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Conserved domains on  [gi|1511945718|ref|NP_001354154|]
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carbonic anhydrase 5A, mitochondrial isoform 2 precursor [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 ...
61-258 4.08e-155

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 cd03118:

Pssm-ID: 469577  Cd Length: 236  Bit Score: 432.73  E-value: 4.08e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIQWRDSVYDPQLKPLRVSYEAASCLYIWNTGYLFQVEFDDATEASGISGGPLENHYRLKQFHFHWGAVNEGG 140
Cdd:cd03118     1 GTRQSPINIQWRDSVYDPQLAPLRVSYDPATCLYIWNNGYSFQVEFDDSTDKSGISGGPLENHYRLKQFHFHWGANNEWG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 141 SEHTVDGHAYPAELHLVHWNSVKYQNYKEAVVGENGLAVIGVFLKLGAHHQTLQRLVDILPEIKHKDARAAMRPFDPSTL 220
Cdd:cd03118    81 SEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHHEGLQKLVDALPEVRHKDTVVEFNPFDPSCL 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1511945718 221 LPTCWDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:cd03118   161 LPACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQ 198
 
Name Accession Description Interval E-value
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
61-258 4.08e-155

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: 432.73  E-value: 4.08e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIQWRDSVYDPQLKPLRVSYEAASCLYIWNTGYLFQVEFDDATEASGISGGPLENHYRLKQFHFHWGAVNEGG 140
Cdd:cd03118     1 GTRQSPINIQWRDSVYDPQLAPLRVSYDPATCLYIWNNGYSFQVEFDDSTDKSGISGGPLENHYRLKQFHFHWGANNEWG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 141 SEHTVDGHAYPAELHLVHWNSVKYQNYKEAVVGENGLAVIGVFLKLGAHHQTLQRLVDILPEIKHKDARAAMRPFDPSTL 220
Cdd:cd03118    81 SEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHHEGLQKLVDALPEVRHKDTVVEFNPFDPSCL 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1511945718 221 LPTCWDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:cd03118   161 LPACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQ 198
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
52-258 7.92e-95

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 280.31  E-value: 7.92e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  52 WTVPVSVPGGTRQSPINIQWRDSVYDPQLKPLRVSY--EAASCLYIWNTGYLFQVEFDDaTEASGISGGPLENHYRLKQF 129
Cdd:pfam00194   6 WGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGydVPPGKNTLTNNGHTVQVSLDD-GDPSTISGGPLATRYRLVQF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 130 HFHWGAVNEGGSEHTVDGHAYPAELHLVHWNSvKYQNYKEAVVGENGLAVIGVFLKLGAHHQT-LQRLVDILPEIKHKDA 208
Cdd:pfam00194  85 HFHWGSTDSRGSEHTIDGKRYPAELHIVHYNS-KYKSFDEAAKHPDGLAVLGVFFEVGDENNPyLQPIVSALDNIKYKGK 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1511945718 209 RAAMRPFDPSTLLPTCW-DYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:pfam00194 164 SVLLPPFDLSDLLPEDLtSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQ 214
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
60-272 9.19e-95

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: 279.97  E-value: 9.19e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718   60 GGTRQSPINIQWRDSVYDPQLKPLRVSYEAASCLYIWNTGYLFQVEFDDATeaSGISGGPLENHYRLKQFHFHWGAVNEG 139
Cdd:smart01057  21 GGKRQSPIDIVTAEAQYDPSLKPLKLSYDQPTAKRILNNGHTVQVNFDDDG--STLSGGPLPGRYRLKQFHFHWGGSDSE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  140 GSEHTVDGHAYPAELHLVHWNSVKyqNYKEAVVGENGLAVIGVFLKLGAHH-QTLQRLVDILPEIKHKDARAAMRPFDPS 218
Cdd:smart01057  99 GSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEEnPALQAILDHLPLIKYKGQETELTPFDLS 176
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  219 TLLPT-CWDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ-----GALCTHQHLCLLKN 272
Cdd:smart01057 177 SLLPAsTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQlekfrTLLPMEGNEPLVNN 236
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
61-258 9.44e-53

