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Conserved domains on  [gi|157817869|ref|NP_001101130|]
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carbonic anhydrase 1 [Rattus norvegicus]

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 ...
2-261 8.03e-173

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: 476.55  E-value: 8.03e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869   2 ASADWGYDSKNGPDQWSKLYPIANGNNQSPIDIKTSEAKHDSSLKPVSVSYNPATAKEIVNVGHSFHVVFDDSSNQSVLK 81
Cdd:cd03119    1 MSHHWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVSYDPATAKTILNNGHSFNVEFDDTDDRSVLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  82 GGPLADSYRLTQFHFHWGNSNDHGSEHTVDGAKYSGELHLVHWNSaKYSSAAEAISKADGLAIIGVLMKVGPANPNLQKV 161
Cdd:cd03119   81 GGPLTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVGEANPELQKV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 162 LDALSSVKTKGKRAPFTNFDPSSLLPSSLDYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPAVP 241
Cdd:cd03119  160 LDALDSIKTKGKQAPFTNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEPPCP 239
                        250       260
                 ....*....|....*....|
gi 157817869 242 VLSNHRPPQPLKGRTVRASF 261
Cdd:cd03119  240 MVDNWRPPQPLKGRKVRASF 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 ...
2-261 8.03e-173

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: 476.55  E-value: 8.03e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869   2 ASADWGYDSKNGPDQWSKLYPIANGNNQSPIDIKTSEAKHDSSLKPVSVSYNPATAKEIVNVGHSFHVVFDDSSNQSVLK 81
Cdd:cd03119    1 MSHHWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVSYDPATAKTILNNGHSFNVEFDDTDDRSVLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  82 GGPLADSYRLTQFHFHWGNSNDHGSEHTVDGAKYSGELHLVHWNSaKYSSAAEAISKADGLAIIGVLMKVGPANPNLQKV 161
Cdd:cd03119   81 GGPLTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVGEANPELQKV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 162 LDALSSVKTKGKRAPFTNFDPSSLLPSSLDYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPAVP 241
Cdd:cd03119  160 LDALDSIKTKGKQAPFTNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEPPCP 239
                        250       260
                 ....*....|....*....|
gi 157817869 242 VLSNHRPPQPLKGRTVRASF 261
Cdd:cd03119  240 MVDNWRPPQPLKGRKVRASF 259
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
12-261 4.64e-122

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 348.10  E-value: 4.64e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869   12 NGPDQWSKLYPIANGNNQSPIDIKTSEAKHDSSLKPVSVSY--NPATAKEIVNVGHSFHVVFDDSsNQSVLKGGPLADSY 89
Cdd:pfam00194   1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGydVPPGKNTLTNNGHTVQVSLDDG-DPSTISGGPLATRY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869   90 RLTQFHFHWGNSNDHGSEHTVDGAKYSGELHLVHWNSaKYSSAAEAISKADGLAIIGVLMKVGPA-NPNLQKVLDALSSV 168
Cdd:pfam00194  80 RLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNS-KYKSFDEAAKHPDGLAVLGVFFEVGDEnNPYLQPIVSALDNI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  169 KTKGKRAPFTNFDPSSLLPSSL-DYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPAVPVLSNHR 247
Cdd:pfam00194 159 KYKGKSVLLPPFDLSDLLPEDLtSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEPRPLVNNFR 238
                         250
                  ....*....|....
gi 157817869  248 PPQPLKGRTVRASF 261
Cdd:pfam00194 239 PTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
6-256 4.80e-117

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: 335.05  E-value: 4.80e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869     6 WGYDSKNGPDQWSKLYP-IANGNNQSPIDIKTSEAKHDSSLKPVSVSYNPATAKEIVNVGHSFHVVFDDSSnqSVLKGGP 84
Cdd:smart01057   1 WGYEGKNGPEHWGKLDPpFCGGKRQSPIDIVTAEAQYDPSLKPLKLSYDQPTAKRILNNGHTVQVNFDDDG--STLSGGP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869    85 LADSYRLTQFHFHWGNSNDHGSEHTVDGAKYSGELHLVHWNSAKysSAAEAISKADGLAIIGVLMKVGPA-NPNLQKVLD 163
Cdd:smart01057  79 LPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEeNPALQAILD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869   164 ALSSVKTKGKRAPFTNFDPSSLLPSSL-DYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPAVpv 242
Cdd:smart01057 157 HLPLIKYKGQETELTPFDLSSLLPASTrHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEPLV-- 234
                          250
                   ....*....|....
gi 157817869   243 lSNHRPPQPLKGRT 256
Cdd:smart01057 235 -NNARPLQPLNGRV 247
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
2-260 8.09e-71

