NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1556558111|gb|RWQ77673|]
View 

CYTH domain-containing protein [Bacillus cereus]

Protein Classification

YjbK family protein( domain architecture ID 10790522)

YjbK family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YjbK COG4116
Predicted triphosphatase or cyclase YjbK, contains CYTH domain [General function prediction ...
 2-190 1.20e-98

Predicted triphosphatase or cyclase YjbK, contains CYTH domain [General function prediction only];


:

Pssm-ID: 443292  Cd Length: 191  Bit Score: 283.27  E-value: 1.20e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111   2 TQEIEIEFKNIVTKEEFDTLCKSFSI--EAFTKQVNHYFETPDFSLKEAGSALRIRHKGETYTLTLKQPAEIGLLETHQV 79
Cdd:COG4116     1 SQEIEIEFKNLLTKEEYNRLLEHFNFkeEEFFTQTNYYFDTPDFDLKKHGSALRIRTKNDSYELTLKQPAEVGLLETNDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111  80 VTEDEAKMMMETNTIIQGAVVDQLHKLQIPVSALTYMGSLTTERAETLFKGGTLVFDHSFYYNHDDYEIEFEVQDEETGK 159
Cdd:COG4116    81 LSLEEAKALIEGGQLPSGEVADILKELGIDPEELKYFGSLTTTRAEIPYKEGLLVLDHSFYLDQEDYELEFEVTDEEQGK 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1556558111 160 AAFIHLLTQHNIPVRHTNNKVKRFFLAKQKK 190
Cdd:COG4116   161 KVFDELLKEFNIPKRPAKNKIARFYDALKKS 191
 
Name Accession Description Interval E-value
YjbK COG4116
Predicted triphosphatase or cyclase YjbK, contains CYTH domain [General function prediction ...
 2-190 1.20e-98

Predicted triphosphatase or cyclase YjbK, contains CYTH domain [General function prediction only];


Pssm-ID: 443292  Cd Length: 191  Bit Score: 283.27  E-value: 1.20e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111   2 TQEIEIEFKNIVTKEEFDTLCKSFSI--EAFTKQVNHYFETPDFSLKEAGSALRIRHKGETYTLTLKQPAEIGLLETHQV 79
Cdd:COG4116     1 SQEIEIEFKNLLTKEEYNRLLEHFNFkeEEFFTQTNYYFDTPDFDLKKHGSALRIRTKNDSYELTLKQPAEVGLLETNDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111  80 VTEDEAKMMMETNTIIQGAVVDQLHKLQIPVSALTYMGSLTTERAETLFKGGTLVFDHSFYYNHDDYEIEFEVQDEETGK 159
Cdd:COG4116    81 LSLEEAKALIEGGQLPSGEVADILKELGIDPEELKYFGSLTTTRAEIPYKEGLLVLDHSFYLDQEDYELEFEVTDEEQGK 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1556558111 160 AAFIHLLTQHNIPVRHTNNKVKRFFLAKQKK 190
Cdd:COG4116   161 KVFDELLKEFNIPKRPAKNKIARFYDALKKS 191
CYTH-like_Pase_1 cd07762
Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like ...
 5-184 3.18e-88

Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily hydrolyze triphosphate-containing substrates, require metal cations as cofactors, and have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB) and from thiamine triphosphatase. Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. Thiamine triphosphatase is a soluble cytosolic enzyme which converts thiamine triphosphate to thiamine diphosphate. This domain superfamily also contains RNA triphosphatases, membrane-associated polyphosphate polymerases, tripolyphosphatases, nucleoside triphosphatases, nucleoside tetraphosphatases and other proteins with unknown functions. Proteins of this subgroup are of bacterial origin and have not been characterized.