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 172.76  E-value: 9.44e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIqwRDSVyDPQLKPLRVSYEAAScLYIWNTGYLFQVEFDdatEASGISggpLENH-YRLKQFHFHwgavneG 139
Cdd:COG3338    52 GKNQSPIDI--RTAI-KADLPPLKFDYKPTP-LEIVNNGHTIQVNVD---PGSTLT---VDGKrYELKQFHFH------T 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 140 GSEHTVDGHAYPAELHLVHWNSvkyqnykeavvgENGLAVIGVFLKLGAHHQTLQRLVDILPEIKHKDARAAmRPFDPST 219
Cdd:COG3338   116 PSEHTINGKSYPMEAHLVHKDA------------DGELAVVGVLFEEGAENPALAKLWANLPLEAGEEVALD-ATIDLND 182
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1511945718 220 LLPTCWDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:COG3338   183 LLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQ 221
PLN02179 PLN02179
carbonic anhydrase
48-249 1.17e-14

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 71.94  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  48 LHPLWTVPVSvpgGTRQSPINI-QWRDSVYDPQlkPLRVSYEAASCLyIWNTGYLFQVEFDDateasgiSGGPLENH--- 123
Cdd:PLN02179   53 LNPQWKVCST---GKYQSPIDLtDERVSLIHDQ--ALSRHYKPAPAV-IQSRGHDVMVSWKG-------DAGKITIHqtd 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 124 YRLKQFHFHwgavneGGSEHTVDGHAYPAELHLVHWNSvkyqnykeavvgENGLAVIGVFLKLGAHHQTLQRLVDILPEI 203
Cdd:PLN02179  120 YKLVQCHWH------SPSEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLGEPDEFLTKLLNGIKGV 181
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1511945718 204 KHKDARAAMrpFDPSTLLPTCWDYWTYAGSLTTPPLTESVTWIIQK 249
Cdd:PLN02179  182 GKKEINLGI--VDPRDIRFETNNFYRYIGSLTIPPCTEGVIWTVVK 225
 
Name Accession Description Interval E-value
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
61-258 4.08e-155

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: 432.73  E-value: 4.08e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIQWRDSVYDPQLKPLRVSYEAASCLYIWNTGYLFQVEFDDATEASGISGGPLENHYRLKQFHFHWGAVNEGG 140
Cdd:cd03118     1 GTRQSPINIQWRDSVYDPQLAPLRVSYDPATCLYIWNNGYSFQVEFDDSTDKSGISGGPLENHYRLKQFHFHWGANNEWG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 141 SEHTVDGHAYPAELHLVHWNSVKYQNYKEAVVGENGLAVIGVFLKLGAHHQTLQRLVDILPEIKHKDARAAMRPFDPSTL 220
Cdd:cd03118    81 SEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHHEGLQKLVDALPEVRHKDTVVEFNPFDPSCL 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1511945718 221 LPTCWDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:cd03118   161 LPACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQ 198
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
61-258 3.69e-95

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: 280.95  E-value: 3.69e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIQWRDSVYDPQLKPLRVSYEAASCLYIWNTGYLFQVEFDDATEASGISGGPLENHYRLKQFHFHWGAVNEGG 140
Cdd:cd03149     1 GNRQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLSISNNGHSVMVEFDDSDDKTVITGGPLENPYRLKQFHFHWGAKHGSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 141 SEHTVDGHAYPAELHLVHWNSVKYQNYKEAVVGENGLAVIGVFLKLGAHHQTLQRLVDILPEIKHKDARAAMRPFDPSTL 220
Cdd:cd03149    81 SEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETGDEHPGLNRLTDALYMVRFKGTKAQFLDFNPKCL 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1511945718 221 LPTCWDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:cd03149   161 LPKSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQ 198
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
52-258 7.92e-95

