ID M3IIZ9_LEPIT Unreviewed; 960 AA.
AC M3IIZ9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Adenylate/guanylate cyclase catalytic domain protein {ECO:0000313|EMBL:EMG21248.1};
GN ORFNames=LEP1GSC150_3516 {ECO:0000313|EMBL:EMG21248.1};
OS Leptospira interrogans serovar Copenhageni str. LT2050.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1001598 {ECO:0000313|EMBL:EMG21248.1, ECO:0000313|Proteomes:UP000011778};
RN [1] {ECO:0000313|EMBL:EMG21248.1, ECO:0000313|Proteomes:UP000011778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2050 {ECO:0000313|EMBL:EMG21248.1,
RC ECO:0000313|Proteomes:UP000011778};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Tulsiani S.M., Graham G.C., Burns M.-A.,
RA Dohnt M.F., Smythe L.D., McKay D.B., Craig S.B., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (FEB-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:EMG21248.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFMD02000335; EMG21248.1; -; Genomic_DNA.
DR AlphaFoldDB; M3IIZ9; -.
DR Proteomes; UP000011778; 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 CDD; cd18774; PDC2_HK_sensor; 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 361..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 655..707
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 739..871
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 238..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 106646 MW; 9ADA9CC2367BC225 CRC64;
MLEIHRRYLP FGTSGALIFI SDSYTNFSND LSEEISKKEI GTVCFVSSKI DSNAPDSIPT
SVNVLSLLIP PGPETNDSVY SSFLQIQKFL KRGNILFLIA SDCETRFPLL LSKLLLASSP
SLSDSELQNQ ISHLGYSYSE PDQASFRKYI SRHKSLHSIP EIPPGEFSVS IHIARESKRP
STLKYKIKYE PGAENLTQIK AVPYSEEENK KSPSSFQSFP IDAIEIDHLE DTQKLKEFSV
SGESEEPTTT PSSESNHVSL SSESKLELST TETEILSTNS QTSENILTPQ IESIQTENKP
AQEIQLKPQT ESISNTEPIS TSSKIDKNTL DETKTNSPSS ATTQELSTSQ VKSKFPLQIK
LMAVISILMT FTVSTIIFFA SSAFRDDSEV RVLQNNLNLV NILGLKIKTD IKEILTNGKQ
MVGALVQGKQ GISFADIFFQ NDPDFIYAGL FQMEGNIPTM VNEFFNEPYL SELKVSSKEI
SDLVRNRPGL IQKSVLTGGR MENLSAEFKE PILAIAIPSS GSNSKILVLI LRLEKFLNAF
QKQDISEIFL VNGEGDLIAH SDPKLLQSNT NFMNLPIVES MVKSSENTKQ IEYKDKDGNA
WFGSYQKLGF GGAAVVSIVP ENKAFEAVYK IQKTNLLIMG IALCLALIIV FFFAKTITKP
VLNLLRATTE IAQGNFKIKI SSITNDEVGL LTDYFVDMSK GLEEREKVKD ALGRFVNKEI
AEMVLKHELT LGGERKMCAI FFSDIRSFTS ISEKLQPEEV VEFLNEYMTE MVHCVNETHG
IVDKFIGDAI MATWGAAKTS DRDAENAVNG ALMMREALIK FNQGRGGEKK PIIQIGCGLN
FGPVIAGQIG SEQRLEYTVI GDAVNLASRV EALNKPFGTD ILITQDLLDH VSEIFNVEKM
QSIKVKGKEE PQVIYAVLGR KDDPNCPKSL EELRERVGIV WEPPKKGSDS EKEVKYEILD
//