Pssm-ID: 143627  Cd Length: 180  Bit Score: 256.74  E-value: 3.18e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111   5 IEIEFKNIVTKEEFDTLCKSFSIEAFTKQVNHYFETPDFSLKEAGSALRIRHKGETYTLTLKQPAEIGLLETHQVVTEDE 84
Cdd:cd07762     1 LEIEFKNLLTKEEYEQLKNAFDLKDFFKQTNYYFDTPDFALKKKHSALRIREKEGKAELTLKVPQEVGLLETNQPLTLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111  85 AKMMMETNTIIQGAVVDQLHKLQIPVSALTYMGSLTTERAETLFKGGTLVFDHSFYYNHDDYEIEFEVQDEETGKAAFIH 164
Cdd:cd07762    81 AEKLIKGGTLPEGEILDKLKELGIDPSELKLFGSLTTIRAEIPYEGGLLVLDHSLYLGITDYELEYEVDDYEAGKKAFLE 160

                         170       180
                  ....*....|....*....|
gi 1556558111 165 LLTQHNIPVRHTNNKVKRFF 184
Cdd:cd07762   161 LLKQYNIPYRPAKNKIARFL 180
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 4-184 3.46e-28

CYTH domain; These sequences are functionally identified as members of the adenylate cyclase family, which catalyzes the conversion of ATP to 3',5'-cyclic AMP and pyrophosphate. Six distinct non-homologous classes of AC have been identified. The structure of three classes of adenylyl cyclases have been solved.


Pssm-ID: 396490  Cd Length: 172  Bit Score: 103.77  E-value: 3.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111   4 EIEIEFKNIVTKEEFDTLCKS----FSIEAFTKQVNHYFETPDFSLKEAGSALRIRHKGETYT-LTLKQPaeigllethq 78
Cdd:pfam01928   1 MIEIERKFLVSDEEYKDLLLLeklrGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFGNGAYfLTLKGP---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111  79 vVTEDEAKMMMETNTIIQGAVVDQLHKLQIPvsALTYMGSLTTERAETLFKGGTLVFDHSFYYNHDDYEIEFEVQDEETG 158
Cdd:pfam01928  71 -GVDGPFKSREEVNGEVSRDEPDAVELLDGL--GLQPVGSIKKERRRYKVKGVLIALDVVEFLGGAEVELELEVEDEEEL 147

                         170       180
                  ....*....|....*....|....*.
gi 1556558111 159 KAAFIhLLTQHNIPVRHTNNKVKRFF 184
Cdd:pfam01928 148 LEAAE-ELELLRILGLSEESKIARFY 172
 
Name Accession Description Interval E-value
YjbK COG4116
Predicted triphosphatase or cyclase YjbK, contains CYTH domain [General function prediction ...
 2-190 1.20e-98

Predicted triphosphatase or cyclase YjbK, contains CYTH domain [General function prediction only];


Pssm-ID: 443292  Cd Length: 191  Bit Score: 283.27  E-value: 1.20e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111   2 TQEIEIEFKNIVTKEEFDTLCKSFSI--EAFTKQVNHYFETPDFSLKEAGSALRIRHKGETYTLTLKQPAEIGLLETHQV 79
Cdd:COG4116     1 SQEIEIEFKNLLTKEEYNRLLEHFNFkeEEFFTQTNYYFDTPDFDLKKHGSALRIRTKNDSYELTLKQPAEVGLLETNDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111  80 VTEDEAKMMMETNTIIQGAVVDQLHKLQIPVSALTYMGSLTTERAETLFKGGTLVFDHSFYYNHDDYEIEFEVQDEETGK 159
Cdd:COG4116    81 LSLEEAKALIEGGQLPSGEVADILKELGIDPEELKYFGSLTTTRAEIPYKEGLLVLDHSFYLDQEDYELEFEVTDEEQGK 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1556558111 160 AAFIHLLTQHNIPVRHTNNKVKRFFLAKQKK 190
Cdd:COG4116   161 KVFDELLKEFNIPKRPAKNKIARFYDALKKS 191
CYTH-like_Pase_1 cd07762
Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like ...
 5-184 3.18e-88

Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily hydrolyze triphosphate-containing substrates, require metal cations as cofactors, and have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB) and from thiamine triphosphatase. Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. Thiamine triphosphatase is a soluble cytosolic enzyme which converts thiamine triphosphate to thiamine diphosphate. This domain superfamily also contains RNA triphosphatases, membrane-associated polyphosphate polymerases, tripolyphosphatases, nucleoside triphosphatases, nucleoside tetraphosphatases and other proteins with unknown functions. Proteins of this subgroup are of bacterial origin and have not been characterized.


