ID I2AAK2_9MYCO Unreviewed; 528 AA.
AC I2AAK2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Adenylate cyclase {ECO:0008006|Google:ProtNLM};
GN ORFNames=W7S_06715 {ECO:0000313|EMBL:AFJ34326.1};
OS Mycobacterium sp. MOTT36Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1168287 {ECO:0000313|EMBL:AFJ34326.1, ECO:0000313|Proteomes:UP000002868};
RN [1] {ECO:0000313|EMBL:AFJ34326.1, ECO:0000313|Proteomes:UP000002868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOTT36Y {ECO:0000313|EMBL:AFJ34326.1,
RC ECO:0000313|Proteomes:UP000002868};
RX PubMed=22815454; DOI=10.1128/JB.00752-12;
RA Kim B.J., Choi B.S., Choi I.Y., Lee J.H., Chun J., Hong S.H., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare clinical strain
RT MOTT-36Y, belonging to the INT5 genotype.";
RL J. Bacteriol. 194:4141-4142(2012).
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; CP003491; AFJ34326.1; -; Genomic_DNA.
DR AlphaFoldDB; I2AAK2; -.
DR KEGG; mmm:W7S_06715; -.
DR PATRIC; fig|1168287.3.peg.1372; -.
DR HOGENOM; CLU_025433_2_1_11; -.
DR Proteomes; UP000002868; Chromosome.
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; 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; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR PANTHER; PTHR43081:SF17; BLL5647 PROTEIN; 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 39..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 264..316
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 348..472
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 528 AA; 57390 MW; 78C93178CB187047 CRC64;
MLERVTRQSG RLPETPAYGS LLLGRVSESQ GRRRVRIQII MTVLVLGANL IGIAVALFLV
TVAIPVPSVF DDAPAWITFG ASPAYIVAAS AWGTYWITRR TVIALRWAIE EREPTPEDER
NTFVAPWRIA LVDLVLWGVG TILLTTLYGM VNTLFIPRFL LVVSFGGVVV ATASYLLAEF
ALRPVAAQAL EAGPPPRRFA AGIMGRTMVV WFLGSAVPVI GIMMLALFEL VLRNLTQTQF
AVAVFIVSMA PLIFGCVLMW ILAWLTATPV RVVRAALARV ERGDLRGDLV VFDGTELGEL
QRGFNTMVDG LRERERVRDL FGRHVGREVA LAAERERPKL GGEERHVAVV FIDIVGSTQL
VTSQPPAEVV AVLNRFFAIV VEEVDRYCGL VNKFEGDATL AIFGAPNRLD SPEDAALAAA
RCIAERLADE MSDLEAGIGV AAGQVVAGNV GAKERFEYTV IGEPVNEAAR LCELAKSHTN
RLLATADAIE GASENERARW SLGETVTLRG HERPTRLASL VDAPSSAQ
//
