ID K9VMH3_9CYAN Unreviewed; 675 AA.
AC K9VMH3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Adenylate/guanylate cyclase with GAF and PAS/PAC sensors {ECO:0000313|EMBL:AFZ08739.1};
GN ORFNames=Osc7112_4433 {ECO:0000313|EMBL:AFZ08739.1};
OS Oscillatoria nigro-viridis PCC 7112.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ08739.1, ECO:0000313|Proteomes:UP000010478};
RN [1] {ECO:0000313|EMBL:AFZ08739.1, ECO:0000313|Proteomes:UP000010478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ08739.1,
RC ECO:0000313|Proteomes:UP000010478};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Oscillatoria sp. PCC 7112.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR EMBL; CP003614; AFZ08739.1; -; Genomic_DNA.
DR RefSeq; WP_015177981.1; NC_019729.1.
DR AlphaFoldDB; K9VMH3; -.
DR STRING; 179408.Osc7112_4433; -.
DR KEGG; oni:Osc7112_4433; -.
DR PATRIC; fig|179408.3.peg.5503; -.
DR eggNOG; COG2114; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_000445_110_3_3; -.
DR OrthoDB; 456159at2; -.
DR Proteomes; UP000010478; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07302; CHD; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd19920; REC_PA4781-like; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR11920:SF335; GUANYLATE CYCLASE 32E; 1.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lyase {ECO:0000256|RuleBase:RU000405};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000010478};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 13..129
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 338..379
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 413..465
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 501..628
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 135..172
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 62
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 675 AA; 75126 MW; 4298B6298A3E2223 CRC64;
MMNDHPLPAI PKDILIVDDM PDNLRLLSTM LTSHGYHVRK AINGNLALQG AQISPPDLIL
LDINMPQMNG YEVCEQLKLS EKSKDIPVIF ISALDDVLEK VKAFQVGGVD YITKPFQVEE
VLARVQNQLS LRSLQSKLQL QARELHDRNS RLQEEIAERQ RAEESIRFLL ETTRAIGEAV
DFHSALEVIL HQVGETIGWD VGEAWIPDAE GTVLQSARGW YASNARMDAF RRQSEQLTFA
MNIGLPGRVW ASKQAEWVED ISRGYPDFFR SQIALELGFK AGFGVPILVG DEVLAVLVFF
KSSSGGKDAR FIDVFNAVGT QLGSLIQRKQ AEELLRIAQE KYHSIVENAM EGIFQSTPSG
GYLSANPALA KLYGYDSPEE LMSEIKNIAQ QLYVDPERRL EFVAAMDAEN AVSGFESMVC
RKDGRRIWVS ENVRAVRDSK GELLYYEGTV SDITERKLAQ EALKVQQEQS EKLLLNILPK
PIAERLKAEQ STIADSFAQV SVLFADIVGF TELSARMSPT ELVKRLNVIF SHFDQLAEKY
GVEKIKTIGD AYMVVGGLPT PRQDHAEAIA QMALGMQAKI AKLCAETGEK LAIRVGINSG
PVVAGVIGVS KFTYDLWGDT VNVAARMEAT GFAGSIQVTD VTYELLKDKY LFERRGVIPV
KGKGDMMTYW LLQKK
//
