ID A0A093EVH8_TYTAL Unreviewed; 1146 AA.
AC A0A093EVH8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Protein kinase C-binding protein 1 {ECO:0000313|EMBL:KFV48185.1};
DE Flags: Fragment;
GN ORFNames=N341_11174 {ECO:0000313|EMBL:KFV48185.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV48185.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV48185.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV48185.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KK380632; KFV48185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093EVH8; -.
DR Proteomes; UP000054190; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; 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:SF3; PROTEIN KINASE C-BINDING PROTEIN 1; 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}; Kinase {ECO:0000313|EMBL:KFV48185.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW Transferase {ECO:0000313|EMBL:KFV48185.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 80..125
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 157..227
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 269..319
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 969..1003
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 916..965
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 14..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV48185.1"
FT NON_TER 1146
FT /evidence="ECO:0000313|EMBL:KFV48185.1"
SQ SEQUENCE 1146 AA; 127277 MW; 9B6F2A9AD1A185EF CRC64;
DPGSAERTAQ KRKFPSPPHS SNGHSPQDAS TSPIKKKKKP GLLNSNNKEQ SELRHGPFYY
MKQPLTTDPV DVVPQDGRND FYCWVCHREG QVLCCELCPR VYHAKCLKLT AEPEGDWFCP
ECEKITVAEC IETQSKAMTM LTIEQLSYLL KFALQKMKQP GTEPFQKPVS LDQHPDYAEY
IFHPMDLCTL EKNVKKKMYG CTEAFLADAK WILHNCIIYN GGNHKLTQTA KVIIKICEHE
MNEIEVCPEC YLAACQKREN WFCEPCSNPH PLVWAKLKGF PFWPAKALRD KDGQVDARFF
GQHDRAWVPI NNCYLMSKEI PFSVKKTKSI FNSAMQEMEV YVDNIRRKFG VFNYAPFRTP
YTPNNQYQML LDPTNPTAGT AKTDKQEKIK LNFDMTASPK ILMSKSMLSS STGRRISLTD
MPRSPMSTNS SVHTGSDVEQ DAEKKATSSH FSASEESMDF IEKNTASPAP TRTGQAGSLS
GSPKPFSPQA STPISAKQER TSTPGSILNL NLDRSKAEMD LKELSESVQQ QTTPVQLISP
KRQIRSRFQL NLDKTIESCK AQLGINEISE AVYTAVEHSD SEDSEKSDTS DSEYSDEDQK
SKNDQDDGED KEGTRSDKES LSLKKKPKAP AQNEDKEELK STSPEVEKTD DPVKEKAIID
TEKEFSEKGK SLQHPAKEKL KGKDETDSPT VHLGLDSDSE SELVIDLGDD HCGREGRKTK
KESKEPPPKQ DVVGKTPPSS SASTQPLPET PVLTRSAAQT PPAGVTATTS ASSTVSAPSA
ATGSPVKKQR PLLPKETAPA VQRVVSRAST VQQKEITQST STSTITLVTS TQPISMVTSS
GSASTLSSSV NTDLPIATAS ADVAADIAKY TSKMMDAIKG TMTEIYNDLS KNTTGSTIAE
IRRLRIEIEK LQWLHQQELS EMKHNLELTM AEMRQSLEQE RDRLIAEVKK QLELEKQQAV
DETKKKQWCA NCKKEAIFYC CWNTSYCDYP CQQAHWPEHM KSCTQSATAT QQEADTEIST
ETLNKSSQPS SSVQSTPTET ASTPKEKEGS ADKSKETKGD WTSFSLSLQD PSVIGKHSKL
GSYSNRCDKQ PAYKTGPGTA DHHLYSNYSA HNYHSCSGKS FCWDSGNESW SSVCSDHNAS
PSTKSL
//
