ID S5TGK8_9CORY Unreviewed; 508 AA.
AC S5TGK8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Adenylate cyclase {ECO:0000313|EMBL:AGS33813.1};
GN ORFNames=B841_01650 {ECO:0000313|EMBL:AGS33813.1};
OS Corynebacterium maris DSM 45190.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS33813.1, ECO:0000313|Proteomes:UP000015388};
RN [1] {ECO:0000313|EMBL:AGS33813.1, ECO:0000313|Proteomes:UP000015388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT 45190).";
RL Submitted (NOV-2012) 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; CP003924; AGS33813.1; -; Genomic_DNA.
DR RefSeq; WP_020933748.1; NC_021915.1.
DR AlphaFoldDB; S5TGK8; -.
DR STRING; 1224163.B841_01650; -.
DR KEGG; cmd:B841_01650; -.
DR PATRIC; fig|1224163.3.peg.333; -.
DR eggNOG; COG2114; Bacteria.
DR eggNOG; COG2972; Bacteria.
DR HOGENOM; CLU_025433_2_0_11; -.
DR OrthoDB; 368920at2; -.
DR Proteomes; UP000015388; 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:UP000015388};
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..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..297
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 329..451
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 508 AA; 55079 MW; 490AADBE08E3EE75 CRC64;
MDRLLRGLKW LWGTSWPLYA ALVLGANVVG AAAVMLFLRY LVPTEDLNAV QVDNSSINAI
GLIYAAFAVL VGVIVTFQLF RPVLDWQRDP DSHDANMVRN LVMRLPIYQA GVAAVIWLIG
IAIAVAVAAT AAARLALVTG VTLALAAMVV VLLTYLQAER LVRPIAAEAL ARRFEDSTME
PPIRTRLLMT WGMTTGIPVA GIGLMVLGHW AGYFTDTAVD ILPATVALAA TALITGYFGT
RLATASVTDP ILELQEAINR VRRGDTDAQV DIYDGSEIGV LQAGFNEMMR GLKDRQRVRD
LFGSYVGTEV AERALEEQPE LGGEDRRVAV IFVDVIGSTT FAVNHTPEEV VSELNNFFDV
VVEVVHRNRG VINKFQGDAA LAIFGAPLNL NDATSHALTA ARELRTELRG LRLEAGIGVA
SGHVVAGHIG GHDRFEYTVI GDAVNQAARL TDLAKDTPGR ILTNMSTLRG ANEAERARWT
AMKSIELRGR HQMTQLARPI RSTLADRS
//
