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Conserved domains on  [gi|157831396|pdb|1HUG|A]
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Chain A, CARBONIC ANHYDRASE I

Protein Classification

carbonic anhydrase family protein( domain architecture ID 275)

carbonic anhydrase family protein similar to carbonic anhydrase, which catalyzes the reversible hydration of gaseous carbon dioxide to carbonic acid

CATH:  3.10.200.10
Gene Ontology:  GO:0004089|GO:0008270|GO:0006730
PubMed:  10978542|18336305
SCOP:  4002732

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 ...
1-260 0e+00

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: 508.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A        1 ASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLK 80
Cdd:cd03119   1 MSHHWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVSYDPATAKTILNNGHSFNVEFDDTDDRSVLR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       81 GGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKV 160
Cdd:cd03119  81 GGPLTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVGEANPELQKV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      161 LDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVP 240
Cdd:cd03119 160 LDALDSIKTKGKQAPFTNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEPPCP 239
                       250       260
                ....*....|....*....|
1HUG_A      241 MQHNNRPTQPLKGRTVRASF 260
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 ...
1-260 0e+00

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: 508.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A        1 ASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLK 80
Cdd:cd03119   1 MSHHWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVSYDPATAKTILNNGHSFNVEFDDTDDRSVLR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       81 GGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKV 160
Cdd:cd03119  81 GGPLTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVGEANPELQKV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      161 LDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVP 240
Cdd:cd03119 160 LDALDSIKTKGKQAPFTNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEPPCP 239
                       250       260
                ....*....|....*....|
1HUG_A      241 MQHNNRPTQPLKGRTVRASF 260
Cdd:cd03119 240 MVDNWRPPQPLKGRKVRASF 259
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
11-260 2.74e-123

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 351.18  E-value: 2.74e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A         11 NGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSY--NPATAKEIINVGHSFHVNFeDNDNRSVLKGGPFSDSY 88
Cdd:pfam00194   1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGydVPPGKNTLTNNGHTVQVSL-DDGDPSTISGGPLATRY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A         89 RLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMKVG-EANPKLQKVLDALQAI 167
Cdd:pfam00194  80 RLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNS-KYKSFDEAAKHPDGLAVLGVFFEVGdENNPYLQPIVSALDNI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A        168 KTKGKRAPFTNFDPSTLLPSSL-DFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNR 246
Cdd:pfam00194 159 KYKGKSVLLPPFDLSDLLPEDLtSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEPRPLVNNFR 238
                         250
                  ....*....|....
1HUG_A        247 PTQPLKGRTVRASF 260
Cdd:pfam00194 239 PTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
5-255 3.37e-120

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: 343.14  E-value: 3.37e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A           5 WGYDDKNGPEQWSKLYP-IANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFedNDNRSVLKGGP 83
Cdd:smart01057   1 WGYEGKNGPEHWGKLDPpFCGGKRQSPIDIVTAEAQYDPSLKPLKLSYDQPTAKRILNNGHTVQVNF--DDDGSTLSGGP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A          84 FSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKysSLAEAASKADGLAVIGVLMKVG-EANPKLQKVLD 162
Cdd:smart01057  79 LPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGaEENPALQAILD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A         163 ALQAIKTKGKRAPFTNFDPSTLLPSSL-DFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDnavPM 241
Cdd:smart01057 157 HLPLIKYKGQETELTPFDLSSLLPASTrHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNE---PL 233
                          250
                   ....*....|....
1HUG_A         242 QHNNRPTQPLKGRT 255
Cdd:smart01057 234 VNNARPLQPLNGRV 247
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
1-259 5.78e-75

