ID   Q1CVS0_MYXXD            Unreviewed;       497 AA.
AC   Q1CVS0;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=Response regulator/adenylate cyclase {ECO:0000313|EMBL:ABF91318.1};
DE            EC=4.6.1.1 {ECO:0000313|EMBL:ABF91318.1};
GN   OrderedLocusNames=MXAN_7396 {ECO:0000313|EMBL:ABF91318.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF91318.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF91318.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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DR   EMBL; CP000113; ABF91318.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1CVS0; -.
DR   IntAct; Q1CVS0; 25.
DR   STRING; 246197.MXAN_7396; -.
DR   EnsemblBacteria; ABF91318; ABF91318; MXAN_7396.
DR   KEGG; mxa:MXAN_7396; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG2114; Bacteria.
DR   HOGENOM; CLU_000445_110_0_7; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR037257; T2SS_E_N_sf.
DR   PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR   PANTHER; PTHR43081:SF1; PH-SENSITIVE ADENYLATE CYCLASE RV1264; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF160246; EspE N-terminal domain-like; 2.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:ABF91318.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402}.
FT   DOMAIN          154..269
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          311..451
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   MOD_RES         203
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   497 AA;  53205 MW;  E84FFDB9A74F28F1 CRC64;
     MGGGCDVHSP TMSASSPLFG DLLLKLGIVS PGQVQEALAL QALTGQRVGE ALISLGYVTR
     EQIQDALGEA LGLHQDKSPL QPALGELLVG LKYVTLAQLD EALARQRRDG RKLGEILVEL
     GHCTYKQIYE ALGLQNRIAG RQDLPRPSSD GRRRVVVVDD SPLACAFVQE GLVALGYEVL
     CFQDPFEALE SMGRLQPVIV LSDLEMPGLD GVELCRRLKE GPSHAVPAII LTANDVEAER
     VRGLRAGADD YVNKSASMDE LAARIESVVR RTGETERMRK LFARYTSDAV VEEILKSADA
     VVLTGEKREV TLLFADIRNF TGLAESLPPE QVVGVLNQVL GRMSDAVLTC GGTLDKFLGD
     GLMAVFGAPV ARPDDALRAL QSAKMMMDAL TDLRIEAEAE WAAGGREGQP LVLELGIGIN
     SGVVVAGNIG STVRAEYTCI GDAVNVAARL CALAGPGEIL VGERTRELVD ANETAFEDLP
     PVRLKGKQQP VPLFRAL
//