NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1069043505|gb|OEH07517|]
View 

CYTH domain-containing protein [Enterobacter roggenkampii]

Protein Classification

inorganic triphosphatase( domain architecture ID 11459565)

inorganic triphosphatase catalyzes the hydrolysis of inorganic or nucleoside-linked triphosphate-containing substrates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 1-245 7.03e-101

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


:

Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 301.04  E-value: 7.03e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505   1 MAQEIELKFIVEKDSVDALRQH--LHTLSGEHHAPVQLLNIYYETPDNWLRRHDMGLRIRGASGRYEMTMKIAGRVVGGL 78
Cdd:COG3025     1 MAREIELKLLVDPEALPALRQHplLAGLAVGEPATRRLENTYFDTPDLDLRRAGIGLRVRREGGRWEQTLKTAGQVVGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505  79 HQRPEYNIDISQPELELERFPAEVWPEGELPATLAEQVQPLFSTDFWREKWLVT-EGKSRIEIALDLGEVKAGEYQEPIC 157
Cdd:COG3025    81 HQRPEWEVPLPSPEPDLSLLPDEPLPELLDAAALGAALQPVFTTDFERTTWLLTlADGSLIEVALDQGEIRAGERREPIC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505 158 ELELELLEGDANDVLKLARRLVNQSGLRQGSLSKAARGYHLAAGNAPRVLKETTIlRVAPKASVEQGLEAALELALSQWQ 237
Cdd:COG3025   161 ELELELKSGDPAALFALALELAEALPLRLSSLSKAERGYRLAAGAPAAPVKALPV-ALDPDMTAEEAFRAILRACLAHLQ 239


                  ....*...
gi 1069043505 238 YHEELWVR 245
Cdd:COG3025   240 ANEEALLR 247
 
Name Accession Description Interval E-value
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 1-245 7.03e-101

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


Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 301.04  E-value: 7.03e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505   1 MAQEIELKFIVEKDSVDALRQH--LHTLSGEHHAPVQLLNIYYETPDNWLRRHDMGLRIRGASGRYEMTMKIAGRVVGGL 78
Cdd:COG3025     1 MAREIELKLLVDPEALPALRQHplLAGLAVGEPATRRLENTYFDTPDLDLRRAGIGLRVRREGGRWEQTLKTAGQVVGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505  79 HQRPEYNIDISQPELELERFPAEVWPEGELPATLAEQVQPLFSTDFWREKWLVT-EGKSRIEIALDLGEVKAGEYQEPIC 157
Cdd:COG3025    81 HQRPEWEVPLPSPEPDLSLLPDEPLPELLDAAALGAALQPVFTTDFERTTWLLTlADGSLIEVALDQGEIRAGERREPIC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505 158 ELELELLEGDANDVLKLARRLVNQSGLRQGSLSKAARGYHLAAGNAPRVLKETTIlRVAPKASVEQGLEAALELALSQWQ 237
Cdd:COG3025   161 ELELELKSGDPAALFALALELAEALPLRLSSLSKAERGYRLAAGAPAAPVKALPV-ALDPDMTAEEAFRAILRACLAHLQ 239


                  ....*...
gi 1069043505 238 YHEELWVR 245
Cdd:COG3025   240 ANEEALLR 247
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 4-198 1.19e-70

