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Conserved domains on  [gi|1539931753|emb|VEF95393|]
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carbonic anhydrase 2 YadF [Escherichia marmotae]

Protein Classification

carbonic anhydrase( domain architecture ID 10793390)

carbonic anhydrase (CA) catalyzes the zinc-dependent reversible hydration of carbon dioxide into bicarbonate and a proton

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10437 PRK10437
carbonic anhydrase; Provisional
 1-220 9.39e-180

carbonic anhydrase; Provisional


:

Pssm-ID: 182460  Cd Length: 220  Bit Score: 490.98  E-value: 9.39e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753   1 MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV 80
Cdd:PRK10437    1 MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  81 VQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPPERRLDTLCELNVMEQVYNLGH 160
Cdd:PRK10437   81 VQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPQERRLDTLCELNVMEQVYNLGH 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753 161 STIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLEQRYRHGISNLKLKHINHK 220
Cdd:PRK10437  161 STIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLEQRYRHGISNLKLKHANHK 220
 
Name Accession Description Interval E-value
PRK10437 PRK10437
carbonic anhydrase; Provisional
 1-220 9.39e-180

carbonic anhydrase; Provisional


Pssm-ID: 182460  Cd Length: 220  Bit Score: 490.98  E-value: 9.39e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753   1 MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV 80
Cdd:PRK10437    1 MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  81 VQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPPERRLDTLCELNVMEQVYNLGH 160
Cdd:PRK10437   81 VQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPQERRLDTLCELNVMEQVYNLGH 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753 161 STIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLEQRYRHGISNLKLKHINHK 220
Cdd:PRK10437  161 STIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLEQRYRHGISNLKLKHANHK 220
beta_CA_cladeA cd00883
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
 11-191 1.52e-112

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 238448  Cd Length: 182  Bit Score: 319.51  E-value: 1.52e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  11 NALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSVVQYAVDVLEV 90
Cdd:cd00883     1 NRAWAEEKKAKDPDFFPRLAKGQTPEYLWIGCSDSRVPENTILGLLPGEVFVHRNIANLVSPTDLNCLSVLQYAVDVLKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  91 EHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEM-PPERRLDTLCELNVMEQVYNLGHSTIMQSAWK 169
Cdd:cd00883    81 KHIIVCGHYGCGGVKAALTGKRLGLLDNWLRPIRDVYRLHAAELDALeDEEERVDRLVELNVVEQVKNLCKTPIVQDAWK 160

                         170       180
                  ....*....|....*....|..
gi 1539931753 170 RGQKVTIHGWAYGIHDGLLRDL 191
Cdd:cd00883   161 RGQELEVHGWVYDLGDGLLRDL 182
CynT COG0288
Carbonic anhydrase [Inorganic ion transport and metabolism];
1-202 1.46e-96

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 440057  Cd Length: 204  Bit Score: 279.74  E-value: 1.46e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753   1 MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV 80
Cdd:COG0288     1 MEALKRLLEGNRRFVAGKFPQDPERFEELAKGQHPFALVIGCSDSRVPPELIFDQGPGDLFVVRNAGNVVPPYDPGVLAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  81 VQYAVDVLEVEHIIICGHYGCGGVQAAVEN---PELGLINNWLLHIRDIWFKHSSLLGEMPPERRLDTLCELNVMEQVYN 157
Cdd:COG0288    81 IEYAVEVLGVKLIVVLGHSGCGAVKAALDGlelEELGLIGNWLRHIRPAVERVRAELPAADGEERLDRLVELNVREQVEN 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1539931753 158 LGHSTIMQSAWKRGQkVTIHGWAYGIHDGLLRDLDVTATNRETLE 202
Cdd:COG0288   161 LRTSPIVREAVAAGK-LKVHGWVYDLATGRVEFLDPEGGGFEPLP 204
Pro_CA pfam00484
Carbonic anhydrase; This family includes carbonic anhydrases as well as a family of ...
 38-188 4.08e-76

Carbonic anhydrase; This family includes carbonic anhydrases as well as a family of non-functional homologs related to YbcF.


