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Conserved domains on  [gi|28269695|ref|NP_444300|]
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carbonic anhydrase 7 isoform a [Mus musculus]

Protein Classification

alpha_CA_VII domain-containing protein( domain architecture ID 10123556)

alpha_CA_VII domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
27-262 5.32e-180

Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme VII. CA VII is the most active cytosolic enzyme after CA II, and may be highly expressed in the brain. Human CA VII may be a target of antiepileptic sulfonamides/sulfamates.


:

Pssm-ID: 239402  Cd Length: 236  Bit Score: 493.97  E-value: 5.32e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  27 GDRQSPINIISSQAVYSPSLQPLELFYEACMSLSITNNGHSVQVDFNDSDDRTVVSGGPLEGPYRLKQLHFHWGKKRDMG 106
Cdd:cd03149   1 GNRQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLSISNNGHSVMVEFDDSDDKTVITGGPLENPYRLKQFHFHWGAKHGSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 107 SEHTVDGKSFPSELHLVHWNAKKYSTFGEAAAAPDGLAVVGVFLETGDEHPSMNRLTDALYMVRFKDTKAQFSCFNPKCL 186
Cdd:cd03149  81 SEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETGDEHPGLNRLTDALYMVRFKGTKAQFLDFNPKCL 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28269695 187 LPTSRHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDERIHMVDNFRPPQPLKGRVVKASF 262
Cdd:cd03149 161 LPKSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHMVNNFRPPQPLKGRTVRASF 236
 
Name Accession Description Interval E-value
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
27-262 5.32e-180

Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme VII. CA VII is the most active cytosolic enzyme after CA II, and may be highly expressed in the brain. Human CA VII may be a target of antiepileptic sulfonamides/sulfamates.


Pssm-ID: 239402  Cd Length: 236  Bit Score: 493.97  E-value: 5.32e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  27 GDRQSPINIISSQAVYSPSLQPLELFYEACMSLSITNNGHSVQVDFNDSDDRTVVSGGPLEGPYRLKQLHFHWGKKRDMG 106
Cdd:cd03149   1 GNRQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLSISNNGHSVMVEFDDSDDKTVITGGPLENPYRLKQFHFHWGAKHGSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 107 SEHTVDGKSFPSELHLVHWNAKKYSTFGEAAAAPDGLAVVGVFLETGDEHPSMNRLTDALYMVRFKDTKAQFSCFNPKCL 186
Cdd:cd03149  81 SEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETGDEHPGLNRLTDALYMVRFKGTKAQFLDFNPKCL 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28269695 187 LPTSRHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDERIHMVDNFRPPQPLKGRVVKASF 262
Cdd:cd03149 161 LPKSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHMVNNFRPPQPLKGRTVRASF 236
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
7-257 8.03e-130

Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse the reversible hydration of carbon dioxide to bicarbonate.. CAs have essential roles in facilitating the transport of carbon dioxide and protons in the intracellular space, across biological membranes and in the layers of the extracellular space; they are also involved in many other processes, from respiration and photosynthesis in eukaryotes to cyanate degradation in prokaryotes. There are five known evolutionarily distinct CA families (alpha, beta, gamma, delta and epsilon) that have no significant sequence identity and have structurally distinct overall folds. Some CAs are membrane-bound, while others act in the cytosol; there are several related proteins that lack enzymatic activity. The active site of alpha-CAs is well described, consisting of a zinc ion coordinated through 3 histidine residues and a water molecule/hydroxide ion that acts as a potent nucleophile. The enzyme employs a two-step mechanism: in the first step, there is a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide; in the second step, the active site is regenerated by the ionisation of the zinc-bound water molecule and the removal of a proton from the active site. Beta- and gamma-CAs also employ a zinc hydroxide mechanism, although at least some beta-class enzymes do not have water directly coordinated to the metal ion.


Pssm-ID: 215000 [Multi-domain]  Cd Length: 247  Bit Score: 367.41  E-value: 8.03e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695      7 WGYGQDDGPSNWHKLYP-IAQGDRQSPINIISSQAVYSPSLQPLELFYEACMSLSITNNGHSVQVDFNDsdDRTVVSGGP 85
Cdd:smart01057   1 WGYEGKNGPEHWGKLDPpFCGGKRQSPIDIVTAEAQYDPSLKPLKLSYDQPTAKRILNNGHTVQVNFDD--DGSTLSGGP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695     86 LEGPYRLKQLHFHWGKKRDMGSEHTVDGKSFPSELHLVHWNAKKysTFGEAAAAPDGLAVVGVFLETGDEH-PSMNRLTD 164
Cdd:smart01057  79 LPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEEnPALQAILD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695    165 ALYMVRFKDTKAQFSCFNPKCLLPTS-RHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDErihM 243
Cdd:smart01057 157 HLPLIKYKGQETELTPFDLSSLLPAStRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEP---L 233
                          250
                   ....*....|....
gi 28269695    244 VDNFRPPQPLKGRV 257
Cdd:smart01057 234 VNNARPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
25-256 4.40e-123

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 425516  Cd Length: 230  Bit Score: 349.60  E-value: 4.40e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695    25 AQGDRQSPINIISSQAVYSPSLQPLEL--FYEACMSLSITNNGHSVQVDFndsDDRTVVSGGPLEGPYRLKQLHFHWGKK 102
Cdd:pfam00194   1 CGGKRQSPINIDTRKVRYDPSLGPLTFsgYDKPPTKKTLVNNGHTVQVTL---DDKPSISGGPLAGTYRLVQFHFHWGSE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695   103 RDMGSEHTVDGKSFPSELHLVHWNaKKYSTFGEAAAAPDGLAVVGVFLETGDEH-PSMNRLTDALYMVRFKDTKAQFSCF 181
Cdd:pfam00194  78 DSVGSEHTIDGKRYPAELHIVHYN-SKYGSFSEALDKPDGLAVLGVFFEVGDSNnPALDKIVSALGNIKYKGQSVTLPNF 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28269695   182 NPKCLLPTS-RHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDEriHMVDNFRPPQPLKGR 256
Cdd:pfam00194 157 PLSDLLPENlRDYYTYPGSLTTPPCSESVTWIVFKEPISISEEQLEKFRTLLFTSGGEP--PLVNNFRPTQPLNGR 230
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
7-258 4.07e-60

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 225875 [Multi-domain]  Cd Length: 250  Bit Score: 190.72  E-value: 4.07e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695   7 WGYGQDDGPSNWHKLYP----IAQGDRQSPINIisSQAVYSPSLQPLELFYEAcMSLSITNNGHSVQVDFNDSDDRTVVS 82
Cdd:COG3338  28 WGYTGKEGPEHWGELSPdfeaCAEGKNQSPIDI--EHAVDVQDKPPLQLNYQP-SAVTIKNNGHTIQVNFEPGSNHLRYD 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  83 GGPlegpYRLKQLHFHwgkkrdMGSEHTVDGKSFPSELHLVHWNAKkystfgeaaaapDGLAVVGVFLETGDEHPSMNRL 162
Cdd:COG3338 105 GKT----YQLVQFHFH------APSEHLVDGKSFPMEAHFVHKDAK------------GTLAVLAVLLQAGAENPELAPL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 163 TDALyMVRFKDTKAQFSCFNPKCLLPTSRHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLlftsedderih 242
Cdd:COG3338 163 WEGF-PQKPGEEETLDETIDLNAFLPESRNYYTYNGSLTTPPCSEGVTWIVLKEPIEVSQEQIAEFSKL----------- 230
                       250
                ....*....|....*.
gi 28269695 243 MVDNFRPPQPLKGRVV 258
Cdd:COG3338 231 MGHNARPVQPLNDRLI 246
PLN02202 PLN02202
carbonate dehydratase
7-259 2.66e-23

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 95.89  E-value: 2.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695    7 WGYGQDDGPSNWHKLYP----IAQGDRQSPINIISSQAVYSPSLQPLELFYeACMSLSITNNGHSVQVDFNDSDDRTVVS 82
Cdd:PLN02202  31 FGYKGKNGPNQWGHLNPhftkCAVGKLQSPIDIQRRQIFYNHKLESIHRDY-YFTNATLVNHVCNVAMFFGEGAGDVIID 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695   83 ggplEGPYRLKQLHFHwgkkrdMGSEHTVDGKSFPSELHLVHwnakkystfgeaaAAPDG-LAVVGVFLETGDEHPSMNR 161
Cdd:PLN02202 110 ----NKNYTLLQMHWH------TPSEHHLHGVQYAAELHMVH-------------QAKDGsFAVVASLFKIGTEEPFLSQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  162 LTDALYMV---RFKDT---KAQFSCFNPKCLLPTSRHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTS 235
Cdd:PLN02202 167 MKDKLVKLkeeRFKGNhtaQVEVGKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPLDKS 246
                        250       260
                 ....*....|....*....|....
gi 28269695  236 edderihMVDNFRPPQPLKGRVVK 259
Cdd:PLN02202 247 -------FKNNSRPCQPLNGRRVE 263
 
Name Accession Description Interval E-value
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
27-262 5.32e-180

Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme VII. CA VII is the most active cytosolic enzyme after CA II, and may be highly expressed in the brain. Human CA VII may be a target of antiepileptic sulfonamides/sulfamates.


