ID A0A316V2G5_9BASI Unreviewed; 1287 AA.
AC A0A316V2G5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FA14DRAFT_182538 {ECO:0000313|EMBL:PWN31747.1};
OS Meira miltonrushii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Brachybasidiaceae; Meira.
OX NCBI_TaxID=1280837 {ECO:0000313|EMBL:PWN31747.1, ECO:0000313|Proteomes:UP000245771};
RN [1] {ECO:0000313|EMBL:PWN31747.1, ECO:0000313|Proteomes:UP000245771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3882 {ECO:0000313|EMBL:PWN31747.1,
RC ECO:0000313|Proteomes:UP000245771};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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DR EMBL; KZ819607; PWN31747.1; -; Genomic_DNA.
DR STRING; 1280837.A0A316V2G5; -.
DR InParanoid; A0A316V2G5; -.
DR OrthoDB; 1409291at2759; -.
DR Proteomes; UP000245771; Unassembled WGS sequence.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd15571; ePHD; 1.
DR CDD; cd15497; PHD1_Snt2p_like; 1.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR029617; Snt2.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47672; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR PANTHER; PTHR47672:SF1; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00320; GATA; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 3.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000245771};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 37..170
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 207..259
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 590..636
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 817..867
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 910..1045
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 282..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1287 AA; 140998 MW; 2D0C74595402556F CRC64;
MAAIATSSAS STLSKSGSAA SIRPALPMTR VTIRDGTSIA INDHIYISSP WAPGAGEPYF
IARVMEFVTA SASRKGAAVV ASSSGTLQVR ANIYLRQRDI THRAIYDPRL LVATMHSDVF
ALENIRGKCQ VRHRDLIGDA PAVSAWKKTD DHFYFHQLFD RFLHKSFDVI PTDRVHNAPK
DVLTTLRNRY SFIVAEPGLS IDICGPVRSC SVCDEWAAGS ESVRCDTCKE YFHMTCLTPP
LVAKPAKGYS WTCAPCSKKR EQSQGLPMTR AAAMDASIAL TAGGGSSNMN SPSEDDASSV
SRLPGNQGSL RMGPGTRGRG RGRGRGRGRG RGGYSTTSRF ANGSEESSVS DQSREVSPAS
STVSDRKTLD DERGTRCFNR WPFRYFGEHT TAKDVLDPYD SIYPLAAPRL GVKFQVPVIT
WQEQQDLGLG VYVRPENNEA AILTEEIKQQ QTKRPPGRPP KIKKSTDTGG TNTPVLSTLP
LPSIDGTSSA GGGTPAPGLP SIETPKPPTE KDFERGLDES VDVLWKPKVV VDKVMDAYMR
LCDKHFQAHA HEVGLLNRAA QLMVIHKGNG PEALANLSRS TDDQLDIIHW SPKESKQFEK
AIAEFGADVK SLKRAIPTKT PGQIVRKLYS WKGQKLGEQW QEERQKSAEG NMDEDAVSKE
DSGVTRAVSP SLSIWNDDNE ASTSKTIVIP APSSLGTQAS SISTTNVSTS LQSGSTTPTS
VNKICKMCTT TQSPSWYKGP YSWHNRRLCV NCGIYWRKYA AESPSEILTR KREAQEESAA
VPSHVTKVAK LARSESVKGS SNTSTPPPVP TVTKFEPGKC VLCKKMEPKR NLIQCRQCSL
SVHQGCFGLT DEEVASEIWY CDACMNEKTL DAALIPRCIL CPKPPLPAEI PVVAPTVRPV
GRPRKNAANT QAASAVPIAP LDALDAYKPT ECNNWTHLLC ALYINELAFT EPEQMKIVEG
AGNLPFWRYE AVCDLCEKKE GACVSCSEPS CKRTFHVSCA HKQNGFTMGL DLTPVKSTRR
DTVATATFKG ETGHMAAAVY CDIHADVAKF RNLIDLSEID PNADISTNSR ESKTATQIFA
LTHKNVKAPS SGLSVGGATA SYDPTSYPLL RRAKRFDVLL GNGTIWHFSS NENKPNRKSL
TTTSGFNRAP ISKEGSLLSL IGSNAMKTNG VNFQDTKQPL RHLNGNAAKS SSTASLPREC
LRCATEFSPY WWPMPEEAEV EVQSPDEYGD WFHRFQGLRK EEQAWKESGR LYSDFEERLS
PREVSSLQRP VLCVQCRHRV GPDLSKV
//