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 228.23  E-value: 5.78e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A        1 ASPDWGYDDKNGPEQWSKLYPI----ANGNNQSPVDIKTSEtkhDTSLKPISVSYNPaTAKEIINVGHSFHVNFEDNDNR 76
Cdd:COG3338  24 SAPHWSYEGETGPEHWGELSPEfatcATGKNQSPIDIRTAI---KADLPPLKFDYKP-TPLEIVNNGHTIQVNVDPGSTL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       77 SVlkGGpfsDSYRLFQFHFHwgstneHGSEHTVDGVKYSAELHVAHwnsakysslaeaASKADGLAVIGVLMKVGEANPK 156
Cdd:COG3338 100 TV--DG---KRYELKQFHFH------TPSEHTINGKSYPMEAHLVH------------KDADGELAVVGVLFEEGAENPA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      157 LQKVLDALQAiKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLlsnvegd 236
Cdd:COG3338 157 LAKLWANLPL-EAGEEVALDATIDLNDLLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARL------- 228
                       250       260
                ....*....|....*....|...
1HUG_A      237 navpMQHNNRPTQPLKGRTVRAS 259
Cdd:COG3338 229 ----YPNNARPVQPLNGRLILES 247
PLN02202 PLN02202
carbonate dehydratase
5-256 3.10e-25

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 100.90  E-value: 3.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A         5 WGYDDKNGPEQWSKLYP----IANGNNQSPVDIKTSETKHDTSLKPISVSY---NPATAKEIINVGHSFHVNFEDN--DN 75
Cdd:PLN02202  31 FGYKGKNGPNQWGHLNPhftkCAVGKLQSPIDIQRRQIFYNHKLESIHRDYyftNATLVNHVCNVAMFFGEGAGDViiDN 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A        76 RSvlkggpfsdsYRLFQFHFHwgstneHGSEHTVDGVKYSAELHVAHwnsakysslaeaASKADGLAVIGVLMKVGEANP 155
Cdd:PLN02202 111 KN----------YTLLQMHWH------TPSEHHLHGVQYAAELHMVH------------QAKDGSFAVVASLFKIGTEEP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       156 KLQKVLDALQAIKTKGKRAPFT------NFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSL 229
Cdd:PLN02202 163 FLSQMKDKLVKLKEERFKGNHTaqvevgKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSP 242
                        250       260
                 ....*....|....*....|....*..
1HUG_A       230 LSNvegdnavPMQHNNRPTQPLKGRTV 256
Cdd:PLN02202 243 LDK-------SFKNNSRPCQPLNGRRV 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 ...
1-260 0e+00

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: 508.13  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A        1 ASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLK 80
Cdd:cd03119   1 MSHHWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVSYDPATAKTILNNGHSFNVEFDDTDDRSVLR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       81 GGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKV 160
Cdd:cd03119  81 GGPLTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVGEANPELQKV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      161 LDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVP 240
Cdd:cd03119 160 LDALDSIKTKGKQAPFTNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEPPCP 239
                       250       260
                ....*....|....*....|
1HUG_A      241 MQHNNRPTQPLKGRTVRASF 260
Cdd:cd03119 240 MVDNWRPPQPLKGRKVRASF 259
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
11-260 2.74e-123

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 351.18  E-value: 2.74e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A         11 NGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSY--NPATAKEIINVGHSFHVNFeDNDNRSVLKGGPFSDSY 88
Cdd:pfam00194   1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGydVPPGKNTLTNNGHTVQVSL-DDGDPSTISGGPLATRY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A         89 RLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMKVG-EANPKLQKVLDALQAI 167
Cdd:pfam00194  80 RLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNS-KYKSFDEAAKHPDGLAVLGVFFEVGdENNPYLQPIVSALDNI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A        168 KTKGKRAPFTNFDPSTLLPSSL-DFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNR 246
Cdd:pfam00194 159 KYKGKSVLLPPFDLSDLLPEDLtSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEPRPLVNNFR 238
                         250
                  ....*....|....
1HUG_A        247 PTQPLKGRTVRASF 260
Cdd:pfam00194 239 PTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
5-255 3.37e-120

