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Conserved domains on  [gi|746089240|ref|WP_039156031|]
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MULTISPECIES: CYTH domain-containing protein [Lactobacillus]

Protein Classification

CYTH domain-containing protein( domain architecture ID 10166815)

CYTH domain-containing protein belongs to the triphosphate tunnel metalloenzyme (TTM)-like superfamily of enzymes that 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; may function as an adenylate cyclase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYTH-like_Pase_1 cd07762
Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like ...
 5-203 1.94e-55

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: 173.92  E-value: 1.94e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240   5 LEIESKTLLDKDTYEKMRDAFTAKSDFIQKNYYFDTPDFDLKNSDASLRIRILVDHAEQTIKVKETKpkenkysERVEIN 84
Cdd:cd07762    1 LEIEFKNLLTKEEYEQLKNAFDLKDFFKQTNYYFDTPDFALKKKHSALRIREKEGKAELTLKVPQEV-------GLLETN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240  85 DLLSVAQAEQMAQSAYegtffLFGGDVGNYLQKHYSKesIHSLKLISWSQTRRILAVGpENCELTLDLTEFPdGYYDFEL 164
Cdd:cd07762   74 QPLTLEEAEKLIKGGT-----LPEGEILDKLKELGID--PSELKLFGSLTTIRAEIPY-EGGLLVLDHSLYL-GITDYEL 144

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 746089240 165 EIENDDPATIKKVLAELEKQFDFKANKentNQSKVKRAW 203
Cdd:cd07762  145 EYEVDDYEAGKKAFLELLKQYNIPYRP---AKNKIARFL 180
 
Name Accession Description Interval E-value
CYTH-like_Pase_1 cd07762
Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like ...
 5-203 1.94e-55

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: 173.92  E-value: 1.94e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240   5 LEIESKTLLDKDTYEKMRDAFTAKSDFIQKNYYFDTPDFDLKNSDASLRIRILVDHAEQTIKVKETKpkenkysERVEIN 84
Cdd:cd07762    1 LEIEFKNLLTKEEYEQLKNAFDLKDFFKQTNYYFDTPDFALKKKHSALRIREKEGKAELTLKVPQEV-------GLLETN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240  85 DLLSVAQAEQMAQSAYegtffLFGGDVGNYLQKHYSKesIHSLKLISWSQTRRILAVGpENCELTLDLTEFPdGYYDFEL 164
Cdd:cd07762   74 QPLTLEEAEKLIKGGT-----LPEGEILDKLKELGID--PSELKLFGSLTTIRAEIPY-EGGLLVLDHSLYL-GITDYEL 144

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 746089240 165 EIENDDPATIKKVLAELEKQFDFKANKentNQSKVKRAW 203
Cdd:cd07762  145 EYEVDDYEAGKKAFLELLKQYNIPYRP---AKNKIARFL 180
YjbK COG4116
Predicted triphosphatase or cyclase YjbK, contains CYTH domain [General function prediction ...
 2-207 1.88e-40

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


Pssm-ID: 443292  Cd Length: 191  Bit Score: 136.12  E-value: 1.88e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240   2 SKNLEIESKTLLDKDTYEKMRDAFTAKSD--FIQKNYYFDTPDFDLKNSDASLRIRILVDHAEQTIKVKETKPkenkyse 79
Cdd:COG4116    1 SQEIEIEFKNLLTKEEYNRLLEHFNFKEEefFTQTNYYFDTPDFDLKKHGSALRIRTKNDSYELTLKQPAEVG------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240  80 RVEINDLLSVAQAEQMAQSAYegtffLFGGDVGNYLQKHysKESIHSLKLISWSQTRRILAVGPeNCELTLDLTEFPDgY 159
Cdd:COG4116   74 LLETNDPLSLEEAKALIEGGQ-----LPSGEVADILKEL--GIDPEELKYFGSLTTTRAEIPYK-EGLLVLDHSFYLD-Q 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 746089240 160 YDFELEIENDDPATIKKVLAELEKQFDFkanKENTNQSKVKRAWEHKK 207
Cdd:COG4116  145 EDYELEFEVTDEEQGKKVFDELLKEFNI---PKRPAKNKIARFYDALK 189
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 4-183 9.89e-13

