ID A1UJT8_MYCSK Unreviewed; 486 AA.
AC A1UJT8;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Putative adenylate/guanylate cyclase {ECO:0000313|EMBL:ABL93096.1};
DE Flags: Precursor;
GN OrderedLocusNames=Mkms_3904 {ECO:0000313|EMBL:ABL93096.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL93096.1};
RN [1] {ECO:0000313|EMBL:ABL93096.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL93096.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; CP000518; ABL93096.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UJT8; -.
DR STRING; 189918.Mkms_3904; -.
DR KEGG; mkm:Mkms_3904; -.
DR HOGENOM; CLU_025433_2_0_11; -.
DR OrthoDB; 368920at2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR16305; TESTICULAR SOLUBLE ADENYLYL CYCLASE; 1.
DR PANTHER; PTHR16305:SF35; TRANSCRIPTIONAL ACTIVATOR DOMAIN; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 228..280
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 311..433
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 486 AA; 51209 MW; 0A8FCA9B542B02CC CRC64;
MRARYAAGLA TAFLLTAAEV TAIVVTLGVE RVAGAEALLT ARNLFAVVGL IAAGVLGTTV
GGLAALAPAF RRLSDGRDSP ESRRATTNIT ARLSAALLTP WAVAAGVLIA LNLRAGAEPL
LVIITAAMFG ATATVCTGFL FTQRTLRPLM AVLTTEVDQA EVVPGVRGRL VLMWTVCTAL
PGAGIVTLVA LQRLGLLVDD PASIELPVLV LALVAVLLGL RTLIVVSRSI SDPVHDVVEA
MGEIERGGAG RLVDVYDRSE IGHLQSGFNR MVIGLQERDR LRDLFGRHVG PEVVRRAEAA
TGAEGGVRYA AILFVDLVGS TRLAIGRDPQ RVAELLNDFF QVVVAAVDHR HGLINKFQGD
AALAVFGVPL AIDRPADAAL ATARTLAAQL RSRPLDFGIG VSAGPVFAGN IGAENRYEYT
VIGDPVNEAA RLADQAKASD ERVLCSGAVC ERADPQERSH WSAQGEVLLR GRVDPTPIFT
PCENTR
//