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: 343.14  E-value: 3.37e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A           5 WGYDDKNGPEQWSKLYP-IANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFedNDNRSVLKGGP 83
Cdd:smart01057   1 WGYEGKNGPEHWGKLDPpFCGGKRQSPIDIVTAEAQYDPSLKPLKLSYDQPTAKRILNNGHTVQVNF--DDDGSTLSGGP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A          84 FSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKysSLAEAASKADGLAVIGVLMKVG-EANPKLQKVLD 162
Cdd:smart01057  79 LPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGaEENPALQAILD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A         163 ALQAIKTKGKRAPFTNFDPSTLLPSSL-DFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDnavPM 241
Cdd:smart01057 157 HLPLIKYKGQETELTPFDLSSLLPASTrHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNE---PL 233
                          250
                   ....*....|....
1HUG_A         242 QHNNRPTQPLKGRT 255
Cdd:smart01057 234 VNNARPLQPLNGRV 247
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
25-260 1.33e-117

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: 336.04  E-value: 1.33e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       25 GNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHG 104
Cdd:cd03149   1 GNRQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLSISNNGHSVMVEFDDSDDKTVITGGPLENPYRLKQFHFHWGAKHGSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      105 SEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTL 184
Cdd:cd03149  81 SEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETGDEHPGLNRLTDALYMVRFKGTKAQFLDFNPKCL 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1HUG_A      185 LPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF 260
Cdd:cd03149 161 LPKSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHMVNNFRPPQPLKGRTVRASF 236
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
25-257 5.84e-107

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: 308.83  E-value: 5.84e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       25 GNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDnrSVLKGGPFSDSYRLFQFHFHWGSTNEHG 104
Cdd:cd00326   1 GKRQSPINIVTSAVVYDPSLPPLNFDYYPTTSLTLVNNGHTVQVNFDDDG--GTLSGGGLPGRYKLVQFHFHWGSENSPG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      105 SEHTVDGVKYSAELHVAHWNSAKYSSlaEAASKADGLAVIGVLMKVGEA-NPKLQKVLDALQAIKTKGKRAPFTNFDPST 183
Cdd:cd00326  79 SEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKeNPFLKKILDALPKIKYKGKETTLPPFDLSD 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1HUG_A      184 LLPSSL-DFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGdnavPMQHNNRPTQPLKGRTVR 257
Cdd:cd00326 157 LLPSSLrDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDREGK----PLVNNYRPVQPLNGRVVY 227
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
25-260 5.69e-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: 301.38  E-value: 5.69e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       25 GNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHG 104
Cdd:cd03118   1 GTRQSPINIQWRDSVYDPQLAPLRVSYDPATCLYIWNNGYSFQVEFDDSTDKSGISGGPLENHYRLKQFHFHWGANNEWG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      105 SEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTL 184
Cdd:cd03118  81 SEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHHEGLQKLVDALPEVRHKDTVVEFNPFDPSCL 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1HUG_A      185 LPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF 260
Cdd:cd03118 161 LPACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLFTSRGEEEKVMVNNFRPLQPLMNRKVRSSF 236
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
1-259 5.78e-75

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 228.23  E-value: 5.78e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A        1 ASPDWGYDDKNGPEQWSKLYPI----ANGNNQSPVDIKTSEtkhDTSLKPISVSYNPaTAKEIINVGHSFHVNFEDNDNR 76
Cdd:COG3338  24 SAPHWSYEGETGPEHWGELSPEfatcATGKNQSPIDIRTAI---KADLPPLKFDYKP-TPLEIVNNGHTIQVNVDPGSTL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       77 SVlkGGpfsDSYRLFQFHFHwgstneHGSEHTVDGVKYSAELHVAHwnsakysslaeaASKADGLAVIGVLMKVGEANPK 156
Cdd:COG3338 100 TV--DG---KRYELKQFHFH------TPSEHTINGKSYPMEAHLVH------------KDADGELAVVGVLFEEGAENPA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      157 LQKVLDALQAiKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLlsnvegd 236
Cdd:COG3338 157 LAKLWANLPL-EAGEEVALDATIDLNDLLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARL------- 228
                       250       260
                ....*....|....*....|...
1HUG_A      237 navpMQHNNRPTQPLKGRTVRAS 259
Cdd:COG3338 229 ----YPNNARPVQPLNGRLILES 247
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
12-260 2.05e-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: 221.80  E-value: 2.05e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       12 GPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPIS-VSYNPATAKE--IINVGHSFHVNFEdndNRSVLKGGPFSDsY 88
Cdd:cd03123   1 GEDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLElVGYDLPGTEEftLTNNGHTVQLSLP---PTMHIRGGPGTE-Y 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       89 RLFQFHFHWGSTNE-HGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEA-NPKLQKVLDALQA 166
Cdd:cd03123  77 TAAQLHLHWGGRGSlSGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPeNTYYEKIISHLHE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      167 IKTKGKRAPFTNFDPSTLLPSSLD-FWTYPGSLTHPPLYESVTWIICKESISVSSEQLAqfrsLLSN-VEGDNAVPMQHN 244
Cdd:cd03123 157 IKYKGQETTVPGFNVRELLPEDLShYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLE----TLENtLMDTHNKTLQNN 232
                       250
                ....*....|....*.
1HUG_A      245 NRPTQPLKGRTVRASF 260
Cdd:cd03123 233 YRATQPLNGRVVEASF 248
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
15-260 1.97e-70

