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Conserved domains on  [gi|395132469|ref|NP_001257429|]
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carbonic anhydrase 6 isoform 2 precursor [Homo sapiens]

Protein Classification

carbonic anhydrase family protein; carbonic anhydrase( domain architecture ID 10123247)

carbonic anhydrase family protein similar to carbonic anhydrase, which catalyzes the reversible hydration of gaseous carbon dioxide to carbonic acid; carbonic anhydrase (CA) catalyzes the zinc-dependent reversible hydration of carbon dioxide into bicarbonate and a proton

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
31-279 1.13e-174

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: 483.13  E-value: 1.13e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  31 DEAHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMTVADGTVYIAQQM 110
Cdd:cd03125    1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNNGHTVQIDLPPTMSITTGDGTVYTAVQM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 111 HFHWGGASSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNYPENTYYSNFISHLANIKYP 190
Cdd:cd03125   81 HFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSKYKSYEEAKDKPDGLAVLAFLYKVGHYAENTYYSDFISKLAKIKYA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 191 GQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRNKTIHNDYRRTQPLN 270
Cdd:cd03125  161 GQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLENTLMDHHNKTIRNDYRRTQPLN 240

                 ....*....
gi 395132469 271 HRVVESNFP 279
Cdd:cd03125  241 HRVVEANFL 249
 
Name Accession Description Interval E-value
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
31-279 1.13e-174

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: 483.13  E-value: 1.13e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  31 DEAHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMTVADGTVYIAQQM 110
Cdd:cd03125    1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNNGHTVQIDLPPTMSITTGDGTVYTAVQM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 111 HFHWGGASSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNYPENTYYSNFISHLANIKYP 190
Cdd:cd03125   81 HFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSKYKSYEEAKDKPDGLAVLAFLYKVGHYAENTYYSDFISKLAKIKYA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 191 GQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRNKTIHNDYRRTQPLN 270
Cdd:cd03125  161 GQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLENTLMDHHNKTIRNDYRRTQPLN 240

                 ....*....
gi 395132469 271 HRVVESNFP 279
Cdd:cd03125  241 HRVVEANFL 249
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
30-278 3.70e-117

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 337.70  E-value: 3.70e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469   30 LDEAHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMTVADG---TVYI 106
Cdd:pfam00194   1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNTLTNNGHTVQVSLDDGDPSTISGGplaTRYR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  107 AQQMHFHWGgaSSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVkNYPENTYYSNFISHLAN 186
Cdd:pfam00194  81 LVQFHFHWG--STDSRGSEHTIDGKRYPAELHIVHYNSKYKSFDEAAKHPDGLAVLGVFFEV-GDENNPYLQPIVSALDN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  187 IKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRNKT---IHNDY 263
Cdd:pfam00194 158 IKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEprpLVNNF 237
                         250
                  ....*....|....*
gi 395132469  264 RRTQPLNHRVVESNF 278
Cdd:pfam00194 238 RPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
23-273 5.44e-98

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: 288.83  E-value: 5.44e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469    23 WTYsEGALDEAHWPQHYPA-CGGQRQSPINLQRTKVRYNPSLKGLNMTGYetQAGEFPMVNNGHTVQISLPSTMrMTVAD 101
Cdd:smart01057   1 WGY-EGKNGPEHWGKLDPPfCGGKRQSPIDIVTAEAQYDPSLKPLKLSYD--QPTAKRILNNGHTVQVNFDDDG-STLSG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469   102 G---TVYIAQQMHFHWGGASSEisGSEHTVDGIRHVIEIHIVHYNSKyKSYDIAQDAPDGLAVLAAFVEVKNyPENTYYS 178
Cdd:smart01057  77 GplpGRYRLKQFHFHWGGSDSE--GSEHTIDGKRFPLELHLVHYNSK-GSFSEAVSKPGGLAVVAVFFKVGA-EENPALQ 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469   179 NFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRNKT 258
Cdd:smart01057 153 AILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEP 232
                          250
                   ....*....|....*
gi 395132469   259 IHNDYRRTQPLNHRV 273
Cdd:smart01057 233 LVNNARPLQPLNGRV 247
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
17-274 3.94e-56

