NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|147796316|emb|CAN72544|]
View 

hypothetical protein VITISV_036603 [Vitis vinifera]

Protein Classification

CYTH domain-containing protein; polyphosphate polymerase domain-containing protein( domain architecture ID 10164209)

CYTH domain-containing protein such as inorganic triphosphatase, which catalyzes the hydrolysis of inorganic or nucleoside-linked triphosphate-containing substrates| polyphosphate (polyP) polymerase domain-containing protein similar to yeast vacuolar transport chaperone (VTC) proteins VTC-2, -3 and- 4, which are components of the integral membrane VTC complex; the polyP polymerase domain generates polyP from ATP by a phosphotransfer reaction releasing ADP

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 2-172 9.24e-31

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: 110.62  E-value: 9.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316   2 EVEVKLRLPDAASHQKLSDL---LAPFHVKTLIQENIFFDGAaaELSSKFAVLRLRFYDLDSRCVLSLKSQPqisnGISR 78
Cdd:cd07374    1 EVERKFRVPDDAVLPLLLGVpgvLGVGEPETVQLRAIYFDTP--DLRLARAGLRLRRRTGGADAGWHLKLPG----GISR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316  79 AKEVEEEIEPLIGRACVAEPWRfksmssriikrlRDEFEVGDEGLVCLGGFRNVRAVYAWNG---LNLELDETLFDF--- 152
Cdd:cd07374   75 RTEVRAPLGDAAAVAPLLLAAA------------LVLAVTRGLPLRPVATIETTRTVYRLLDaggVLAELDLDTVTArvl 142

                        170       180
                 ....*....|....*....|...
gi 147796316 153 ---GTNYEIECESSEPERAKKLL 172
Cdd:cd07374  143 dggGTQYWREVEVELPDGDEALL 165
 
Name Accession Description Interval E-value
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 2-172 9.24e-31

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: 110.62  E-value: 9.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316   2 EVEVKLRLPDAASHQKLSDL---LAPFHVKTLIQENIFFDGAaaELSSKFAVLRLRFYDLDSRCVLSLKSQPqisnGISR 78
Cdd:cd07374    1 EVERKFRVPDDAVLPLLLGVpgvLGVGEPETVQLRAIYFDTP--DLRLARAGLRLRRRTGGADAGWHLKLPG----GISR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316  79 AKEVEEEIEPLIGRACVAEPWRfksmssriikrlRDEFEVGDEGLVCLGGFRNVRAVYAWNG---LNLELDETLFDF--- 152
Cdd:cd07374   75 RTEVRAPLGDAAAVAPLLLAAA------------LVLAVTRGLPLRPVATIETTRTVYRLLDaggVLAELDLDTVTArvl 142

                        170       180
                 ....*....|....*....|...
gi 147796316 153 ---GTNYEIECESSEPERAKKLL 172
Cdd:cd07374  143 dggGTQYWREVEVELPDGDEALL 165
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 1-173 2.27e-12

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: 62.56  E-value: 2.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316    1 MEVEVKLRLPDAASHQKLS-DLLAPFHVKTLIQENIFFDGAAAELSSKFAVLRLRFYDlDSRCVLSLKSqpqisNGISRA 79
Cdd:pfam01928   2 IEIERKFLVSDEEYKDLLLlEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFG-NGAYFLTLKG-----PGVDGP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316   80 KEVEEEIEPLIGRaCVAEPwrfksmsSRIIKRLrdefevgdeGLVCLGGFRNVRAVYAWNGLNLELDETLFDFGTNYEIE 159
Cdd:pfam01928  76 FKSREEVNGEVSR-DEPDA-------VELLDGL---------GLQPVGSIKKERRRYKVKGVLIALDVVEFLGGAEVELE 138

                         170
                  ....*....|....
gi 147796316  160 CESSEPERAKKLLE 173
Cdd:pfam01928 139 LEVEDEEELLEAAE 152
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 1-182 1.62e-08

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: 51.80  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316   1 MEVEVKLRLPDAAS-HQKLSDLLAPFhVKTLIQENIFFDGAAAELSSKFAVLRLRfyDLDSRCVLSLKSQPQISNGISRa 79
Cdd:COG1437    1 IEVEVKVRVIDLEEvRERLEELGAEL-VGEEHQIDIYYDAPDRDFAETDEALRIR--RGGGRATLTYKGPKLDEGSKTR- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316  80 KEVEEEIEPligracvaepwrFKSMsSRIIKRLrdefevgdeGLVCLGGFRNVRAVYAWNGLNLELDET--LFDFGtnyE 157
Cdd:COG1437   77 EEIETEVDD------------GEAM-EAILEAL---------GFRPVATVEKTREIYKLGGVTVTLDEVegLGPFV---E 131

                        170       180
                 ....*....|....*....|....*.
gi 147796316 158 IECESS-EPERAKKLLEGFLEENGIS 182
Cdd:COG1437  132 IEGEAEdEVEAAREAIEEVLAELGLD 157
 
Name Accession Description Interval E-value
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 2-172 9.24e-31