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: 217.03  E-value: 1.97e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       15 QWSKLYPIANGNNQSPVDIKTSETKHDTSLK--PISVSYNPATAKEIINVGHSFHVNFEdndNRSVLKGGPF--SDSYRL 90
Cdd:cd03120   3 EWGLLFPEANGEYQSPINLNSREARYDPSLLevRLSPNYVVCRDCEVINDGHTIQIILK---SKSVLSGGPLpqGHEFEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       91 FQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTK 170
Cdd:cd03120  80 AEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIGKEHVGLKAVTEILQDIQYK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      171 GKRAPFTNFDPSTLLPSSL--DFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVP-----MQH 243
Cdd:cd03120 160 GKSKTIPCFNPNTLLPDPLlrDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLRTHVKGAELVEgcdglLGD 239
                       250
                ....*....|....*..
1HUG_A      244 NNRPTQPLKGRTVRASF 260
Cdd:cd03120 240 NFRPTQPLSDRVIRAAF 256
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
12-256 2.04e-68

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: 210.59  E-value: 2.04e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       12 GPEQWSKLYPI----ANGNNQSPVDIKTSETKHDtSLKPISVSYNPaTAKEIINVGHSFHVNFEDNDNRSVLKGGpfsdS 87
Cdd:cd03124   1 GPEHWGNLDPEfalcATGKNQSPIDITTKAVVSD-KLPPLNYNYKP-TSATLVNNGHTIQVNFEGNGGTLTIDGE----T 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       88 YRLFQFHFHwgstneHGSEHTVDGVKYSAELHVAHwnsakysslaeaASKADGLAVIGVLMKVGEANPKLQKVLDALQAI 167
Cdd:cd03124  75 YQLLQFHFH------SPSEHLINGKRYPLEAHLVH------------KSKDGQLAVVAVLFEEGKENPFLKKILDNMPKK 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      168 KTKGKRAPfTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNvegdnavpmqHNNRP 247
Cdd:cd03124 137 EGTEVNLP-AILDPNELLPESRSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAAVYP----------NNARP 205

                ....*....
1HUG_A      248 TQPLKGRTV 256
Cdd:cd03124 206 VQPLNGREV 214
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
25-256 1.78e-64

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: 200.96  E-value: 1.78e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       25 GNNQSPVDIKTSETKHDTSLKPIS-VSYNPATA-KEIINVGHSFHVNFEDNdnrSVLKGGPFSDSYRLFQFHFHWGSTNE 102
Cdd:cd03117   1 GKRQSPINIVTKKVQYDENLTPFTfTGYDDTTTnWTITNNGHTVQVTLPDG---AKISGGGLPGTYKALQFHFHWGSNGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      103 HGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMKVGE-ANPKLQKVLDALQAIKTKGKRAPFTNFDP 181
Cdd:cd03117  78 PGSEHTIDGERYPMELHIVHIKE-SYNSLLEALKDSDGLAVLGFFIEEGEeENTNFDPLISALSNIPQKGGSTNLTPFSL 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1HUG_A      182 STLLPS--SLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLsNVEGDNAVPMQHNNRPTQPLKGRTV 256
Cdd:cd03117 157 RSLLPSvlLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVL-FFDTDNGQPMVNNFRPVQPLNGRVV 232
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
12-257 6.84e-64

