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Conserved domains on  [gi|634743300|ref|NP_001278896|]
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carbonic anhydrase 1 isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
alpha_CA super family cl00012
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 9-195 1.80e-132

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.


The actual alignment was detected with superfamily member cd03119:

Pssm-ID: 469577 [Multi-domain]  Cd Length: 259  Bit Score: 371.77  E-value: 1.80e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300   9 DDKNVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMKVGEA 88
Cdd:cd03119   74 DDRSVLRGGPLTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVGEA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  89 NPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNV 168
Cdd:cd03119  153 NPELQKVLDALDSIKTKGKQAPFTNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNA 232

                        170       180
                 ....*....|....*....|....*..
gi 634743300 169 EGDNAVPMQHNNRPTQPLKGRTVRASF 195
Cdd:cd03119  233 EGEPPCPMVDNWRPPQPLKGRKVRASF 259
 
Name Accession Description Interval E-value
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
 9-195 1.80e-132

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: 371.77  E-value: 1.80e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300   9 DDKNVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMKVGEA 88
Cdd:cd03119   74 DDRSVLRGGPLTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVGEA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  89 NPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNV 168
Cdd:cd03119  153 NPELQKVLDALDSIKTKGKQAPFTNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNA 232

                        170       180
                 ....*....|....*....|....*..
gi 634743300 169 EGDNAVPMQHNNRPTQPLKGRTVRASF 195
Cdd:cd03119  233 EGEPPCPMVDNWRPPQPLKGRKVRASF 259
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
5-195 2.28e-98

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 284.93  E-value: 2.28e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300    5 DWGYDDKNVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMK 84
Cdd:pfam00194  61 SLDDGDPSTISGGPLATRYRLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNS-KYKSFDEAAKHPDGLAVLGVFFE 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300   85 VG-EANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSL-DFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFR 162
Cdd:pfam00194 140 VGdENNPYLQPIVSALDNIKYKGKSVLLPPFDLSDLLPEDLtSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFR 219

                         170       180       190
                  ....*....|....*....|....*....|...
gi 634743300  163 SLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF 195
Cdd:pfam00194 220 TLLFSDGGEEPRPLVNNFRPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 9-190 1.16e-86

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: 255.32  E-value: 1.16e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300     9 DDKNVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKysSLAEAASKADGLAVIGVLMKVG-E 87
Cdd:smart01057  69 DDGSTLSGGPLPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGaE 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300    88 ANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSL-DFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLS 166
Cdd:smart01057 147 ENPALQAILDHLPLIKYKGQETELTPFDLSSLLPASTrHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLP 226

                          170       180
                   ....*....|....*....|....
gi 634743300   167 NVEGDnavPMQHNNRPTQPLKGRT 190
Cdd:smart01057 227 MEGNE---PLVNNARPLQPLNGRV 247
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
23-194 1.50e-50

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 163.52  E-value: 1.50e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  23 YRLFQFHFHwgstneHGSEHTVDGVKYSAELHVAHwnsakysslaeaASKADGLAVIGVLMKVGEANPKLQKVLDALQAi 102
Cdd:COG3338  106 YELKQFHFH------TPSEHTINGKSYPMEAHLVH------------KDADGELAVVGVLFEEGAENPALAKLWANLPL- 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300 103 KTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLlsnvegdnavpMQHNNRP 182
Cdd:COG3338  167 EAGEEVALDATIDLNDLLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARL-----------YPNNARP 235

                        170
                 ....*....|..
gi 634743300 183 TQPLKGRTVRAS 194
Cdd:COG3338  236 VQPLNGRLILES 247
PLN02202 PLN02202
carbonate dehydratase
 22-191 9.24e-18

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 78.95  E-value: 9.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  22 SYRLFQFHFHwgstneHGSEHTVDGVKYSAELHVAHwnsakysslaeaASKADGLAVIGVLMKVGEANPKLQKVLDALQA 101
Cdd:PLN02202 112 NYTLLQMHWH------TPSEHHLHGVQYAAELHMVH------------QAKDGSFAVVASLFKIGTEEPFLSQMKDKLVK 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300 102 IKTKGKRAPFT------NFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNvegdnavP 175
Cdd:PLN02202 174 LKEERFKGNHTaqvevgKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPLDK-------S 246

                        170
                 ....*....|....*.
gi 634743300 176 MQHNNRPTQPLKGRTV 191
Cdd:PLN02202 247 FKNNSRPCQPLNGRRV 262
 
Name Accession Description Interval E-value
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
 9-195 1.80e-132