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 217.83  E-value: 8.09e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869   2 ASADWGYDSKNGPDQWSKLYPI----ANGNNQSPIDIKTSEAKHdssLKPVSVSYNPaTAKEIVNVGHSFHVVFDDSSNQ 77
Cdd:COG3338   24 SAPHWSYEGETGPEHWGELSPEfatcATGKNQSPIDIRTAIKAD---LPPLKFDYKP-TPLEIVNNGHTIQVNVDPGSTL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  78 SVlkGGplaDSYRLTQFHFHwgnsndHGSEHTVDGAKYSGELHLVHwnsakyssaaeaISKADGLAIIGVLMKVGPANPN 157
Cdd:COG3338  100 TV--DG---KRYELKQFHFH------TPSEHTINGKSYPMEAHLVH------------KDADGELAVVGVLFEEGAENPA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 158 LQKVLDALSSVKTKgKRAPFTNFDPSSLLPSSLDYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSsaege 237
Cdd:COG3338  157 LAKLWANLPLEAGE-EVALDATIDLNDLLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARLYP----- 230
                        250       260
                 ....*....|....*....|...
gi 157817869 238 pavpvlSNHRPPQPLKGRTVRAS 260
Cdd:COG3338  231 ------NNARPVQPLNGRLILES 247
PLN02202 PLN02202
carbonate dehydratase
6-257 4.21e-26

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 103.21  E-value: 4.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869   6 WGYDSKNGPDQWSKLYP----IANGNNQSPIDIKTSEAKHDSSLKPVSVSY---NPATAKEIVNVGhsfhVVFDDSSNQS 78
Cdd:PLN02202  31 FGYKGKNGPNQWGHLNPhftkCAVGKLQSPIDIQRRQIFYNHKLESIHRDYyftNATLVNHVCNVA----MFFGEGAGDV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  79 VLKGgplaDSYRLTQFHFHwgnsndHGSEHTVDGAKYSGELHLVHWnsakyssaaeaiSKADGLAIIGVLMKVGPANPNL 158
Cdd:PLN02202 107 IIDN----KNYTLLQMHWH------TPSEHHLHGVQYAAELHMVHQ------------AKDGSFAVVASLFKIGTEEPFL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 159 QKVLDALSSVKTKGKRAPFT------NFDPSSLLPSSLDYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLS 232
Cdd:PLN02202 165 SQMKDKLVKLKEERFKGNHTaqvevgKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPLD 244
                        250       260
                 ....*....|....*....|....*
gi 157817869 233 SAegepavpVLSNHRPPQPLKGRTV 257
Cdd:PLN02202 245 KS-------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 ...
2-261 8.03e-173

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: 476.55  E-value: 8.03e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869   2 ASADWGYDSKNGPDQWSKLYPIANGNNQSPIDIKTSEAKHDSSLKPVSVSYNPATAKEIVNVGHSFHVVFDDSSNQSVLK 81
Cdd:cd03119    1 MSHHWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVSYDPATAKTILNNGHSFNVEFDDTDDRSVLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  82 GGPLADSYRLTQFHFHWGNSNDHGSEHTVDGAKYSGELHLVHWNSaKYSSAAEAISKADGLAIIGVLMKVGPANPNLQKV 161
Cdd:cd03119   81 GGPLTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVGEANPELQKV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 162 LDALSSVKTKGKRAPFTNFDPSSLLPSSLDYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPAVP 241
Cdd:cd03119  160 LDALDSIKTKGKQAPFTNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEPPCP 239
                        250       260
                 ....*....|....*....|
gi 157817869 242 VLSNHRPPQPLKGRTVRASF 261
Cdd:cd03119  240 MVDNWRPPQPLKGRKVRASF 259
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
12-261 4.64e-122