Pssm-ID: 239402  Cd Length: 236  Bit Score: 493.97  E-value: 5.32e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  27 GDRQSPINIISSQAVYSPSLQPLELFYEACMSLSITNNGHSVQVDFNDSDDRTVVSGGPLEGPYRLKQLHFHWGKKRDMG 106
Cdd:cd03149   1 GNRQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLSISNNGHSVMVEFDDSDDKTVITGGPLENPYRLKQFHFHWGAKHGSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 107 SEHTVDGKSFPSELHLVHWNAKKYSTFGEAAAAPDGLAVVGVFLETGDEHPSMNRLTDALYMVRFKDTKAQFSCFNPKCL 186
Cdd:cd03149  81 SEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETGDEHPGLNRLTDALYMVRFKGTKAQFLDFNPKCL 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28269695 187 LPTSRHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDERIHMVDNFRPPQPLKGRVVKASF 262
Cdd:cd03149 161 LPKSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHMVNNFRPPQPLKGRTVRASF 236
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
5-262 1.74e-143

Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozymes I, II, and III, which are cytoplasmic enzymes. CA I, for example, is expressed in erythrocyes of many vertebrates; CA II is the most active cytosolic isozyme; while it is being expressed nearly ubiquitously, it comprises 95% of the renal carbonic anhydrase and is required for renal acidification; CA III has been implicated in protection from the damaging effect of oxidizing agents in hepatocytes. CAXIII may play important physiological roles in several organs.


Pssm-ID: 239393 [Multi-domain]  Cd Length: 259  Bit Score: 402.59  E-value: 1.74e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695   5 HCWGYGQDDGPSNWHKLYPIAQGDRQSPINIISSQAVYSPSLQPLELFYEACMSLSITNNGHSVQVDFNDSDDRTVVSGG 84
Cdd:cd03119   3 HHWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVSYDPATAKTILNNGHSFNVEFDDTDDRSVLRGG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  85 PLEGPYRLKQLHFHWGKKRDMGSEHTVDGKSFPSELHLVHWNAKkYSTFGEAAAAPDGLAVVGVFLETGDEHPSMNRLTD 164
Cdd:cd03119  83 PLTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNSK-YGSFGEAAKQPDGLAVVGVFLKVGEANPELQKVLD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 165 ALYMVRFKDTKAQFSCFNPKCLLPTSRHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDERIHMV 244
Cdd:cd03119 162 ALDSIKTKGKQAPFTNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEPPCPMV 241
                       250
                ....*....|....*...
gi 28269695 245 DNFRPPQPLKGRVVKASF 262
Cdd:cd03119 242 DNWRPPQPLKGRKVRASF 259
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
7-257 8.03e-130

Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse the reversible hydration of carbon dioxide to bicarbonate.. CAs have essential roles in facilitating the transport of carbon dioxide and protons in the intracellular space, across biological membranes and in the layers of the extracellular space; they are also involved in many other processes, from respiration and photosynthesis in eukaryotes to cyanate degradation in prokaryotes. There are five known evolutionarily distinct CA families (alpha, beta, gamma, delta and epsilon) that have no significant sequence identity and have structurally distinct overall folds. Some CAs are membrane-bound, while others act in the cytosol; there are several related proteins that lack enzymatic activity. The active site of alpha-CAs is well described, consisting of a zinc ion coordinated through 3 histidine residues and a water molecule/hydroxide ion that acts as a potent nucleophile. The enzyme employs a two-step mechanism: in the first step, there is a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide; in the second step, the active site is regenerated by the ionisation of the zinc-bound water molecule and the removal of a proton from the active site. Beta- and gamma-CAs also employ a zinc hydroxide mechanism, although at least some beta-class enzymes do not have water directly coordinated to the metal ion.


