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Conserved domains on  [gi|815688606|ref|WP_046423543|]
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CYTH domain-containing protein [Burkholderia vietnamiensis]

Protein Classification

CYTH domain-containing protein( domain architecture ID 10166798)

CYTH domain-containing protein such as inorganic triphosphatase, which catalyzes the hydrolysis of inorganic or nucleoside-linked triphosphate-containing substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 4-205 1.86e-59

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: 184.74  E-value: 1.86e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606   4 EREIKLALPAGQAEAARHF--FETLTGEAGQTITLANVYYDTPELALAQSKSAVRVRRTPHGWLQTFKTVGSAEAGLHRR 81
Cdd:cd07756    1 EIELKLLLPPEDLEALAAHplLAALAAGRAQTRRLHNTYFDTPDLALRRAGIALRVRREGGQWVQTLKTAGSVVGGLHQR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606  82 HEWELPVAGDALEIDALvAACDVPEAATALRDAAPaLHALFRTDFSRTLWRVAIGGATVEAAVDVGEIVvqtpSDTRREP 161
Cdd:cd07756   81 PEWEVPLPGPAPDLDLA-SILPDGELLEALAALAA-LVPLFTTDFERTVWLLRLGGSEIEVALDQGEIR----AGDRSEP 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 815688606 162 ISEIELELIDGPEAALATLAAELQQALPgLAPENISKAQRGYRL 205
Cdd:cd07756  155 ICEIELELKSGDPAALFALARRLAERLP-LRLSNRSKAERGYRL 197
 
Name Accession Description Interval E-value
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 4-205 1.86e-59

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: 184.74  E-value: 1.86e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606   4 EREIKLALPAGQAEAARHF--FETLTGEAGQTITLANVYYDTPELALAQSKSAVRVRRTPHGWLQTFKTVGSAEAGLHRR 81
Cdd:cd07756    1 EIELKLLLPPEDLEALAAHplLAALAAGRAQTRRLHNTYFDTPDLALRRAGIALRVRREGGQWVQTLKTAGSVVGGLHQR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606  82 HEWELPVAGDALEIDALvAACDVPEAATALRDAAPaLHALFRTDFSRTLWRVAIGGATVEAAVDVGEIVvqtpSDTRREP 161
Cdd:cd07756   81 PEWEVPLPGPAPDLDLA-SILPDGELLEALAALAA-LVPLFTTDFERTVWLLRLGGSEIEVALDQGEIR----AGDRSEP 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 815688606 162 ISEIELELIDGPEAALATLAAELQQALPgLAPENISKAQRGYRL 205
Cdd:cd07756  155 ICEIELELKSGDPAALFALARRLAERLP-LRLSNRSKAERGYRL 197
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 1-207 1.84e-53

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


Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 171.62  E-value: 1.84e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606   1 MAIEREIKLALPAGQAEAAR--HFFETLTGEAGQTITLANVYYDTPELALAQSKSAVRVRRTPHGWLQTFKTVGSAEAGL 78
Cdd:COG3025    1 MAREIELKLLVDPEALPALRqhPLLAGLAVGEPATRRLENTYFDTPDLDLRRAGIGLRVRREGGRWEQTLKTAGQVVGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606  79 HRRHEWELPVAGDALEIDALVAACdVPEAATALRDAAPaLHALFRTDFSRTLWRVA-IGGATVEAAVDVGEIVVQtpsdT 157
Cdd:COG3025   81 HQRPEWEVPLPSPEPDLSLLPDEP-LPELLDAAALGAA-LQPVFTTDFERTTWLLTlADGSLIEVALDQGEIRAG----E 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 815688606 158 RREPISEIELELIDGPEAALATLAAELQQALPgLAPENISKAQRGYRLRA 207
Cdd:COG3025  155 RREPICELELELKSGDPAALFALALELAEALP-LRLSSLSKAERGYRLAA 203
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 2-203 2.04e-18

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: 78.73  E-value: 2.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606    2 AIEREIKLALPAGQAEAARHFfETLTGEAGQTITLANVYYDTPELALAQSKSAVRVRRTPHGW-LQTFKTVGSAEAGLHR 80
Cdd:pfam01928   1 MIEIERKFLVSDEEYKDLLLL-EKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFGNGAyFLTLKGPGVDGPFKSR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606   81 rhewelpvagdaLEIDALVAAcDVPEAATALRdaAPALHALFRTDFSRTLWRVAIggatVEAAVDVGEIVVqtpsdtrre 160
Cdd:pfam01928  80 ------------EEVNGEVSR-DEPDAVELLD--GLGLQPVGSIKKERRRYKVKG----VLIALDVVEFLG--------- 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 815688606  161 pISEIELELIDGPeAALATLAAELQQALPGLAPENISKAQRGY 203
Cdd:pfam01928 132 -GAEVELELEVED-EEELLEAAEELELLRILGLSEESKIARFY 172
 
Name Accession Description Interval E-value
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 4-205 1.86e-59

