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Conserved domains on  [gi|1948555436|gb|QQA81553|]
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CYTH domain-containing protein [Stenotrophomonas maltophilia]

Protein Classification

CYTH family protein( domain architecture ID 10006810)

CYTH family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYTH COG2954
CYTH domain, found in class IV adenylate cyclase and various triphosphatases [General function ...
 1-161 6.52e-97

CYTH domain, found in class IV adenylate cyclase and various triphosphatases [General function prediction only];


:

Pssm-ID: 442195  Cd Length: 157  Bit Score: 276.28  E-value: 6.52e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948555436   1 MGIEIERKFLVINDGWRSAAHRVIPMAQGYINdmgaldrGTQNASVRVRIEGDHAALNLKSRTIGHTRQEFDYPIPVEDA 80
Cdd:COG2954     1 MALEIERKFLVKGDPWRALATRGTRIRQGYLS-------TDPERTVRVRIKGDQAFLTIKGKGSGLSREEFEYEIPLADA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948555436  81 RALLALCVGGLIDKRRHLVEHAGLTWEVDEFLGDNAGLVVAEVELDSADQAIELPDWAGAEVTDDARYYNVALASHPYSQ 160
Cdd:COG2954    74 EELLELCEGPVIEKTRYLVPHGGHTWEVDEFEGENAGLVVAEVELPSEDEPFELPDWLGEEVTGDPRYYNSNLAKHPYSQ 153


                  .
gi 1948555436 161 W 161
Cdd:COG2954   154 W 154
 
Name Accession Description Interval E-value
CYTH COG2954
CYTH domain, found in class IV adenylate cyclase and various triphosphatases [General function ...
 1-161 6.52e-97

CYTH domain, found in class IV adenylate cyclase and various triphosphatases [General function prediction only];


Pssm-ID: 442195  Cd Length: 157  Bit Score: 276.28  E-value: 6.52e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948555436   1 MGIEIERKFLVINDGWRSAAHRVIPMAQGYINdmgaldrGTQNASVRVRIEGDHAALNLKSRTIGHTRQEFDYPIPVEDA 80
Cdd:COG2954     1 MALEIERKFLVKGDPWRALATRGTRIRQGYLS-------TDPERTVRVRIKGDQAFLTIKGKGSGLSREEFEYEIPLADA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948555436  81 RALLALCVGGLIDKRRHLVEHAGLTWEVDEFLGDNAGLVVAEVELDSADQAIELPDWAGAEVTDDARYYNVALASHPYSQ 160
Cdd:COG2954    74 EELLELCEGPVIEKTRYLVPHGGHTWEVDEFEGENAGLVVAEVELPSEDEPFELPDWLGEEVTGDPRYYNSNLAKHPYSQ 153


                  .
gi 1948555436 161 W 161
Cdd:COG2954   154 W 154
CYTH-like_CthTTM-like_1 cd07891
CYTH-like Clostridium thermocellum TTM-like subgroup 1; This subgroup contains the ...
 3-157 1.03e-86

CYTH-like Clostridium thermocellum TTM-like subgroup 1; This subgroup contains the triphosphate tunnel metalloenzyme (TTM) from Clostridium thermocellum (CthTTM) and similar proteins. These are found primarily in bacteria. CthTTM is a metal dependent tripolyphosphatase, nucleoside triphosphatase, and nucleoside tetraphosphatase. It hydrolyzes the beta-gamma phosphoanhydride linkage of triphosphate-containing substrates including tripolyphosphate, nucleoside triphosphates and nucleoside tetraphosphates. These substrates are hydrolyzed, releasing Pi. Mg++ or Mn++ are required for the enzyme's activity. CthTTM appears to have no adenylate cyclase activity. This subgroup consists chiefly of bacterial sequences. These enzymes are members of the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily, which have a unique active site located within an eight-stranded beta barrel.


