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Database: UniProt
Entry: D8FWP9_9CYAN
LinkDB: D8FWP9_9CYAN
Original site: D8FWP9_9CYAN 
ID   D8FWP9_9CYAN            Unreviewed;       912 AA.
AC   D8FWP9;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=PAS domain S-box protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=OSCI_1090019 {ECO:0000313|EMBL:CBN54789.1};
OS   Kamptonema sp. PCC 6506.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Kamptonema.
OX   NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN54789.1, ECO:0000313|Proteomes:UP000004532};
RN   [1] {ECO:0000313|Proteomes:UP000004532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX   PubMed=20675499; DOI=10.1128/JB.00704-10;
RA   Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT   "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT   reveals several gene clusters responsible for the biosynthesis of toxins
RT   and secondary metabolites.";
RL   J. Bacteriol. 192:5264-5265(2010).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC       {ECO:0000256|ARBA:ARBA00005381}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   EMBL; CACA01000105; CBN54789.1; -; Genomic_DNA.
DR   RefSeq; WP_007354014.1; NZ_CACA01000105.1.
DR   AlphaFoldDB; D8FWP9; -.
DR   OrthoDB; 436222at2; -.
DR   Proteomes; UP000004532; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd12913; PDC1_MCP_like; 1.
DR   CDD; cd12912; PDC2_MCP_like; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR033479; dCache_1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR11920:SF335; GUANYLATE CYCLASE 32E; 1.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF08448; PAS_4; 2.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          377..429
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          573..645
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          647..700
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          736..863
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   COILED          684..711
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   912 AA;  103068 MW;  4A09F5C874039055 CRC64;
     MLLKALTRRI AKGSQKIPLR LVLVVPFVLQ IFGTVGLTGY ISLRNGQIAV NDVAQQLQVE
     IGVRIEQMLT HYLQLPIVIN RINVNAMKLN QLNTKDTSSM TRHFWNQRLL FDSVKISAIY
     FGSNEGEFFG LGWQDNQSWQ IGRSGKQTKS RFHSYAIDNE GNPTTLLEVG NVYDPRRRPW
     YKKAVAVGKS VWSEIYIDFK EPRLKITLAQ PIYNNLGKLG GVVGVDFILS DIQDFLKSIK
     IGKTGHTFII ERSGLLVASS TDQQLFTRDK NGKIKERIQA KDSSTLVIKA TAEYLNSQKE
     KLTKINSVQH FIFEIDGTKQ FLQVTPLKDA RGIDWLIIIV VPESDFMEQI HANTRTTIWL
     CLGALIVATA LGIFTAHWIT APILRLSEAT QALAKGELDR KVKEKGTREL KVLASSFNQM
     AHQLKKTFAT LEKTNEILEA KVKKRTAALT ESELQNRAIL AAIPDLMIRL SKEGVYLEFI
     PSKDSEAILL VNNDRIGKHI SEVLPPDIAE LQLQYINRTI ATGETQIYEH QFWSGGQLCE
     QEVRIVVSRT NEVLLIVRDI TERKRLEREL SQTSRFLNSI VENIPLALFV KDVKDDFRYV
     LWNRAAEKVY SIPRNQVIGH TIYNFMNIEI AASVQSEHQT IIEGGKLIVD EEIFNSKFKG
     NIWQRIMKLP LINEQGEVTH LMYIAEDITE RKQAEEALRI AQEQSERLLL NILPKTIADK
     LKQNQSAIAE QFEEATILFA DIVGFTPLSA RTPPIELVSL LNHIFSTFDE LAELHGLEKI
     KTIGDAYMVA GGLPVPMEFH AEAVAQMALD MQTAIARFQA EKGQPFQIRI GINTGAVVAG
     VIGIKKFIYD LWGNTVNIAS RMESQGIPGR IQVTNATYKR LKDKYLFEER GAIAIKGKGE
     MITYWLTGKK VD
//
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