIPS VTNPENLPCL PNIPPIQLED AGSSSLDALL
     SRYILASTYP QLGLGPPGNM NLSHGPSTHS PGSSGLSNSH TPVRPSSTSS TGSRGSCGSA
     GRPGPASGPM EQQVRVKQEP GAEKECGFSG TTTSNVKTEQ GKDGGRSACM MSSSESRRTP
     PLPVLGSVTS GSSVQDILKK VGEHVKTEPQ DQEACSGANR PGNAPITTSS TSTVASAALL
     TNGKGAASAA LRSPRTAQGT NQSGAGGKED DPNEDWCAVC NNGGELLCCD RCPKVFHITC
     HIPTLKCSPS GEWMCTFCRS LASPEMEYQP DDEPRGEKDN SEQGLSPEDQ RRCERLLLYV
     FCHDLSEGFQ EPVPPSIPNY YKIIKKPMDL TLVKQKLQLK HVQHYQSPKD FVSDVRLVFS
     NCAKYNEMSR IIQVYDEEKQ SNVQADSEVA EAGKAVSLYF EERLLELYPD ESFPEVPEEP
     EVPEVPEEPQ APAGEEADLT EDSEDEFVQP KRKRLKTDEK PMHIK
//
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