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: 200.33  E-value: 6.84e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       12 GPEQWSKLYPIAN----GNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHsfHVNFE-DNDNRSVLKGGPFSD 86
Cdd:cd03121   1 GPSFWGLVNSAWNlcskGRRQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGTFYNTGR--HVSFRpDKDPVVNISGGPLSY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       87 SYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGE-ANPKLQKVLDALQ 165
Cdd:cd03121  79 RYRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGEtSNPELRRLTNRDT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      166 A--IKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQH 243
Cdd:cd03121 159 ItsIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEKAPMSP 238
                       250
                ....*....|....
1HUG_A      244 NNRPTQPLKGRTVR 257
Cdd:cd03121 239 NFRPVQPLNNRPVR 252
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
12-260 1.31e-63

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: 199.29  E-value: 1.31e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       12 GPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPIS-VSYNPATAKEII--NVGHSFHVNFEDNDNrsvLKGGPFSdsY 88
Cdd:cd03126   1 GENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEfHGYNVSGTEQFTltNNGHTVQLSLPPTMH---IGGLPFK--Y 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       89 RLFQFHFHWGSTNE-HGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAI 167
Cdd:cd03126  76 TASQLHLHWGQRGSpEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVGPFNPSYEKIFSHLHEV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      168 KTKGKRAPFTNFDPSTLLPSSLD-FWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNR 246
Cdd:cd03126 156 KYKDQKVSVPGFNVQELLPKRLDeYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALETALYSTEEDESREMVNNYR 235
                       250
                ....*....|....
1HUG_A      247 PTQPLKGRTVRASF 260
Cdd:cd03126 236 QVQPFNERLVFASF 249
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
12-260 3.32e-55

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: 177.84  E-value: 3.32e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       12 GPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISV---SYNPATAKEIINVGHSFHVNFEDNdnRSVLKGgpFSDSY 88
Cdd:cd03150   1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELlgfDLPPSPSLRLLNNGHTVQLSLPSG--LRMALG--PGQEY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       89 RLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAkYSSLAEAASKADGLAVIGVLMKVG-EANPKLQKVLDALQAI 167
Cdd:cd03150  77 RALQLHLHWGAAGRPGSEHTVDGHRFPAEIHVVHLSTA-FANLDEALGRPGGLAVLAAFLAEGlHENSAYEQLLSRLSEI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      168 KTKGKRAPFTNFDPSTLLPSSLD-FWTYPGSLTHPPLYESVTWIICKESISVSSEQLAqfrSLLSNVEGDNAVPMQHNNR 246
Cdd:cd03150 156 SEEESETVVPGLDVSALLPSDLSrYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLH---TLSDSLWGPHDSRLQLNFR 232
                       250
                ....*....|....
1HUG_A      247 PTQPLKGRTVRASF 260
Cdd:cd03150 233 ATQPLNGRKIEASF 246
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
12-260 2.38e-52

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: 170.74  E-value: 2.38e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       12 GPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKE--IINVGHSFHVNFEDNDNRSVLKGGPfsdsYR 89
Cdd:cd03125   1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEftMTNNGHTVQIDLPPTMSITTGDGTV----YT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       90 LFQFHFHWG--STNEHGSEHTVDGVKYSAELHVAHWNSaKYSSLAEAASKADGLAVIGVLMKVGEA--NPKLQKVLDALQ 165
Cdd:cd03125  77 AVQMHFHWGgrDSEISGSEHTIDGMRYVAELHIVHYNS-KYKSYEEAKDKPDGLAVLAFLYKVGHYaeNTYYSDFISKLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      166 AIKTKGKRAPFTNFDPSTLLPSSLD-FWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLsnvegdnavpMQHN 244
Cdd:cd03125 156 KIKYAGQTTTLTSLDVRDMLPENLHhYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLENTL----------MDHH 225
                       250       260
                ....*....|....*....|...
1HUG_A      245 N-------RPTQPLKGRTVRASF 260
Cdd:cd03125 226 NktirndyRRTQPLNHRVVEANF 248
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
12-256 2.14e-51