Pssm-ID: 143627  Cd Length: 180  Bit Score: 256.74  E-value: 3.18e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111   5 IEIEFKNIVTKEEFDTLCKSFSIEAFTKQVNHYFETPDFSLKEAGSALRIRHKGETYTLTLKQPAEIGLLETHQVVTEDE 84
Cdd:cd07762     1 LEIEFKNLLTKEEYEQLKNAFDLKDFFKQTNYYFDTPDFALKKKHSALRIREKEGKAELTLKVPQEVGLLETNQPLTLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111  85 AKMMMETNTIIQGAVVDQLHKLQIPVSALTYMGSLTTERAETLFKGGTLVFDHSFYYNHDDYEIEFEVQDEETGKAAFIH 164
Cdd:cd07762    81 AEKLIKGGTLPEGEILDKLKELGIDPSELKLFGSLTTIRAEIPYEGGLLVLDHSLYLGITDYELEYEVDDYEAGKKAFLE 160

                         170       180
                  ....*....|....*....|
gi 1556558111 165 LLTQHNIPVRHTNNKVKRFF 184
Cdd:cd07762   161 LLKQYNIPYRPAKNKIARFL 180
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 4-184 3.46e-28

CYTH domain; These sequences are functionally identified as members of the adenylate cyclase family, which catalyzes the conversion of ATP to 3',5'-cyclic AMP and pyrophosphate. Six distinct non-homologous classes of AC have been identified. The structure of three classes of adenylyl cyclases have been solved.


Pssm-ID: 396490  Cd Length: 172  Bit Score: 103.77  E-value: 3.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111   4 EIEIEFKNIVTKEEFDTLCKS----FSIEAFTKQVNHYFETPDFSLKEAGSALRIRHKGETYT-LTLKQPaeigllethq 78
Cdd:pfam01928   1 MIEIERKFLVSDEEYKDLLLLeklrGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFGNGAYfLTLKGP---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111  79 vVTEDEAKMMMETNTIIQGAVVDQLHKLQIPvsALTYMGSLTTERAETLFKGGTLVFDHSFYYNHDDYEIEFEVQDEETG 158
Cdd:pfam01928  71 -GVDGPFKSREEVNGEVSRDEPDAVELLDGL--GLQPVGSIKKERRRYKVKGVLIALDVVEFLGGAEVELELEVEDEEEL 147

                         170       180
                  ....*....|....*....|....*.
gi 1556558111 159 KAAFIhLLTQHNIPVRHTNNKVKRFF 184
Cdd:pfam01928 148 LEAAE-ELELLRILGLSEESKIARFY 172
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 1-78 1.63e-11

Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and metabolism];


Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 61.07  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111   1 MTQEIEIEFknIVTKEEFDTLCKSFSIEAFTKQ-------VNHYFETPDFSLKEAGSALRIRHKGETYTLTLKQPAEI-- 71
Cdd:COG3025     1 MAREIELKL--LVDPEALPALRQHPLLAGLAVGepatrrlENTYFDTPDLDLRRAGIGLRVRREGGRWEQTLKTAGQVvg 78


                  ....*..
gi 1556558111  72 GLletHQ 78
Cdd:COG3025    79 GL---HQ 82
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 6-66 1.19e-08

Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This subgroup belongs to the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily. Members of this superfamily hydrolyze triphosphate-containing substrates, require metal cations as cofactors, and have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). A number of proteins in this subgroup also contain a C-terminal CHAD (Conserved Histidine Alpha-helical Domain) domain which may participate in metal chelation or act as a phosphor-acceptor. The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB) and from thiamine triphosphatase. Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. Thiamine triphosphatase is a soluble cytosolic enzyme which converts thiamine triphosphate to thiamine diphosphate. This domain superfamily also contains RNA triphosphatases, membrane-associated polyphosphate polymerases, tripolyphosphatases, nucleoside triphosphatases, nucleoside tetraphosphatases and other proteins with unknown functions. Proteins of this subgroup have not been characterized.


