ID G0HFA1_CORVD Unreviewed; 528 AA.
AC G0HFA1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Adenylate cyclase {ECO:0000313|EMBL:AEK37790.1};
GN Name=cya {ECO:0000313|EMBL:AEK37790.1};
GN OrderedLocusNames=CVAR_2445 {ECO:0000313|EMBL:AEK37790.1};
OS Corynebacterium variabile (strain DSM 44702 / CIP 107183 / JCM 12073 /
OS NCIMB 30131) (Corynebacterium mooreparkense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK37790.1, ECO:0000313|Proteomes:UP000006659};
RN [1] {ECO:0000313|EMBL:AEK37790.1, ECO:0000313|Proteomes:UP000006659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC {ECO:0000313|Proteomes:UP000006659};
RX PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA Schroeder J., Maus I., Trost E., Tauch A.;
RT "Complete genome sequence of Corynebacterium variabile DSM 44702 isolated
RT from the surface of smear-ripened cheeses and insights into cheese ripening
RT and flavor generation.";
RL BMC Genomics 12:545-545(2011).
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; CP002917; AEK37790.1; -; Genomic_DNA.
DR RefSeq; WP_014010943.1; NC_015859.1.
DR AlphaFoldDB; G0HFA1; -.
DR STRING; 858619.CVAR_2445; -.
DR KEGG; cva:CVAR_2445; -.
DR eggNOG; COG2114; Bacteria.
DR eggNOG; COG2972; Bacteria.
DR HOGENOM; CLU_025433_2_1_11; -.
DR Proteomes; UP000006659; 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 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 246..298
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 330..452
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 501..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 57484 MW; 65AF37A3A5382811 CRC64;
MQRLARYIRW AWGTSWPFYA LSVLVVNVIG ALGVASFLRF LVPLPGAREF LSVSTLTLSL
YVGYFIFALV VGVGTTLHFF TPVLGWERAP AGYDPRMIRR LVLRIPSFQA LLGGGLWAVG
VVMFTVVAAV EVSREWALTV AVTATLGGAM VVLMTYMVAE RMVRPVSVRA LKPEYGSPGK
IAPLSRQITF VWILTSAVPV VGVVLMVSAQ ASGFFGGDAT EILPGVLALS LTELFTGFSG
TRLMTMTVVD PIRELRVAMN RVRRGDTHAQ VRVYDSSEIG VLQAGFNEMM SGLQEREQVR
KLFGRYVGDE VARRAMEEKP RLGGENRQVG VVFVDVVGST GFAVSREPQE VVQALNRFFD
IVVEVVHRNK GIINKFEGDA ALAVFGAPLP LDDIAGHTLA AARELKTELA AQELPAGIGA
AVGRVVAGHI GAKNRFEYTV IGDAVNAAAR LTDVAKETPG RVLTTATTVR QANEAEQARW
TMMKSVELRG RREMTQLARP IRPTRAERAA EREGERATEM TAGPKPEQ
//
