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Database: UniProt
Entry: A0A1U7R3M3_ALLSI
LinkDB: A0A1U7R3M3_ALLSI
Original site: A0A1U7R3M3_ALLSI 
ID   A0A1U7R3M3_ALLSI        Unreviewed;      1219 AA.
AC   A0A1U7R3M3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Protein kinase C-binding protein 1 isoform X3 {ECO:0000313|RefSeq:XP_006016757.1};
GN   Name=ZMYND8 {ECO:0000313|RefSeq:XP_006016757.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006016757.1};
RN   [1] {ECO:0000313|RefSeq:XP_006016757.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; XP_006016757.1; XM_006016695.3.
DR   AlphaFoldDB; A0A1U7R3M3; -.
DR   GeneID; 102379005; -.
DR   KEGG; asn:102379005; -.
DR   CTD; 23613; -.
DR   eggNOG; KOG3612; Eukaryota.
DR   OrthoDB; 764287at2759; -.
DR   Proteomes; UP000189705; Unplaced.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; 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};
KW   Kinase {ECO:0000313|RefSeq:XP_006016757.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW   Transferase {ECO:0000313|RefSeq:XP_006016757.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   DOMAIN          129..174
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          206..276
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          318..368
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   DOMAIN          1067..1101
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          453..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1105..1160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1021..1063
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..741
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..779
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..831
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        853..904
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1105..1142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1219 AA;  135305 MW;  2479B0ADF7564CEB CRC64;
     MHPQSLAEEE IKAEQDVVEG MDISTRSKGQ GTLDQGLYAC NFAACDTSVD PGSAERTAQK
     RKFPSPPHSS NGHSPQDAST SPIKKKKKPG LLNSNNKEQS ELRHGPFYYM KQPLTTDPVD
     VVPQDGRNDF YCWVCHREGQ VLCCELCPRV YHAKCLKLTA EPEGDWFCPE CEKITVAECI
     ETQSKAMTML TIEQLSYLLK FALQKMKQPG TEPFQKPVSL DQHPDYAEYI FHPMDLCTLE
     KNVKKKMYGC TEAFLADAKW ILHNCIIYNG GNHKLTQTAK VIIKICEHEM NEIEVCPECY
     LAACQKRENW FCEPCSNPHP LVWAKLKGFP FWPAKALRDK DGQVDARFFG QHDRAWVPIN
     NCYLMSKEIP FSVKKTKSIF NSAMQEMEVY VDNIRRKFGV FNYAPFRTPY TPNNQYQMLL
     DPANPSAGTA KTDKQEKIKL NFDMTASPKI LMSKPMLSSS TGRRISLTDM PRSPMSTNSS
     VHTGSDVEQD AEKKASSSHF SASEESMDFI DKSTASPAPT RTGQAGSVSG SPKPFSPQAS
     TPIAAKQERT STPGSILNLN LDRSKAEMDL KELSESVQQQ STPVPLISPK RQIRSRFQLN
     LDKTIESCKA QLGINEISED VYTAVEHSDS EDSEKSDTSD SEYITDEDQK SKNDQEDGED
     KESGRSDKES LTMKKKPKTP AQVEDKEELK STSPSAEKTD VPVKEKANTD SEKEFSEKGK
     SLQHPAKEKL KGKDETDSPT VHLGLDSDSE SELVIDLGED HCGREGRKNK KEPKEPPPKQ
     DVAGKIPPSS NASNPPPPSE SPVLTRSAAQ TPPAGVTATT SATSTVSAPA AATGSPVKKQ
     RPLLPKETAP AVQRVVWNSS NKFQTSSQKW HMQKVQRQQQ QQQSQQSQSQ QPQSSQGTRY
     QTRQAVKAVQ QKEITQSTST STITLVTSTQ PVSMVTSSGS ASTLSSSVNT DLPIATASAD
     VAADIAKYTS KMMDAIKGTM TEIYNDLSKN TTGSTIAEIR RLRIEIEKLQ WLHQPELSEM
     KHNLELTMAE MRQSLEQERD RLIAEVKKQL EMEKQQAVDE TKKKQWCANC KKEAIFYCCW
     NTSYCDYPCQ QAHWPEHMKS CTQSATATQQ ETDPEISTEA LNKSTQPSSS AQPTPTETAS
     TPKEKESAAD KSKESVTIAT GVTSNQPIKL VQVPQTTYIP TTQPTITIPV VVSPSAGTVA
     MRTGVQYVQT TMPVQVRRV
//
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