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: 184.74  E-value: 1.86e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606   4 EREIKLALPAGQAEAARHF--FETLTGEAGQTITLANVYYDTPELALAQSKSAVRVRRTPHGWLQTFKTVGSAEAGLHRR 81
Cdd:cd07756    1 EIELKLLLPPEDLEALAAHplLAALAAGRAQTRRLHNTYFDTPDLALRRAGIALRVRREGGQWVQTLKTAGSVVGGLHQR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606  82 HEWELPVAGDALEIDALvAACDVPEAATALRDAAPaLHALFRTDFSRTLWRVAIGGATVEAAVDVGEIVvqtpSDTRREP 161
Cdd:cd07756   81 PEWEVPLPGPAPDLDLA-SILPDGELLEALAALAA-LVPLFTTDFERTVWLLRLGGSEIEVALDQGEIR----AGDRSEP 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 815688606 162 ISEIELELIDGPEAALATLAAELQQALPgLAPENISKAQRGYRL 205
Cdd:cd07756  155 ICEIELELKSGDPAALFALARRLAERLP-LRLSNRSKAERGYRL 197
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 1-207 1.84e-53

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


Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 171.62  E-value: 1.84e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606   1 MAIEREIKLALPAGQAEAAR--HFFETLTGEAGQTITLANVYYDTPELALAQSKSAVRVRRTPHGWLQTFKTVGSAEAGL 78
Cdd:COG3025    1 MAREIELKLLVDPEALPALRqhPLLAGLAVGEPATRRLENTYFDTPDLDLRRAGIGLRVRREGGRWEQTLKTAGQVVGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606  79 HRRHEWELPVAGDALEIDALVAACdVPEAATALRDAAPaLHALFRTDFSRTLWRVA-IGGATVEAAVDVGEIVVQtpsdT 157
Cdd:COG3025   81 HQRPEWEVPLPSPEPDLSLLPDEP-LPELLDAAALGAA-LQPVFTTDFERTTWLLTlADGSLIEVALDQGEIRAG----E 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 815688606 158 RREPISEIELELIDGPEAALATLAAELQQALPgLAPENISKAQRGYRLRA 207
Cdd:COG3025  155 RREPICELELELKSGDPAALFALALELAEALP-LRLSSLSKAERGYRLAA 203
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 2-203 2.04e-18

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: 78.73  E-value: 2.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606    2 AIEREIKLALPAGQAEAARHFfETLTGEAGQTITLANVYYDTPELALAQSKSAVRVRRTPHGW-LQTFKTVGSAEAGLHR 80
Cdd:pfam01928   1 MIEIERKFLVSDEEYKDLLLL-EKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFGNGAyFLTLKGPGVDGPFKSR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606   81 rhewelpvagdaLEIDALVAAcDVPEAATALRdaAPALHALFRTDFSRTLWRVAIggatVEAAVDVGEIVVqtpsdtrre 160
Cdd:pfam01928  80 ------------EEVNGEVSR-DEPDAVELLD--GLGLQPVGSIKKERRRYKVKG----VLIALDVVEFLG--------- 131

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 815688606  161 pISEIELELIDGPeAALATLAAELQQALPGLAPENISKAQRGY 203
Cdd:pfam01928 132 -GAEVELELEVED-EEELLEAAEELELLRILGLSEESKIARFY 172
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 4-172 6.32e-11

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: 58.62  E-value: 6.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606   4 EREIKLALPAGQAEAAR-HFFETLTGEAGQTITLANVYYDTPELALAQSKSAVRVRRTPHGWLQTFKTvgsaEAGLHRRH 82
Cdd:cd07374    1 EVERKFRVPDDAVLPLLlGVPGVLGVGEPETVQLRAIYFDTPDLRLARAGLRLRRRTGGADAGWHLKL----PGGISRRT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606  83 EWELPVAGDALEIDALVAACDVPEAATALrdaapALHALFRTDFSRTLWRV-AIGGATVEAAVDVGEIVVQTPSDTRREp 161
Cdd:cd07374   77 EVRAPLGDAAAVAPLLLAAALVLAVTRGL-----PLRPVATIETTRTVYRLlDAGGVLAELDLDTVTARVLDGGGTQYW- 150

                        170
                 ....*....|.
gi 815688606 162 iSEIELELIDG 172
Cdd:cd07374  151 -REVEVELPDG 160
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 3-94 8.67e-06

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: 44.48  E-value: 8.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606   3 IEREIKLALPAgqAEAARHFFETLTGEAGQTITLANVYYDTPELALAQSKSAVRVRRTPHGWLQTFKtvGS-AEAGLHRR 81
Cdd:COG1437    1 IEVEVKVRVID--LEEVRERLEELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRRGGGRATLTYK--GPkLDEGSKTR 76

                         90
                 ....*....|....
gi 815688606  82 HEWELPVA-GDALE 94
Cdd:COG1437   77 EEIETEVDdGEAME 90
CYTH-like_Pase_1 cd07762
Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like ...
 3-70 6.10e-04

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: 39.10  E-value: 6.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815688606   3 IEREIKLALPAGQAEAARHFFEtltgeAGQTITLANVYYDTPELALAQSKSAVRVRRTPHGWLQTFKT 70
Cdd:cd07762    1 LEIEFKNLLTKEEYEQLKNAFD-----LKDFFKQTNYYFDTPDFALKKKHSALRIREKEGKAELTLKV 63
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
 4-94 1.99e-03

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: 37.63  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815688606   4 EREIKLALPagQAEAARHFFETLTGEAGQTITLANVYYDTPELALAQSKSAVRVRRTP--HGWLQTFKtvGSAEAGLHR- 80
Cdd:cd07890    1 EVEIKARVD--DLEALRERLAALGGAEGGREFQEDIYFDHPDRDLAATDEALRLRRMGdsGKTLLTYK--GPKLDGGPKv 76

                         90
                 ....*....|....*
gi 815688606  81 RHEWELPVA-GDALE 94
Cdd:cd07890   77 REEIETEVAdPEAMK 91
 
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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