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 348.10  E-value: 4.64e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869   12 NGPDQWSKLYPIANGNNQSPIDIKTSEAKHDSSLKPVSVSY--NPATAKEIVNVGHSFHVVFDDSsNQSVLKGGPLADSY 89
Cdd:pfam00194   1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGydVPPGKNTLTNNGHTVQVSLDDG-DPSTISGGPLATRY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869   90 RLTQFHFHWGNSNDHGSEHTVDGAKYSGELHLVHWNSaKYSSAAEAISKADGLAIIGVLMKVGPA-NPNLQKVLDALSSV 168
Cdd:pfam00194  80 RLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNS-KYKSFDEAAKHPDGLAVLGVFFEVGDEnNPYLQPIVSALDNI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  169 KTKGKRAPFTNFDPSSLLPSSL-DYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPAVPVLSNHR 247
Cdd:pfam00194 159 KYKGKSVLLPPFDLSDLLPEDLtSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEPRPLVNNFR 238
                         250
                  ....*....|....
gi 157817869  248 PPQPLKGRTVRASF 261
Cdd:pfam00194 239 PTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
6-256 4.80e-117

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: 335.05  E-value: 4.80e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869     6 WGYDSKNGPDQWSKLYP-IANGNNQSPIDIKTSEAKHDSSLKPVSVSYNPATAKEIVNVGHSFHVVFDDSSnqSVLKGGP 84
Cdd:smart01057   1 WGYEGKNGPEHWGKLDPpFCGGKRQSPIDIVTAEAQYDPSLKPLKLSYDQPTAKRILNNGHTVQVNFDDDG--STLSGGP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869    85 LADSYRLTQFHFHWGNSNDHGSEHTVDGAKYSGELHLVHWNSAKysSAAEAISKADGLAIIGVLMKVGPA-NPNLQKVLD 163
Cdd:smart01057  79 LPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEeNPALQAILD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869   164 ALSSVKTKGKRAPFTNFDPSSLLPSSL-DYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPAVpv 242
Cdd:smart01057 157 HLPLIKYKGQETELTPFDLSSLLPASTrHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEPLV-- 234
                          250
                   ....*....|....
gi 157817869   243 lSNHRPPQPLKGRT 256
Cdd:smart01057 235 -NNARPLQPLNGRV 247
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
26-261 6.91e-114

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: 326.79  E-value: 6.91e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  26 GNNQSPIDIKTSEAKHDSSLKPVSVSYNPATAKEIVNVGHSFHVVFDDSSNQSVLKGGPLADSYRLTQFHFHWGNSNDHG 105
Cdd:cd03149    1 GNRQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLSISNNGHSVMVEFDDSDDKTVITGGPLENPYRLKQFHFHWGAKHGSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 106 SEHTVDGAKYSGELHLVHWNSAKYSSAAEAISKADGLAIIGVLMKVGPANPNLQKVLDALSSVKTKGKRAPFTNFDPSSL 185
Cdd:cd03149   81 SEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETGDEHPGLNRLTDALYMVRFKGTKAQFLDFNPKCL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157817869 186 LPSSLDYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPAVPVLSNHRPPQPLKGRTVRASF 261
Cdd:cd03149  161 LPKSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHMVNNFRPPQPLKGRTVRASF 236
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
26-261 2.38e-104

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: 302.53  E-value: 2.38e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  26 GNNQSPIDIKTSEAKHDSSLKPVSVSYNPATAKEIVNVGHSFHVVFDDSSNQSVLKGGPLADSYRLTQFHFHWGNSNDHG 105
Cdd:cd03118    1 GTRQSPINIQWRDSVYDPQLAPLRVSYDPATCLYIWNNGYSFQVEFDDSTDKSGISGGPLENHYRLKQFHFHWGANNEWG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 106 SEHTVDGAKYSGELHLVHWNSAKYSSAAEAISKADGLAIIGVLMKVGPANPNLQKVLDALSSVKTKGKRAPFTNFDPSSL 185
Cdd:cd03118   81 SEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHHEGLQKLVDALPEVRHKDTVVEFNPFDPSCL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157817869 186 LPSSLDYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPAVPVLSNHRPPQPLKGRTVRASF 261
Cdd:cd03118  161 LPACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLFTSRGEEEKVMVNNFRPLQPLMNRKVRSSF 236
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
26-258 3.43e-103

