ID M3CNP1_LEPIR Unreviewed; 749 AA.
AC M3CNP1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Adenylate/guanylate cyclase catalytic domain protein {ECO:0000313|EMBL:EMF43124.1};
GN ORFNames=LEP1GSC067_4074 {ECO:0000313|EMBL:EMF43124.1};
OS Leptospira interrogans serovar Lora str. TE 1992.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193028 {ECO:0000313|EMBL:EMF43124.1, ECO:0000313|Proteomes:UP000011754};
RN [1] {ECO:0000313|EMBL:EMF43124.1, ECO:0000313|Proteomes:UP000011754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TE 1992 {ECO:0000313|EMBL:EMF43124.1,
RC ECO:0000313|Proteomes:UP000011754};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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:EMF43124.1}.
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DR EMBL; AKWW02000030; EMF43124.1; -; Genomic_DNA.
DR AlphaFoldDB; M3CNP1; -.
DR Proteomes; UP000011754; 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; 1.10.8.500; HAMP domain in histidine kinase; 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; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR43081:SF16; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 170..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 454..506
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 538..670
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 749 AA; 85011 MW; 5DE920EA2B3BE347 CRC64;
MTEDKTFLFC SRLKEGGMLD RWKDKNDKSV RWEELPNLHS DLQDLDLIIR SLISEKLSLG
IREIIFCLSA EQALSLKKSR DFLKLIKDLK RAGFTISSAD KDKILSTNVE SSSKFFRYLE
NRSRNVNCLV WTEDLALSQI ESKYYDFLNH FHGYKFESFR PSRFTIRVKL LSIVSAIITL
SMGLMITMAT YFFRKYSEIL IQEYNLSLAR MTGIQLSGQL KETTRKIQDF RSEDSEKFFR
TNSNAVAYVR FKNKTVNSAL EIDSLFWNSK FLKSNSVVPD PTNLKNALEK SFSRLSGTLE
VLNVSNEFGF PAVAVLLPVG VEISGLVFSA SEFLGSFLSV RQTDFFQMIV VDSSGNLIAH
SNDKEAVSGK DYKKHPLVEN MLRSPSDNGS QRFDFEGREV LGSYQQLEVG GLGIISTLDA
DIAFEAVYKI RRQNFWIMIS VLSVAFFVVF VFSRTLTIPI IQLLSATKKV EQGNYAVDIR
ATTHDEVGVL TNSFLRMARG LEEREKIKNT FGKFVNKEIA ERALSSDLKL GGENREVTVF
FSDLRNFTGM SEKMKPEEVV EFLNQYFTEM VECIYLTQGI VDKFIGDAVM AHWGALVYDG
NEAKNSINAA LLMRRALIEF NLKGKEIGRP FTRFGCGINS GPVIVGQIGS EKKLEFTVIG
DTVNLASRIE YLNKEFGTDI LISESTYQQA KDHFNFVELP PVWIRGKEKP QVVYAVLGWK
DDQDCPKSLE ELRTLCGIPD PENPSRSLA
//