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: 371.77  E-value: 1.80e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300   9 DDKNVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMKVGEA 88
Cdd:cd03119   74 DDRSVLRGGPLTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVGEA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  89 NPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNV 168
Cdd:cd03119  153 NPELQKVLDALDSIKTKGKQAPFTNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNA 232

                        170       180
                 ....*....|....*....|....*..
gi 634743300 169 EGDNAVPMQHNNRPTQPLKGRTVRASF 195
Cdd:cd03119  233 EGEPPCPMVDNWRPPQPLKGRKVRASF 259
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
5-195 2.28e-98

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 284.93  E-value: 2.28e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300    5 DWGYDDKNVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMK 84
Cdd:pfam00194  61 SLDDGDPSTISGGPLATRYRLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNS-KYKSFDEAAKHPDGLAVLGVFFE 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300   85 VG-EANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSL-DFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFR 162
Cdd:pfam00194 140 VGdENNPYLQPIVSALDNIKYKGKSVLLPPFDLSDLLPEDLtSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFR 219

                         170       180       190
                  ....*....|....*....|....*....|...
gi 634743300  163 SLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF 195
Cdd:pfam00194 220 TLLFSDGGEEPRPLVNNFRPTQPLNGRVVFASF 252
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
 8-195 4.49e-97

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: 281.34  E-value: 4.49e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300   8 YDDKNVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGE 87
Cdd:cd03149   49 SDDKTVITGGPLENPYRLKQFHFHWGAKHGSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETGD 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  88 ANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSN 167
Cdd:cd03149  129 EHPGLNRLTDALYMVRFKGTKAQFLDFNPKCLLPKSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFT 208

                        170       180
                 ....*....|....*....|....*...
gi 634743300 168 VEGDNAVPMQHNNRPTQPLKGRTVRASF 195
Cdd:cd03149  209 SEEDQRNHMVNNFRPPQPLKGRTVRASF 236
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 9-192 1.92e-87

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: 256.44  E-value: 1.92e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300   9 DDKNVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSlaEAASKADGLAVIGVLMKVGEA 88
Cdd:cd00326   48 DDGGTLSGGGLPGRYKLVQFHFHWGSENSPGSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEK 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  89 -NPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSL-DFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLS 166
Cdd:cd00326  126 eNPFLKKILDALPKIKYKGKETTLPPFDLSDLLPSSLrDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLD 205

                        170       180
                 ....*....|....*....|....*.
gi 634743300 167 NVEGdnavPMQHNNRPTQPLKGRTVR 192
Cdd:cd00326  206 REGK----PLVNNYRPVQPLNGRVVY 227
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 9-190 1.16e-86

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: 255.32  E-value: 1.16e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300     9 DDKNVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKysSLAEAASKADGLAVIGVLMKVG-E 87
Cdd:smart01057  69 DDGSTLSGGPLPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGaE 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300    88 ANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSL-DFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLS 166
Cdd:smart01057 147 ENPALQAILDHLPLIKYKGQETELTPFDLSSLLPASTrHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLP 226

                          170       180
                   ....*....|....*....|....
gi 634743300   167 NVEGDnavPMQHNNRPTQPLKGRT 190
Cdd:smart01057 227 MEGNE---PLVNNARPLQPLNGRV 247
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
 10-195 6.44e-86

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: 252.84  E-value: 6.44e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  10 DKNVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEAN 89
Cdd:cd03118   51 DKSGISGGPLENHYRLKQFHFHWGANNEWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHH 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  90 PKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVE 169
Cdd:cd03118  131 EGLQKLVDALPEVRHKDTVVEFNPFDPSCLLPACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLFTSR 210

                        170       180
                 ....*....|....*....|....*.
gi 634743300 170 GDNAVPMQHNNRPTQPLKGRTVRASF 195
Cdd:cd03118  211 GEEEKVMVNNFRPLQPLMNRKVRSSF 236
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
 14-195 8.02e-61

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: 189.83  E-value: 8.02e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  14 LKGGPFSDsYRLFQFHFHWGSTNE-HGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEA-NPK 91
Cdd:cd03123   68 IRGGPGTE-YTAAQLHLHWGGRGSlSGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPeNTY 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  92 LQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLD-FWTYPGSLTHPPLYESVTWIICKESISVSSEQLAqfrsLLSN-VE 169
Cdd:cd03123  147 YEKIISHLHEIKYKGQETTVPGFNVRELLPEDLShYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLE----TLENtLM 222