Pssm-ID: 459828  Cd Length: 156  Bit Score: 226.24  E-value: 4.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  38 LWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSVVQYAVDVLEVEHIIICGHYGCGGVQAAVENP----EL 113
Cdd:pfam00484   2 LIIGCSDSRVPPELIFDTGPGDLFVVRNAGNLVPPYDLNVLASIEYAVEVLKVKHIVVCGHSGCGAVKAALDAAgpaeLP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1539931753 114 GLINNWLLHIRDIWFKHSSLLGEM-PPERRLDTLCELNVMEQVYNLGHSTIMQSAWKRGQkVTIHGWAYGIHDGLL 188
Cdd:pfam00484  82 GFIDNWLRHIRPAVERVAEELESLdDPEERDDALEELNVREQVENLRTFPIVREAVAKGK-LKIHGWVYDLETGEV 156
Pro_CA smart00947
Carbonic anhydrase; Carbonic anhydrases (CA) are zinc metalloenzymes which catalyze the ...
 30-191 2.93e-70

Carbonic anhydrase; Carbonic anhydrases (CA) are zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. In Escherichia coli, CA (gene cynT) is involved in recycling carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (gene cynS). By this action, it prevents the depletion of cellular bicarbonate. In photosynthetic bacteria and plant chloroplast, CA is essential to inorganic carbon fixation. Prokaryotic and plant chloroplast CA are structurally and evolutionary related and form a family distinct from the one which groups the many different forms of eukaryotic CA's.


Pssm-ID: 214929 [Multi-domain]  Cd Length: 154  Bit Score: 211.21  E-value: 2.93e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753   30 AQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSVVQYAVDVLEVEHIIICGHYGCGGVQAAVE 109
Cdd:smart00947   1 AKGQHPKALIIGCSDSRVPPELIFGLGPGDLFVIRNAGNIVPPYDDGVLASLEYAVEVLGVKEIVVCGHTDCGAVKAALD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  110 nPELGLINNWLLHIRDIWFKHSSLLGEMpperrlDTLCELNVMEQVYNLGHSTIMQSAWKRGqKVTIHGWAYGIHDGLLR 189
Cdd:smart00947  81 -DEPGLIDNWLERIRPARERALEELGDV------DALEELNVRDQVENLRTSPAIREAVAKG-KLKVHGWVYDIETGKLE 152


                   ..
gi 1539931753  190 DL 191
Cdd:smart00947 153 VL 154
 
Name Accession Description Interval E-value
PRK10437 PRK10437
carbonic anhydrase; Provisional
 1-220 9.39e-180

carbonic anhydrase; Provisional


Pssm-ID: 182460  Cd Length: 220  Bit Score: 490.98  E-value: 9.39e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753   1 MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV 80
Cdd:PRK10437    1 MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  81 VQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPPERRLDTLCELNVMEQVYNLGH 160
Cdd:PRK10437   81 VQYAVDVLEVEHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEMPQERRLDTLCELNVMEQVYNLGH 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753 161 STIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLEQRYRHGISNLKLKHINHK 220
Cdd:PRK10437  161 STIMQSAWKRGQKVTIHGWAYGIHDGLLRDLDVTATNRETLEQRYRHGISNLKLKHANHK 220
beta_CA_cladeA cd00883
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
 11-191 1.52e-112

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 238448  Cd Length: 182  Bit Score: 319.51  E-value: 1.52e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  11 NALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSVVQYAVDVLEV 90
Cdd:cd00883     1 NRAWAEEKKAKDPDFFPRLAKGQTPEYLWIGCSDSRVPENTILGLLPGEVFVHRNIANLVSPTDLNCLSVLQYAVDVLKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  91 EHIIICGHYGCGGVQAAVENPELGLINNWLLHIRDIWFKHSSLLGEM-PPERRLDTLCELNVMEQVYNLGHSTIMQSAWK 169
Cdd:cd00883    81 KHIIVCGHYGCGGVKAALTGKRLGLLDNWLRPIRDVYRLHAAELDALeDEEERVDRLVELNVVEQVKNLCKTPIVQDAWK 160

