ID A0A9W6EWX6_9CHLO Unreviewed; 2463 AA.
AC A0A9W6EWX6;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=PLESTBF000962 {ECO:0000313|EMBL:GLC47715.1};
GN ORFNames=PLESTB_000018100 {ECO:0000313|EMBL:GLC47715.1};
OS Pleodorina starrii.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Pleodorina.
OX NCBI_TaxID=330485 {ECO:0000313|EMBL:GLC47715.1, ECO:0000313|Proteomes:UP001165080};
RN [1] {ECO:0000313|EMBL:GLC47715.1, ECO:0000313|Proteomes:UP001165080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4479 {ECO:0000313|EMBL:GLC47715.1,
RC ECO:0000313|Proteomes:UP001165080};
RX PubMed=37296191;
RA Takahashi K., Suzuki S., Kawai-Toyooka H., Yamamoto K., Hamaji T.,
RA Ootsuki R., Yamaguchi H., Kawachi M., Higashiyama T., Nozaki H.;
RT "Reorganization of the ancestral sex-determining regions during the
RT evolution of trioecy in Pleodorina starrii.";
RL Commun. Biol. 6:0-0(2023).
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:GLC47715.1}.
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DR EMBL; BRXU01000001; GLC47715.1; -; Genomic_DNA.
DR Proteomes; UP001165080; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:UniProtKB-ARBA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProtKB-ARBA.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd15519; PHD1_Lid2p_like; 1.
DR Gene3D; 3.30.890.10; Methyl-cpg-binding Protein 2, Chain A; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_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; PTHR47162:SF10; METHYL-CPG-BINDING DOMAIN-CONTAINING PROTEIN 9 ISOFORM X1; 1.
DR PANTHER; PTHR47162; OS02G0192300 PROTEIN; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP001165080};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 117..192
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 1230..1280
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1688..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1806..1854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1871..1890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2003..2056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2075..2463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..89
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..191
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..226
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..238
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..359
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..590
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1183
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1197
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1322
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1568
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1688..1698
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1747
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1810..1819
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1830..1844
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1871..1882
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2003..2020
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2021..2033
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2104..2121
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2151..2162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2163..2184
