ID A0A1Y1UM83_9TREE Unreviewed; 1062 AA.
AC A0A1Y1UM83;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=PHD-zinc-finger like domain-domain-containing protein {ECO:0000313|EMBL:ORX39102.1};
GN ORFNames=BD324DRAFT_618522 {ECO:0000313|EMBL:ORX39102.1};
OS Kockovaella imperatae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cuniculitremaceae; Kockovaella.
OX NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX39102.1, ECO:0000313|Proteomes:UP000193218};
RN [1] {ECO:0000313|EMBL:ORX39102.1, ECO:0000313|Proteomes:UP000193218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX39102.1,
RC ECO:0000313|Proteomes:UP000193218};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J., Labutti K.,
RA Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R., Bowen B.P.,
RA Lipzen A., Sullivan W., Andreopoulos W.B., Clum A., Lindquist E., Daum C.,
RA Northen T.R., Ramamoorthy G., Schmitz R.J., Gryganskyi A., Culley D.,
RA Magnuson J., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORX39102.1}.
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DR EMBL; NBSH01000003; ORX39102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1UM83; -.
DR STRING; 4999.A0A1Y1UM83; -.
DR InParanoid; A0A1Y1UM83; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000193218; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR CDD; cd05839; PWWP_BRPF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13793:SF164; BROMODOMAIN-CONTAINING PROTEIN, 140KD, ISOFORM A; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF00855; PWWP; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000193218};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 134..184
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 188..300
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 491..561
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 940..1017
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 302..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..799
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 120340 MW; D650BACB3569CE30 CRC64;
MPILESAADQ KYQHSLPTVS FRIVEDDKAL LAPAGVHSEQ SRSYGYNDFS DFERPEFYIR
YIEPIEAELK GQVEYDMDEQ DQAWLDNINA ERKKDQSGPI SYEVFEIMVD KLEKEWFDLI
KRVPQPASHL PVEDSRCSIC DDPEGENSNA IVFCDGCNLA VHQDCYGVPY IPEGQWLCRK
CTVAPENPVS CLFCPNEGGA FKQTTTGHWA HLLCSIWIPE VTVSNAIYME PVDGVEMVPK
SRWKLICSLC RERVGACIQC DNKSCFTAFH VTCARQMGLL MSMKAMSTDG QLRAFCEKHL
PAGSQDDFDE DEDEDGSNYS GTPVAQPPPK PRVQHRLPKR KIGPVTTKSA RAHTKSYRPG
PPIVPQVIVQ TLLDYIAKFL IRKKQPFVER LCRYWSLKRE ARRGAPLLKR LHLEPWTAAS
ASKQQTDAEK ATKLKFLTML RNDLEKVRLL AELVRKREKE KLRQTQLIND MVDQFIFPYY
GRLRLTLEKI SAMDRQEIFL HPINAMEVPD YYDVVKEPMC WLYIDDKIER NRYRNVEEFK
HDVNLVLDNA ILYNAPETTF SRIAKRIKAN AKPLLEDLDS ILEWSSLRPS LADGDEPMTA
DDVEPSGDLE PSLVLLSSLL AKPAGGTEGS VDHLAELFRF ALDKPRAPTP PPEPPKKRNY
MSAEDKKRRW EEREQQAKQR VAARSSRATA AAARAFEEEA GLDTQHTPKA SGQRTRGRDK
HVEEQEVAAH ASHSNQVGVV GYETVAVLSD RERRAQERTL DLVTEDVDNQ DLFKRFNVGW
VLPEGSKRRR PDKPERPPDP PKTQVTQAKS EPSPEPDEPL EHRPLPSSRP SSLTPVSSSS
SSATEPLPEP ARPRRGAPAV QAEDIYRSGR KRKQPDSPEP VNNTKKRKAK EVEEDPKPET
RASVTSHKPP SRPRPRRSTA APRSVSAKPA GDEEEDPYPP STLVWAKLTS FPFFPAEIID
QDDDDPSEIP PSVFKNRAQA EKDNGATGQR TWLVRFFDAQ ASYGWIPASR LDLLGEDNNL
DEMYLAGKEK SRVKGFKSAH VKTACRKAYR EALAQMEVEE DE
//