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 182.01  E-value: 3.94e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  17 AQHVSDWTYsEGALDEAHWPQ---HYPACG-GQRQSPINLqRTKVRynPSLKGLNMTgYetQAGEFPMVNNGHTVQISLP 92
Cdd:COG3338   22 AASAPHWSY-EGETGPEHWGElspEFATCAtGKNQSPIDI-RTAIK--ADLPPLKFD-Y--KPTPLEIVNNGHTIQVNVD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  93 STMRMTVaDGTVYIAQQMHFHwggasseiSGSEHTVDGIRHVIEIHIVHynskyksydiaQDAPDGLAVLAAFVEVKNyp 172
Cdd:COG3338   95 PGSTLTV-DGKRYELKQFHFH--------TPSEHTINGKSYPMEAHLVH-----------KDADGELAVVGVLFEEGA-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 173 ENTYYSNFISHLAniKYPGQRTTL-TGLDVQDMLPRNLqHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLEnsl 251
Cdd:COG3338  153 ENPALAKLWANLP--LEAGEEVALdATIDLNDLLPEDR-SYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFA--- 226
                        250       260
                 ....*....|....*....|...
gi 395132469 252 ldhrnKTIHNDYRRTQPLNHRVV 274
Cdd:COG3338  227 -----RLYPNNARPVQPLNGRLI 244
PLN02202 PLN02202
carbonate dehydratase
33-275 1.46e-22

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 95.12  E-value: 1.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  33 AHWPQHYPACG-GQRQSPINLQRTKVRYNPSLKGLNMTGYETQAgefPMVNNGHTVQISLPSTMRMTVADGTVYIAQQMH 111
Cdd:PLN02202  43 GHLNPHFTKCAvGKLQSPIDIQRRQIFYNHKLESIHRDYYFTNA---TLVNHVCNVAMFFGEGAGDVIIDNKNYTLLQMH 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 112 FHwggasseiSGSEHTVDGIRHVIEIHIVHynskyksydiaqDAPDG-LAVLAAFVEVKNypENTYYSNFISHLANIK-- 188
Cdd:PLN02202 120 WH--------TPSEHHLHGVQYAAELHMVH------------QAKDGsFAVVASLFKIGT--EEPFLSQMKDKLVKLKee 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 189 -YPGQRTTLTGLDVQDM--LPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLldhrNKTIHNDYRR 265
Cdd:PLN02202 178 rFKGNHTAQVEVGKIDTrhIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPL----DKSFKNNSRP 253
                        250
                 ....*....|
gi 395132469 266 TQPLNHRVVE 275
Cdd:PLN02202 254 CQPLNGRRVE 263
 
Name Accession Description Interval E-value
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
31-279 1.13e-174

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: 483.13  E-value: 1.13e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  31 DEAHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMTVADGTVYIAQQM 110
Cdd:cd03125    1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNNGHTVQIDLPPTMSITTGDGTVYTAVQM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 111 HFHWGGASSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNYPENTYYSNFISHLANIKYP 190
Cdd:cd03125   81 HFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSKYKSYEEAKDKPDGLAVLAFLYKVGHYAENTYYSDFISKLAKIKYA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 191 GQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRNKTIHNDYRRTQPLN 270
Cdd:cd03125  161 GQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLENTLMDHHNKTIRNDYRRTQPLN 240

                 ....*....
gi 395132469 271 HRVVESNFP 279
Cdd:cd03125  241 HRVVEANFL 249
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
31-278 1.45e-158

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: 442.52  E-value: 1.45e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  31 DEAHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTGYETQAG-EFPMVNNGHTVQISLPSTMRMTVADGTVYIAQQ 109
Cdd:cd03123    1 GEDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTeEFTLTNNGHTVQLSLPPTMHIRGGPGTEYTAAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 110 MHFHWGGASSeISGSEHTVDGIRHVIEIHIVHYNS-KYKSYDIAQDAPDGLAVLAAFVEVKnYPENTYYSNFISHLANIK 188
Cdd:cd03123   81 LHLHWGGRGS-LSGSEHTIDGIRFAAELHIVHYNSdKYSSFDEAADKPDGLAVLAILIEVG-YPENTYYEKIISHLHEIK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 189 YPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRNKTIHNDYRRTQP 268
Cdd:cd03123  159 YKGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLETLENTLMDTHNKTLQNNYRATQP 238
                        250
                 ....*....|
gi 395132469 269 LNHRVVESNF 278
Cdd:cd03123  239 LNGRVVEASF 248
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
30-278 3.70e-117

