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Database: UniProt
Entry: W5M8L3_LEPOC
LinkDB: W5M8L3_LEPOC
Original site: W5M8L3_LEPOC 
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
//
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