                         170       180
                  ....*....|....*....|..
gi 1539931753 170 RGQKVTIHGWAYGIHDGLLRDL 191
Cdd:cd00883   161 RGQELEVHGWVYDLGDGLLRDL 182
CynT COG0288
Carbonic anhydrase [Inorganic ion transport and metabolism];
1-202 1.46e-96

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 440057  Cd Length: 204  Bit Score: 279.74  E-value: 1.46e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753   1 MKDIDTLISNNALWSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSV 80
Cdd:COG0288     1 MEALKRLLEGNRRFVAGKFPQDPERFEELAKGQHPFALVIGCSDSRVPPELIFDQGPGDLFVVRNAGNVVPPYDPGVLAS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  81 VQYAVDVLEVEHIIICGHYGCGGVQAAVEN---PELGLINNWLLHIRDIWFKHSSLLGEMPPERRLDTLCELNVMEQVYN 157
Cdd:COG0288    81 IEYAVEVLGVKLIVVLGHSGCGAVKAALDGlelEELGLIGNWLRHIRPAVERVRAELPAADGEERLDRLVELNVREQVEN 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1539931753 158 LGHSTIMQSAWKRGQkVTIHGWAYGIHDGLLRDLDVTATNRETLE 202
Cdd:COG0288   161 LRTSPIVREAVAAGK-LKVHGWVYDLATGRVEFLDPEGGGFEPLP 204
Pro_CA pfam00484
Carbonic anhydrase; This family includes carbonic anhydrases as well as a family of ...
 38-188 4.08e-76

Carbonic anhydrase; This family includes carbonic anhydrases as well as a family of non-functional homologs related to YbcF.


Pssm-ID: 459828  Cd Length: 156  Bit Score: 226.24  E-value: 4.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  38 LWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSVVQYAVDVLEVEHIIICGHYGCGGVQAAVENP----EL 113
Cdd:pfam00484   2 LIIGCSDSRVPPELIFDTGPGDLFVVRNAGNLVPPYDLNVLASIEYAVEVLKVKHIVVCGHSGCGAVKAALDAAgpaeLP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1539931753 114 GLINNWLLHIRDIWFKHSSLLGEM-PPERRLDTLCELNVMEQVYNLGHSTIMQSAWKRGQkVTIHGWAYGIHDGLL 188
Cdd:pfam00484  82 GFIDNWLRHIRPAVERVAEELESLdDPEERDDALEELNVREQVENLRTFPIVREAVAKGK-LKIHGWVYDLETGEV 156
Pro_CA smart00947
Carbonic anhydrase; Carbonic anhydrases (CA) are zinc metalloenzymes which catalyze the ...
 30-191 2.93e-70

Carbonic anhydrase; Carbonic anhydrases (CA) are zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. In Escherichia coli, CA (gene cynT) is involved in recycling carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (gene cynS). By this action, it prevents the depletion of cellular bicarbonate. In photosynthetic bacteria and plant chloroplast, CA is essential to inorganic carbon fixation. Prokaryotic and plant chloroplast CA are structurally and evolutionary related and form a family distinct from the one which groups the many different forms of eukaryotic CA's.


Pssm-ID: 214929 [Multi-domain]  Cd Length: 154  Bit Score: 211.21  E-value: 2.93e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753   30 AQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSVVQYAVDVLEVEHIIICGHYGCGGVQAAVE 109
Cdd:smart00947   1 AKGQHPKALIIGCSDSRVPPELIFGLGPGDLFVIRNAGNIVPPYDDGVLASLEYAVEVLGVKEIVVCGHTDCGAVKAALD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  110 nPELGLINNWLLHIRDIWFKHSSLLGEMpperrlDTLCELNVMEQVYNLGHSTIMQSAWKRGqKVTIHGWAYGIHDGLLR 189
Cdd:smart00947  81 -DEPGLIDNWLERIRPARERALEELGDV------DALEELNVRDQVENLRTSPAIREAVAKG-KLKVHGWVYDIETGKLE 152


                   ..
gi 1539931753  190 DL 191
Cdd:smart00947 153 VL 154
beta_CA cd00382
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
 33-191 2.74e-53

