ID M3YM29_MUSPF Unreviewed; 1343 AA.
AC M3YM29;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Tripartite motif containing 66 {ECO:0000313|Ensembl:ENSMPUP00000012386.1};
GN Name=TRIM66 {ECO:0000313|Ensembl:ENSMPUP00000012386.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000012386.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000012386.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
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DR EMBL; AEYP01030127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9669.ENSMPUP00000012386; -.
DR Ensembl; ENSMPUT00000012587.1; ENSMPUP00000012386.1; ENSMPUG00000012480.1.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159240; -.
DR HOGENOM; CLU_005817_1_0_1; -.
DR InParanoid; M3YM29; -.
DR OMA; PQDFQWP; -.
DR GO; GO:0010369; C:chromocenter; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR CDD; cd19811; Bbox1_TRIM66; 1.
DR CDD; cd19794; Bbox2_TRIM66-like; 1.
DR CDD; cd05502; Bromo_tif1_like; 1.
DR CDD; cd16449; RING-HC; 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; IPR037372; TRIM66_Bbox1_Znf.
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 PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR PANTHER; PTHR45915:SF7; TRIPARTITE MOTIF-CONTAINING PROTEIN 66; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00643; zf-B_box; 1.
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 SUPFAM; SSF57850; RING/U-box; 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; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 28..79
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 102..137
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 162..203
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 1097..1144
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1185..1257
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 540..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 232..288
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 540..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1343 AA; 148416 MW; 17CC3A2AAA51EFBB CRC64;
VLPGLFRNIP HPKEKHRSGQ MEALVQTCSV CRQDLHDMGA RFLPCQHLLC KGCFQGLIQE
LRQVAKVLGG KLISCPGCKR VYLTRDVTEH FFLQCVSTGQ SKMARNCSEC KEKRAAHILC
TYCNRWLCSS CTEEHRHGPA PGGPLFPRAH KGPPGVSGGS GDFALYCPLH TQEVLKLFCE
TCDVLTCHSC LMVEHKEHRC RHLEEVLQNQ RMLLESVTTQ VAHKKSSLQT SAKQIEDRIF
EVKHQHRKVE NQIKMAKMVL MNELNKQANG LIEELEGITN ERKRKLEQQL QNIMVLNRQF
EHVQNFINWA VCSKTSVPFL FSKELIVFQM QRLLETNCNT DPGSPWSIRF TWEPNFWTKQ
LASLGCITTE GGQLSRADTP AYGGLQGPSS FYQSHQSPVA QQETLSHPSH KFQSPALCSS
SVCCSHCSPA SPSLKGQVPP PSIHTAHSFR QPSEMASQQL GSLQCSTLLP REKELACHPQ
PPKLMQPWLE TQPPVEQENT SQRLAPQLTS QPVCIVPPQD VQQGAHAQPT LQTPSIQVQF
GHHQKLKLSH FQQQPPQQLP PLPPPPPPPQ QPPPPIPPSQ HLTSSQHGSP PGPACSQNVD
IMHHKFELEE MQKDLELLLQ AQQPSLQLNQ TKSPQHLQQT IVGQINYIVR QPAPVQSQSQ
EDAVQASDEP SASEGPKPAL PLDKNTAANL PQAPGEETPP GVPPLDGTIQ HSSPNVVRKH
STSVSIMGFS NTLEMELSST RLARTLEPQI QSVSSLTAAP SHMVPSLLSS TPTTVSGLMS
GQNQAMPSLT VSHLQTVPSL VRSTPQSMPG LMNESSQAIT SLASDHSQAR PNPMSGTTQT
MPSLATCPLQ SMPPASDMQP ETGSSCSPGS GRTGGSLCPA DGADPSLGNA LCKMENEDST
RFTDSLGQDA TTPGLEVSKD LAVPSELEEP INLSVKKPPL VPAVNTSMAL QQYRNPKEHE
HFEQGAVETD AKENQSIRPF HSEPKIPYVR LERLKICAAS SGEMPVFKLK PQKNEQDGSF
LLIIECGTES SSMSIKVSQN NMPDAIQAPS LGGRKVTVTS LAGQQTPEGE GVSPEEQRLI
PRTPGAKKGP PVPMENEDFC AVCLNGGELL CCDRCPKVFH LSCHLPALLG FPGGDWVCTL
CRSLTQPEME YDCENARYYQ PGTRATPGLS VYDQKKCEKL VLSLCCNSLS LPFHEPVSPL
ARHYYQIIKR PMDLSIIRRK LQKKDPAHYT TPEEVVSDVR LMFWNCAKFN YPDSEVAEAG
RCLEVFFEGW LKEIYPEKRF AQPRQEDSDS EEVSSESGYS TPQGFPWPPY VQEGIQPKRR
RRHMENEKAK RMSFRLASSV SQV
//