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2195..2217
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2257..2273
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2282..2303
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2306..2321
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2413..2440
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2452..2463
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2463 AA; 255140 MW; 39570A51847363E2 CRC64;
MASEEDTNME PAAEKEEQQQ QQPKEKEKKE RSIAEIAAAA SEGDDDEEMA EAEAGGGPSA
QTPAATAAGS DGKAAAGGAA SDAAGTASSG AGGGASGKKA PVERPTREDA AVVEKLRAYV
ASLGGTLAPG WMGVYRMRVG GNSAGQYDLY YRSPEGRMIR SRAEVLRILG LDPSGGAGGS
GSAKKAVSAG PKSHKKKAAA AQPAEESATP AEGAAGAAEA AAEAGKTPGG SRGGGAGASA
GKWTLPVELP RAEAAAAAKE RAAGLGLEPP FTTDRGVTVL SLGTFHKAHG FCDATHIWPL
GYRAAWMPPH DSTTAAAAAA TKSKSKKKDK DAAADKGASE AAEPAATAAE GTDAPAADGS
AEQKQKPEAE AEPPEAPAAA SAADPPPPLP YRFISEIRTD SEGPAFAVLL EPNPDAPAAA
AADGAAAAAA AAAEPLLVHT AVSPDVVWSA VADLQVGAAA AVKRAKPSGA GAQPTAAQRA
LAAMPPLGKV WGMDCFGLSD VRVLQLLEAL PGVEAAEEYL YVQQRNSWEL EASSIATKRG
VVLTAAPNRR AAAAATKQRK RQQQLSIEAF VGRPPPSPKA AEGSEPPAGE AGEGLEDVAA
AAAKATGDGG GGAGKKSATK SKGGSRMTRE DLEVRGVLDR LVERVSLVMA EPDEKERQKM
LKAMEKSDRA AARRREKAAE KAAGGGATPA AADKDKEKEK DKEKKEKEKK EKEKKGKEKE
KKDKAEKEKK EKLPKTKAAK DKDAATDAAA KVGAAAADAA ATDGAAAAPP PLPGNQVDER
TLPTAEVPAP PGMPLQLLYP VAGGAAEAAA EGAAAAAAAS SLGMEEVQQL LSVYQFLWDH
RKLLGMEGRV PSLADLLAVV SEPPARLPAP ARRAADEVHL ALVRLLVGEA LDELLAYVAE
TSNLARRDIA AAVPPITAAT WPELARRYLA AAAAARYLAT SEPRSSALVS LQLPGQLQNM
EPADWLHYLL AGLNFPHLLS RIALLPQASS RWAADALLAA DDARARAAAE RALQGVQSFD
LQHLDGEGQV RRGRRLLHAL LTLPEGGEQL GFYAPEFGEV LRAPRGLDLH MVAARLDAGL
YHSTGDWLQA VATDVRSALA LWRGALGKRK DIPGHQDARA ALADEAERKL NELLASPDTA
LALPPPPADG AAAAAAAAKA DADGDAEMQD AGGSGGKGAG KAGGKSRKAS RSARRRKPAE
DGSQGAAEEE EEEDKDPCSL DNPTRLFNPR DGCRVCWLDE DKNRILLCDG CDGEYHCYCV
EPPLLEVPDG AWFCPSCTAR GLGLAKVEDE DEDLMDVDAA AGERRSTPRA ATPNRAAAGG
ASISPSDGSD PGRTPCSPAF QHCHSHSHLV SDLHDRAEAR RPQPHGAAAA AAAAAAAALA
PAPALPAGAR ASGMAETGEA PLAIPPDVPE GPRVTLRANS RPGLQELAGL LRLAHLLGNY
DYATGGPAGP TAAAAAAAAA ASAGGWTPSR RLALLSALCD LAMDTNALRN SLDEIVETRK
KARVEANAIR SKARQMQEEQ TAAKKAAAEK ENAPKPEGDA DANVNAAAGA AAAAAAGKGG
KGSKGGKGGA KDGKAGKGAK ADKGAEATGK EGAEEEGGTP EDKDGKEDGK EVTAAKSRNR
RTHLSVLPEA ELKRLMSLEV QVEGLAVRQE ALGEDRHGSR YWWLGADHLN PQGPQGVVLV
EQLPPGHAAA EQARAAKAFG EREAARRKED EEEQARKAQR EEAKRRKAAD GGEGEGGGQE
EEEELDEWGL PKERPRQRAV AIGVDAAPGR SWAVFHTADQ LNDLLGWLNP KGLREGPLRT
ALLRARDRSA ASQAPAAQAG DKQKQPPAPQ EAEQQPQPEA PAAEGGSGQP PPPLLCPCVS
VAAAGGRRGG AAARQGSVAP PDAAEDGAEP AEAMALRTEL LALHRGLPAE AFSRFWGSPA
RQEQWCAFVG AAASPQQVCA ALTTMEAMLV DEAFRPHWRL YCMPAQHPDL CTTWAAAWYR
LSGLQGAIRK QIIPQRELHH QAAAAAETAG GRKGASAAAG GKKDKSATAK KQEVATAPPE
RYSSRRGGAS VPALPDISNV RSREAAALLS SNLAVGGKGH KDAKGQKDAG GAGGRGQKRA
RSAEEDEGDD DDDEEQDEDA ENAAAGRKRG KRAATATAKD RSRRPASGGG RGKDGKAKKE
QSEEGEVVEE EEEDQDAEEE EEEGGSDREA LASGLEDEEE EDDDDEDEDD ESSDEEGDGG
RKRRSRPSRA SARLQKKSER SAPQTRRSSR LRKGEASDED GSSGDEEEEE EEDARPAKRT
RGAAAVVKAA AVGRGRTTRS SRAAAEESED EEEEEDGDSE DEGGRAAPAK GAQGRTRGGS
TAPASKPQAN GAAKPAMGSR AAAILANRKR ALADWSEESE EEEDGRRSSG SGGASGSEDE
PPPAAAAARR RGGAAAAAAP ASGKRGSGRQ QEQQQAAARR PPTRRMARSE VEYDVEDFDD
LNT
//