Pssm-ID: 143629  Cd Length: 148  Bit Score: 250.11  E-value: 1.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948555436   3 IEIERKFLVINDGWRSAAHRVIPMAQGYINDmgaldrgTQNASVRVRIEGDHAALNLKSRTIGHTRQEFDYPIPVEDARA 82
Cdd:cd07891     1 LEIERKFLVKGDAWRALAAKGVRIRQGYLST-------DPERTVRVRIAGDRAYLTIKGPTNGLSRYEFEYEIPLADAEE 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948555436  83 LLALCVGGLIDKRRHLVEHAGLTWEVDEFLGDNAGLVVAEVELDSADQAIELPDWAGAEVTDDARYYNVALASHP 157
Cdd:cd07891    74 LLALCEGPVIEKTRYRVPHGGHTWEVDVFHGENAGLVVAEIELPSEDEPFELPDWLGREVTGDPRYYNASLAKHP 148
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 3-149 6.18e-17

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: 73.34  E-value: 6.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948555436   3 IEIERKFLVIN---------DGWRSAAHRVIPMAQGYINDMGALDRGTQnASVRVRIEGDHA-ALNLKSRTIGHTRQEF- 71
Cdd:pfam01928   2 IEIERKFLVSDeeykdllllEKLRGKAEGPEEQRDIYFDTPDRDLARTD-EALRIRRFGNGAyFLTLKGPGVDGPFKSRe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948555436  72 --------DYPIPVEDARALLALCVGGL-IDKRRHLVEHAGLTWEVDEFLGdnaglvVAEVELDSADQAIELPDWAGAE- 141
Cdd:pfam01928  81 evngevsrDEPDAVELLDGLGLQPVGSIkKERRRYKVKGVLIALDVVEFLG------GAEVELELEVEDEEELLEAAEEl 154

                         170
                  ....*....|....*...
gi 1948555436 142 ----------VTDDARYY 149
Cdd:pfam01928 155 ellrilglseESKIARFY 172
 
Name Accession Description Interval E-value
CYTH COG2954
CYTH domain, found in class IV adenylate cyclase and various triphosphatases [General function ...
 1-161 6.52e-97

CYTH domain, found in class IV adenylate cyclase and various triphosphatases [General function prediction only];


Pssm-ID: 442195  Cd Length: 157  Bit Score: 276.28  E-value: 6.52e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948555436   1 MGIEIERKFLVINDGWRSAAHRVIPMAQGYINdmgaldrGTQNASVRVRIEGDHAALNLKSRTIGHTRQEFDYPIPVEDA 80
Cdd:COG2954     1 MALEIERKFLVKGDPWRALATRGTRIRQGYLS-------TDPERTVRVRIKGDQAFLTIKGKGSGLSREEFEYEIPLADA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948555436  81 RALLALCVGGLIDKRRHLVEHAGLTWEVDEFLGDNAGLVVAEVELDSADQAIELPDWAGAEVTDDARYYNVALASHPYSQ 160
Cdd:COG2954    74 EELLELCEGPVIEKTRYLVPHGGHTWEVDEFEGENAGLVVAEVELPSEDEPFELPDWLGEEVTGDPRYYNSNLAKHPYSQ 153


                  .
gi 1948555436 161 W 161
Cdd:COG2954   154 W 154
CYTH-like_CthTTM-like_1 cd07891
CYTH-like Clostridium thermocellum TTM-like subgroup 1; This subgroup contains the ...
 3-157 1.03e-86

CYTH-like Clostridium thermocellum TTM-like subgroup 1; This subgroup contains the triphosphate tunnel metalloenzyme (TTM) from Clostridium thermocellum (CthTTM) and similar proteins. These are found primarily in bacteria. CthTTM is a metal dependent tripolyphosphatase, nucleoside triphosphatase, and nucleoside tetraphosphatase. It hydrolyzes the beta-gamma phosphoanhydride linkage of triphosphate-containing substrates including tripolyphosphate, nucleoside triphosphates and nucleoside tetraphosphates. These substrates are hydrolyzed, releasing Pi. Mg++ or Mn++ are required for the enzyme's activity. CthTTM appears to have no adenylate cyclase activity. This subgroup consists chiefly of bacterial sequences. These enzymes are members of the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily, which have a unique active site located within an eight-stranded beta barrel.