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: 221.34  E-value: 1.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505   4 EIELKFIVEKDSVDALRQHlHTLSGEHHAP---VQLLNIYYETPDNWLRRHDMGLRIRGASGRYEMTMKIAGRVVGGLHQ 80
Cdd:cd07756     1 EIELKLLLPPEDLEALAAH-PLLAALAAGRaqtRRLHNTYFDTPDLALRRAGIALRVRREGGQWVQTLKTAGSVVGGLHQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505  81 RPEYNIDISQPELELERfpAEVWPEGELPATLA--EQVQPLFSTDFWREKWLVTEGKSRIEIALDLGEVKAGEYQEPICE 158
Cdd:cd07756    80 RPEWEVPLPGPAPDLDL--ASILPDGELLEALAalAALVPLFTTDFERTVWLLRLGGSEIEVALDQGEIRAGDRSEPICE 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1069043505 159 LELELLEGDANDVLKLARRLVNQSGLRQGSLSKAARGYHL 198
Cdd:cd07756   158 IELELKSGDPAALFALARRLAERLPLRLSNRSKAERGYRL 197
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 2-196 5.80e-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: 108.78  E-value: 5.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505   2 AQEIELKFIVEKDSVDAlRQHLHTLSGEHHAPVQLLNIYYETPDNWLRRHDMGLRIRGA-SGRYEMTMKIAGrVVGGLHQ 80
Cdd:pfam01928   1 MIEIERKFLVSDEEYKD-LLLLEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFgNGAYFLTLKGPG-VDGPFKS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505  81 RPEYNIDISQPELElerfpaevwpegELPATLAEQVQPLFSTDFWREKWLVTEgksrIEIALDLGEVKAGEYQEpicele 160
Cdd:pfam01928  79 REEVNGEVSRDEPD------------AVELLDGLGLQPVGSIKKERRRYKVKG----VLIALDVVEFLGGAEVE------ 136

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1069043505 161 LELLEGDANDVLKLARRLVNQSGLRQGSLSKAARGY 196
Cdd:pfam01928 137 LELEVEDEEELLEAAEELELLRILGLSEESKIARFY 172
 
Name Accession Description Interval E-value
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 1-245 7.03e-101

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


Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 301.04  E-value: 7.03e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505   1 MAQEIELKFIVEKDSVDALRQH--LHTLSGEHHAPVQLLNIYYETPDNWLRRHDMGLRIRGASGRYEMTMKIAGRVVGGL 78
Cdd:COG3025     1 MAREIELKLLVDPEALPALRQHplLAGLAVGEPATRRLENTYFDTPDLDLRRAGIGLRVRREGGRWEQTLKTAGQVVGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505  79 HQRPEYNIDISQPELELERFPAEVWPEGELPATLAEQVQPLFSTDFWREKWLVT-EGKSRIEIALDLGEVKAGEYQEPIC 157
Cdd:COG3025    81 HQRPEWEVPLPSPEPDLSLLPDEPLPELLDAAALGAALQPVFTTDFERTTWLLTlADGSLIEVALDQGEIRAGERREPIC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505 158 ELELELLEGDANDVLKLARRLVNQSGLRQGSLSKAARGYHLAAGNAPRVLKETTIlRVAPKASVEQGLEAALELALSQWQ 237
Cdd:COG3025   161 ELELELKSGDPAALFALALELAEALPLRLSSLSKAERGYRLAAGAPAAPVKALPV-ALDPDMTAEEAFRAILRACLAHLQ 239


                  ....*...
gi 1069043505 238 YHEELWVR 245
Cdd:COG3025   240 ANEEALLR 247
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 4-198 1.19e-70

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: 221.34  E-value: 1.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505   4 EIELKFIVEKDSVDALRQHlHTLSGEHHAP---VQLLNIYYETPDNWLRRHDMGLRIRGASGRYEMTMKIAGRVVGGLHQ 80
Cdd:cd07756     1 EIELKLLLPPEDLEALAAH-PLLAALAAGRaqtRRLHNTYFDTPDLALRRAGIALRVRREGGQWVQTLKTAGSVVGGLHQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505  81 RPEYNIDISQPELELERfpAEVWPEGELPATLA--EQVQPLFSTDFWREKWLVTEGKSRIEIALDLGEVKAGEYQEPICE 158
Cdd:cd07756    80 RPEWEVPLPGPAPDLDL--ASILPDGELLEALAalAALVPLFTTDFERTVWLLRLGGSEIEVALDQGEIRAGDRSEPICE 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1069043505 159 LELELLEGDANDVLKLARRLVNQSGLRQGSLSKAARGYHL 198
Cdd:cd07756   158 IELELKSGDPAALFALARRLAERLPLRLSNRSKAERGYRL 197
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 2-196 5.80e-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: 108.78  E-value: 5.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505   2 AQEIELKFIVEKDSVDAlRQHLHTLSGEHHAPVQLLNIYYETPDNWLRRHDMGLRIRGA-SGRYEMTMKIAGrVVGGLHQ 80
Cdd:pfam01928   1 MIEIERKFLVSDEEYKD-LLLLEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFgNGAYFLTLKGPG-VDGPFKS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505  81 RPEYNIDISQPELElerfpaevwpegELPATLAEQVQPLFSTDFWREKWLVTEgksrIEIALDLGEVKAGEYQEpicele 160
Cdd:pfam01928  79 REEVNGEVSRDEPD------------AVELLDGLGLQPVGSIKKERRRYKVKG----VLIALDVVEFLGGAEVE------ 136