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 337.70  E-value: 3.70e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469   30 LDEAHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMTVADG---TVYI 106
Cdd:pfam00194   1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNTLTNNGHTVQVSLDDGDPSTISGGplaTRYR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  107 AQQMHFHWGgaSSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVkNYPENTYYSNFISHLAN 186
Cdd:pfam00194  81 LVQFHFHWG--STDSRGSEHTIDGKRYPAELHIVHYNSKYKSFDEAAKHPDGLAVLGVFFEV-GDENNPYLQPIVSALDN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  187 IKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRNKT---IHNDY 263
Cdd:pfam00194 158 IKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEprpLVNNF 237
                         250
                  ....*....|....*
gi 395132469  264 RRTQPLNHRVVESNF 278
Cdd:pfam00194 238 RPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
23-273 5.44e-98

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: 288.83  E-value: 5.44e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469    23 WTYsEGALDEAHWPQHYPA-CGGQRQSPINLQRTKVRYNPSLKGLNMTGYetQAGEFPMVNNGHTVQISLPSTMrMTVAD 101
Cdd:smart01057   1 WGY-EGKNGPEHWGKLDPPfCGGKRQSPIDIVTAEAQYDPSLKPLKLSYD--QPTAKRILNNGHTVQVNFDDDG-STLSG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469   102 G---TVYIAQQMHFHWGGASSEisGSEHTVDGIRHVIEIHIVHYNSKyKSYDIAQDAPDGLAVLAAFVEVKNyPENTYYS 178
Cdd:smart01057  77 GplpGRYRLKQFHFHWGGSDSE--GSEHTIDGKRFPLELHLVHYNSK-GSFSEAVSKPGGLAVVAVFFKVGA-EENPALQ 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469   179 NFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRNKT 258
Cdd:smart01057 153 AILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEP 232
                          250
                   ....*....|....*
gi 395132469   259 IHNDYRRTQPLNHRV 273
Cdd:smart01057 233 LVNNARPLQPLNGRV 247
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
44-275 3.85e-91

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: 270.69  E-value: 3.85e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  44 GQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGEfpMVNNGHTVQISLPSTM-RMTVAD-GTVYIAQQMHFHWGGASSEi 121
Cdd:cd00326    1 GKRQSPINIVTSAVVYDPSLPPLNFDYYPTTSLT--LVNNGHTVQVNFDDDGgTLSGGGlPGRYKLVQFHFHWGSENSP- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 122 sGSEHTVDGIRHVIEIHIVHYNSKYKSYDiAQDAPDGLAVLAAFVEVKNyPENTYYSNFISHLANIKYPGQRTTLTGLDV 201
Cdd:cd00326   78 -GSEHTIDGKRYPLELHLVHYNSDYYSSE-AAKKPGGLAVLGVFFEVGE-KENPFLKKILDALPKIKYKGKETTLPPFDL 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 395132469 202 QDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENsLLDHRNKTIHNDYRRTQPLNHRVVE 275
Cdd:cd00326  155 SDLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRS-LLDREGKPLVNNYRPVQPLNGRVVY 227
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
31-279 1.62e-83

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: 252.18  E-value: 1.62e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  31 DEAHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTGYE-TQAGEFPMVNNGHTVQISLPSTMRMTVADGTVYIAQQ 109
Cdd:cd03150    1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDlPPSPSLRLLNNGHTVQLSLPSGLRMALGPGQEYRALQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 110 MHFHWGGAssEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNYpENTYYSNFISHLANIKY 189
Cdd:cd03150   81 LHLHWGAA--GRPGSEHTVDGHRFPAEIHVVHLSTAFANLDEALGRPGGLAVLAAFLAEGLH-ENSAYEQLLSRLSEISE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 190 PGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRNKTIHNDYRRTQPL 269
Cdd:cd03150  158 EESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHDSRLQLNFRATQPL 237
                        250
                 ....*....|
gi 395132469 270 NHRVVESNFP 279
Cdd:cd03150  238 NGRKIEASFP 247
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
44-274 2.07e-75

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: 231.00  E-value: 2.07e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  44 GQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMTVAD-GTVYIAQQMHFHWGGASSEis 122
Cdd:cd03117    1 GKRQSPINIVTKKVQYDENLTPFTFTGYDDTTTNWTITNNGHTVQVTLPDGAKISGGGlPGTYKALQFHFHWGSNGSP-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 123 GSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNyPENTYYSNFISHLANIKYPGQRTTLTGLDVQ 202
Cdd:cd03117   79 GSEHTIDGERYPMELHIVHIKESYNSLLEALKDSDGLAVLGFFIEEGE-EENTNFDPLISALSNIPQKGGSTNLTPFSLR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 395132469 203 DMLP-RNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHR--NKTIHNDYRRTQPLNHRVV 274
Cdd:cd03117  158 SLLPsVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTdnGQPMVNNFRPVQPLNGRVV 232
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
32-278 1.20e-73

