ID D8F5U2_9DELT Unreviewed; 583 AA.
AC D8F5U2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Adenylate and Guanylate cyclase catalytic domain protein {ECO:0000313|EMBL:EFK08884.1};
GN ORFNames=NPH_5353 {ECO:0000313|EMBL:EFK08884.1};
OS delta proteobacterium NaphS2.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK08884.1, ECO:0000313|Proteomes:UP000003834};
RN [1] {ECO:0000313|EMBL:EFK08884.1, ECO:0000313|Proteomes:UP000003834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NaphS2 {ECO:0000313|EMBL:EFK08884.1,
RC ECO:0000313|Proteomes:UP000003834};
RX PubMed=21124915; DOI=10.1371/journal.pone.0014072;
RA Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., Mouser P.,
RA Lipton M.S., Deboy R., Methe B.A.;
RT "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and Analysis of
RT Differential Gene Expression during Anaerobic Growth on Naphthalene.";
RL PLoS ONE 5:E14072-E14072(2010).
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFK08884.1}.
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DR EMBL; ADZZ01000346; EFK08884.1; -; Genomic_DNA.
DR AlphaFoldDB; D8F5U2; -.
DR OrthoDB; 5427828at2; -.
DR Proteomes; UP000003834; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
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 Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
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; PF00672; HAMP; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00304; HAMP; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003834};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 305..357
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 391..524
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 583 AA; 65210 MW; 9474BF155E02E63D CRC64;
MVINSLQKRL GLLILLPVAL LLLFVGIFGF IYMRGTLLAE WQDASIVKLQ RAAHQIDMRL
GRITDWLHLF HHTSQGRGGP VIQDWILEQL REMKGVESAE LKWKDDRGSE SSMMMGMGMG
GRRSSGGRRM MRFHRAKPFE VTSPRYDAQK GKETVTLTSQ LKDASDKVVG TLEVTVRLDY
LLEGVKDFGW WQTEQACLID EAGKYLCHTK LVMKKGIFFG ETDEPFERAL LKAAKEKPYG
TILGPGAPPE IVGGFYRLRN APWTVVLFAE GDKVLAPIIH FRNYYFAGGI LAILIILIFI
RSVVGGMVHS FTAISKTAEK VAKGDYTKPI PVRGRDEIAQ LTQSFNTMME GLKERDFIAN
TFGRYVDQGI AKELLKRPEA SRLGGQKREV AILMSDIRGF TPLSETLSPE KIIALLNRYF
GELIGVIEIH QGIIVDFFGD AILVFFDPFD EPVTSVIQEA VQCAFAMQEG MREFNREMRS
ENLPSLQMGI GINAGEVVVG NIGSESRAKY GIVGSPVNLT QRIQSTAEPG EVIISDSVYR
YVQEDVNVTR KLRTTLKGVQ EETTLYAAEA RVVKEPIIMA QET
//
