ID A0A3B4FN72_9CICH Unreviewed; 1217 AA.
AC A0A3B4FN72;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Tripartite motif-containing protein 66-like {ECO:0000313|Ensembl:ENSPNYP00000010701.1, ECO:0000313|RefSeq:XP_005724378.1};
GN Name=TRIM66 {ECO:0000313|Ensembl:ENSPNYP00000010701.1};
GN Synonyms=LOC102209605 {ECO:0000313|RefSeq:XP_005724378.1,
GN ECO:0000313|RefSeq:XP_005724379.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000010701.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000010701.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005724378.1, ECO:0000313|RefSeq:XP_005724379.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_005724378.1; XM_005724321.2.
DR RefSeq; XP_005724379.1; XM_005724322.2.
DR STRING; 303518.ENSPNYP00000010684; -.
DR Ensembl; ENSPNYT00000010945.1; ENSPNYP00000010684.1; ENSPNYG00000008112.1.
DR Ensembl; ENSPNYT00000010964.1; ENSPNYP00000010701.1; ENSPNYG00000008112.1.
DR GeneID; 102209605; -.
DR CTD; 9866; -.
DR GeneTree; ENSGT00940000159240; -.
DR OrthoDB; 56754at2759; -.
DR Proteomes; UP000261460; Unplaced.
DR Proteomes; UP000695023; Unplaced.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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); 1.
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; 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; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
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.
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:UP000695023};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 1..35
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 81..122
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 986..1033
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1073..1145
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 43..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 137..211
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 372..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1217 AA; 135764 MW; 39B01920CFDDE6B9 CRC64;
MEKSCSECTE PTLAQSLCTL CNKWLCYQCT DVHQHLRTPN TSQYMESHQQ QRPSATQFPE
LHQRGSSSLP PTGQGPGSYP WSLLMCHSHR QEPLELFCES CDLLCCSSCH LSSHKNHRVV
QIGKALQDQQ WLFESLMVQV EEKRSAVENS AKQIEERLHG VKIAHRKAEN QIKMAKMIMM
NELNKRANLL IEQLEKIAEG FQQRLEDQLQ GAIEICGQLD HIQKFITWAM THHCTSPVLF
SRALISLQMQ QLLEASHHSD SWSPVKIKFN WDASYWTKQI SCLGQLTVEG GNCAYPPGLA
CSSIMRPQPI TCLTLPPVFH RGREPGCGYQ ACCEPQMCCL HGIHSQPDLP SLDKSQLDTT
LYNSSCAQPA HISASQHQNQ QIQRFWDQES SLQRPPPASP VPNRRHNQLS RSRASASQPQ
AADSQPHSQS KSYLSHHQHR KEVLPNTQAR LSAERGRPNR RRGKLSTSRS LQQELSYTAL
ERDPMSEENR VETHRVEETC GQIAVAERRE MLDQEPVQQQ QQQQVLLCLS GVRKEQKRTN
SALIVKDHRD ARRSTSLEVT VTAHECVSDV QNSSRLSTGS VCSRRKRRSQ SIPTELAAPS
ASPYAERPTG WARSLEAGAA NKYYVLDPRQ RRASDGVLCV AKETSTEPPL MSYKTEPDHP
ITYINEEIGF DANKKCSFSS NSNSSDVQND SARPRVPVIC LERLKILVSQ LPPHGRRQSD
PLPASGTDKS ETLPQGITGE SETSGATRVL AAPKRQTCNE STAQSDCSDS NIGVPVPRKE
STLLSADSEY VAPSFYELDL DSDSDPRSVS EEAVISQADS DPQLDSDASP DSDPNAPSSS
EAELECRAEQ KSAEMGLCGD SEPSLEYEAD PESDAGPDGR GLDADTESGD AETESDIQPV
YDPTFQGETD SDVVSDQPPD SQGSVASELD VDSEPELTTD DPQPLRSDLD EEIGPGQRPL
LIANPVVPGD TEEVQTEQDS TELESEDFCA VCLIGGDLLC CDRCPKVFHL SCHIPPLPTF
PSGDWVCTLC RDVLHQGVEY NGDNERASGE NASANLLSPC DQKKCERLTL LILSNILSAP
FQEPVSPLAR HYYQIIKRPM DLSVIRAKLS KGNTQCYSSP DEFVADMYLM FRNCAKFNYP
DSEVAQAGRS LEAFFTSNLK EVFPGRVFPM AEVDSDSDEY DEAYRTTESG FPWPERREQC
HRKRKRRQSL KSRRHHF
//