ID M4BTB4_HYAAE Unreviewed; 1026 AA.
AC M4BTB4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=CG-1 domain-containing protein {ECO:0000259|PROSITE:PS51437};
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:HpaP809699, 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:HpaP809699}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP809699};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the CAMTA family.
CC {ECO:0000256|ARBA:ARBA00008267}.
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DR EMBL; JH597831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M4BTB4; -.
DR EnsemblProtists; HpaT809699; HpaP809699; HpaG809699.
DR VEuPathDB; FungiDB:HpaG809699; -.
DR eggNOG; KOG0505; Eukaryota.
DR eggNOG; KOG0520; Eukaryota.
DR HOGENOM; CLU_006458_0_0_1; -.
DR InParanoid; M4BTB4; -.
DR OMA; FARMKTH; -.
DR Proteomes; UP000011713; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR CDD; cd00603; IPT_PCSR; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005559; CG-1_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23335; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR CAMTA; 1.
DR PANTHER; PTHR23335:SF0; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR, ISOFORM F; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF03859; CG-1; 1.
DR Pfam; PF00612; IQ; 2.
DR SMART; SM00248; ANK; 2.
DR SMART; SM01076; CG-1; 1.
DR SMART; SM00015; IQ; 3.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS51437; CG_1; 1.
DR PROSITE; PS50096; IQ; 2.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000011713};
KW Transcription {ECO:0000256|ARBA:ARBA00023163}.
FT DOMAIN 6..134
FT /note="CG-1"
FT /evidence="ECO:0000259|PROSITE:PS51437"
FT REPEAT 570..602
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 603..635
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 215..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1026 AA; 113455 MW; 09993ECB20787655 CRC64;
MNQARAAFLC NEATRRWLVK DELVFLLLHY KMVAVPLLRS VQFRPPSGTL LFCNTLEVSD
YKKDGWHWQK RKDKSGRVRE DRAKLVINRE VIVLGTYVHS AEISTFHRRI YYMRDSMKNI
VLVHYLDEMN KGCVGCPVST YVTKTRNEID RSLSVATVSM PPFQRQYSQK LVSSDKTEGS
IMDGSRTTLR RTASMDSSDA ISPSLKGDSM DGINTGLCAD EQTNDPDSLI SLGERNSGSE
GRRTFKLAEI SDFSPDWDFE DGGAKVLICL AANLPKSVAH DTMNLFVQFG TKRTRAEIVS
DTVLRCIAPS CTNPGSVHMY VCHWREALQQ EAFQLSQRKK FTYRSYRWAS PSLVGQVAKD
EQAIDLPEVS VPRAVHSASG MGKRSRTRAV HSSAGDECIR PLNNVLGSNR SLSTYVESDL
DERQCKIRVV ERLSEFHQVI QTKPEESAVG IIDSGVPGRF SGEESMFADA RGGSILRSEQ
PSGRVCSSSC QEQISSEHVP QSSSRVGPPV SSTSFGATST SLDDCAIEAL SDNELEQLSE
KLLERVVRQL VTVAHTSEEL LEELNSLDEA GLSLLHYVSF YNYSQLVLLL LAHGAQINQQ
STQGQTALHL AAGCGHDQVI DVLQQSGADL QVLDFEGLTA ADRADKSGHA DVAAKLYRCM
GDGTPIDSGV TDEIYGTLME IDDISTPYMD AGDMGLLESI EDSEFSVGPP HLYPNSCESP
YGARLPSKTV SRIGETQEHN RKLLLGAFST MSLHDKCALS LSISRESAGH AAWRRESIAE
EDLLISSSTS SSEVSAGFGF SKIASMDAAD LADGHFVLPS PQNDSDVHSV IADNEESLNK
LQVAMELMGP EERQSLEDEV KVLQHGIRAW LLKRNCRNMR ETTIQLREAT QSIKQQEDTE
HFPTGTNKQS ERERAAITVQ AATRTMLARR SFLQTKHVAI KLQAATRGVL CRKHFARMKT
HALASLVIQR NVREWWNKQP TAARSEGFGN KAGNVEEKDD DTKDGKSSSS PDAHERALCN
ESCHNL
//