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 280.31  E-value: 7.92e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  52 WTVPVSVPGGTRQSPINIQWRDSVYDPQLKPLRVSY--EAASCLYIWNTGYLFQVEFDDaTEASGISGGPLENHYRLKQF 129
Cdd:pfam00194   6 WGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGydVPPGKNTLTNNGHTVQVSLDD-GDPSTISGGPLATRYRLVQF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 130 HFHWGAVNEGGSEHTVDGHAYPAELHLVHWNSvKYQNYKEAVVGENGLAVIGVFLKLGAHHQT-LQRLVDILPEIKHKDA 208
Cdd:pfam00194  85 HFHWGSTDSRGSEHTIDGKRYPAELHIVHYNS-KYKSFDEAAKHPDGLAVLGVFFEVGDENNPyLQPIVSALDNIKYKGK 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1511945718 209 RAAMRPFDPSTLLPTCW-DYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:pfam00194 164 SVLLPPFDLSDLLPEDLtSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQ 214
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
60-272 9.19e-95

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: 279.97  E-value: 9.19e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718   60 GGTRQSPINIQWRDSVYDPQLKPLRVSYEAASCLYIWNTGYLFQVEFDDATeaSGISGGPLENHYRLKQFHFHWGAVNEG 139
Cdd:smart01057  21 GGKRQSPIDIVTAEAQYDPSLKPLKLSYDQPTAKRILNNGHTVQVNFDDDG--STLSGGPLPGRYRLKQFHFHWGGSDSE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  140 GSEHTVDGHAYPAELHLVHWNSVKyqNYKEAVVGENGLAVIGVFLKLGAHH-QTLQRLVDILPEIKHKDARAAMRPFDPS 218
Cdd:smart01057  99 GSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEEnPALQAILDHLPLIKYKGQETELTPFDLS 176
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  219 TLLPT-CWDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ-----GALCTHQHLCLLKN 272
Cdd:smart01057 177 SLLPAsTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQlekfrTLLPMEGNEPLVNN 236
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
61-260 2.61e-93

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: 277.01  E-value: 2.61e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIQWRDSVYDPQLKPLRVSYEAASCLYIWNTGYLFQVEFDDATEASGISGGPLENHYRLKQFHFHWGAVNEGG 140
Cdd:cd03119    25 GDRQSPIDIKTKDAKHDPSLKPLSVSYDPATAKTILNNGHSFNVEFDDTDDRSVLRGGPLTGSYRLRQFHFHWGSSDDHG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 141 SEHTVDGHAYPAELHLVHWNSvKYQNYKEAVVGENGLAVIGVFLKLGAHHQTLQRLVDILPEIKHKDARAAMRPFDPSTL 220
Cdd:cd03119   105 SEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVGEANPELQKVLDALDSIKTKGKQAPFTNFDPSCL 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1511945718 221 LPTCWDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQGA 260
Cdd:cd03119   184 LPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMA 223
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
61-258 1.73e-92

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: 273.77  E-value: 1.73e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIQWRDSVYDPQLKPLRVSYEAASCLYIWNTGYLFQVEFDDatEASGISGGPLENHYRLKQFHFHWGAVNEGG 140
Cdd:cd00326     1 GKRQSPINIVTSAVVYDPSLPPLNFDYYPTTSLTLVNNGHTVQVNFDD--DGGTLSGGGLPGRYKLVQFHFHWGSENSPG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 141 SEHTVDGHAYPAELHLVHWNSVKYQNykEAVVGENGLAVIGVFLKLG-AHHQTLQRLVDILPEIKHKDARAAMRPFDPST 219
Cdd:cd00326    79 SEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGeKENPFLKKILDALPKIKYKGKETTLPPFDLSD 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1511945718 220 LLPTC-WDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:cd00326   157 LLPSSlRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQ 196
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
61-258 9.44e-53