Pssm-ID: 143624 [Multi-domain]  Cd Length: 197  Bit Score: 52.62  E-value: 1.19e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1556558111   6 EIEFKNIVTKEEFDTLCKS------FSIEAFTKQ-VNHYFETPDFSLKEAGSALRIRHKGETYTLTLK 66
Cdd:cd07756     1 EIELKLLLPPEDLEALAAHpllaalAAGRAQTRRlHNTYFDTPDLALRRAGIALRVRREGGQWVQTLK 68
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 31-68 2.84e-07

Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) [Signal transduction mechanisms, General function prediction only];


Pssm-ID: 441046  Cd Length: 173  Bit Score: 48.33  E-value: 2.84e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1556558111  31 TKQVNHYFETPDFSLKEAGSALRIRHKGETYTLTLKQP 68
Cdd:COG1437    30 EHQIDIYYDAPDRDFAETDEALRIRRGGGRATLTYKGP 67
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 33-162 2.82e-06

CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like superfamily enzymes hydrolyze triphosphate-containing substrates and require metal cations as cofactors. They have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB), and from thiamine triphosphatase. Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. Thiamine triphosphatase is a soluble cytosolic enzyme which converts thiamine triphosphate to thiamine diphosphate. This domain superfamily also contains RNA triphosphatases, membrane-associated polyphosphate polymerases, tripolyphosphatases, nucleoside triphosphatases, nucleoside tetraphosphatases and other proteins with unknown functions.


Pssm-ID: 143620  Cd Length: 174  Bit Score: 45.52  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111  33 QVNHYFETPDFSLKEAGSALRIRHKGETYTLTLKQPAEIGLLETHQVVTEDEAKMMMETNTIIQGAVVDQLHKLQiPVsa 112
Cdd:cd07374    34 LRAIYFDTPDLRLARAGLRLRRRTGGADAGWHLKLPGGISRRTEVRAPLGDAAAVAPLLLAAALVLAVTRGLPLR-PV-- 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1556558111 113 ltymGSLTTERAET-LFKGGTLVF----DHSFYYNHDD----YEIEFEVQDEETGKAAF 162
Cdd:cd07374   111 ----ATIETTRTVYrLLDAGGVLAeldlDTVTARVLDGggtqYWREVEVELPDGDEALL 165
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
 4-87 3.44e-05

Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup contains class IV ACs and similar proteins. AC catalyzes the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. cAMP is a key signaling molecule which conveys a variety of signals in different cell types. In prokaryotes, cAMP is a catabolite derepression signal which triggers the expression of metabolic pathways including the lactose operon. Six non-homologous classes of ACs have been identified (I-VI). Class IV ACs are found in this group. In bacteria, the gene encoding Class IV AC has been designated cyaB and the protein as AC2. AC-IV occurs in addition to AC-I in bacterial pathogens such as Yersinia pestis (plague disease). The role of AC-IV is unknown but it has been speculated that it may be a factor in pathogenesis, perhaps providing cAMP for a secondary internal signaling function, or for secretion and uptake into host cells, where it may disrupt normal cellular processes. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel.


Pssm-ID: 143628  Cd Length: 169  Bit Score: 42.26  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1556558111   4 EIEIEFKnIVTKEEFDTLCKSFSIEAFT--KQVNHYFETPDFSLKEAGSALRIRHKGET--YTLTLKQPAEIGLLET--- 76
Cdd:cd07890     1 EVEIKAR-VDDLEALRERLAALGGAEGGreFQEDIYFDHPDRDLAATDEALRLRRMGDSgkTLLTYKGPKLDGGPKVree 79

                          90
                  ....*....|.
gi 1556558111  77 HQVVTEDEAKM 87
Cdd:cd07890    80 IETEVADPEAM 90
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH