ID A0A073CE14_PLAAG Unreviewed; 563 AA.
AC A0A073CE14;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Two-component response regulator {ECO:0000313|EMBL:KEI66351.1};
DE EC=4.6.1.1 {ECO:0000313|EMBL:KEI66351.1};
GN ORFNames=A19Y_1279 {ECO:0000313|EMBL:KEI66351.1};
OS Planktothrix agardhii NIVA-CYA 126/8.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI66351.1, ECO:0000313|Proteomes:UP000027395};
RN [1] {ECO:0000313|EMBL:KEI66351.1, ECO:0000313|Proteomes:UP000027395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI66351.1,
RC ECO:0000313|Proteomes:UP000027395};
RX PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA Christiansen G., Goesmann A., Kurmayer R.;
RT "Elucidation of insertion elements encoded on plasmids and in vitro
RT construction of shuttle vectors from the toxic cyanobacterium
RT Planktothrix.";
RL Appl. Environ. Microbiol. 80:4887-4897(2014).
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DR EMBL; CM002803; KEI66351.1; -; Genomic_DNA.
DR RefSeq; WP_042152940.1; NZ_CM002803.1.
DR AlphaFoldDB; A0A073CE14; -.
DR STRING; 388467.A19Y_1279; -.
DR PATRIC; fig|388467.6.peg.1217; -.
DR eggNOG; COG2208; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR HOGENOM; CLU_477929_0_0_3; -.
DR Proteomes; UP000027395; Chromosome.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd17569; REC_HupR-like; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.140.590; -; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43156:SF2; MULTIDOMAIN REGULATORY PROTEIN RV1364C; 1.
DR PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lyase {ECO:0000313|EMBL:KEI66351.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000027395};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 59
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 563 AA; 63261 MW; 2D2AAF0EF2CED169 CRC64;
MSRGDGRKLK LMVVDDEPDN LDLLFRTFRR DFQVFKADSA LKALQILDDE GEMAVIISDQ
RMPEMNGTEF LGKTVERFPD TIRILLTGYT DVEDLVEAIN SGQVFKYITK PWNPEELKSV
IQQASETYKF FKQRTNTLRR ALRRESLYND VVSALRESLD HSSMLQTIVR TLGETFNATG
CCIRSAEAGK LSAQTFSYGG ETENVQTWLS QLETSMQRVL ESREIKIQQR ENSNPVSQIV
LPLTYQHDLL AVLAIYQENS PSPWSEDDIQ LLEVVSEQAS LALSQAKLYQ RTLELAEQMQ
NELKVASQIQ NNLLRQSWPE FETLRVQACC HPAREVGGDF FEVFTHPQGD IWVGLGDVSG
KGVPAALFMA SAISVMRREL SVETSPEPDQ VMQNLNSILS DDLVSNNHFI TMVVARYTPS
TGHLAYANAG HIYPLVWSRL NSNLGENHPH LSVPLEPLFL KTRGIPLGIL PVWRGKGDSL
TLNPGDIFLV TSDGITEATV VQETSDGSPA IRSMLQQEGL WKLLQQQEKL NLDGLLAAIR
EHNPVQEDDQ TILSLEVLLT DEN
//