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 172.76  E-value: 9.44e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIqwRDSVyDPQLKPLRVSYEAAScLYIWNTGYLFQVEFDdatEASGISggpLENH-YRLKQFHFHwgavneG 139
Cdd:COG3338    52 GKNQSPIDI--RTAI-KADLPPLKFDYKPTP-LEIVNNGHTIQVNVD---PGSTLT---VDGKrYELKQFHFH------T 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 140 GSEHTVDGHAYPAELHLVHWNSvkyqnykeavvgENGLAVIGVFLKLGAHHQTLQRLVDILPEIKHKDARAAmRPFDPST 219
Cdd:COG3338   116 PSEHTINGKSYPMEAHLVHKDA------------DGELAVVGVLFEEGAENPALAKLWANLPLEAGEEVALD-ATIDLND 182
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1511945718 220 LLPTCWDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:COG3338   183 LLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQ 221
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
60-258 2.63e-52

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: 171.72  E-value: 2.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  60 GGTRQSPINIQWRDSVYDPQLKPLR-VSYE--AASCLYIWNTGYLFQVEFDDATEasgISGGPlENHYRLKQFHFHWGAV 136
Cdd:cd03123    13 GGKRQSPIDIQTDIVQFDPSLPPLElVGYDlpGTEEFTLTNNGHTVQLSLPPTMH---IRGGP-GTEYTAAQLHLHWGGR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 137 NE-GGSEHTVDGHAYPAELHLVHWNSVKYQNYKEAVVGENGLAVIGVFLKLGAHHQT-LQRLVDILPEIKHKDARAAMRP 214
Cdd:cd03123    89 GSlSGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTyYEKIISHLHEIKYKGQETTVPG 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1511945718 215 FDPSTLLPTCWD-YWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:cd03123   169 FNVRELLPEDLShYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQ 213
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
61-258 8.55e-52

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: 170.14  E-value: 8.55e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIQWRDSVYDPQLKPLR-VSY-EAASCLYIWNTGYLFQVEFDDATEasgISGGPLENHYRLKQFHFHWGAVNE 138
Cdd:cd03117     1 GKRQSPINIVTKKVQYDENLTPFTfTGYdDTTTNWTITNNGHTVQVTLPDGAK---ISGGGLPGTYKALQFHFHWGSNGS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 139 GGSEHTVDGHAYPAELHLVHWNSvKYQNYKEAVVGENGLAVIGVFLKLGA-HHQTLQRLVDILPEIKHKDARAAMRPFDP 217
Cdd:cd03117    78 PGSEHTIDGERYPMELHIVHIKE-SYNSLLEALKDSDGLAVLGFFIEEGEeENTNFDPLISALSNIPQKGGSTNLTPFSL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1511945718 218 STLLPTcWD---YWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:cd03117   157 RSLLPS-VLltkYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQ 199
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
61-258 2.89e-51

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: 169.27  E-value: 2.89e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIQWRDSVYDPQLKPLRVSYEAASC--LYIWNTGYLFQVEFddaTEASGISGGPL-ENH-YRLKQFHFHWGAV 136
Cdd:cd03120    13 GEYQSPINLNSREARYDPSLLEVRLSPNYVVCrdCEVINDGHTIQIIL---KSKSVLSGGPLpQGHeFELAEVRFHWGRE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 137 NEGGSEHTVDGHAYPAELHLVHWNSVKYQNYKEAVVGENGLAVIGVFLKLGAHHQTLQRLVDILPEIKHKDARAAMRPFD 216
Cdd:cd03120    90 NQRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIGKEHVGLKAVTEILQDIQYKGKSKTIPCFN 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1511945718 217 PSTLL--PTCWDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:cd03120   170 PNTLLpdPLLRDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQ 213
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
61-252 8.52e-50

