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
//