ID W2ZEE6_PHYPR Unreviewed; 1021 AA.
AC W2ZEE6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=CG-1 domain-containing protein {ECO:0000259|PROSITE:PS51437};
GN ORFNames=F442_07931 {ECO:0000313|EMBL:ETP45668.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP45668.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP45668.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP45668.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CAMTA family.
CC {ECO:0000256|ARBA:ARBA00008267}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETP45668.1}.
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DR EMBL; ANIY01001670; ETP45668.1; -; Genomic_DNA.
DR AlphaFoldDB; W2ZEE6; -.
DR EnsemblProtists; ETP45668; ETP45668; F442_07931.
DR Proteomes; UP000018948; 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; 1.
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; 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; 3.
DR SMART; SM01076; CG-1; 1.
DR SMART; SM00015; IQ; 3.
DR SUPFAM; SSF48403; Ankyrin repeat; 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|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000018948}.
FT DOMAIN 11..139
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 381..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 879..909
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 385..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 112432 MW; E4064F167E61EB6A CRC64;
MISGNGIQAR AASLRQEATR RWLVKDELIF LLLHYKLVGV PILHSLQLRP PSGTLLFYDT
QKISDYKRDG WHWQKRKDKS GRVREDRAKL VINREVIILG TYVHSAETST FHRRIYSVRD
SKDTIVLVHY FDEANKDPAI RQLSLTSIKT NQSTSKGVKR SLPVAVTRGV IPLRQPSPPQ
PLSSEETVDS IMKNCFDMDF EPHGALYQTS SLNMSDADLQ LLKDSAMEEI SADDLFNDLA
SATSPEKDTS GLGGQQTFEL VEISDFSPDW DFGDGGAKVL ICLAAKLPER LALDPMKLFV
QFGMKRARAE KVSETVLRCT APSSLELGSV DMFVCHFGGS LECIQLTHKK QFTYRSHYQV
SPSLIGRIAR DKRVSEAGAI DPLDLTTPST PSAFGTGKRG RSPTVLSQSP VMKRSEDKFT
GSNRNLSTYV ESDLDERQCK IRVVERLSEF HQAIRTKTAE PAPIDPPAFA GSDSDDRNAT
LRREENSSLP TTLPTSGSST SQVAHPQQSS VKTESSDSST ALDDCTIETL SDNDLEQLSE
KLLERVVRQL ITVAHTSEEL LDELNSLDET GLSLLHYVSF YNYSQLVPVL VAHGAHINQQ
STQGQTALHL AAGCGHDEVV DVLLESGADL QVRDFDGLTA ADRAEKSGHA DVAAKLHHHM
GDDSSDLGTV DEIYGFGGSP MEIDDAPTPY TDAGDMGLLA ENDHVASNVH PPRSHSNSCE
SPCESNLSSK MTSYVGANQE HNRKLLLGAF STMSLHDKCA LSLTISRDSG GHVSRRRESS
VGEDVLINSP SSSTGTSAGF GSSPASMVGM DANLVGARLV LSGAENDSDV QSVIAEDEEG
LNKLQAAMEL MGPEERQSLE DEVKVLQHGI RAWLLKRNCK NMRETTKQLR EATQSIEDQQ
KQQEAAEQCS LVSSELSERE RAAVTVQAAT RSMLARRSFL QTKHVAIKFQ AATRGVLCRK
NFARMKAHAL ASLVIQRNVR EWWNKQPAAT RIDKETDDPE KDTEEEKTPI PEDAYEAQRS
L
//