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: 227.03  E-value: 1.20e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  32 EAHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGE-FPMVNNGHTVQISLPSTMRMTVADGTvYIAQQM 110
Cdd:cd03126    2 ENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEqFTLTNNGHTVQLSLPPTMHIGGLPFK-YTASQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 111 HFHWGGASSEiSGSEHTVDGIRHVIEIHIVHYNS-KYKSYDIAQDAPDGLAVLAAFVEVKnyPENTYYSNFISHLANIKY 189
Cdd:cd03126   81 HLHWGQRGSP-EGSEHTISGKHFAAELHIVHYNSdKYPDISTAMNKSQGLAVLGILIEVG--PFNPSYEKIFSHLHEVKY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 190 PGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLL-DHRN--KTIHNDYRRT 266
Cdd:cd03126  158 KDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALETALYsTEEDesREMVNNYRQV 237
                        250
                 ....*....|..
gi 395132469 267 QPLNHRVVESNF 278
Cdd:cd03126  238 QPFNERLVFASF 249
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
21-278 5.40e-61

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: 194.97  E-value: 5.40e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  21 SDWTYSEGALDEaHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTgYEtQAGEFPMVNNGHTVQISLPSTMRMTVA 100
Cdd:cd03119    3 HHWGYDSHNGPE-HWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVS-YD-PATAKTILNNGHSFNVEFDDTDDRSVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 101 DG----TVYIAQQMHFHWGgaSSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNypENTY 176
Cdd:cd03119   80 RGgpltGSYRLRQFHFHWG--SSDDHGSEHTVDGVKYAAELHLVHWNSKYGSFGEAAKQPDGLAVVGVFLKVGE--ANPE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 177 YSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQhYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRN 256
Cdd:cd03119  156 LQKVLDALDSIKTKGKQAPFTNFDPSCLLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEG 234
                        250       260
                 ....*....|....*....|....*.
gi 395132469 257 KT----IHNdYRRTQPLNHRVVESNF 278
Cdd:cd03119  235 EPpcpmVDN-WRPPQPLKGRKVRASF 259
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
17-274 3.94e-56

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 182.01  E-value: 3.94e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  17 AQHVSDWTYsEGALDEAHWPQ---HYPACG-GQRQSPINLqRTKVRynPSLKGLNMTgYetQAGEFPMVNNGHTVQISLP 92
Cdd:COG3338   22 AASAPHWSY-EGETGPEHWGElspEFATCAtGKNQSPIDI-RTAIK--ADLPPLKFD-Y--KPTPLEIVNNGHTIQVNVD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  93 STMRMTVaDGTVYIAQQMHFHwggasseiSGSEHTVDGIRHVIEIHIVHynskyksydiaQDAPDGLAVLAAFVEVKNyp 172
Cdd:COG3338   95 PGSTLTV-DGKRYELKQFHFH--------TPSEHTINGKSYPMEAHLVH-----------KDADGELAVVGVLFEEGA-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 173 ENTYYSNFISHLAniKYPGQRTTL-TGLDVQDMLPRNLqHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLEnsl 251
Cdd:COG3338  153 ENPALAKLWANLP--LEAGEEVALdATIDLNDLLPEDR-SYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFA--- 226
                        250       260
                 ....*....|....*....|...
gi 395132469 252 ldhrnKTIHNDYRRTQPLNHRVV 274
Cdd:COG3338  227 -----RLYPNNARPVQPLNGRLI 244
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
44-278 4.92e-53

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: 173.87  E-value: 4.92e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  44 GQRQSPINLQRTKVRYNPSLKGLNMTgYETqAGEFPMVNNGHTVQISLPSTMRMTVADG----TVYIAQQMHFHWGGASS 119
Cdd:cd03149    1 GNRQSPIDIVSSEAVYDPKLKPLSLS-YDP-CTSLSISNNGHSVMVEFDDSDDKTVITGgpleNPYRLKQFHFHWGAKHG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 120 eiSGSEHTVDGIRHVIEIHIVHYNS-KYKSYDIAQDAPDGLAVLAAFVEVKNypENTYYSNFISHLANIKYPGQRTTLTG 198
Cdd:cd03149   79 --SGSEHTVDGKTFPSELHLVHWNAkKYKSFGEAAAAPDGLAVLGVFLETGD--EHPGLNRLTDALYMVRFKGTKAQFLD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 199 LDVQDMLPRNLqHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLL----DHRNKTIhNDYRRTQPLNHRVV 274
Cdd:cd03149  155 FNPKCLLPKSL-DYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFtseeDQRNHMV-NNFRPPQPLKGRTV 232