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: 63.71  E-value: 9.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240    4 NLEIESKTLLDKDTYEKMRDA----FTAKSDFIQKNYYFDTPDFDLKNSDASLRIRILVDHAE-QTIKVKETkpkENKYS 78
Cdd:pfam01928   1 MIEIERKFLVSDEEYKDLLLLeklrGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFGNGAYfLTLKGPGV---DGPFK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240   79 ERVEINDLLSvAQAEQMAQsayegtffLFGGDvgnylqkhyskesiHSLKLISWSQTRRILAVGpeNCELTLDLTEFpDG 158
Cdd:pfam01928  78 SREEVNGEVS-RDEPDAVE--------LLDGL--------------GLQPVGSIKKERRRYKVK--GVLIALDVVEF-LG 131

                         170       180
                  ....*....|....*....|....*
gi 746089240  159 YYDFELEIENDDPATIKKVLAELEK 183
Cdd:pfam01928 132 GAEVELELEVEDEEELLEAAEELEL 156
 
Name Accession Description Interval E-value
CYTH-like_Pase_1 cd07762
Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like ...
 5-203 1.94e-55

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: 173.92  E-value: 1.94e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240   5 LEIESKTLLDKDTYEKMRDAFTAKSDFIQKNYYFDTPDFDLKNSDASLRIRILVDHAEQTIKVKETKpkenkysERVEIN 84
Cdd:cd07762    1 LEIEFKNLLTKEEYEQLKNAFDLKDFFKQTNYYFDTPDFALKKKHSALRIREKEGKAELTLKVPQEV-------GLLETN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240  85 DLLSVAQAEQMAQSAYegtffLFGGDVGNYLQKHYSKesIHSLKLISWSQTRRILAVGpENCELTLDLTEFPdGYYDFEL 164
Cdd:cd07762   74 QPLTLEEAEKLIKGGT-----LPEGEILDKLKELGID--PSELKLFGSLTTIRAEIPY-EGGLLVLDHSLYL-GITDYEL 144

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 746089240 165 EIENDDPATIKKVLAELEKQFDFKANKentNQSKVKRAW 203
Cdd:cd07762  145 EYEVDDYEAGKKAFLELLKQYNIPYRP---AKNKIARFL 180
YjbK COG4116
Predicted triphosphatase or cyclase YjbK, contains CYTH domain [General function prediction ...
 2-207 1.88e-40

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


Pssm-ID: 443292  Cd Length: 191  Bit Score: 136.12  E-value: 1.88e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240   2 SKNLEIESKTLLDKDTYEKMRDAFTAKSD--FIQKNYYFDTPDFDLKNSDASLRIRILVDHAEQTIKVKETKPkenkyse 79
Cdd:COG4116    1 SQEIEIEFKNLLTKEEYNRLLEHFNFKEEefFTQTNYYFDTPDFDLKKHGSALRIRTKNDSYELTLKQPAEVG------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240  80 RVEINDLLSVAQAEQMAQSAYegtffLFGGDVGNYLQKHysKESIHSLKLISWSQTRRILAVGPeNCELTLDLTEFPDgY 159
Cdd:COG4116   74 LLETNDPLSLEEAKALIEGGQ-----LPSGEVADILKEL--GIDPEELKYFGSLTTTRAEIPYK-EGLLVLDHSFYLD-Q 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 746089240 160 YDFELEIENDDPATIKKVLAELEKQFDFkanKENTNQSKVKRAWEHKK 207
Cdd:COG4116  145 EDYELEFEVTDEEQGKKVFDELLKEFNI---PKRPAKNKIARFYDALK 189
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 4-183 9.89e-13

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: 63.71  E-value: 9.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240    4 NLEIESKTLLDKDTYEKMRDA----FTAKSDFIQKNYYFDTPDFDLKNSDASLRIRILVDHAE-QTIKVKETkpkENKYS 78
Cdd:pfam01928   1 MIEIERKFLVSDEEYKDLLLLeklrGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFGNGAYfLTLKGPGV---DGPFK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240   79 ERVEINDLLSvAQAEQMAQsayegtffLFGGDvgnylqkhyskesiHSLKLISWSQTRRILAVGpeNCELTLDLTEFpDG 158
Cdd:pfam01928  78 SREEVNGEVS-RDEPDAVE--------LLDGL--------------GLQPVGSIKKERRRYKVK--GVLIALDVVEF-LG 131

                         170       180
                  ....*....|....*....|....*
gi 746089240  159 YYDFELEIENDDPATIKKVLAELEK 183
Cdd:pfam01928 132 GAEVELELEVEDEEELLEAAEELEL 156
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
 6-185 1.40e-09

