ID A0A1L7D102_9CORY Unreviewed; 504 AA.
AC A0A1L7D102;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Adenylate cyclase {ECO:0000313|EMBL:APT91770.1};
GN ORFNames=CPHO_01240 {ECO:0000313|EMBL:APT91770.1};
OS Corynebacterium phocae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=161895 {ECO:0000313|EMBL:APT91770.1, ECO:0000313|Proteomes:UP000185491};
RN [1] {ECO:0000313|EMBL:APT91770.1, ECO:0000313|Proteomes:UP000185491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M408/89/1 {ECO:0000313|EMBL:APT91770.1,
RC ECO:0000313|Proteomes:UP000185491};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium phocae M408/89/1(T)(=DSM
RT 44612(T)), isolated from the common seal (Phoca vitulina).";
RL Submitted (AUG-2014) 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; CP009249; APT91770.1; -; Genomic_DNA.
DR RefSeq; WP_075732527.1; NZ_VXKJ01000006.1.
DR AlphaFoldDB; A0A1L7D102; -.
DR STRING; 161895.CPHO_01240; -.
DR KEGG; cpho:CPHO_01240; -.
DR OrthoDB; 368920at2; -.
DR Proteomes; UP000185491; 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 Reference proteome {ECO:0000313|Proteomes:UP000185491};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 241..293
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 325..447
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 504 AA; 55607 MW; BD37EAAF2852A84E CRC64;
MRRLLRAASW LMHTNWPVYA ALVLGGNLLG AVAIMTFVRF LPMTEVDEFA RNTPHLGVIG
IVYLLFAIAV GMLATITLFR PVLDWQRHPE NYDPNMIRGL VLRIPAYQAV ITALVWGIGI
ITAAVMALNS SLRLAVVMTV STTLAGMVIV LLTYLQAENL VRPIAATALA RRFEDSTLEP
PIKFRLLTAW VMTSGLPLVG IIMLTWARHS NWLQDGISVH VAALAAAALA TGFAGTYYAM
HSVVDPIIEL KDAIMRVRRG DNTVEVDIYD GSELGVLQSG FNEMMRGLRE RQRVREVFGR
YVGNEVAQRA LDEHPQLGGE YRTVAVIFID VIGSTTYATE HTAEEVVDAL NKFFEVVVDV
VHRNRGIINK FQGDAALAIF GAPSNVYDST SMALQAAREL RLELKDLELQ AGVGVCAGHV
VAGHIGGKER FEYTVIGDAV NEAARLTEWA KDTPGRVLTN AATLKTANEA EQARWTYMKS
IELRGRRRMT RLARPIRATL ADRS
//