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Database: UniProt
Entry: M3H3H7_9LEPT
LinkDB: M3H3H7_9LEPT
Original site: M3H3H7_9LEPT 
ID   M3H3H7_9LEPT            Unreviewed;       427 AA.
AC   M3H3H7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Adenylate/guanylate cyclase catalytic domain protein {ECO:0000313|EMBL:EMF83666.1};
GN   ORFNames=LEP1GSC188_1309 {ECO:0000313|EMBL:EMF83666.1};
OS   Leptospira weilii serovar Topaz str. LT2116.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1088540 {ECO:0000313|EMBL:EMF83666.1, ECO:0000313|Proteomes:UP000011770};
RN   [1] {ECO:0000313|EMBL:EMF83666.1, ECO:0000313|Proteomes:UP000011770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2116 {ECO:0000313|EMBL:EMF83666.1,
RC   ECO:0000313|Proteomes:UP000011770};
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 (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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:EMF83666.1}.
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DR   EMBL; AHOR02000012; EMF83666.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3H3H7; -.
DR   Proteomes; UP000011770; 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   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
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   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011770};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        46..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          243..378
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   427 AA;  48419 MW;  E433EDA0D9ED128E CRC64;
     MPDSVLEVLK KEERSGIIIT NYFRYLIALF FLLQIVVNVN SGNHKFNLIA FLIYLSLTFV
     HTIVIRVSPL SVVSVFNYIT LFTEYLLILG VLLFYTFTTK NVDLGFALKN PINLFFLFPI
     IYSLLQFKIR FVFIGLFLFY LIYYSILWVA VSQGQLIYTK DWGSYVSGPN ILIEDIVAGK
     PGLYFCFAMM ISTGIFRTIS MVKRIGIVEG QKTELSRYFS PKIVNEMVEN PETFQSGNRQ
     IVSILFLDIR NFTSMSENMD PKELGELLSE FRKIMTECVF ENNGTLDKYI GDAVMATFGT
     PHPSPSAEVD ARNAVGCGVI MQKRLTEWNL LRKSEGKTPI SIGIGIHTGE VFAGNVGSDL
     HREYSVIGDA VNTASRIESL CKVLKKPFLI SKETMELLGG KYTLNRMPRV KVKGKEEPLQ
     IYEVVWG
//
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