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Database: UniProt
Entry: M6D1T0_9LEPT
LinkDB: M6D1T0_9LEPT
Original site: M6D1T0_9LEPT 
ID   M6D1T0_9LEPT            Unreviewed;       724 AA.
AC   M6D1T0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Adenylate/guanylate cyclase catalytic domain protein {ECO:0000313|EMBL:EMJ96656.1};
GN   ORFNames=LEP1GSC194_4408 {ECO:0000313|EMBL:EMJ96656.1};
OS   Leptospira alstonii serovar Sichuan str. 79601.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1218565 {ECO:0000313|EMBL:EMJ96656.1, ECO:0000313|Proteomes:UP000011988};
RN   [1] {ECO:0000313|EMBL:EMJ96656.1, ECO:0000313|Proteomes:UP000011988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=79601 {ECO:0000313|EMBL:EMJ96656.1,
RC   ECO:0000313|Proteomes:UP000011988};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Galloway R.L., 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:EMJ96656.1}.
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DR   EMBL; ANIK01000016; EMJ96656.1; -; Genomic_DNA.
DR   RefSeq; WP_020772410.1; NZ_ANIK01000016.1.
DR   AlphaFoldDB; M6D1T0; -.
DR   PATRIC; fig|1218565.3.peg.1037; -.
DR   OrthoDB; 9806704at2; -.
DR   Proteomes; UP000011988; 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; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43081:SF16; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1.
DR   PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR   Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        228..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        293..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        322..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        350..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          458..597
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REPEAT          660..693
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ   SEQUENCE   724 AA;  82724 MW;  EE3423F64287B80B CRC64;
     MKTILFFLCT FIPSLIFSEN QDSWKPIDLR KVNWIATDEF QKEYPNGIDP TLPTVKKIST
     FPIVLNEIFE TPIGRGLKEY TLQTRFHIEG DFRNTKVYKP IFLYLESIGE NWEIFLNGHS
     LAREIHLDSS GKEMFVRRTI RSFRLPVDSS LLRSGENLLT FHLIGDVPAS AFSKNVDLGF
     YIDGDYSLTT EQKLSGEIST LVNLCLNTIY VFFGLYHLLI YAKRREDLYN LYFGIFSVFM
     ALYSLSRSNI AFDVIHDTTW ITRIEYSSVS LLSPLFLLFM QDYFYGRAKF SKVLFGILVL
     DVIIAAITLV EPFRYTMTSL RIWQISILPT LVYLLYFMSK ALYFRKKDAI LLATSMFTVV
     FIAVYDVIDS VFFQSGIRFT QFAYFLFVVA LTVILANRFI SLYRQSEDLN IELSQQKLEL
     ARQKNAFFRF VPVQFLNVLG KNSAVEVNLG DSVLKEMSVL FTDIRSFTTI SEQMTPEENF
     RFINDYLASM EPVVQKHEGF VDKFMGDGIL ALFSGEGEAI QSRLYGKTSA DKAILAAIEM
     KKAVQAINAE AKDSHFRGLR IGIGINTGNL MLGTVGSRSR LDTTVIGDTV NVASRLESLT
     NLYRADILIT KNTLSCMTIA DDLAIREIDS VVVKGKTDPI IIYEVYEADV PHIRKLKDTT
     LPLITRGIIL YKVADFQEAL INFEQALKVF PEDIVSILYR KRCQEYIASP PNGNWIGVQH
     LLEK
//
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