ID R0K1Y5_ANAPL Unreviewed; 1183 AA.
AC R0K1Y5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Protein kinase C-binding protein 1 {ECO:0000313|EMBL:EOB03647.1};
DE Flags: Fragment;
GN ORFNames=Anapl_02445 {ECO:0000313|EMBL:EOB03647.1};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOB03647.1, ECO:0000313|Proteomes:UP000296049};
RN [1] {ECO:0000313|Proteomes:UP000296049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749191; DOI=10.1038/ng.2657;
RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA Rao M., Pitel F., Wang J., Li N.;
RT "The duck genome and transcriptome provide insight into an avian influenza
RT virus reservoir species.";
RL Nat. Genet. 45:776-783(2013).
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DR EMBL; KB742845; EOB03647.1; -; Genomic_DNA.
DR AlphaFoldDB; R0K1Y5; -.
DR Proteomes; UP000296049; 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:EOB03647.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000296049};
KW Transferase {ECO:0000313|EMBL:EOB03647.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 81..126
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 158..228
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 270..320
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1017..1051
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 964..1013
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 15..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOB03647.1"
FT NON_TER 1183
FT /evidence="ECO:0000313|EMBL:EOB03647.1"
SQ SEQUENCE 1183 AA; 132040 MW; B7C1E4B925E9DF75 CRC64;
IDPGSVERTA QKRKFPSPPH SSNGHSPQDA STSPIKKKKK PGLLNSNNKE QSELRHGPFY
YMKQPLTTDP VDVVPQDGRN DFYCWVCHRE GQVLCCELCP RVYHAKCLKL TAEPEGDWFC
PECEKITVAE CIETQSKAMT MLTIEQLSYL LKFALQKMKQ PGTEPFQKPV SLDQHPDYAE
YIFHPMDLCT LEKNVKKKMY GCTEAFLADA KWILHNCIIY NGGNHKLTQT AKVIIKICEH
EMNEIEVCPE CYLAACQKRE NWFCEPCSNP HPLVWAKLKG FPFWPAKALR DKDGQVDARF
FGQHDRAWVP INNCYLMSKE IPFSVKKTKS IFNSAMQEME VYVDNIRRKF GVFNYAPFRT
PYTPNNQYQM LLDPANPTAG TAKTDKQEKI KLNFDMTASP KILMSKPMLS SSTGRRISLT
DMPRSPMSTN SSVHTGSDVE QDAEKKATSS HFSASEESMD FTEKNTASPA PTRTGQAGSL
SGSPKPFSPQ ASTPISAKQE RTSTPGSILN LNLDRSKAEM DLKELSESVQ QQSTPVPLIS
PKRQIRSRFQ LNLDKTIESC KAQLGINEIS EAVYTAVEHS DSEDSEKSDT SDSEYSDEDQ
KSKNDQEDGE DKEGTRSDKE SLSLKKKPKP PAQNEDKEEL KSTSPEVEKT DDPVKEKAIT
DTEKEFSEKG KSLQHPAKEK LKSKDETDSP TVHLGLDSDS ESELVIDLGD DHCGREGRKN
KKESKEPPPK QDVVGKTPPS SSASTQPLPE TPVLTRSAAQ TPPAGVTATT STTSTVSAPS
AATGSPVKKQ RPLLPKETAP AVQRVVWNSS NKFQTSSQKW HMQKMQRQQQ QQQNQQSQSQ
QPQSSQGTRY QTRQAVKAVQ QKEITQSTST STITLVTSTQ PISMVTSSGS ANTLSSSVNT
DLPIATASAD VAADIAKYTS KMMDAIKGTM TEIYNDLSKN TTGSTIAEIR RLRIEIEKLQ
WLHQQELSEM KHNLELTMAE MRQSLEQERD RLIAEVKKQL EMEKQQAVDE TKKKQWCANC
KKEAIFYCCW NTSYCDYPCQ QAHWPEHMKS CTQSATATQQ ETDNEISTET LNKTSQPSSS
VQPTPTETAS TPKEKEVSSD KSKESVTCSF WSGSFDTSCL LISNTDCSTS KPFLPGDHSC
SGKSFCWDSG NENWSSVCSD HNASPSTKSL TANKKSIQLL EKI
//