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: 110.62  E-value: 9.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316   2 EVEVKLRLPDAASHQKLSDL---LAPFHVKTLIQENIFFDGAaaELSSKFAVLRLRFYDLDSRCVLSLKSQPqisnGISR 78
Cdd:cd07374    1 EVERKFRVPDDAVLPLLLGVpgvLGVGEPETVQLRAIYFDTP--DLRLARAGLRLRRRTGGADAGWHLKLPG----GISR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316  79 AKEVEEEIEPLIGRACVAEPWRfksmssriikrlRDEFEVGDEGLVCLGGFRNVRAVYAWNG---LNLELDETLFDF--- 152
Cdd:cd07374   75 RTEVRAPLGDAAAVAPLLLAAA------------LVLAVTRGLPLRPVATIETTRTVYRLLDaggVLAELDLDTVTArvl 142

                        170       180
                 ....*....|....*....|...
gi 147796316 153 ---GTNYEIECESSEPERAKKLL 172
Cdd:cd07374  143 dggGTQYWREVEVELPDGDEALL 165
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 1-173 2.27e-12

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: 62.56  E-value: 2.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316    1 MEVEVKLRLPDAASHQKLS-DLLAPFHVKTLIQENIFFDGAAAELSSKFAVLRLRFYDlDSRCVLSLKSqpqisNGISRA 79
Cdd:pfam01928   2 IEIERKFLVSDEEYKDLLLlEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFG-NGAYFLTLKG-----PGVDGP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316   80 KEVEEEIEPLIGRaCVAEPwrfksmsSRIIKRLrdefevgdeGLVCLGGFRNVRAVYAWNGLNLELDETLFDFGTNYEIE 159
Cdd:pfam01928  76 FKSREEVNGEVSR-DEPDA-------VELLDGL---------GLQPVGSIKKERRRYKVKGVLIALDVVEFLGGAEVELE 138

                         170
                  ....*....|....
gi 147796316  160 CESSEPERAKKLLE 173
Cdd:pfam01928 139 LEVEDEEELLEAAE 152
CYTH-like_Pase_1 cd07762
Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like ...
 2-194 8.04e-10

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: 55.67  E-value: 8.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316   2 EVEVKLRLpDAASHQKLSDLLapFHVKTLIQENIFFDGAAAELSSKFAVLRLRFYDldSRCVLSLKsQPQisngisraKE 81
Cdd:cd07762    2 EIEFKNLL-TKEEYEQLKNAF--DLKDFFKQTNYYFDTPDFALKKKHSALRIREKE--GKAELTLK-VPQ--------EV 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316  82 VEEEIEPLIGRAcVAEPWRFKS-MSSRIIKRLRDEFEVGDEGLVCLGGFRNVRAVYAWNGLNLELDETLFDFGTNYEIEC 160
Cdd:cd07762   68 GLLETNQPLTLE-EAEKLIKGGtLPEGEILDKLKELGIDPSELKLFGSLTTIRAEIPYEGGLLVLDHSLYLGITDYELEY 146

                        170       180       190
                 ....*....|....*....|....*....|....
gi 147796316 161 ESSEPERAKKLLEGFLEENGISFSNAEaSKFAVF 194
Cdd:cd07762  147 EVDDYEAGKKAFLELLKQYNIPYRPAK-NKIARF 179
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 1-182 1.62e-08

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: 51.80  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316   1 MEVEVKLRLPDAAS-HQKLSDLLAPFhVKTLIQENIFFDGAAAELSSKFAVLRLRfyDLDSRCVLSLKSQPQISNGISRa 79
Cdd:COG1437    1 IEVEVKVRVIDLEEvRERLEELGAEL-VGEEHQIDIYYDAPDRDFAETDEALRIR--RGGGRATLTYKGPKLDEGSKTR- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316  80 KEVEEEIEPligracvaepwrFKSMsSRIIKRLrdefevgdeGLVCLGGFRNVRAVYAWNGLNLELDET--LFDFGtnyE 157
Cdd:COG1437   77 EEIETEVDD------------GEAM-EAILEAL---------GFRPVATVEKTREIYKLGGVTVTLDEVegLGPFV---E 131

                        170       180
                 ....*....|....*....|....*.
gi 147796316 158 IECESS-EPERAKKLLEGFLEENGIS 182
Cdd:COG1437  132 IEGEAEdEVEAAREAIEEVLAELGLD 157
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
 2-182 4.47e-08

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: 50.73  E-value: 4.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316   2 EVEVKLRLPDAAS-HQKLSDLLApFHVKTLIQENIFFDGAAAELSSKFAVLRLRFYDLDSRCVLSLKSQPQisngiSRAK 80
Cdd:cd07890    1 EVEIKARVDDLEAlRERLAALGG-AEGGREFQEDIYFDHPDRDLAATDEALRLRRMGDSGKTLLTYKGPKL-----DGGP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147796316  81 EVEEEIEpligrACVAEPwrfKSMSSrIIKRLrdefevgdeGLVCLGGFRNVRAVYAWNGLNLELDEtLFDFGTNYEIEC 160
Cdd:cd07890   75 KVREEIE-----TEVADP---EAMKE-ILERL---------GFGPVGRVKKEREIYLLGQTRVHLDR-VEGLGDFVEIEV 135

                        170       180
                 ....*....|....*....|..
gi 147796316 161 ESSEPERAKKLLEGFLEENGIS 182
Cdd:cd07890  136 VLEDIEEAEEGLGEAAELLGLL 157
 
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