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: 168.30  E-value: 2.14e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       12 GPEQWSKLYPIAN-GNNQSPVDIKTSETKHDTSLKPI--SVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSY 88
Cdd:cd03122   1 NPKHWAKKYPACGeGRQQSPIDIVEDTQVQRQGLQPLhfDGYEELTASTTLENTGKTVILRLEGNSSDPFVSGGPLLGRY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       89 RLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSlAEAASKADGLAVIGVLMKVG-EANPKLQKVLDALQAI 167
Cdd:cd03122  81 KFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDS-FEAIKSPGGVLALAYLFELShEDNPFLDPIIEGLRNV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A      168 KTKGKRAPFTNFDPSTLLPSSLD-FWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLL----SNVEGDNavPMQ 242
Cdd:cd03122 160 SRPGKEVELPPFPLSDLLPPFTDkYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLtrrqDGVMSGD--YLP 237
                       250
                ....*....|....
1HUG_A      243 HNNRPTQPLKGRTV 256
Cdd:cd03122 238 NNGRPQQPLGSRTV 251
PLN02202 PLN02202
carbonate dehydratase
5-256 3.10e-25

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 100.90  E-value: 3.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A         5 WGYDDKNGPEQWSKLYP----IANGNNQSPVDIKTSETKHDTSLKPISVSY---NPATAKEIINVGHSFHVNFEDN--DN 75
Cdd:PLN02202  31 FGYKGKNGPNQWGHLNPhftkCAVGKLQSPIDIQRRQIFYNHKLESIHRDYyftNATLVNHVCNVAMFFGEGAGDViiDN 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A        76 RSvlkggpfsdsYRLFQFHFHwgstneHGSEHTVDGVKYSAELHVAHwnsakysslaeaASKADGLAVIGVLMKVGEANP 155
Cdd:PLN02202 111 KN----------YTLLQMHWH------TPSEHHLHGVQYAAELHMVH------------QAKDGSFAVVASLFKIGTEEP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A       156 KLQKVLDALQAIKTKGKRAPFT------NFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSL 229
Cdd:PLN02202 163 FLSQMKDKLVKLKEERFKGNHTaqvevgKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSP 242
                        250       260
                 ....*....|....*....|....*..
1HUG_A       230 LSNvegdnavPMQHNNRPTQPLKGRTV 256
Cdd:PLN02202 243 LDK-------SFKNNSRPCQPLNGRRV 262
PLN02179 PLN02179
carbonic anhydrase
3-213 1.94e-24

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 97.74  E-value: 1.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A         3 PDWGYDDKN--GPEQWSKLYP----IANGNNQSPVDIKTSETK--HDTSLkpiSVSYNPATAKeIINVGHSFHVNFEDND 74
Cdd:PLN02179  35 PLFTYKQKTekGPAEWGKLNPqwkvCSTGKYQSPIDLTDERVSliHDQAL---SRHYKPAPAV-IQSRGHDVMVSWKGDA 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1HUG_A        75 NRSVLKggpfSDSYRLFQFHFHwgstneHGSEHTVDGVKYSAELHVAHwnsakysslaeaASKADGLAVIGVLMKVGEAN 154
Cdd:PLN02179 111 GKITIH----QTDYKLVQCHWH------SPSEHTINGTSYDLELHMVH------------TSASGKTAVVGVLYKLGEPD 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
1HUG_A       155 PKLQKVLDALQAIKTKgkRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICK 213
Cdd:PLN02179 169 EFLTKLLNGIKGVGKK--EINLGIVDPRDIRFETNNFYRYIGSLTIPPCTEGVIWTVVK 225
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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