                        170       180
                 ....*....|....*....|....*.
gi 634743300 170 GDNAVPMQHNNRPTQPLKGRTVRASF 195
Cdd:cd03123  223 DTHNKTLQNNYRATQPLNGRVVEASF 248
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
 11-195 2.62e-57

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: 180.82  E-value: 2.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  11 KNVLKGGPF--SDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEA 88
Cdd:cd03120   63 KSVLSGGPLpqGHEFELAEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIGKE 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  89 NPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSL--DFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLS 166
Cdd:cd03120  143 HVGLKAVTEILQDIQYKGKSKTIPCFNPNTLLPDPLlrDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLRT 222

                        170       180       190
                 ....*....|....*....|....*....|....
gi 634743300 167 NVEGDNAVP-----MQHNNRPTQPLKGRTVRASF 195
Cdd:cd03120  223 HVKGAELVEgcdglLGDNFRPTQPLSDRVIRAAF 256
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
 16-192 1.43e-54

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: 174.14  E-value: 1.43e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  16 GGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGE-ANPKLQK 94
Cdd:cd03121   73 GGPLSYRYRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGEtSNPELRR 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  95 VLDALQA--IKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDN 172
Cdd:cd03121  153 LTNRDTItsIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQE 232

                        170       180
                 ....*....|....*....|
gi 634743300 173 AVPMQHNNRPTQPLKGRTVR 192
Cdd:cd03121  233 KAPMSPNFRPVQPLNNRPVR 252
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
 14-191 1.56e-54

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: 173.22  E-value: 1.56e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  14 LKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMKVGE-ANPKL 92
Cdd:cd03117   54 ISGGGLPGTYKALQFHFHWGSNGSPGSEHTIDGERYPMELHIVHIKE-SYNSLLEALKDSDGLAVLGFFIEEGEeENTNF 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  93 QKVLDALQAIKTKGKRAPFTNFDPSTLLPS--SLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLsNVEG 170
Cdd:cd03117  133 DPLISALSNIPQKGGSTNLTPFSLRSLLPSvlLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVL-FFDT 211

                        170       180
                 ....*....|....*....|.
gi 634743300 171 DNAVPMQHNNRPTQPLKGRTV 191
Cdd:cd03117  212 DNGQPMVNNFRPVQPLNGRVV 232
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
 14-195 1.17e-53

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: 171.56  E-value: 1.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  14 LKGGPFSdsYRLFQFHFHWGSTNE-HGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKL 92
Cdd:cd03126   68 IGGLPFK--YTASQLHLHWGQRGSpEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVGPFNPSY 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  93 QKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLD-FWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGD 171
Cdd:cd03126  146 EKIFSHLHEVKYKDQKVSVPGFNVQELLPKRLDeYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALETALYSTEED 225

                        170       180
                 ....*....|....*....|....
gi 634743300 172 NAVPMQHNNRPTQPLKGRTVRASF 195
Cdd:cd03126  226 ESREMVNNYRQVQPFNERLVFASF 249
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
23-194 1.50e-50

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 163.52  E-value: 1.50e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  23 YRLFQFHFHwgstneHGSEHTVDGVKYSAELHVAHwnsakysslaeaASKADGLAVIGVLMKVGEANPKLQKVLDALQAi 102
Cdd:COG3338  106 YELKQFHFH------TPSEHTINGKSYPMEAHLVH------------KDADGELAVVGVLFEEGAENPALAKLWANLPL- 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300 103 KTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLlsnvegdnavpMQHNNRP 182
Cdd:COG3338  167 EAGEEVALDATIDLNDLLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARL-----------YPNNARP 235

                        170
                 ....*....|..
gi 634743300 183 TQPLKGRTVRAS 194
Cdd:COG3338  236 VQPLNGRLILES 247
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
 22-191 8.23e-50

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: 160.51  E-value: 8.23e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  22 SYRLFQFHFHwgstneHGSEHTVDGVKYSAELHVAHwnsakysslaeaASKADGLAVIGVLMKVGEANPKLQKVLDALQA 101
Cdd:cd03124   74 TYQLLQFHFH------SPSEHLINGKRYPLEAHLVH------------KSKDGQLAVVAVLFEEGKENPFLKKILDNMPK 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300 102 IKTKGKRAPfTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNvegdnavpmqHNNR 181
Cdd:cd03124  136 KEGTEVNLP-AILDPNELLPESRSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAAVYP----------NNAR 204