Pssm-ID: 143629  Cd Length: 148  Bit Score: 250.11  E-value: 1.03e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948555436   3 IEIERKFLVINDGWRSAAHRVIPMAQGYINDmgaldrgTQNASVRVRIEGDHAALNLKSRTIGHTRQEFDYPIPVEDARA 82
Cdd:cd07891     1 LEIERKFLVKGDAWRALAAKGVRIRQGYLST-------DPERTVRVRIAGDRAYLTIKGPTNGLSRYEFEYEIPLADAEE 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1948555436  83 LLALCVGGLIDKRRHLVEHAGLTWEVDEFLGDNAGLVVAEVELDSADQAIELPDWAGAEVTDDARYYNVALASHP 157
Cdd:cd07891    74 LLALCEGPVIEKTRYRVPHGGHTWEVDVFHGENAGLVVAEIELPSEDEPFELPDWLGREVTGDPRYYNASLAKHP 148
CYTH-like_CthTTM-like cd07761
Clostridium thermocellum (Cth)TTM and similar proteins, a subgroup of the CYTH-like ...
 3-155 2.82e-39

Clostridium thermocellum (Cth)TTM and similar proteins, a subgroup of the CYTH-like superfamily; CthTTM is a metal dependent tripolyphosphatase, nucleoside triphosphatase, and nucleoside tetraphosphatase. It hydrolyzes the beta-gamma phosphoanhydride linkage of triphosphate-containing substrates including tripolyphosphate, nucleoside triphosphates and nucleoside tetraphosphates. These substrates are hydrolyzed, releasing Pi. Mg++ or Mn++ are required for the enzyme's activity. CthTTM appears to have no adenylate cyclase activity. This subgroup consists chiefly of bacterial sequences. Members of the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily have a unique active site located within an eight-stranded beta barrel.


Pssm-ID: 143626  Cd Length: 146  Bit Score: 130.04  E-value: 2.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948555436   3 IEIERKFLV--INDGWRSAAHRviPMAQGYIndmgaldrgTQNASVRVRIEGDHAALNLKSRTiGHTRQEFDYPIPVEDA 80
Cdd:cd07761     1 MEIERKFLVneLPAGLESYKKV--EIRQGYL---------SINPEVRIRSKGEKYILTVKSGG-GLVREEIEIEIDKKEF 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1948555436  81 RALLALCVGGLIDKRRHLVE-HAGLTWEVDEFLGDNAGLVVAEVELDSADQAI--ELPDWAGAEVTDDARYYNVALAS 155
Cdd:cd07761    69 EHLLEKTEGNLIEKTRYLIPlEGGLLAELDVFEGRLTGLVYAEVEFPSEEAARafSPPAWFGKEVTEDPRYKNKNLAL 146
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 3-149 6.18e-17

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: 73.34  E-value: 6.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948555436   3 IEIERKFLVIN---------DGWRSAAHRVIPMAQGYINDMGALDRGTQnASVRVRIEGDHA-ALNLKSRTIGHTRQEF- 71
Cdd:pfam01928   2 IEIERKFLVSDeeykdllllEKLRGKAEGPEEQRDIYFDTPDRDLARTD-EALRIRRFGNGAyFLTLKGPGVDGPFKSRe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948555436  72 --------DYPIPVEDARALLALCVGGL-IDKRRHLVEHAGLTWEVDEFLGdnaglvVAEVELDSADQAIELPDWAGAE- 141
Cdd:pfam01928  81 evngevsrDEPDAVELLDGLGLQPVGSIkKERRRYKVKGVLIALDVVEFLG------GAEVELELEVEDEEELLEAAEEl 154

                         170
                  ....*....|....*...
gi 1948555436 142 ----------VTDDARYY 149
Cdd:pfam01928 155 ellrilglseESKIARFY 172
 
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.
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