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1069043505 161 LELLEGDANDVLKLARRLVNQSGLRQGSLSKAARGY 196
Cdd:pfam01928 137 LELEVEDEEELLEAAEELELLRILGLSEESKIARFY 172
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 4-157 5.98e-17

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: 78.26  E-value: 5.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505   4 EIELKFIVEKDSVDALRQHL-HTLSGEHHAPVQLLNIYYETPDNWLRRHDMGLRIRGASGRYEMTMKIAGRVvgglHQRP 82
Cdd:cd07374     1 EVERKFRVPDDAVLPLLLGVpGVLGVGEPETVQLRAIYFDTPDLRLARAGLRLRRRTGGADAGWHLKLPGGI----SRRT 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1069043505  83 EYNIDISQPELELerfPAEVWPEGELPATLAEQVQPLFSTDFWREKW-LVTEGKSRIEIALDLGEVKAGEYQEPIC 157
Cdd:cd07374    77 EVRAPLGDAAAVA---PLLLAAALVLAVTRGLPLRPVATIETTRTVYrLLDAGGVLAELDLDTVTARVLDGGGTQY 149
CYTH-like_Pase_1 cd07762
Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like ...
 4-94 4.20e-13

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: 67.22  E-value: 4.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505   4 EIELKFIVEKDSVDALRQHLHtlsgeHHAPVQLLNIYYETPDNWLRRHDMGLRIRGASGRYEMTMKIAGRvvgglHQRPE 83
Cdd:cd07762     2 EIEFKNLLTKEEYEQLKNAFD-----LKDFFKQTNYYFDTPDFALKKKHSALRIREKEGKAELTLKVPQE-----VGLLE 71

                          90
                  ....*....|.
gi 1069043505  84 YNIDISQPELE 94
Cdd:cd07762    72 TNQPLTLEEAE 82
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 4-92 8.21e-10

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: 57.58  E-value: 8.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505   4 EIELKFIVekDSVDALRQHLHTLSGEHHAPVQLLNIYYETPDNWLRRHDMGLRIRGASGRYEMTMKIAgRVVGGLHQRPE 83
Cdd:COG1437     2 EVEVKVRV--IDLEEVRERLEELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRRGGGRATLTYKGP-KLDEGSKTREE 78


                  ....*....
gi 1069043505  84 YNIDISQPE 92
Cdd:COG1437    79 IETEVDDGE 87
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
 4-92 3.27e-06

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: 46.88  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069043505   4 EIELKFIVekDSVDALRQHLHTLSGEHHAPVQLLNIYYETPDNWLRRHDMGLRIR--GASGRYEMTMKIAgRVVGGLHQR 81
Cdd:cd07890     1 EVEIKARV--DDLEALRERLAALGGAEGGREFQEDIYFDHPDRDLAATDEALRLRrmGDSGKTLLTYKGP-KLDGGPKVR 77

                          90
                  ....*....|.
gi 1069043505  82 PEYNIDISQPE 92
Cdd:cd07890    78 EEIETEVADPE 88
 
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