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Database: UniProt
Entry: T1KY63_TETUR
LinkDB: T1KY63_TETUR
Original site: T1KY63_TETUR 
ID   T1KY63_TETUR            Unreviewed;       789 AA.
AC   T1KY63;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Protein kinase C-binding protein 1 {ECO:0008006|Google:ProtNLM};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur26g02600.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur26g02600.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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DR   EMBL; CAEY01000699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1KY63; -.
DR   STRING; 32264.T1KY63; -.
DR   EnsemblMetazoa; tetur26g02600.1; tetur26g02600.1; tetur26g02600.
DR   eggNOG; KOG3612; Eukaryota.
DR   HOGENOM; CLU_355781_0_0_1; -.
DR   OMA; HQLVYAK; -.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR000313; PWWP_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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; ZINC FINGER, MYND-TYPE-CONTAINING 8; 1.
DR   Pfam; PF00439; Bromodomain; 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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   DOMAIN          159..219
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          259..321
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          364..416
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   DOMAIN          706..740
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          751..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          642..691
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        14..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   789 AA;  89954 MW;  27D431ABC47C7A8B CRC64;
     MKIVDPASDV SPPPPQSSES SSQSHPSSSL SSQILNVSTP DPSTTQDQLG ALASTKPQET
     SDIANIKNNS IASESTKIDD QPELLTNSAD EMVEMQDTEN GISNHGGSPS CEISMKPKSQ
     GKKRPIDEVT RDQNEPTIES AEKKLAQHHY KNDKRQEKDD YCWICHKEKG NNYITCKSCP
     RSYHRKCLPP DNSASSELFE ANKNCANNSD WICIECSAIN KSEDLASKSS TLSHLNPHDF
     SELLMFAVQT IKATADRSFH QPVSDAVFPD YRSFIKHPMD FSTIERNIRS KVYKSTDSLM
     ADIKYIVHNC YIYNSPNHPL TKNANYFLKV AKNEMQEIEI CFNCFRNFYT FKDKDWFTEP
     CARPHILVYA KMRGYPPWPA KVVRYDKEKN EVDVRFFGAH DRSWVPVEQC SLLTKPNSTK
     SAKGSGKGQK NSKYDSALNE LALHVKRLNE LFPFKFHYAK SKQPINVNKL YICDGLEDEE
     MSSLDDDRDS DLNEDKLVID ETGDDLEIAE SDGKGLKSEK VESSSELSPS PDPPTIPEKP
     VKSEAPIPKL TIPKSIKIPL RSPQVQQQQS PQQPNASPKK DETPKSVKKK TSQGKVKKDK
     EKVENEKTPL SVKKSGSAKK KVPVKVEENE STKIFDELEA LRKKYEFEKM MHKEQLKEIE
     HNQNLKIREM RESWQKENER ALKELTTTLE EKYRKEIEET KKKLWCSECL KEAMYFCCWN
     TSYCSLDCQK AQWPKHASKC QQQSHWQQTN SQSTANQQQY NQSNQQQPQL QTASINNNTS
     TTSYNSTVN
//
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