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 238224 [Multi-domain]  Cd Length: 119  Bit Score: 166.91  E-value: 2.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  33 QKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSVVQYAVDVLEVEHIIICGHYGCGGVQAavenpe 112
Cdd:cd00382     1 QKPKALIIGCSDSRVPPELIFGLGPGDLFVVRNAGNLVPPYDLDVLASLEYAVEVLGVKHIIVCGHTDCGAVKA------ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1539931753 113 lglinnwllhirdiwfkhssllgempperrldtLCELNVMEQVYNLGHSTIMQsAWKRGQKVTIHGWAYGIHDGLLRDL 191
Cdd:cd00382    75 ---------------------------------LVEENVREQVENLRSHPLIQ-EAVAPGELKVHGWVYDIETGKLEVL 119
beta_CA_cladeB cd00884
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
 20-188 3.86e-45

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 238449  Cd Length: 190  Bit Score: 148.46  E-value: 3.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  20 EEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLV--IHTDLNCLSV---VQYAVDVLEVEHII 94
Cdd:cd00884    11 PEERELFEKLAKGQSPKALFIACSDSRVVPALITQTQPGELFVVRNVGNLVppYEPDGGFHGTsaaIEYAVAVLKVEHIV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  95 ICGHYGCGGVQAAVE----NPELGLINNWLLHIRDIWFKHSSLLGEMPPERRLDTLCELNVMEQVYNL-GHSTImQSAWK 169
Cdd:cd00884    91 VCGHSDCGGIRALLSpedlLDKLPFIGKWLRIAEPAKEVVLAELSHADFDDQLRALEKENVLLSLENLlTYPFV-RERLE 169

                         170
                  ....*....|....*....
gi 1539931753 170 RGqKVTIHGWAYGIHDGLL 188
Cdd:cd00884   170 AG-TLSLHGWYYDIETGEL 187
PLN00416 PLN00416
carbonate dehydratase
 20-120 1.47e-20

carbonate dehydratase


Pssm-ID: 177809  Cd Length: 258  Bit Score: 86.63  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  20 EEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDL----NCLSVVQYAVDVLEVEHIII 95
Cdd:PLN00416   65 LKNSTLFNHLAKTQTPKFLVFACSDSRVCPSHILNFQPGEAFVVRNIANMVPPFDQkrhsGVGAAVEYAVVHLKVENILV 144

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1539931753  96 CGHYGCGGVQA--AVEN----PELGLINNWL 120
Cdd:PLN00416  145 IGHSCCGGIKGlmSIEDdaapTQSDFIENWV 175
PLN02154 PLN02154
carbonic anhydrase
 26-185 4.39e-19

carbonic anhydrase


Pssm-ID: 215111  Cd Length: 290  Bit Score: 83.26  E-value: 4.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  26 FEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVI-----HTDLNclSVVQYAVDVLEVEHIIICGHYG 100
Cdd:PLN02154   98 FKALAIAQSPKVMVIGCADSRVCPSYVLGFQPGEAFTIRNVANLVTpvqngPTETN--SALEFAVTTLQVENIIVMGHSN 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753 101 CGGVQAAV-----ENPELGLINNWLLHIRDIWFKHSSLLGEMPPERRLDTLCELNVMEQVYNLGHSTIMQSAWKRGQkVT 175
Cdd:PLN02154  176 CGGIAALMshqnhQGQHSSLVERWVMNGKAAKLRTQLASSHLSFDEQCRNCEKESIKDSVMNLITYSWIRDRVKRGE-VK 254

                         170
                  ....*....|
gi 1539931753 176 IHGWAYGIHD 185
Cdd:PLN02154  255 IHGCYYNLSD 264
PLN03006 PLN03006
carbonate dehydratase
 14-121 5.73e-18

carbonate dehydratase


Pssm-ID: 178583  Cd Length: 301  Bit Score: 80.56  E-value: 5.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  14 WSKMLVEEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTD---LNCLSVVQYAVDVLEV 90
Cdd:PLN03006   92 FKKLKYMDDFEHYKNLADAQAPKFLVIACADSRVCPSAVLGFQPGDAFTVRNIANLVPPYEsgpTETKAALEFSVNTLNV 171