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: 54.97  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240   6 EIESKTLLDkdTYEKMRDAFTAKSDF-----IQKNYYFDTPDFDLKNSDASLRIRILVDHAEQTIKVKETK----PKENK 76
Cdd:cd07890    1 EVEIKARVD--DLEALRERLAALGGAeggreFQEDIYFDHPDRDLAATDEALRLRRMGDSGKTLLTYKGPKldggPKVRE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240  77 YSErVEINDLlsvAQAEQMAQSAYEGTFFlfggdvgnylqkHYSKEsihslkliswsqtRRILAVGpeNCELTLDLTEfp 156
Cdd:cd07890   79 EIE-TEVADP---EAMKEILERLGFGPVG------------RVKKE-------------REIYLLG--QTRVHLDRVE-- 125

                        170       180       190
                 ....*....|....*....|....*....|
gi 746089240 157 dGYYDF-ELEIENDDPATIKKVLAELEKQF 185
Cdd:cd07890  126 -GLGDFvEIEVVLEDIEEAEEGLGEAAELL 154
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 6-66 3.72e-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: 51.47  E-value: 3.72e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 746089240   6 EIESKTLLDKDTYEKMR--DAFTAKSDFIQ-----KNYYFDTPDFDLKNSDASLRIRILVDHAEQTIK 66
Cdd:cd07756    1 EIELKLLLPPEDLEALAahPLLAALAAGRAqtrrlHNTYFDTPDLALRRAGIALRVRREGGQWVQTLK 68
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 5-182 1.35e-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: 49.49  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240   5 LEIESKTLLDkdTYEKMRDA-----FTAKSDFIQKNYYFDTPDFDLKNSDASLRIRILVDHAEQTIKvkeTKPKENKYSE 79
Cdd:COG1437    1 IEVEVKVRVI--DLEEVRERleelgAELVGEEHQIDIYYDAPDRDFAETDEALRIRRGGGRATLTYK---GPKLDEGSKT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240  80 RVEINdlLSVAQAEQMAQsayegtffLFggdvgnylqkhyskESIHSLKLISWSQTRRILAVGpeNCELTLDLTefpDGY 159
Cdd:COG1437   76 REEIE--TEVDDGEAMEA--------IL--------------EALGFRPVATVEKTREIYKLG--GVTVTLDEV---EGL 126

                        170       180
                 ....*....|....*....|....*....
gi 746089240 160 YDF-ELEIENDDPAT-----IKKVLAELE 182
Cdd:COG1437  127 GPFvEIEGEAEDEVEaareaIEEVLAELG 155
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 4-66 1.46e-06

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


Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 47.20  E-value: 1.46e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240   4 NLEIESKTLLDKDTYEKMRDAFTAKSDFIQK-------NYYFDTPDFDLKNSDASLRIRILVDHAEQTIK 66
Cdd:COG3025    2 AREIELKLLVDPEALPALRQHPLLAGLAVGEpatrrleNTYFDTPDLDLRRAGIGLRVRREGGRWEQTLK 71
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 6-186 4.33e-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: 45.14  E-value: 4.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240   6 EIESKTLLDKDTYEKMRDAFTAKS------DFIQKNYYFDTPDFDLKNSDASLRIRILVDHAEQTIKVKETKpkenkySE 79
Cdd:cd07374    1 EVERKFRVPDDAVLPLLLGVPGVLgvgepeTVQLRAIYFDTPDLRLARAGLRLRRRTGGADAGWHLKLPGGI------SR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240  80 RVEINDLLSVAQAEQMAQSAYEGTFFLFGGdvgnylqkhyskesiHSLKLISWSQTRR----ILAVGPENCELTLDL--- 152
Cdd:cd07374   75 RTEVRAPLGDAAAVAPLLLAAALVLAVTRG---------------LPLRPVATIETTRtvyrLLDAGGVLAELDLDTvta 139

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 746089240 153 --TEFPDGYYDFELEIENDDPATikKVLAELEKQFD 186
Cdd:cd07374  140 rvLDGGGTQYWREVEVELPDGDE--ALLDALERRLT 173
CYTH COG2954
CYTH domain, found in class IV adenylate cyclase and various triphosphatases [General function ...
 5-95 8.93e-03

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


Pssm-ID: 442195  Cd Length: 157  Bit Score: 35.53  E-value: 8.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746089240   5 LEIESKTLLDKDTYekmRDAFTAKSDFIQknYYFDTPDfdlknsDASLRIRILVDHAEQTIKVKETKPKenkyseRVEIN 84
Cdd:COG2954    3 LEIERKFLVKGDPW---RALATRGTRIRQ--GYLSTDP------ERTVRVRIKGDQAFLTIKGKGSGLS------REEFE 65

                         90
                 ....*....|.
gi 746089240  85 DLLSVAQAEQM 95
Cdd:COG2954   66 YEIPLADAEEL 76
 
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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