                 ....
gi 395132469 275 ESNF 278
Cdd:cd03149  233 RASF 236
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
34-276 2.59e-52

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: 171.30  E-value: 2.59e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  34 HWPQ---HYPACG-GQRQSPINLQRTKVRYNpSLKGLNMTGYETQAGefpMVNNGHTVQISLPSTM-RMTVaDGTVYIAQ 108
Cdd:cd03124    4 HWGNldpEFALCAtGKNQSPIDITTKAVVSD-KLPPLNYNYKPTSAT---LVNNGHTIQVNFEGNGgTLTI-DGETYQLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 109 QMHFHwggasseiSGSEHTVDGIRHVIEIHIVHynskyksydiaQDAPDGLAVLAAFVEVknYPENTyysnFISHLAN-- 186
Cdd:cd03124   79 QFHFH--------SPSEHLINGKRYPLEAHLVH-----------KSKDGQLAVVAVLFEE--GKENP----FLKKILDnm 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 187 IKYPGQRTTLT-GLDVQDMLPRNLqHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLenslldhRNKTIHNDYRR 265
Cdd:cd03124  134 PKKEGTEVNLPaILDPNELLPESR-SYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKF-------RAAVYPNNARP 205
                        250
                 ....*....|.
gi 395132469 266 TQPLNHRVVES 276
Cdd:cd03124  206 VQPLNGREVLL 216
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
34-276 1.84e-50

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: 167.53  E-value: 1.84e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  34 HWPQHYPACG-GQRQSPINLQR-TKVRYNpSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMTVADG----TVYIA 107
Cdd:cd03122    4 HWAKKYPACGeGRQQSPIDIVEdTQVQRQ-GLQPLHFDGYEELTASTTLENTGKTVILRLEGNSSDPFVSGgpllGRYKF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 108 QQMHFHWGGASSEisGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNyPENTYYSNFISHLANI 187
Cdd:cd03122   83 SEITFHWGTCNSD--GSEHSIDGHKFPLEMQILHRNTDFFDSFEAIKSPGGVLALAYLFELSH-EDNPFLDPIIEGLRNV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 188 KYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLeNSLLDHRN------KTIHN 261
Cdd:cd03122  160 SRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAF-RELLTRRQdgvmsgDYLPN 238
                        250
                 ....*....|....*
gi 395132469 262 DYRRTQPLNHRVVES 276
Cdd:cd03122  239 NGRPQQPLGSRTVFS 253
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
44-278 2.64e-39

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: 138.05  E-value: 2.64e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  44 GQRQSPINLQRTKVRYNPSLKGLNmTGYETQAGEFpMVNNGHTVQISLP-STMRMTVADGTV---YIAQQMHFHWGgASS 119
Cdd:cd03118    1 GTRQSPINIQWRDSVYDPQLAPLR-VSYDPATCLY-IWNNGYSFQVEFDdSTDKSGISGGPLenhYRLKQFHFHWG-ANN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 120 EiSGSEHTVDGIRHVIEIHIVHYNS-KYKSYDIAQDAPDGLAVLAAFVEVKNYPENtyYSNFISHLANIKYPGQRTTLTG 198
Cdd:cd03118   78 E-WGSEHTVDGHTYPAELHLVHWNSvKYENFEEAVMEENGLAVIGVFLKLGAHHEG--LQKLVDALPEVRHKDTVVEFNP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 199 LDVQDMLPRNLQhYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHR---NKTIHNDYRRTQPLNHRVVE 275
Cdd:cd03118  155 FDPSCLLPACRD-YWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLFTSRgeeEKVMVNNFRPLQPLMNRKVR 233

                 ...
gi 395132469 276 SNF 278
Cdd:cd03118  234 SSF 236
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
44-277 6.29e-37