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: 165.66  E-value: 8.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIQWRDSVYDPQLKPLRVSYEAASCLYIWNTGYLFQVEFDDATEASgISGGPLENHYRLKQFHFHWGAVNEGG 140
Cdd:cd03121    18 GRRQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGTFYNTGRHVSFRPDKDPVVN-ISGGPLSYRYRLEEIRLHFGREDEQG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 141 SEHTVDGHAYPAELHLVHWNSVKYQNYKEAVVGENGLAVIGVFLKLG-AHHQTLQRLV--DILPEIKHKDARAAMRPFDP 217
Cdd:cd03121    97 SEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGeTSNPELRRLTnrDTITSIRYKGDAYFLQDLSI 176
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1511945718 218 STLLPTCWDYWTYAGSLTTPPLTESVTWIIQKEPV 252
Cdd:cd03121   177 ELLLPETDHYITYEGSLTSPGCHETVTWIILNKPI 211
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
61-258 5.16e-49

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: 162.06  E-value: 5.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIQWRDSVYDpQLKPLRVSYEAAScLYIWNTGYLFQVEFDDatEASGISggpLENH-YRLKQFHFHwgavneG 139
Cdd:cd03124    18 GKNQSPIDITTKAVVSD-KLPPLNYNYKPTS-ATLVNNGHTIQVNFEG--NGGTLT---IDGEtYQLLQFHFH------S 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 140 GSEHTVDGHAYPAELHLVHWNSvkyqnykeavvgENGLAVIGVFLKLGAHHQTLQRLVDILPEIKHKDARAAMrPFDPST 219
Cdd:cd03124    85 PSEHLINGKRYPLEAHLVHKSK------------DGQLAVVAVLFEEGKENPFLKKILDNMPKKEGTEVNLPA-ILDPNE 151
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1511945718 220 LLPTCWDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:cd03124   152 LLPESRSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQ 190
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
55-265 1.71e-41

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: 143.82  E-value: 1.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  55 PVSVP--GGTRQSPINIQwRDSV-YDPQLKPLR-VSYE--AASCLYIWNTGYLFQVEFddateASGISGGPLENHYRLKQ 128
Cdd:cd03126     6 PKKYPfcGGVAQSPIDIH-TDILqYDSSLPPLEfHGYNvsGTEQFTLTNNGHTVQLSL-----PPTMHIGGLPFKYTASQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 129 FHFHWGAVNE-GGSEHTVDGHAYPAELHLVHWNSVKYQNYKEAVVGENGLAVIGVFLKLGAHHQTLQRLVDILPEIKHKD 207
Cdd:cd03126    80 LHLHWGQRGSpEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVGPFNPSYEKIFSHLHEVKYKD 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1511945718 208 ARAAMRPFDPSTLLPTCWD-YWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ-----GAL-CTHQ 265
Cdd:cd03126   160 QKVSVPGFNVQELLPKRLDeYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQllaleTALySTEE 224
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
50-258 6.48e-40

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: 139.71  E-value: 6.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  50 PLWTVPVSVPGGTRQSPINIQWRDSVYDPQLKPLRV-SYE--AASCLYIWNTGYLFQVEFDDATEasgISGGPlENHYRL 126
Cdd:cd03150     3 PPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELlGFDlpPSPSLRLLNNGHTVQLSLPSGLR---MALGP-GQEYRA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 127 KQFHFHWGAVNEGGSEHTVDGHAYPAELHLVHWNSvKYQNYKEAVVGENGLAVIGVFLKLGAH-HQTLQRLVDILPEIKH 205
Cdd:cd03150    79 LQLHLHWGAAGRPGSEHTVDGHRFPAEIHVVHLST-AFANLDEALGRPGGLAVLAAFLAEGLHeNSAYEQLLSRLSEISE 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1511945718 206 KDARAAMRPFDPSTLLPTCWD-YWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:cd03150   158 EESETVVPGLDVSALLPSDLSrYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQ 211
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
60-258 6.99e-40