Pssm-ID: 215000 [Multi-domain]  Cd Length: 247  Bit Score: 367.41  E-value: 8.03e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695      7 WGYGQDDGPSNWHKLYP-IAQGDRQSPINIISSQAVYSPSLQPLELFYEACMSLSITNNGHSVQVDFNDsdDRTVVSGGP 85
Cdd:smart01057   1 WGYEGKNGPEHWGKLDPpFCGGKRQSPIDIVTAEAQYDPSLKPLKLSYDQPTAKRILNNGHTVQVNFDD--DGSTLSGGP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695     86 LEGPYRLKQLHFHWGKKRDMGSEHTVDGKSFPSELHLVHWNAKKysTFGEAAAAPDGLAVVGVFLETGDEH-PSMNRLTD 164
Cdd:smart01057  79 LPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEEnPALQAILD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695    165 ALYMVRFKDTKAQFSCFNPKCLLPTS-RHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDErihM 243
Cdd:smart01057 157 HLPLIKYKGQETELTPFDLSSLLPAStRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEP---L 233
                          250
                   ....*....|....
gi 28269695    244 VDNFRPPQPLKGRV 257
Cdd:smart01057 234 VNNARPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
25-256 4.40e-123

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 425516  Cd Length: 230  Bit Score: 349.60  E-value: 4.40e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695    25 AQGDRQSPINIISSQAVYSPSLQPLEL--FYEACMSLSITNNGHSVQVDFndsDDRTVVSGGPLEGPYRLKQLHFHWGKK 102
Cdd:pfam00194   1 CGGKRQSPINIDTRKVRYDPSLGPLTFsgYDKPPTKKTLVNNGHTVQVTL---DDKPSISGGPLAGTYRLVQFHFHWGSE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695   103 RDMGSEHTVDGKSFPSELHLVHWNaKKYSTFGEAAAAPDGLAVVGVFLETGDEH-PSMNRLTDALYMVRFKDTKAQFSCF 181
Cdd:pfam00194  78 DSVGSEHTIDGKRYPAELHIVHYN-SKYGSFSEALDKPDGLAVLGVFFEVGDSNnPALDKIVSALGNIKYKGQSVTLPNF 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28269695   182 NPKCLLPTS-RHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDEriHMVDNFRPPQPLKGR 256
Cdd:pfam00194 157 PLSDLLPENlRDYYTYPGSLTTPPCSESVTWIVFKEPISISEEQLEKFRTLLFTSGGEP--PLVNNFRPTQPLNGR 230
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
27-262 4.19e-120

Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme V. CA V is the mitochondrial isozyme, which may play a role in gluconeogenesis and ureagenesis and possibly also in lipogenesis.


Pssm-ID: 239392  Cd Length: 236  Bit Score: 342.59  E-value: 4.19e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  27 GDRQSPINIISSQAVYSPSLQPLELFYEACMSLSITNNGHSVQVDFNDSDDRTVVSGGPLEGPYRLKQLHFHWGKKRDMG 106
Cdd:cd03118   1 GTRQSPINIQWRDSVYDPQLAPLRVSYDPATCLYIWNNGYSFQVEFDDSTDKSGISGGPLENHYRLKQFHFHWGANNEWG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 107 SEHTVDGKSFPSELHLVHWNAKKYSTFGEAAAAPDGLAVVGVFLETGDEHPSMNRLTDALYMVRFKDTKAQFSCFNPKCL 186
Cdd:cd03118  81 SEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHHEGLQKLVDALPEVRHKDTVVEFNPFDPSCL 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28269695 187 LPTSRHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDERIHMVDNFRPPQPLKGRVVKASF 262
Cdd:cd03118 161 LPACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLFTSRGEEEKVMVNNFRPLQPLMNRKVRSSF 236
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
27-258 4.91e-117

Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues and a fourth conserved histidine plays a potential role in proton transfer.


Pssm-ID: 238200  Cd Length: 227  Bit Score: 334.25  E-value: 4.91e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  27 GDRQSPINIISSQAVYSPSLQPLELFYEACMSLSITNNGHSVQVDFNDsdDRTVVSGGPLEGPYRLKQLHFHWGKKRDMG 106
Cdd:cd00326   1 GKRQSPINIVTSAVVYDPSLPPLNFDYYPTTSLTLVNNGHTVQVNFDD--DGGTLSGGGLPGRYKLVQFHFHWGSENSPG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 107 SEHTVDGKSFPSELHLVHWNAKKYSTfgEAAAAPDGLAVVGVFLETGD-EHPSMNRLTDALYMVRFKDTKAQFSCFNPKC 185
Cdd:cd00326  79 SEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEkENPFLKKILDALPKIKYKGKETTLPPFDLSD 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28269695 186 LLPTS-RHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDderiHMVDNFRPPQPLKGRVV 258
Cdd:cd00326 157 LLPSSlRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDREGK----PLVNNYRPVQPLNGRVV 226
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
14-262 8.62e-83

Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Alpha CAs are mostly monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the secreted CA VI, which is found in saliva, for example, and the membrane proteins CA IX, XII, and XIV.