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1539931753  91 EHIIICGHYGCGGVQAAVENPELG----LINNWLL 121
Cdd:PLN03006  172 ENILVIGHSRCGGIQALMKMEDEGdsrsFIHNWVV 206
beta_CA_cladeC cd03378
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
 27-109 5.78e-17

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 239473 [Multi-domain]  Cd Length: 154  Bit Score: 74.48  E-value: 5.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  27 EKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVihtDLNCLSVVQYAVDVLEVEHIIICGHYGCGGVQA 106
Cdd:cd03378    31 RELAKGQKPFAVILSCSDSRVPPEIIFDQGLGDLFVVRVAGNIV---DDDVLGSLEYAVEVLGVPLVVVLGHESCGAVAA 107


                  ...
gi 1539931753 107 AVE 109
Cdd:cd03378   108 AAV 110
PLN03014 PLN03014
carbonic anhydrase
 20-129 1.06e-16

carbonic anhydrase


Pssm-ID: 178588 [Multi-domain]  Cd Length: 347  Bit Score: 77.47  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  20 EEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDL----NCLSVVQYAVDVLEVEHIII 95
Cdd:PLN03014  145 ETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKvkygGVGAAIEYAVLHLKVENIVV 224

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1539931753  96 CGHYGCGGVQAAVENPELGliNNWLLHIRDiWFK 129
Cdd:PLN03014  225 IGHSACGGIKGLMSFPLDG--NNSTDFIED-WVK 255
PLN03019 PLN03019
carbonic anhydrase
 20-129 7.04e-16

carbonic anhydrase


Pssm-ID: 166660  Cd Length: 330  Bit Score: 74.80  E-value: 7.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  20 EEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTD----LNCLSVVQYAVDVLEVEHIII 95
Cdd:PLN03019  140 ETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFHPGDAFVVRNIANMVPPFDkvkyAGVGAAIEYAVLHLKVENIVV 219

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1539931753  96 CGHYGCGGVQAAVENPELGliNNWLLHIRDiWFK 129
Cdd:PLN03019  220 IGHSACGGIKGLMSFPLDG--NNSTDFIED-WVK 250
PRK15219 PRK15219
carbonic anhydrase; Provisional
 30-186 4.66e-09

carbonic anhydrase; Provisional


Pssm-ID: 237927 [Multi-domain]  Cd Length: 245  Bit Score: 54.84  E-value: 4.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  30 AQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRnVANLVIHTDLncLSVVQYAVDVLEVEHIIICGHYGCGGVQAAVE 109
Cdd:PRK15219   85 AAGQYPAAVILSCIDSRAPAEIILDTGIGETFNSR-VAGNISNDDL--LGSMEFACAVAGAKVVLVMGHTACGAVKGAID 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753 110 NPELGLINNWLLHIrdiwfKHSSLLGEMPPERR------LDTLCELNVMEQVYNL-GHSTIMQSAWKRGqKVTIHGWAYG 182
Cdd:PRK15219  162 NVELGNLTGLLDRI-----KPAIEVTEFDGERSsknykfVDAVARKNVELTIENIrKNSPILRKLEQEG-KIKIVGSMYN 235


                  ....
gi 1539931753 183 IHDG 186
Cdd:PRK15219  236 LNGG 239
beta_CA_cladeD cd03379
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
 34-189 1.05e-05

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 239474  Cd Length: 142  Bit Score: 43.78  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539931753  34 KPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTDLNCLSVVQYAvdvLEVEHIIICGHYGCGgvQAAVENPEL 113
Cdd:cd03379     2 ARKLAIVTCMDARLDPEKALGLKLGDAKVIRNAGGRVTDDAIRSLVVSVYL---LGTREIIVIHHTDCG--MLTFTDEEL 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539931753 114 --GLINNWLLHIRDIWFKHSSLLGempperrLDTLCElNVMEQVYNLGHSTIMQSawkrgqKVTIHGWAYGIHDGLLR 189
Cdd:cd03379    77 keKMKERGIAEAYGGIDKEFWFLG-------FDDLEE-SVREDVERIRNHPLIPD------DVPVHGYVYDVKTGKLT 140
 
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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