                        170
                 ....*....|
gi 634743300 182 PTQPLKGRTV 191
Cdd:cd03124  205 PVQPLNGREV 214
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 19-195 1.72e-47

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: 155.50  E-value: 1.72e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  19 FSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAkYSSLAEAASKADGLAVIGVLMKVG-EANPKLQKVLD 97
Cdd:cd03150   72 PGQEYRALQLHLHWGAAGRPGSEHTVDGHRFPAEIHVVHLSTA-FANLDEALGRPGGLAVLAAFLAEGlHENSAYEQLLS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  98 ALQAIKTKGKRAPFTNFDPSTLLPSSLD-FWTYPGSLTHPPLYESVTWIICKESISVSSEQLAqfrSLLSNVEGDNAVPM 176
Cdd:cd03150  151 RLSEISEEESETVVPGLDVSALLPSDLSrYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLH---TLSDSLWGPHDSRL 227

                        170
                 ....*....|....*....
gi 634743300 177 QHNNRPTQPLKGRTVRASF 195
Cdd:cd03150  228 QLNFRATQPLNGRKIEASF 246
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 14-191 1.40e-45

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: 150.97  E-value: 1.40e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  14 LKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSlAEAASKADGLAVIGVLMKVG-EANPKL 92
Cdd:cd03122   71 VSGGPLLGRYKFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDS-FEAIKSPGGVLALAYLFELShEDNPFL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  93 QKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLD-FWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLL----SN 167
Cdd:cd03122  150 DPIIEGLRNVSRPGKEVELPPFPLSDLLPPFTDkYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLtrrqDG 229

                        170       180
                 ....*....|....*....|....
gi 634743300 168 VEGDNavPMQHNNRPTQPLKGRTV 191
Cdd:cd03122  230 VMSGD--YLPNNGRPQQPLGSRTV 251
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 23-195 6.04e-42

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: 141.46  E-value: 6.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  23 YRLFQFHFHWG--STNEHGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMKVGEA--NPKLQKVLDA 98
Cdd:cd03125   75 YTAVQMHFHWGgrDSEISGSEHTIDGMRYVAELHIVHYNS-KYKSYEEAKDKPDGLAVLAFLYKVGHYaeNTYYSDFISK 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  99 LQAIKTKGKRAPFTNFDPSTLLPSSLD-FWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLsnvegdnavpMQ 177
Cdd:cd03125  154 LAKIKYAGQTTTLTSLDVRDMLPENLHhYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLENTL----------MD 223

                        170       180
                 ....*....|....*....|....*
gi 634743300 178 HNN-------RPTQPLKGRTVRASF 195
Cdd:cd03125  224 HHNktirndyRRTQPLNHRVVEANF 248
PLN02202 PLN02202
carbonate dehydratase
 22-191 9.24e-18

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 78.95  E-value: 9.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  22 SYRLFQFHFHwgstneHGSEHTVDGVKYSAELHVAHwnsakysslaeaASKADGLAVIGVLMKVGEANPKLQKVLDALQA 101
Cdd:PLN02202 112 NYTLLQMHWH------TPSEHHLHGVQYAAELHMVH------------QAKDGSFAVVASLFKIGTEEPFLSQMKDKLVK 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300 102 IKTKGKRAPFT------NFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNvegdnavP 175
Cdd:PLN02202 174 LKEERFKGNHTaqvevgKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPLDK-------S 246

                        170
                 ....*....|....*.
gi 634743300 176 MQHNNRPTQPLKGRTV 191
Cdd:PLN02202 247 FKNNSRPCQPLNGRRV 262
PLN02179 PLN02179
carbonic anhydrase
 23-148 1.23e-15

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 72.32  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 634743300  23 YRLFQFHFHwgstneHGSEHTVDGVKYSAELHVAHwnsakysslaeaASKADGLAVIGVLMKVGEANPKLQKVLDALQAI 102
Cdd:PLN02179 120 YKLVQCHWH------SPSEHTINGTSYDLELHMVH------------TSASGKTAVVGVLYKLGEPDEFLTKLLNGIKGV 181

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 634743300 103 KTKgkRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICK 148
Cdd:PLN02179 182 GKK--EINLGIVDPRDIRFETNNFYRYIGSLTIPPCTEGVIWTVVK 225
 
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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