Pssm-ID: 239397 [Multi-domain]  Cd Length: 248  Bit Score: 248.38  E-value: 8.62e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  14 GPSNWHKLYPIAQGDRQSPINIISSQAVYSPSLQPLELF-YE--ACMSLSITNNGHSVQVDFNDsddrTVVSGGPLEGPY 90
Cdd:cd03123   1 GEDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVgYDlpGTEEFTLTNNGHTVQLSLPP----TMHIRGGPGTEY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  91 RLKQLHFHWGKKRDM-GSEHTVDGKSFPSELHLVHWNAKKYSTFGEAAAAPDGLAVVGVFLETGD-EHPSMNRLTDALYM 168
Cdd:cd03123  77 TAAQLHLHWGGRGSLsGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYpENTYYEKIISHLHE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 169 VRFKDTKAQFSCFNPKCLLPTS-RHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDErihMVDNF 247
Cdd:cd03123 157 IKYKGQETTVPGFNVRELLPEDlSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLETLENTLMDTHNKT---LQNNY 233
                       250
                ....*....|....*
gi 28269695 248 RPPQPLKGRVVKASF 262
Cdd:cd03123 234 RATQPLNGRVVEASF 248
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
27-260 1.20e-80

Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This subgroup, restricted to animals, contains isozyme IV and similar proteins such as mouse CA XV. Isozymes IV is attached to membranes via a glycosylphosphatidylinositol (GPI) tail. In mammals, Isozyme IV plays crucial roles in kidney and lung function, amongst others. This subgroup also contains the dual domain CA from the giant clam, Tridacna gigas. T. gigas CA plays a role in the movement of inorganic carbon from the surrounding seawater to the symbiotic algae found in the clam's tissues. CA XV is expressed in several species but not in humans or chimps. Similar to isozyme CA IV, CA XV attaches to membranes via a GPI tail.


Pssm-ID: 239391  Cd Length: 234  Bit Score: 242.18  E-value: 1.20e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  27 GDRQSPINIISSQAVYSPSLQPLEL--FYEACMSLSITNNGHSVQVDFNDsddRTVVSGGPLEGPYRLKQLHFHWGKKRD 104
Cdd:cd03117   1 GKRQSPINIVTKKVQYDENLTPFTFtgYDDTTTNWTITNNGHTVQVTLPD---GAKISGGGLPGTYKALQFHFHWGSNGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 105 MGSEHTVDGKSFPSELHLVHWNAKKYSTfGEAAAAPDGLAVVGVFLETGDEHP-SMNRLTDALYMVRFKDTKAQFSCFNP 183
Cdd:cd03117  78 PGSEHTIDGERYPMELHIVHIKESYNSL-LEALKDSDGLAVLGFFIEEGEEENtNFDPLISALSNIPQKGGSTNLTPFSL 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28269695 184 KCLLPT--SRHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDERiHMVDNFRPPQPLKGRVVKA 260
Cdd:cd03117 157 RSLLPSvlLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNGQ-PMVNNFRPVQPLNGRVVYA 234
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
18-262 3.20e-79

Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. CARP VIII may play roles in various biological processes of the central nervous system, and could be involved in protein-protein interactions. CARP VIII has been shown to bind inositol 1,4,5-triphosphate (IP3) receptor type I (IP3RI), reducing the affinity of the receptor for IP3. IP3RI is an intracellular IP3-gated Ca2+ channel located on intracellular Ca2+ stores. IP3RI converts IP3 signaling into Ca2+ signaling thereby participating in a variety of cell functions.


Pssm-ID: 239394  Cd Length: 256  Bit Score: 239.37  E-value: 3.20e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  18 WHKLYPIAQGDRQSPINIISSQAVYSPSLQ--PLELFYEACMSLSITNNGHSVQVDFNDsddRTVVSGGPL--EGPYRLK 93
Cdd:cd03120   4 WGLLFPEANGEYQSPINLNSREARYDPSLLevRLSPNYVVCRDCEVINDGHTIQIILKS---KSVLSGGPLpqGHEFELA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  94 QLHFHWGKKRDMGSEHTVDGKSFPSELHLVHWNAKKYSTFGEAAAAPDGLAVVGVFLETGDEHPSMNRLTDALYMVRFKD 173
Cdd:cd03120  81 EVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIGKEHVGLKAVTEILQDIQYKG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 174 TKAQFSCFNPKCLLPTS--RHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDERIH-----MVDN 246
Cdd:cd03120 161 KSKTIPCFNPNTLLPDPllRDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLRTHVKGAELVEgcdglLGDN 240
                       250
                ....*....|....*.
gi 28269695 247 FRPPQPLKGRVVKASF 262
Cdd:cd03120 241 FRPTQPLSDRVIRAAF 256
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
14-259 1.47e-73

Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup contains carbonic anhydrase related proteins (CARPs) X and XI, which have been implicated in various biological processes of the central nervous system. CARPs are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. CARP XI plays a role in the development of gastrointestinal stromal tumors.