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: 299.20  E-value: 3.43e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  26 GNNQSPIDIKTSEAKHDSSLKPVSVSYNPATAKEIVNVGHSFHVVFDDssNQSVLKGGPLADSYRLTQFHFHWGNSNDHG 105
Cdd:cd00326    1 GKRQSPINIVTSAVVYDPSLPPLNFDYYPTTSLTLVNNGHTVQVNFDD--DGGTLSGGGLPGRYKLVQFHFHWGSENSPG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 106 SEHTVDGAKYSGELHLVHWNSAKYSSaaEAISKADGLAIIGVLMKVGPA-NPNLQKVLDALSSVKTKGKRAPFTNFDPSS 184
Cdd:cd00326   79 SEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKeNPFLKKILDALPKIKYKGKETTLPPFDLSD 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157817869 185 LLPSSL-DYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGepavPVLSNHRPPQPLKGRTVR 258
Cdd:cd00326  157 LLPSSLrDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDREGK----PLVNNYRPVQPLNGRVVY 227
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
13-261 5.19e-72

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: 220.64  E-value: 5.19e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  13 GPDQWSKLYPIANGNNQSPIDIKTSEAKHDSSLKPVS-VSYNPATAKE--IVNVGHSFHVvfdDSSNQSVLKGGPlADSY 89
Cdd:cd03123    1 GEDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLElVGYDLPGTEEftLTNNGHTVQL---SLPPTMHIRGGP-GTEY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  90 RLTQFHFHWGNSND-HGSEHTVDGAKYSGELHLVHWNSAKYSSAAEAISKADGLAIIGVLMKVGPA-NPNLQKVLDALSS 167
Cdd:cd03123   77 TAAQLHLHWGGRGSlSGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPeNTYYEKIISHLHE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 168 VKTKGKRAPFTNFDPSSLLPSSLD-YWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPAVpvlSNH 246
Cdd:cd03123  157 IKYKGQETTVPGFNVRELLPEDLShYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLETLENTLMDTHNKTLQ---NNY 233
                        250
                 ....*....|....*
gi 157817869 247 RPPQPLKGRTVRASF 261
Cdd:cd03123  234 RATQPLNGRVVEASF 248
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
2-260 8.09e-71

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 217.83  E-value: 8.09e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869   2 ASADWGYDSKNGPDQWSKLYPI----ANGNNQSPIDIKTSEAKHdssLKPVSVSYNPaTAKEIVNVGHSFHVVFDDSSNQ 77
Cdd:COG3338   24 SAPHWSYEGETGPEHWGELSPEfatcATGKNQSPIDIRTAIKAD---LPPLKFDYKP-TPLEIVNNGHTIQVNVDPGSTL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  78 SVlkGGplaDSYRLTQFHFHwgnsndHGSEHTVDGAKYSGELHLVHwnsakyssaaeaISKADGLAIIGVLMKVGPANPN 157
Cdd:COG3338  100 TV--DG---KRYELKQFHFH------TPSEHTINGKSYPMEAHLVH------------KDADGELAVVGVLFEEGAENPA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 158 LQKVLDALSSVKTKgKRAPFTNFDPSSLLPSSLDYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSsaege 237
Cdd:COG3338  157 LAKLWANLPLEAGE-EVALDATIDLNDLLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARLYP----- 230
                        250       260
                 ....*....|....*....|...
gi 157817869 238 pavpvlSNHRPPQPLKGRTVRAS 260
Cdd:COG3338  231 ------NNARPVQPLNGRLILES 247
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
13-261 1.78e-68