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: 132.54  E-value: 6.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  44 GQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGEFpmVNNGHTVQISLPSTMRMTVADGTV---YIAQQMHFHWGGASSE 120
Cdd:cd03121   18 GRRQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGTF--YNTGRHVSFRPDKDPVVNISGGPLsyrYRLEEIRLHFGREDEQ 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 121 isGSEHTVDGIRHVIEIHIVHYNSK-YKSYDIAQDAPDGLAVLAAFVEVKNYPentyySNFISHLAN------IKYPGQR 193
Cdd:cd03121   96 --GSEHTVNGQAFPGEVQLIHYNSElYPNFSEASKSPNGLVIVSLFVKIGETS-----NPELRRLTNrdtitsIRYKGDA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 194 TTLTGLDVQDMLPrNLQHYYTYHGSLTTPPCTENVHWFVLADFV---KLSRTQVWKLENSLLDHRNKTIHNDYRRTQPLN 270
Cdd:cd03121  169 YFLQDLSIELLLP-ETDHYITYEGSLTSPGCHETVTWIILNKPIyitKEQMHSLRLLSQNSPSQEKAPMSPNFRPVQPLN 247

                 ....*..
gi 395132469 271 HRVVESN 277
Cdd:cd03121  248 NRPVRTN 254
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
33-278 7.87e-37

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: 132.29  E-value: 7.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  33 AHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMT---VADGTVYIAQQ 109
Cdd:cd03120    2 VEWGLLFPEANGEYQSPINLNSREARYDPSLLEVRLSPNYVVCRDCEVINDGHTIQIILKSKSVLSggpLPQGHEFELAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 110 MHFHWGGASSEisGSEHTVDGIRHVIEIHIVHYNSK-YKSYDIAQDAPDGLAVLAAFVEVKNypENTYYSNFISHLANIK 188
Cdd:cd03120   82 VRFHWGRENQR--GSEHTVNFKAFPMELHLIHWNSTlYSSLEEAMGKPHGIAIIALFVQIGK--EHVGLKAVTEILQDIQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 189 YPGQRTTLTGLDVQDMLPRN-LQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQV---WKLEN-----SLLDHRNKTI 259
Cdd:cd03120  158 YKGKSKTIPCFNPNTLLPDPlLRDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIeefRRLRThvkgaELVEGCDGLL 237
                        250
                 ....*....|....*....
gi 395132469 260 HNDYRRTQPLNHRVVESNF 278
Cdd:cd03120  238 GDNFRPTQPLSDRVIRAAF 256
PLN02202 PLN02202
carbonate dehydratase
33-275 1.46e-22

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 95.12  E-value: 1.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  33 AHWPQHYPACG-GQRQSPINLQRTKVRYNPSLKGLNMTGYETQAgefPMVNNGHTVQISLPSTMRMTVADGTVYIAQQMH 111
Cdd:PLN02202  43 GHLNPHFTKCAvGKLQSPIDIQRRQIFYNHKLESIHRDYYFTNA---TLVNHVCNVAMFFGEGAGDVIIDNKNYTLLQMH 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 112 FHwggasseiSGSEHTVDGIRHVIEIHIVHynskyksydiaqDAPDG-LAVLAAFVEVKNypENTYYSNFISHLANIK-- 188
Cdd:PLN02202 120 WH--------TPSEHHLHGVQYAAELHMVH------------QAKDGsFAVVASLFKIGT--EEPFLSQMKDKLVKLKee 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 189 -YPGQRTTLTGLDVQDM--LPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLldhrNKTIHNDYRR 265
Cdd:PLN02202 178 rFKGNHTAQVEVGKIDTrhIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPL----DKSFKNNSRP 253
                        250
                 ....*....|
gi 395132469 266 TQPLNHRVVE 275
Cdd:PLN02202 254 CQPLNGRRVE 263
PLN02179 PLN02179
carbonic anhydrase
38-232 2.22e-11

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 62.69  E-value: 2.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469  38 HYPACG-GQRQSPINLQRTKVrynpSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMTVADGTVYIAQQMHFHwgg 116
Cdd:PLN02179  56 QWKVCStGKYQSPIDLTDERV----SLIHDQALSRHYKPAPAVIQSRGHDVMVSWKGDAGKITIHQTDYKLVQCHWH--- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132469 117 asseiSGSEHTVDGIRHVIEIHIVHYNSKYKSydiaqdapdglAVLAAFVEVKNYPEntyysnFISHLAN-IKYPGQRTT 195
Cdd:PLN02179 129 -----SPSEHTINGTSYDLELHMVHTSASGKT-----------AVVGVLYKLGEPDE------FLTKLLNgIKGVGKKEI 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 395132469 196 LTGLdvqdMLPRNLQ----HYYTYHGSLTTPPCTENVHWFV 232
Cdd:PLN02179 187 NLGI----VDPRDIRfetnNFYRYIGSLTIPPCTEGVIWTV 223
 
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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