Pssm-ID: 239395 [Multi-domain]  Cd Length: 256  Bit Score: 224.98  E-value: 1.47e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  14 GPSNWHKLYP----IAQGDRQSPINIISSQAVYSPSLQPLELFYEACMSLSITNNGHSVQVdFNDSDDRTVVSGGPLEGP 89
Cdd:cd03121   1 GPSFWGLVNSawnlCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGTFYNTGRHVSF-RPDKDPVVNISGGPLSYR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  90 YRLKQLHFHWGKKRDMGSEHTVDGKSFPSELHLVHWNAKKYSTFGEAAAAPDGLAVVGVFLETGDE-HPSMNRLT--DAL 166
Cdd:cd03121  80 YRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETsNPELRRLTnrDTI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 167 YMVRFKDTKAQFSCFNPKCLLPTSRHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDERIHMVDN 246
Cdd:cd03121 160 TSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEKAPMSPN 239
                       250
                ....*....|...
gi 28269695 247 FRPPQPLKGRVVK 259
Cdd:cd03121 240 FRPVQPLNNRPVR 252
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
14-262 1.14e-72

Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the membrane proteins CA XII and XIV.


Pssm-ID: 239400  Cd Length: 249  Bit Score: 222.79  E-value: 1.14e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  14 GPSNWHKLYPIAQGDRQSPINIISSQAVYSPSLQPLELF-YE--ACMSLSITNNGHSVQVDFNDSddrTVVSGGPLEgpY 90
Cdd:cd03126   1 GENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHgYNvsGTEQFTLTNNGHTVQLSLPPT---MHIGGLPFK--Y 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  91 RLKQLHFHWGKKRDM-GSEHTVDGKSFPSELHLVHWNAKKYSTFGEAAAAPDGLAVVGVFLETGDEHPSMNRLTDALYMV 169
Cdd:cd03126  76 TASQLHLHWGQRGSPeGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVGPFNPSYEKIFSHLHEV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 170 RFKDTKAQFSCFNPKCLLPTS-RHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDDERIHMVDNFR 248
Cdd:cd03126 156 KYKDQKVSVPGFNVQELLPKRlDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALETALYSTEEDESREMVNNYR 235
                       250
                ....*....|....
gi 28269695 249 PPQPLKGRVVKASF 262
Cdd:cd03126 236 QVQPFNERLVFASF 249
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
14-258 2.00e-71

Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This sub-family includes bacterial carbonic anhydrase alpha, as well as plant enzymes such as tobacco nectarin III and yam dioscorin and, carbonic anhydrases from molluscs, such as nacrein, which are part of the organic matrix layer in shells. Other members of this family may be involved in maintaining pH balance, in facilitating transport of carbon dioxide or carbonic acid, or in sensing carbon dioxide levels in the environment. Dioscorin is the major storage protein of yam tubers and may play a role as an antioxidant. Tobacco Nectarin may play a role in the maintenace of pH and oxidative balance in nectar. Mollusc nacrein may participate in calcium carbonate crystal formation of the nacreous layer. This subfamily also includes three alpha carbonic anhydrases from Chlamydomonas reinhardtii (CAH 1-3). CAHs1-2 are localized in the periplasmic space. CAH1 faciliates the movement of carbon dioxide across the plasma membrane when the medium is alkaline. CAH3 is localized to the thylakoid lumen and provides CO2 to Rubisco.


Pssm-ID: 239398 [Multi-domain]  Cd Length: 216  Bit Score: 218.29  E-value: 2.00e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  14 GPSNWHKLYPI----AQGDRQSPINIISSQAVYSpSLQPLELFYEaCMSLSITNNGHSVQVDFNDSDDRTVVSGGPlegp 89
Cdd:cd03124   1 GPEHWGNLDPEfalcATGKNQSPIDITTKAVVSD-KLPPLNYNYK-PTSATLVNNGHTIQVNFEGNGGTLTIDGET---- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  90 YRLKQLHFHwgkkrdMGSEHTVDGKSFPSELHLVHWNAKKystfgeaaaapdGLAVVGVFLETGDEHPSMNRLTDAlyMV 169
Cdd:cd03124  75 YQLLQFHFH------SPSEHLINGKRYPLEAHLVHKSKDG------------QLAVVAVLFEEGKENPFLKKILDN--MP 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 170 RFKDTKAQ-FSCFNPKCLLPTSRHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTsedderihmvDNFR 248
Cdd:cd03124 135 KKEGTEVNlPAILDPNELLPESRSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAAVYP----------NNAR 204
                       250
                ....*....|
gi 28269695 249 PPQPLKGRVV 258
Cdd:cd03124 205 PVQPLNGREV 214
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
14-263 2.37e-62

Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the secreted CA VI, which is found in saliva.