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: 212.00  E-value: 1.78e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  13 GPDQWSKLYPIANGNNQSPIDIKTSEAKHDSSLKPVS-VSYNPATAKE--IVNVGHSFHVvfddsSNQSVLKGGPLADSY 89
Cdd:cd03126    1 GENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEfHGYNVSGTEQftLTNNGHTVQL-----SLPPTMHIGGLPFKY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  90 RLTQFHFHWGNSND-HGSEHTVDGAKYSGELHLVHWNSAKYSSAAEAISKADGLAIIGVLMKVGPANPNLQKVLDALSSV 168
Cdd:cd03126   76 TASQLHLHWGQRGSpEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVGPFNPSYEKIFSHLHEV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 169 KTKGKRAPFTNFDPSSLLPSSLD-YWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPAVPVLSNHR 247
Cdd:cd03126  156 KYKDQKVSVPGFNVQELLPKRLDeYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALETALYSTEEDESREMVNNYR 235
                        250
                 ....*....|....
gi 157817869 248 PPQPLKGRTVRASF 261
Cdd:cd03126  236 QVQPFNERLVFASF 249
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
13-257 4.22e-66

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: 204.43  E-value: 4.22e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  13 GPDQWSKLYPI----ANGNNQSPIDIKTSEAKHDSsLKPVSVSYNPaTAKEIVNVGHSFHVVFDDSSNQSVLKGGpladS 88
Cdd:cd03124    1 GPEHWGNLDPEfalcATGKNQSPIDITTKAVVSDK-LPPLNYNYKP-TSATLVNNGHTIQVNFEGNGGTLTIDGE----T 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  89 YRLTQFHFHwgnsndHGSEHTVDGAKYSGELHLVHwnsakyssaaeaISKADGLAIIGVLMKVGPANPNLQKVLDALSSV 168
Cdd:cd03124   75 YQLLQFHFH------SPSEHLINGKRYPLEAHLVH------------KSKDGQLAVVAVLFEEGKENPFLKKILDNMPKK 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 169 KTKGKRAPfTNFDPSSLLPSSLDYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAegepavpvlsNHRP 248
Cdd:cd03124  137 EGTEVNLP-AILDPNELLPESRSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAAVYPN----------NARP 205

                 ....*....
gi 157817869 249 PQPLKGRTV 257
Cdd:cd03124  206 VQPLNGREV 214
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
16-261 4.47e-66

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: 205.86  E-value: 4.47e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  16 QWSKLYPIANGNNQSPIDIKTSEAKHDSSLKPVSVSYNPATAK--EIVNVGHSFHVVFddsSNQSVLKGGPL--ADSYRL 91
Cdd:cd03120    3 EWGLLFPEANGEYQSPINLNSREARYDPSLLEVRLSPNYVVCRdcEVINDGHTIQIIL---KSKSVLSGGPLpqGHEFEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  92 TQFHFHWGNSNDHGSEHTVDGAKYSGELHLVHWNSAKYSSAAEAISKADGLAIIGVLMKVGPANPNLQKVLDALSSVKTK 171
Cdd:cd03120   80 AEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIGKEHVGLKAVTEILQDIQYK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 172 GKRAPFTNFDPSSLLPSSL--DYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPAVPV-----LS 244
Cdd:cd03120  160 GKSKTIPCFNPNTLLPDPLlrDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLRTHVKGAELVEGcdgllGD 239
                        250
                 ....*....|....*..
gi 157817869 245 NHRPPQPLKGRTVRASF 261
Cdd:cd03120  240 NFRPTQPLSDRVIRAAF 256
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
13-258 2.08e-65

