ID A0A3B4GRH1_9CICH Unreviewed; 1072 AA.
AC A0A3B4GRH1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Protein kinase C-binding protein 1-like {ECO:0000313|Ensembl:ENSPNYP00000025767.1};
GN Name=ZMYND8 {ECO:0000313|Ensembl:ENSPNYP00000025767.1};
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:ENSPNYP00000025767.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000025767.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3B4GRH1; -.
DR Ensembl; ENSPNYT00000026403.1; ENSPNYP00000025767.1; ENSPNYG00000019367.1.
DR GeneTree; ENSGT00940000154897; -.
DR Proteomes; UP000261460; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05508; Bromo_RACK7; 1.
DR CDD; cd15538; PHD_PRKCBP1; 1.
DR CDD; cd20160; PWWP_PRKCBP1; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 6.10.140.2220; -; 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; IPR044075; PRKCBP1_PHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR021931; ZMYND8.
DR InterPro; IPR037967; ZMYND8_Bromo_dom.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR002893; Znf_MYND.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46453; PROTEIN KINASE C-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR46453:SF5; PROTEIN KINASE C-BINDING PROTEIN 1 ISOFORM X1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF12064; DUF3544; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00855; PWWP; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 104..149
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 181..251
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 293..343
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1028..1062
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 29..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 975..1016
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 38..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 118583 MW; F0C4CFB14757EF8E CRC64;
MTHFQLSVTF DCTTHLNTCG NVIFSLEEEE EGKTEEQAVT EEMEISTRSK EAGSTERVPP
KRKMPSPSQS SNGHSSAETS PCPVKKKKKP GAVSSSKDQD GRNDFYCWLC HREGQVLCCE
LCPRVYHAKC LKLPAEPEGD WFCPECEKIT VAECIETQSK AMMMLTIDQL SYLLKFALQK
MKQPGTEPFQ KPVSLEQHPD YAEYIFHPMD LCTLEKNVKK KMYGCTEAFL ADAKWILHNC
IIYNGGNHKL TTTAKVIVKI CEHEMNEIEV CPECYLSACQ KRDNWFCEPC SNPHPLVWAK
LKGFPFWPAK ALRDKDGQVD ARFFGQHDRA WVPLNNCYLM SKEIPFSVKK TKSIFNSAMQ
EMEVYVENMR KKFGVFNYAP FRTPYTPDNN FQMLLDPSNP SSGPIKPEKQ EKIKLSFDMT
ASPKIALTRT LLPGAGVGGS AAGRRLPLTD MPRSPMSTNS SAHTGSDGEQ ETTDKSQTKA
SNSQFSTGEE SMDCTVSPAH PRPGGAGGSL DSPKSLPSQA PGIPKQEKTP QTGSILNLNL
DRSKADMDLK ELSETVQQKQ GATPVLTSPK RLIKSRFQLN LDKTIESCKA QLGIGEISVD
VYKGVEHSDS EETDKSDSSD SEYGSDEEQK TKNEQDTAPS EEPQKEPTKT NVKDQPSPSN
EEEGRADLLV ATESAAGEAT VTVSDAQTKE KTSSEVEKES PEKSKAPRES PVPREKSQVK
QETKQTVPVE DSDSERELVI DLGEDYTFSV CLTRNRLTLH VILLILFKPY QLCKASITST
PPSQNSTAPS TPSSVSMQSP VAIPVTVVSF TAPSPATISL ASASSATATP PPSTSTSTTP
ALKKQRPLLP RETVPVVQRA VVWNPTAKFQ TSSQKCTSTS AVTLVSSSPA SVAMMAASSL
GTAAAPSPVA TDLYIPTASA DVAADIAKYT NKIMDAIKGT MSEIYNDLSK NPSGNTVAEI
RRLRIEIEKL QWLHQQELSE MKHNLELTMA EMRQSLEQER ERLVSEVKKQ MELEKQQAVD
ETKKKQWCAN CRKEAIFYCC WNTSYCDYPC QQAHWPEHMK SCTQSGNSAC RH
//
