ID A0A081BPY3_9BACT Unreviewed; 488 AA.
AC A0A081BPY3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Adenylate cyclase {ECO:0000313|EMBL:GAK52449.1};
GN ORFNames=U14_03700 {ECO:0000313|EMBL:GAK52449.1};
OS Candidatus Moduliflexus flocculans.
OC Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK52449.1};
RN [1] {ECO:0000313|EMBL:GAK52449.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA Hugenholtz P.;
RT "First genomic representation of candidate bacterial phylum KSB3 points to
RT enhanced environmental sensing as a trigger of wastewater bulking.";
RL PeerJ 3:e740-e740(2015).
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DR EMBL; DF820458; GAK52449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A081BPY3; -.
DR STRING; 1499966.U14_03700; -.
DR HOGENOM; CLU_000445_110_0_0; -.
DR Proteomes; UP000030700; Unassembled WGS sequence.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
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; PF00989; PAS; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000030700}.
FT DOMAIN 15..138
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 150..221
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 307..439
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT MOD_RES 72
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 488 AA; 54657 MW; B7C3781BF0261A82 CRC64;
MRNSLDSLVD HKQKYILCID DDPGILESLY AHLAEYFGAA YQIEMAESGE EAFEIVNDIV
RENGRVELVI CDQVMPNLLG QYVLERLHQQ DARMMKVLLT GQAGLDAVTY AINHAGLHKY
IEKPWNKYDL LLTAENLLKQ YQMSTALEIE RQRYEMILRS MNNGVVSLDF HGRIISFNHA
AESILGIAAD NVLGRTYFEI FFEYAGNEAL NDIILACINE NHSAAYQEVE FLKKDGHKVP
LGLMISLLQD IDGAELGVLM VFHDLSEIRR YLSLKDTFSR YVTKQVVEKI SVSGENILLG
GEKREVTILF ADIRGFTPMT ERLEPTEVVQ ILNAYFSCMI DVIYEHEGTL DKFLGDGIMC
LFGAPINQPD HAIRAARAAI GMKHALAEFN RRQQEAGQQT LHVGIGINTG DAVVGNVGSE
KRLEYTAIGD NVNLAARLQS IAKGGQILIS NCTYRAIRDL ATINKLPPVK LKGKEQSVQV
YELLDIQA
//