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: 204.18  E-value: 2.08e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  13 GPDQWSKLYPIAN----GNNQSPIDIKTSEAKHDSSLKPVSVSYNPATAKEIVNVGHSFhVVFDDSSNQSVLKGGPLADS 88
Cdd:cd03121    1 GPSFWGLVNSAWNlcskGRRQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGTFYNTGRHV-SFRPDKDPVVNISGGPLSYR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  89 YRLTQFHFHWGNSNDHGSEHTVDGAKYSGELHLVHWNSAKYSSAAEAISKADGLAIIGVLMKVGP-ANPNLQKVL--DAL 165
Cdd:cd03121   80 YRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGEtSNPELRRLTnrDTI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 166 SSVKTKGKRAPFTNFDPSSLLPSSLDYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPAVPVLSN 245
Cdd:cd03121  160 TSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEKAPMSPN 239
                        250
                 ....*....|...
gi 157817869 246 HRPPQPLKGRTVR 258
Cdd:cd03121  240 FRPVQPLNNRPVR 252
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
26-257 1.18e-63

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: 199.03  E-value: 1.18e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  26 GNNQSPIDIKTSEAKHDSSLKPVS-VSYNPATA-KEIVNVGHSFHVVFDDSSNqsvLKGGPLADSYRLTQFHFHWGNSND 103
Cdd:cd03117    1 GKRQSPINIVTKKVQYDENLTPFTfTGYDDTTTnWTITNNGHTVQVTLPDGAK---ISGGGLPGTYKALQFHFHWGSNGS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 104 HGSEHTVDGAKYSGELHLVHWNSaKYSSAAEAISKADGLAIIGVLMKVGP-ANPNLQKVLDALSSVKTKGKRAPFTNFDP 182
Cdd:cd03117   78 PGSEHTIDGERYPMELHIVHIKE-SYNSLLEALKDSDGLAVLGFFIEEGEeENTNFDPLISALSNIPQKGGSTNLTPFSL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157817869 183 SSLLPS--SLDYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEPaVPVLSNHRPPQPLKGRTV 257
Cdd:cd03117  157 RSLLPSvlLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNG-QPMVNNFRPVQPLNGRVV 232
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
13-257 4.78e-52

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: 169.84  E-value: 4.78e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  13 GPDQWSKLYPIAN-GNNQSPIDIKTSEAKHDSSLKPV--SVSYNPATAKEIVNVGHSFHVVFDDSSNQSVLKGGPLADSY 89
Cdd:cd03122    1 NPKHWAKKYPACGeGRQQSPIDIVEDTQVQRQGLQPLhfDGYEELTASTTLENTGKTVILRLEGNSSDPFVSGGPLLGRY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  90 RLTQFHFHWGNSNDHGSEHTVDGAKYSGELHLVHWNSAKYSSaAEAISKADGLAIIGVLMKVGPA-NPNLQKVLDALSSV 168
Cdd:cd03122   81 KFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDS-FEAIKSPGGVLALAYLFELSHEdNPFLDPIIEGLRNV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 169 KTKGKRAPFTNFDPSSLLPSSLD-YWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLS-SAEGEPAVPVL-SN 245
Cdd:cd03122  160 SRPGKEVELPPFPLSDLLPPFTDkYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTrRQDGVMSGDYLpNN 239
                        250
                 ....*....|..
gi 157817869 246 HRPPQPLKGRTV 257
Cdd:cd03122  240 GRPQQPLGSRTV 251
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
13-261 5.63e-52

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: 169.75  E-value: 5.63e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  13 GPDQWSKLYPIANGNNQSPIDIKTSEAKHDSSLKPVSV---SYNPATAKEIVNVGHSFHVVFDDSSNqsvLKGGPlADSY 89
Cdd:cd03150    1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELlgfDLPPSPSLRLLNNGHTVQLSLPSGLR---MALGP-GQEY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  90 RLTQFHFHWGNSNDHGSEHTVDGAKYSGELHLVHWNSAkYSSAAEAISKADGLAIIGVLMKVGP-ANPNLQKVLDALSSV 168
Cdd:cd03150   77 RALQLHLHWGAAGRPGSEHTVDGHRFPAEIHVVHLSTA-FANLDEALGRPGGLAVLAAFLAEGLhENSAYEQLLSRLSEI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 169 KTKGKRAPFTNFDPSSLLPSSLD-YWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRgllSSAEGEPAVPVLSNHR 247
Cdd:cd03150  156 SEEESETVVPGLDVSALLPSDLSrYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLS---DSLWGPHDSRLQLNFR 232
                        250
                 ....*....|....
gi 157817869 248 PPQPLKGRTVRASF 261
Cdd:cd03150  233 ATQPLNGRKIEASF 246
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
16-261 1.67e-50

