ID A0A3Q3FR99_9LABR Unreviewed; 956 AA.
AC A0A3Q3FR99;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=PHD finger protein 20 {ECO:0000313|Ensembl:ENSLBEP00000022347.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000022347.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000022347.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3Q3FR99; -.
DR Ensembl; ENSLBET00000023526.1; ENSLBEP00000022347.1; ENSLBEG00000017148.1.
DR GeneTree; ENSGT00940000156477; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd20104; MBT_PHF20L1-like; 1.
DR CDD; cd15634; PHD_PHF20; 1.
DR CDD; cd20453; Tudor_PHF20; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR041297; Crb2_Tudor.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR043449; PHF20-like.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15856:SF27; PHD FINGER PROTEIN 20; 1.
DR PANTHER; PTHR15856; PHD FINGER PROTEIN 20-RELATED; 1.
DR Pfam; PF02820; MBT; 1.
DR Pfam; PF20826; PHD_5; 1.
DR Pfam; PF18115; Tudor_3; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 377..407
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 142..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 109240 MW; A72B14F13E7B32BE CRC64;
MSKTPPTRRG ISFEVGAQLE ARDSLKNWYA ANIEKIDYEG EKVLIHYRQW SHRYDEWFDW
TSPYLRPVER VQLRRQGLQD DAPIPGFHVN DKVLASWSDC RFYPAKVISV NKDASYTVKF
YDGVIQTVKG IHVKPFIKER GGVCGGKSRS SERNMVRRAP NRRDRRLQEN GGPKNKRARR
STSDQEEESN SEDEEREERV VNEKKEKING ELEASTNIKQ EEEMPEQADQ NKPRDPQKET
ELTNGVKVEE DPENDKERCH VNGEVKKEEM ETDGSETKPY IDLPKPYKDS HSQLSAQSEQ
VSVTMTTNES SGSVEQKPTV QSESSQASAD VPPPQPVKPV RKQGFHNPNR FSREPLYRVI
KNQPPPVLSI NLDHNPFKCS APGCPKSFRK AKLLHYHMKY YHGEEQPLEG ERSPTRNVQT
RASDKQVTGM DGPKRRRTIS ASMHSVGAPG APRGEVKTAG RRTSAPPLVN TQGHQQRALL
REKSKENQLD RNGCHQLYKD SERGGFDIGS LKEKLKEKPK QKDFLRIKLK NKKKKKKAKS
DEDSISDWST DSCGWSDDDF GVDLDVTTPP LSIDSGAVDT NDQEIVRCIC EVEEENDFMI
QCEDCLCWQH GTCMGLLEDN VPDRYTCYIC RDPPGQRQSL RYWYDREWLS NGHMYGLSFL
EENYSHQNAK KITTTHQLLG DVHHVVEILN GLQLKMSVLQ CNTHPDLQLW RQPWKHLERS
QISSDSYRSG DAVPSPMTPD EDMSRGEILM SNALEKLSRA ATAAASSSSC SLSPFPFPSF
QDSYITSEHC YQKPRAYYPA VEQRLVVETR QGSELEDSMR STEELLEREQ RYGSLLETDK
PKSTGTGYKA ALAGSWSQAD TREEDGRDPG ESADISKQHQ QRQINLLDHI DAVQDEVSHR
MDFIERELDV LESWLDYTGE LEPPEPLARL PQLKHRMKQL LTQLGKVQQI ALYSST
//