Pssm-ID: 239399  Cd Length: 249  Bit Score: 196.16  E-value: 2.37e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  14 GPSNWHKLYPIAQGDRQSPINIISSQAVYSPSLQPLELF-YEA-CMSLSITNNGHSVQVDFNDsddrTVVSGGPLEGPYR 91
Cdd:cd03125   1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVgYEKeQGEFTMTNNGHTVQIDLPP----TMSITTGDGTVYT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  92 LKQLHFHWGKkRDM---GSEHTVDGKSFPSELHLVHWNaKKYSTFGEAAAAPDGLAVVGVFLETGD--EHPSMNRLTDAL 166
Cdd:cd03125  77 AVQMHFHWGG-RDSeisGSEHTIDGMRYVAELHIVHYN-SKYKSYEEAKDKPDGLAVLAFLYKVGHyaENTYYSDFISKL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 167 YMVRFKDTKAQFSCFNPKCLLPTS-RHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFtSEDDERIHmvD 245
Cdd:cd03125 155 AKIKYAGQTTTLTSLDVRDMLPENlHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLENTLM-DHHNKTIR--N 231
                       250
                ....*....|....*...
gi 28269695 246 NFRPPQPLKGRVVKASFQ 263
Cdd:cd03125 232 DYRRTQPLNHRVVEANFL 249
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
14-258 2.46e-60

Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. This sub-family of carbonic anhydrase-related domains found in tyrosine phosphatase receptors may play a role in cell adhesion.


Pssm-ID: 239396 [Multi-domain]  Cd Length: 253  Bit Score: 191.03  E-value: 2.46e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  14 GPSNWHKLYP-IAQGDRQSPINIISSQAVYSPSLQPLEL--FYEACMSLSITNNGHSVQVDFNDSDDRTVVSGGPLEGPY 90
Cdd:cd03122   1 NPKHWAKKYPaCGEGRQQSPIDIVEDTQVQRQGLQPLHFdgYEELTASTTLENTGKTVILRLEGNSSDPFVSGGPLLGRY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  91 RLKQLHFHWGKKRDMGSEHTVDGKSFPSELHLVHWNAKKYSTFgEAAAAPDGLAVVGVFLETGDEH-PSMNRLTDALYMV 169
Cdd:cd03122  81 KFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDSF-EAIKSPGGVLALAYLFELSHEDnPFLDPIIEGLRNV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 170 RFKDTKAQFSCFNPKCLLPTSR-HYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTSEDD----ERIHmv 244
Cdd:cd03122 160 SRPGKEVELPPFPLSDLLPPFTdKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDGvmsgDYLP-- 237
                       250
                ....*....|....
gi 28269695 245 DNFRPPQPLKGRVV 258
Cdd:cd03122 238 NNGRPQQPLGSRTV 251
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
7-258 4.07e-60

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 225875 [Multi-domain]  Cd Length: 250  Bit Score: 190.72  E-value: 4.07e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695   7 WGYGQDDGPSNWHKLYP----IAQGDRQSPINIisSQAVYSPSLQPLELFYEAcMSLSITNNGHSVQVDFNDSDDRTVVS 82
Cdd:COG3338  28 WGYTGKEGPEHWGELSPdfeaCAEGKNQSPIDI--EHAVDVQDKPPLQLNYQP-SAVTIKNNGHTIQVNFEPGSNHLRYD 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  83 GGPlegpYRLKQLHFHwgkkrdMGSEHTVDGKSFPSELHLVHWNAKkystfgeaaaapDGLAVVGVFLETGDEHPSMNRL 162
Cdd:COG3338 105 GKT----YQLVQFHFH------APSEHLVDGKSFPMEAHFVHKDAK------------GTLAVLAVLLQAGAENPELAPL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 163 TDALyMVRFKDTKAQFSCFNPKCLLPTSRHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLlftsedderih 242
Cdd:COG3338 163 WEGF-PQKPGEEETLDETIDLNAFLPESRNYYTYNGSLTTPPCSEGVTWIVLKEPIEVSQEQIAEFSKL----------- 230
                       250
                ....*....|....*.
gi 28269695 243 MVDNFRPPQPLKGRVV 258
Cdd:COG3338 231 MGHNARPVQPLNDRLI 246
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
18-262 2.25e-59

Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Alpha CAs are strictly monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the membrane protein CA IX. CA IX is functionally implicated in tumor growth and survival. CA IX is mainly present in solid tumors and its expression in normal tissues is limited to the mucosa of alimentary tract. CA IX is a transmembrane protein with two extracellular domains: carbonic anhydrase and, a proteoglycan-like segment mediating cell-cell adhesion. There is evidence for an involvement of the MAPK pathway in the regulation of CA9 expression.


