ID M4B8U9_HYAAE Unreviewed; 1121 AA.
AC M4B8U9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
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:HpaP802706, 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:HpaP802706}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP802706};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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DR EMBL; JH597989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M4B8U9; -.
DR STRING; 559515.M4B8U9; -.
DR EnsemblProtists; HpaT802706; HpaP802706; HpaG802706.
DR VEuPathDB; FungiDB:HpaG802706; -.
DR eggNOG; ENOG502RRFR; Eukaryota.
DR HOGENOM; CLU_304122_0_0_1; -.
DR InParanoid; M4B8U9; -.
DR OMA; NMEKMIM; -.
DR Proteomes; UP000011713; Unassembled WGS sequence.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22696; E3 UBIQUITIN-PROTEIN LIGASE RNF26; 1.
DR PANTHER; PTHR22696:SF1; E3 UBIQUITIN-PROTEIN LIGASE RNF26; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000011713};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 1067..1110
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 122031 MW; 99FDFE5790CB22E0 CRC64;
MEKMILKNVA ASRNSTKNRA QQIVEALKKK RLLEAEEEDA AVDQAERALK KKKTEPTLSS
SPPSSTDVSA RTALAAGILS PARHSKPQAA PVAAFVSPSR RPAPLLQSPT LLSASPARSQ
GTVKPLHLSS PVRPPRSSVF LASPARLKPR GAGIAASPLR RRQELLTSPL RRGGVAAPSP
KRPLVFDDAA VETGRVMRTG GQPPLLCAAL EQVEVETAVT TTLTMKSGSK LTAKSPFQSF
QAKVRQSPAK LARTMTSPGC EHGRDSQLTR TEAMSVRPRA GPMLVDLTHS GGAVASDARA
TTSTGAVMES GSGGAAPVGR SSSVSTCVSK PMRKFLSSTT RPVVAQRSIC FSTEGVATAL
DVTPDGEIIV VGFIDGSVRL YEMDSSVPSD RHGYLLGHID EQSAQGSSSA HLRVKISPDG
RYVFVGCRQG PRVVMSINLD HYRNEKDGDD DNFEQCHKHF HSNGKLRGFA DVTTYVPQAN
SPHREQQESR DKRSAYYILT GLGVGNLNLW RFVEPELKQE EPIWQHLQNF SAGGNTATAA
AFLASSISSG TLAIAAVCKD KNVRVWPLEF MKQSPSSTGK SNDECAAEPD DIGSFEGNHA
VTSHFNIPNT SDVIAIHGQY AYGISLMGEA YRIYFPDSSN LNSSSLEQAP RQEFELEKIG
GGGGSTSRRS NIMLESLSAS DDGKAIIAVS TEGIFYYSNK LPDVGSSGVA GLCIIGKNAS
ENALFKTPMK VYTPLVTMKG TKVQSEAMMA VVTNPSSEDS ENEDGYINVD LTEVFAARWM
VPSRGNSCWV CGVRNTRHWV GPPESKTIEP ARAQLLAAER KDLLKAQRRR QRALKRAKDA
AGKQKERCHT NGQQTPTSAK TKTKTAPLMS AKKASVQKHS DVRPSSSADG SPEAAESSLS
SVRENGGVDN EDDEDCTGSD DNTPSVASLI SELEHFKKRN AEIKTEWQRR LQGERQLRRK
WKQREEEFLD QLNDSLTKLD AAEVEGDRLR VLLRDAEKRF AFEKACTEQE NSVKARYEQL
CEHMSDKLAL VVDQKRLLEQ TTRSLLAEVD RNVHALKNAV ILEKSECVVC KDQQAVTAVV
PCGHLCFCET DAETYRRSCT SKYPTCPMCQ QEIISLLRIY T
//