ID A0A498NZJ1_LABRO Unreviewed; 563 AA.
AC A0A498NZJ1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 22-FEB-2023, entry version 12.
DE SubName: Full=E3 ubiquitin-ligase TRIM33 isoform X1 {ECO:0000313|EMBL:RXN37712.1};
GN ORFNames=ROHU_001781 {ECO:0000313|EMBL:RXN37712.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN37712.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN37712.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN37712.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN37712.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:RXN37712.1}.
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DR EMBL; QBIY01005484; RXN37712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498NZJ1; -.
DR STRING; 84645.A0A498NZJ1; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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 SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Ligase {ECO:0000313|EMBL:RXN37712.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 322..369
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 409..481
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 61673 MW; DBE510429C458461 CRC64;
MRIATQMSQH PRQGGPPQIT GIQQPPPRLI SMQALQRGGV NGSSHMYPPH HLRMVSAQNR
MPSAQPRLNG QPYPMMQPQL QRQHSNPGHA GPFPVASLHN ISAANPTSPT SASMANAHIH
RGPTSPVVAP IELIPSVTNP ENLPCLPDIP PIQLEDAGSS TLDNILSRYI SASSYPAVGP
TNPSPGPSTH SPGSSGLSNS HTPARPSSTS STGSRGRSAF AFLPHSHSEF KKDILMSSPE
GSLTPPLPVL GSVSTGSVQD ILRTLGENVK SEPQSVQLSS CTNPNSSAPL TNGTTASNRS
QQGSTANANS QTTVGKEDDP NEDWCAVCQN GGELLCCDRC PKVFHMTCHI PTLRSSPSGD
WMCTFCRSLT NPEMEYNCDD DPPSKKDKSE MAMSPEDHRR CERLLLHVFC HELSTEFQEP
VPSSVPNYYK IIKQPMDLTL VKRKLQRKHP LHYKSPKEFV SDVRLVFSNC AKYNEMSRII
QVYDEEKQSN VQADSEVAEA GKAVSLHFEE KLLEIFPDQT FPVVVEKEVR AEAEMDSEDS
DDDVVQPKRK RLKVDAEKLM HIK
//