Pssm-ID: 239403  Cd Length: 247  Bit Score: 188.63  E-value: 2.25e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  18 WHKLYPIAQGDRQSPINIISSQAVYSPSLQPLELF-YE--ACMSLSITNNGHSVQVDFNDSddrTVVSGGPlEGPYRLKQ 94
Cdd:cd03150   5 WPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLgFDlpPSPSLRLLNNGHTVQLSLPSG---LRMALGP-GQEYRALQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  95 LHFHWGKKRDMGSEHTVDGKSFPSELHLVHWNAkKYSTFGEAAAAPDGLAVVGVFLETG-DEHPSMNRLTDALYMVRFKD 173
Cdd:cd03150  81 LHLHWGAAGRPGSEHTVDGHRFPAEIHVVHLST-AFANLDEALGRPGGLAVLAAFLAEGlHENSAYEQLLSRLSEISEEE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695 174 TKAQFSCFNPKCLLPTS-RHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTsEDDERIHMvdNFRPPQP 252
Cdd:cd03150 160 SETVVPGLDVSALLPSDlSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWG-PHDSRLQL--NFRATQP 236
                       250
                ....*....|
gi 28269695 253 LKGRVVKASF 262
Cdd:cd03150 237 LNGRKIEASF 246
PLN02202 PLN02202
carbonate dehydratase
7-259 2.66e-23

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 95.89  E-value: 2.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695    7 WGYGQDDGPSNWHKLYP----IAQGDRQSPINIISSQAVYSPSLQPLELFYeACMSLSITNNGHSVQVDFNDSDDRTVVS 82
Cdd:PLN02202  31 FGYKGKNGPNQWGHLNPhftkCAVGKLQSPIDIQRRQIFYNHKLESIHRDY-YFTNATLVNHVCNVAMFFGEGAGDVIID 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695   83 ggplEGPYRLKQLHFHwgkkrdMGSEHTVDGKSFPSELHLVHwnakkystfgeaaAAPDG-LAVVGVFLETGDEHPSMNR 161
Cdd:PLN02202 110 ----NKNYTLLQMHWH------TPSEHHLHGVQYAAELHMVH-------------QAKDGsFAVVASLFKIGTEEPFLSQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695  162 LTDALYMV---RFKDT---KAQFSCFNPKCLLPTSRHYWTYPGSLTTPPLSESVTWIVLREPIRISERQMEKFRSLLFTS 235
Cdd:PLN02202 167 MKDKLVKLkeeRFKGNhtaQVEVGKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPLDKS 246
                        250       260
                 ....*....|....*....|....
gi 28269695  236 edderihMVDNFRPPQPLKGRVVK 259
Cdd:PLN02202 247 -------FKNNSRPCQPLNGRRVE 263
PLN02179 PLN02179
carbonic anhydrase
12-215 1.04e-17

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 79.64  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695   12 DDGPSNWHKLYP----IAQGDRQSPINIiSSQAVYSPSLQPLELFYEACMSLsITNNGHSVQVDFNDSDDRTVVSggplE 87
Cdd:PLN02179  44 EKGPAEWGKLNPqwkvCSTGKYQSPIDL-TDERVSLIHDQALSRHYKPAPAV-IQSRGHDVMVSWKGDAGKITIH----Q 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28269695   88 GPYRLKQLHFHwgkkrdMGSEHTVDGKSFPSELHLVHWNAKKYStfgeaaaapdglAVVGVFLETGDEHPSMNRLTDALY 167
Cdd:PLN02179 118 TDYKLVQCHWH------SPSEHTINGTSYDLELHMVHTSASGKT------------AVVGVLYKLGEPDEFLTKLLNGIK 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 28269695  168 MVRFKDTkaQFSCFNPKCLLPTSRHYWTYPGSLTTPPLSESVTWIVLR 215
Cdd:PLN02179 180 GVGKKEI--NLGIVDPRDIRFETNNFYRYIGSLTIPPCTEGVIWTVVK 225
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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