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: 139.54  E-value: 6.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  60 GGTRQSPINIQWRDSVYDPQLKPLRVS-YEA-ASCLYIWNTGYLFQVEFDDATEASGISGGPlenhYRLKQFHFHWGAVN 137
Cdd:cd03125    13 GGKRQSPIDIQRREVRFNPSLLQLELVgYEKeQGEFTMTNNGHTVQIDLPPTMSITTGDGTV----YTAVQMHFHWGGRD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 138 E--GGSEHTVDGHAYPAELHLVHWNSvKYQNYKEAVVGENGLAVIGVFLKLGAHHQT--LQRLVDILPEIKHKDARAAMR 213
Cdd:cd03125    89 SeiSGSEHTIDGMRYVAELHIVHYNS-KYKSYEEAKDKPDGLAVLAFLYKVGHYAENtyYSDFISKLAKIKYAGQTTTLT 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1511945718 214 PFDPSTLLP-TCWDYWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:cd03125   168 SLDVRDMLPeNLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQ 213
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
61-258 1.86e-39

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: 138.64  E-value: 1.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIQWRDSVYDPQLKPLRVSYEAASCLYIW--NTGYLFQVEFDDATEASGISGGPLENHYRLKQFHFHWGAVNE 138
Cdd:cd03122    15 GRQQSPIDIVEDTQVQRQGLQPLHFDGYEELTASTTleNTGKTVILRLEGNSSDPFVSGGPLLGRYKFSEITFHWGTCNS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 139 GGSEHTVDGHAYPAELHLVHWNSvKYQNYKEAVVGENGLAVIGVFLKLG-AHHQTLQRLVDILPEIKHKDARAAMRPFDP 217
Cdd:cd03122    95 DGSEHSIDGHKFPLEMQILHRNT-DFFDSFEAIKSPGGVLALAYLFELShEDNPFLDPIIEGLRNVSRPGKEVELPPFPL 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1511945718 218 STLLPTCWD-YWTYAGSLTTPPLTESVTWIIQKEPVEVAPSQ 258
Cdd:cd03122   174 SDLLPPFTDkYYSYEGSLTTPPCSETVEWIVFREPVPISSRQ 215
PLN02179 PLN02179
carbonic anhydrase
48-249 1.17e-14

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 71.94  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  48 LHPLWTVPVSvpgGTRQSPINI-QWRDSVYDPQlkPLRVSYEAASCLyIWNTGYLFQVEFDDateasgiSGGPLENH--- 123
Cdd:PLN02179   53 LNPQWKVCST---GKYQSPIDLtDERVSLIHDQ--ALSRHYKPAPAV-IQSRGHDVMVSWKG-------DAGKITIHqtd 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 124 YRLKQFHFHwgavneGGSEHTVDGHAYPAELHLVHWNSvkyqnykeavvgENGLAVIGVFLKLGAHHQTLQRLVDILPEI 203
Cdd:PLN02179  120 YKLVQCHWH------SPSEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLGEPDEFLTKLLNGIKGV 181
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1511945718 204 KHKDARAAMrpFDPSTLLPTCWDYWTYAGSLTTPPLTESVTWIIQK 249
Cdd:PLN02179  182 GKKEINLGI--VDPRDIRFETNNFYRYIGSLTIPPCTEGVIWTVVK 225
PLN02202 PLN02202
carbonate dehydratase
61-257 7.09e-12

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 64.69  E-value: 7.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718  61 GTRQSPINIQWRDSVYDPQLKPLRVSY---EAASCLYIWNTGYLFqvefddateASGISGGPLEN-HYRLKQFHFHwgav 136
Cdd:PLN02202   55 GKLQSPIDIQRRQIFYNHKLESIHRDYyftNATLVNHVCNVAMFF---------GEGAGDVIIDNkNYTLLQMHWH---- 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511945718 137 neGGSEHTVDGHAYPAELHLVHWnsvkyqnykeavVGENGLAVIGVFLKLGAHHQTLQRLVDILPEIKHK------DARA 210
Cdd:PLN02202  122 --TPSEHHLHGVQYAAELHMVHQ------------AKDGSFAVVASLFKIGTEEPFLSQMKDKLVKLKEErfkgnhTAQV 187
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1511945718 211 AMRPFDPSTLLPTCWDYWTYAGSLTTPPLTESVTWII-------QKEPVEVAPS 257
Cdd:PLN02202  188 EVGKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTIlgkvrsmSKEQVELLRS 241
 
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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