ID A0A1U7R3M8_ALLSI Unreviewed; 1198 AA.
AC A0A1U7R3M8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Protein kinase C-binding protein 1 isoform X5 {ECO:0000313|RefSeq:XP_006016762.1};
GN Name=ZMYND8 {ECO:0000313|RefSeq:XP_006016762.1};
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_006016762.1};
RN [1] {ECO:0000313|RefSeq:XP_006016762.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_006016762.1; XM_006016700.3.
DR AlphaFoldDB; A0A1U7R3M8; -.
DR GeneID; 102379005; -.
DR CTD; 23613; -.
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: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_006016762.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Transferase {ECO:0000313|RefSeq:XP_006016762.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 108..153
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 185..255
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 297..347
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1046..1080
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1000..1042
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 133189 MW; 4BAFD6D187DE3666 CRC64;
MHPQSLAEEE IKAEQDVVEG MDISTRSKDP GSAERTAQKR KFPSPPHSSN GHSPQDASTS
PIKKKKKPGL LNSNNKEQSE LRHGPFYYMK QPLTTDPVDV VPQDGRNDFY CWVCHREGQV
LCCELCPRVY HAKCLKLTAE PEGDWFCPEC EKITVAECIE TQSKAMTMLT IEQLSYLLKF
ALQKMKQPGT EPFQKPVSLD QHPDYAEYIF HPMDLCTLEK NVKKKMYGCT EAFLADAKWI
LHNCIIYNGG NHKLTQTAKV IIKICEHEMN EIEVCPECYL AACQKRENWF CEPCSNPHPL
VWAKLKGFPF WPAKALRDKD GQVDARFFGQ HDRAWVPINN CYLMSKEIPF SVKKTKSIFN
SAMQEMEVYV DNIRRKFGVF NYAPFRTPYT PNNQYQMLLD PANPSAGTAK TDKQEKIKLN
FDMTASPKIL MSKPMLSSST GRRISLTDMP RSPMSTNSSV HTGSDVEQDA EKKASSSHFS
ASEESMDFID KSTASPAPTR TGQAGSVSGS PKPFSPQAST PIAAKQERTS TPGSILNLNL
DRSKAEMDLK ELSESVQQQS TPVPLISPKR QIRSRFQLNL DKTIESCKAQ LGINEISEDV
YTAVEHSDSE DSEKSDTSDS EYITDEDQKS KNDQEDGEDK ESGRSDKESL TMKKKPKTPA
QVEDKEELKS TSPSAEKTDV PVKEKANTDS EKEFSEKGKS LQHPAKEKLK GKDETDSPTV
HLGLDSDSES ELVIDLGEDH CGREGRKNKK EPKEPPPKQD VAGKIPPSSN ASNPPPPSES
PVLTRSAAQT PPAGVTATTS ATSTVSAPAA ATGSPVKKQR PLLPKETAPA VQRVVWNSSN
KFQTSSQKWH MQKVQRQQQQ QQSQQSQSQQ PQSSQGTRYQ TRQAVKAVQQ KEITQSTSTS
TITLVTSTQP VSMVTSSGSA STLSSSVNTD LPIATASADV AADIAKYTSK MMDAIKGTMT
EIYNDLSKNT TGSTIAEIRR LRIEIEKLQW LHQPELSEMK HNLELTMAEM RQSLEQERDR
LIAEVKKQLE MEKQQAVDET KKKQWCANCK KEAIFYCCWN TSYCDYPCQQ AHWPEHMKSC
TQSATATQQE TDPEISTEAL NKSTQPSSSA QPTPTETAST PKEKESAADK SKESVTIATG
VTSNQPIKLV QVPQTTYIPT TQPTITIPVV VSPSAGTVAM RTGVQYVQTT MPVQVRRV
//
