ID A0A0G4ERC7_VITBC Unreviewed; 2226 AA.
AC A0A0G4ERC7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
GN ORFNames=Vbra_22481 {ECO:0000313|EMBL:CEL99842.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEL99842.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEL99842.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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 EMBL; CDMY01000290; CEL99842.1; -; Genomic_DNA.
DR STRING; 1169540.A0A0G4ERC7; -.
DR VEuPathDB; CryptoDB:Vbra_22481; -.
DR InParanoid; A0A0G4ERC7; -.
DR OrthoDB; 5490909at2759; -.
DR PhylomeDB; A0A0G4ERC7; -.
DR Proteomes; UP000041254; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15545; PHD_BAZ2A_like; 1.
DR Gene3D; 1.20.5.2050; -; 7.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001471; AP2/ERF_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; PTHR47177; F18C1.6 PROTEIN; 1.
DR PANTHER; PTHR47177:SF3; F18C1.6 PROTEIN; 1.
DR Pfam; PF00847; AP2; 7.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 1918..1968
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 22..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1553..1624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1750..1921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1971..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2124..2179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..986
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1801..1823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1835..1849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1852..1886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1900..1921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1983..2013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2130..2150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2157..2171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2226 AA; 242834 MW; 680203D25DFD2895 CRC64;
MAATQPASST TGLSALLAAV VNPIPAHPHP HPHPQWQQGD QPPPAGHDLL LNRGGKRQRT
GRGRGRRSAG EVEAQEQDEY TPEHDHDLAA AGHEARGQAG SRGGAAEDHQ ALNPDTHMSP
KEYLPKKPNG RPAPLGLQIV KGKGVRAQLY HPSVGALWGP TRNFDQFQSV RSAFKAACED
REQFVRDIWG PKGEAHQYQL LPGWETVVDD SHQPDRAERV PEQGPTQITT GAPAAQHPDP
PAPGAPHGST PSREGTPPPA GNRQRTSSRQ PKLLLGVLRK KCTPGHLEHQ PEYEAFAFRV
ADEGDGKRFM VTAWRGEGGG TDRPPVCVRA DVTRDHIGRG WDMSMLSDLL VAVHNGTADS
DDRFESVSDV IDGVERTVTQ WKQPAAGLIG VPSPVNDSPP AGAPGPSSVT LAAAGGGGGS
GSADPPLDEP PDDKGLMSAS QSGVRGVSFD NKNGGYWIAT WHEGRRRKRK SFCVKELGFE
EAKDAAIAHR REMERLAVVK KRSKHQSGVS GVSYNGPNKS WVAEWRKGGR KKTKSFSVKQ
LGYEEAKQAA IAHRQKMEQR RHTSEGGATR DESRSCSPPN DDGAIHSVVL PGTPVQSVPL
SAATREAMGA AIDAAWACRQ QEMDMDGTED QQPMTHAQRM VLCREYGQVG HNIGAMLAAV
PSLSFASIDS FVRHELPAMV GQRDGEDIKE AASRFIKQLQ KTNRQHTRLG YEAVTDTATR
HKRALMEQRH SPFERGAPPS SGSDSSGSLE GRTGSPGNKQ RRMDEEDGGL SPSSDRYDLG
GLTGDALGRG LMRRLRQEQP NVHSLCLNNG GVGVSWRATC VFEGYFWDSQ AAAAVDLRQF
GVGEDVTSRE AIFTAFRQAV EYRNALHSSR LGDQAVLIDL SWLEEAQRGA AVDGNSPLER
HRSMPPPLDK RDPMPPRVEP KGRRGRPLHE SSGAPGRATD ALPIGAPGPS CMPPAAAGGG
VAEPPHNEPR RHKGLSAKRR HGHRRQSTVC GERVTPSAGP ADEESAVDRS PSPKTRHTHP
LGSCPPAHDG APTPDASEGR YQSDVRGVSW AKKNKAWRAT WYERGDPKMK SKYFYVKHHG
FDKAKVLTTA TPTAVVNLSH VCRVYQALAE QHRLEMERTG RAVVKQRSGQ SGVKGVRYIE
SSNSWIAEWR EGGGRKSKSF SVKQLGYEKA KQAAIAHRRE MEQRRHTSEG GATREESRSR
SRHNDDDDEI HSARRHGPPS SGSGVGGMEG GDLAAALVEV LSSDGSCGLC WQDGSFRVRV
PSSVGKGAAE RILDVPVVDL SSRSAVIDAF RRAVEQLNRL STASEGEASA PLDISWLDDI
GPHGCNRPRT RRGNRARRKP MPPPSLSEGP SDHTLDSNDL ASSDTRHRHR RRGRSAHRVS
KRPMVDPSGL ESGEPSHRPG SRRDSQDEIM PPPVRPTSEA HRRRDGEQLP HRPGAKRRRG
QSGGGKERIV SARLSEGGGH SLAASLVEQA KRQLADGNRG DADSLGLERR GEEASFVAYR
QDGEARHDER VFSVSDVTSS RLILRAFAQA AHHRNATAGD GAIVVDVRRI KLHPQPTDKH
DADKGTSSGT ASMGPAHKGR EADVGGAGGD NEVDGRGELS SPDEQPRRRA TRGKKKTFVQ
RAHHHSDVKG VYWSEQGQYW QAKWGSKNDG KQENKNFFVR DHGFHKAKAL AEQHRLEMER
TGRASVQKLS KHQSGVRGVH YNETDKSWVA QWREGGRRKS KSFAVAEHGY EPAKQAAIAY
RRAMEERHYT PFGSDSQPVH QPPSPHDSAA GHGRPEAIRP QPLPPAAQEK DIDMRGGSMA
SSRHLGQQSD GQQCSSPHRR ISLSLSSVGR RGPKPRSSEA SRHAEMASPS EKEWQGYSTS
SLSSGGEGGD SDYRDSSSSS PPRRLLPPKS TSRHSGRRGR KRVSTDDIKE AGSDSDDSVR
CLKCGKGDDE QLLLLCDNGG CSAAYHTYCV QLTAVPKGKW FCPECTHSSN APVAAHPHST
GTRQTHRSSD QERGSPRRPA PKRKTVDRKR ARDEADLDGL TGTALAKALA DRLIRRFNDA
CPLANGGVGI CMASPRRFTA YFFKQGKYLG LRKFVIEDPD SRDSTLDALR LCVAYRNTIH
RDQLGDRATI IDLSWLDPQQ QGGKEELGLS VRDQSSDRSP SRKHCRRDAS LASRSPSVAE
RRPSPNSGKT ATAVVGRAAP HRSDVSGVSW YERDQAWRAS WYDKGDPMMK SKYFTVKNHG
FDKAKV
//
