ID I3LY62_ICTTR Unreviewed; 1361 AA.
AC I3LY62;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Tripartite motif containing 66 {ECO:0000313|Ensembl:ENSSTOP00000001081.3};
GN Name=TRIM66 {ECO:0000313|Ensembl:ENSSTOP00000001081.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000001081.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000001081.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AGTP01046072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01046073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01046074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01046075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01046076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01046077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01046078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01046079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01046080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01046081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 43179.ENSSTOP00000001081; -.
DR Ensembl; ENSSTOT00000001208.3; ENSSTOP00000001081.3; ENSSTOG00000001206.3.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159240; -.
DR HOGENOM; CLU_005817_1_0_1; -.
DR InParanoid; I3LY62; -.
DR TreeFam; TF106455; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 31..85
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 108..154
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 168..209
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 1105..1152
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1193..1265
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 441..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 238..294
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 547..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..587
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1361 AA; 151565 MW; E2582F267521DEC0 CRC64;
MDMFMNFKRQ PLADQKLCSR DGHMEAVAQM CSLCRQDLQD EGSWFLPCQH LFCKDCFQGL
MQELNHIARA YGTVPDELIS CPGCKRVYLT RDVTEHFFLQ CFPTGHPKMA RNCSECKEKR
AAHILCTYCN RWLCSSCTEE HRHGPAPGGS IFPRAQKGSS GVNGDSGDFA LYCPLHTHEV
LKLFCETCDV LTCHSCLMVE HKEHRCRHVE EVLQNQRMLL ESVTAQVAHK KSSLQTSAKQ
IEDRIFEVKH QHRKVENQIK MAKMVLMNEL NKQANGLIEE LEGITNERKR KLEQQLQSIV
VLNRQFEHVQ NFINWAVCSK TSVPFLFSKE LIVFQMQRLL ETNCNTDPGS PWSIRFTWEP
NFWTKQLASL GCITTEGGQL SRTDTPAYGG LQGPSSFYQS HQPPVAQQES LSHSSHKFQP
PALCSSSVCC SHCSPISPSL KGQIPPPSIH TTQSFRQPSE MVPQQLGSLQ CSTLLTREKE
LACSSHPPKL LQPWLETQPP VEQENTSQRP GQQQLTSQPV CIVPPQDIQQ GTHAQSTLQT
PSIQVQFGHH QKLKLSHFQQ QPQQQLPPPP PPPPPPLQQP PLPLPPSQHL ASGQHENPPG
PACSQNVDIM HHKFELEEMQ KDLELLLQAQ QPSLQLSQTK SPQHLQQTIV GQINYIVRQP
APVQSQSQED TLQVTDEPPA SEGPKPALPL EKNVAASLPQ TSGEETSHSV PSMDNTNQHS
SPNVVRKNST SVSIMGFSNT LEMELSSTKL ARTLEPQVQS LRSLTPGPPQ AVPSLLSGPP
QAVSSLTSVQ NHTMPSPTTS HLQVIPSLVH GTFQSMPNMM NETSPAITSL ASDHSQARPS
LLSAHTQAVP SLATCPLKSM PLVSDMQLET GSTSSPDPGR AVESLCPKDG VDPSLRNALC
KMESEDSSHF TDSVGQGPMA PGLDVPKDLA ITSELEEPIN LSVKRPPLAP VINTSKALQQ
YRNPQEYQNF EQRPLEMDKK ENQSIRAFNS EPKIPYVRLE RLKICAASSG EMPVFKLKPQ
KNDQDGSFLL VIECGTESSS MSIKVSQDSL PDAIQAPGLG GRKVTVTSLA GQQPPEVEST
NPEEHRLISR IPGAKKGPQV PIENEDFCAV CLNGGELLCC DRCPKVFHLS CHVPALLSFP
GGEWVCTLCC SLTQPEMEYD CENTRYSQPG VRVLPGLSTC DQKKCEKLVL SLCCNSLSLP
FHEPVSPLAR HYYQIIKRPM DLSIIRRKLQ KKDPAHYTTP EEVVSDVRLM FWNCAKFNYP
DSEVAEAGRC LEVFFEGWLK EIYPEKQFAQ PRQQDSDSEE VSSESGCSTP QGFPWPPCVQ
EGIQPKRRRR HMENEKAKRM SFRLANSISQ ISCVNINLVH H
//