ID W5M8L3_LEPOC Unreviewed; 1113 AA.
AC W5M8L3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Zinc finger, MYND-type containing 8 {ECO:0000313|Ensembl:ENSLOCP00000004721.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000004721.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000004721.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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DR EMBL; AHAT01025268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01025269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M8L3; -.
DR STRING; 7918.ENSLOCP00000004721; -.
DR Ensembl; ENSLOCT00000004729.1; ENSLOCP00000004721.1; ENSLOCG00000003951.1.
DR eggNOG; KOG1473; Eukaryota.
DR eggNOG; KOG3612; Eukaryota.
DR GeneTree; ENSGT00940000154897; -.
DR HOGENOM; CLU_008433_0_0_1; -.
DR InParanoid; W5M8L3; -.
DR OMA; MPVQRFN; -.
DR Proteomes; UP000018468; Linkage group LG18.
DR Bgee; ENSLOCG00000003951; Expressed in testis and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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; 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; PF12064; DUF3544; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00855; PWWP; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 106..151
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 183..235
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 291..341
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1021..1055
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 968..1017
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 123571 MW; 2E8D7D84893CAABB CRC64;
SLAEEEIKTE PDVVEGMDIA TRSKVSDPGS AERAAQKRKL PSPPHSSNGH SPTDTSPSPI
KKKKKPGLVN SNNKEQSELR HGPFYYMKQP LTTDPVDVVP QDGRNDFYCW VCHREGQVLC
CELCPRVYHA KCLKLTAEPE GDWFCPECEK ITVAECIETQ SKAMTMLTID QLSYLLKFAL
QKMKQPGTEP FQKPVSLEQH PDYAEYIFHP MDLCTLEKFI KTSVTSFFDR NTVYEVIVVI
FFSGNHKLTA TAKVIVKICE HEMNEIEVCP ECYLSACQKR ENWFCEPCSN PHPLVWAKLK
GFPFWPAKAL RDKDGQVDAR FFGQHDRAWV PINNCYLMSK EIPFSVKKTK SIFNSAMQEM
EIYVENIRKK FGVFNYAPFR TPYTPNNQFQ MLLDPSNPSA GTVKPEKQEK IKFNFDMTAS
PKIILGKTML SGGTGRRISL TEMPRSPMST NSSVHTGSDI EQDTSEKSLK APTSHYSAGE
ESMDYTAVNC ASPASAKTGH AGSVTESPKP FSPQSSTPVT TKQERTSTTG SILNLNLDRS
KAEMDLKELS ESVQQQSTPV VLTSPKRQIR SRFQLNLDKT IESCKAQLGI NEISEDVYTG
VEHSDSEDSE KSDSSDSEYM SDDEQKLKNG QDDGDDKEKS ERDVKKKPKV SPQSEEKERN
VESTAVEKTA ELPAKEKPSP DPKKEPSDKA KGSQHSAKEK PKTKEEGVAG SGDLDVDSDS
DRELVIDLGE DHAGRERKKS KKELPASVSA AKETSAVKPE GAGKAPSSSS ATAQPSGDAS
SAPNVKDPTQ ASITIPINVV SFAATSLIPN TASSAAVKKQ RPLLPRETAP AVQRAVVWNP
TTKFQTSSQK WHMQKAAPQQ PSPSTRYQTR QAVKAVQQKE VTQSTSTSSV TLVTSTPSVS
MITTPVTIAT TSADVAADIA KYTNKIMDAI KGTMTEIYND LSKSTSGNTI AEIRRLRIEI
EKLQWLHQQE LSEMKHNLEL TMAEMRQSLE QERDRLIAEV KKQMELEKQQ AVDETKKKQW
CANCKKEAIF YCCWNTSYCD YPCQQAHWPE HMKSCTQSAT ASQQEPETEV NPDNKTSGQT
TGSHSSPTET TAIPTEKDST AEKNKDNVSV SVS
//