ID M4BQ83_HYAAE Unreviewed; 369 AA.
AC M4BQ83;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP808572, ECO:0000313|Proteomes:UP000011713};
RN [1] {ECO:0000313|Proteomes:UP000011713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX PubMed=21148394; DOI=10.1126/science.1195203;
RA Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA Tyler B.M.;
RT "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT arabidopsidis genome.";
RL Science 330:1549-1551(2010).
RN [2] {ECO:0000313|EnsemblProtists:HpaP808572}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP808572};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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DR EMBL; JH598554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M4BQ83; -.
DR EnsemblProtists; HpaT808572; HpaP808572; HpaG808572.
DR VEuPathDB; FungiDB:HpaG808572; -.
DR eggNOG; KOG0825; Eukaryota.
DR HOGENOM; CLU_063993_1_0_1; -.
DR InParanoid; M4BQ83; -.
DR OMA; HACNCDE; -.
DR Proteomes; UP000011713; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1020.10; TAZ domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR047157; PHRF1-like.
DR InterPro; IPR035898; TAZ_dom_sf.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12618; PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR12618:SF20; PHD AND RING FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57933; TAZ domain; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011713};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 151..201
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 154..199
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 244..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 41029 MW; A00FFAC1079E5E73 CRC64;
MAAVTRERFN WEEAVKQDRD LKRIDAFVKL TVSKCPGQLP PRTDASRGGS RYEPAADPVV
IKAEQHPILR TTLITPSSNG SVPFAPQFID PRDYQSESSS EMDTREVNPM DELSDFESET
PQRQTVLEQV QRMDVEMVAQ DEEKGDDHAK LTVCEICRNS DQENEIILCD DCDAEFHISC
LDPPLLEVPD GTWFCPTCSA KFHNVCDDRV KQELLPTAAD YESSTNAAGY SEVTAPPASV
DTMVTTTTSS SGQADSGGNV LMDGTGGNSD PASIHIAQAL EEDPKKSNAL LIHACNCDEV
QCSDPELNDF CPHMKRFLRS VCWASHSDKW RSYRLARITA ELFAYHAMNC DLLQCNVPLC
VKIREEEIV
//