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: 165.73  E-value: 1.67e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  16 QWSKLYPIANGNNQSPIDIKTSEAKHDSSLKPVSVSYNPATAKE--IVNVGHSfhVVFDDSSNQSVLKGgpLADSYRLTQ 93
Cdd:cd03125    4 HWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEftMTNNGHT--VQIDLPPTMSITTG--DGTVYTAVQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  94 FHFHWG--NSNDHGSEHTVDGAKYSGELHLVHWNSaKYSSAAEAISKADGLAIIGVLMKVG--PANPNLQKVLDALSSVK 169
Cdd:cd03125   80 MHFHWGgrDSEISGSEHTIDGMRYVAELHIVHYNS-KYKSYEEAKDKPDGLAVLAFLYKVGhyAENTYYSDFISKLAKIK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 170 TKGKRAPFTNFDPSSLLPSSLD-YWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLSSAEGEpavPVLSNHRP 248
Cdd:cd03125  159 YAGQTTTLTSLDVRDMLPENLHhYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLENTLMDHHNK---TIRNDYRR 235
                        250
                 ....*....|...
gi 157817869 249 PQPLKGRTVRASF 261
Cdd:cd03125  236 TQPLNHRVVEANF 248
PLN02202 PLN02202
carbonate dehydratase
6-257 4.21e-26

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 103.21  E-value: 4.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869   6 WGYDSKNGPDQWSKLYP----IANGNNQSPIDIKTSEAKHDSSLKPVSVSY---NPATAKEIVNVGhsfhVVFDDSSNQS 78
Cdd:PLN02202  31 FGYKGKNGPNQWGHLNPhftkCAVGKLQSPIDIQRRQIFYNHKLESIHRDYyftNATLVNHVCNVA----MFFGEGAGDV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  79 VLKGgplaDSYRLTQFHFHwgnsndHGSEHTVDGAKYSGELHLVHWnsakyssaaeaiSKADGLAIIGVLMKVGPANPNL 158
Cdd:PLN02202 107 IIDN----KNYTLLQMHWH------TPSEHHLHGVQYAAELHMVHQ------------AKDGSFAVVASLFKIGTEEPFL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869 159 QKVLDALSSVKTKGKRAPFT------NFDPSSLLPSSLDYWTYFGSLTHPPLHESVTWVICKESISLSPEQLAQLRGLLS 232
Cdd:PLN02202 165 SQMKDKLVKLKEERFKGNHTaqvevgKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPLD 244
                        250       260
                 ....*....|....*....|....*
gi 157817869 233 SAegepavpVLSNHRPPQPLKGRTV 257
Cdd:PLN02202 245 KS-------FKNNSRPCQPLNGRRV 262
PLN02179 PLN02179
carbonic anhydrase
10-214 4.42e-23

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 93.89  E-value: 4.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  10 SKNGPDQWSKLYP----IANGNNQSPIDIKTSEAK--HDSSLkpvSVSYNPATAKeIVNVGHSFHVVFDDSSNQSVLKgg 83
Cdd:PLN02179  43 TEKGPAEWGKLNPqwkvCSTGKYQSPIDLTDERVSliHDQAL---SRHYKPAPAV-IQSRGHDVMVSWKGDAGKITIH-- 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817869  84 plADSYRLTQFHFHwgnsndHGSEHTVDGAKYSGELHLVHwnsakyssaaeaISKADGLAIIGVLMKVGPANPNLQKVLD 163
Cdd:PLN02179 117 --QTDYKLVQCHWH------SPSEHTINGTSYDLELHMVH------------TSASGKTAVVGVLYKLGEPDEFLTKLLN 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157817869 164 ALSSVKTkgKRAPFTNFDPSSLLPSSLDYWTYFGSLTHPPLHESVTWVICK 214
Cdd:PLN02179 177 GIKGVGK--KEINLGIVDPRDIRFETNNFYRYIGSLTIPPCTEGVIWTVVK 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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