NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17509323|ref|NP_491189|]
View 

Carbonic anhydrase [Caenorhabditis elegans]

Protein Classification

carbonic anhydrase family protein( domain architecture ID 10123209)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
56-304 7.66e-118

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: 339.72  E-value: 7.66e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  56 GKVLNVPSLGRTQSPIDIVP--VITAFGehLQNAHFEVTYESTGEFKAVNDGNSIWLMREGNSSELAISFLP-EEQYHLD 132
Cdd:cd03122   6 AKKYPACGEGRQQSPIDIVEdtQVQRQG--LQPLHFDGYEELTASTTLENTGKTVILRLEGNSSDPFVSGGPlLGRYKFS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 133 AVNFHWATEPMNGSEHTIGGVGYAGEMHLIHRNTRFATMADALKQPNGVIAIAVFLNESHDDNAVFSPLINLLPQVIYKG 212
Cdd:cd03122  84 EITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEGLRNVSRPG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 213 SECKLCSFDFQTFFPVAekTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVRAGRYDEEFSDKVPMKPLR 292
Cdd:cd03122 164 KEVELPPFPLSDLLPPF--TDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDGVMSGDYLPNNGR 241
                       250
                ....*....|..
gi 17509323 293 PIQNPSSRTIQS 304
Cdd:cd03122 242 PQQPLGSRTVFS 253
 
Name Accession Description Interval E-value
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
56-304 7.66e-118

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: 339.72  E-value: 7.66e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  56 GKVLNVPSLGRTQSPIDIVP--VITAFGehLQNAHFEVTYESTGEFKAVNDGNSIWLMREGNSSELAISFLP-EEQYHLD 132
Cdd:cd03122   6 AKKYPACGEGRQQSPIDIVEdtQVQRQG--LQPLHFDGYEELTASTTLENTGKTVILRLEGNSSDPFVSGGPlLGRYKFS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 133 AVNFHWATEPMNGSEHTIGGVGYAGEMHLIHRNTRFATMADALKQPNGVIAIAVFLNESHDDNAVFSPLINLLPQVIYKG 212
Cdd:cd03122  84 EITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEGLRNVSRPG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 213 SECKLCSFDFQTFFPVAekTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVRAGRYDEEFSDKVPMKPLR 292
Cdd:cd03122 164 KEVELPPFPLSDLLPPF--TDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDGVMSGDYLPNNGR 241
                       250
                ....*....|..
gi 17509323 293 PIQNPSSRTIQS 304
Cdd:cd03122 242 PQQPLGSRTVFS 253
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
63-301 3.41e-68

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: 213.33  E-value: 3.41e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323     63 SLGRTQSPIDIVPVITAFGEHLQNAHFEvtYESTGEFKAVNDGNSIWLMREGNSSELAISFLPEEqYHLDAVNFHWATEP 142
Cdd:smart01057  20 CGGKRQSPIDIVTAEAQYDPSLKPLKLS--YDQPTAKRILNNGHTVQVNFDDDGSTLSGGPLPGR-YRLKQFHFHWGGSD 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323    143 MNGSEHTIGGVGYAGEMHLIHRNTRfATMADALKQPNGVIAIAVFLNESHDDNAVFSPLINLLPQVIYKGSECKLCSFDF 222
Cdd:smart01057  97 SEGSEHTIDGKRFPLELHLVHYNSK-GSFSEAVSKPGGLAVVAVFFKVGAEENPALQAILDHLPLIKYKGQETELTPFDL 175
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17509323    223 QTFFPvaEKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVRAGRYDEEFSDKVpmkplRPIQNPSSRT 301
Cdd:smart01057 176 SSLLP--ASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEPLVNNA-----RPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
65-306 5.05e-58

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 187.09  E-value: 5.05e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323    65 GRTQSPIDIVPVITAFGEHLQNAHFEVTYESTGEFKAVNDGNSIWL-MREGNSSELAISFLPEeQYHLDAVNFHWATEPM 143
Cdd:pfam00194  15 GKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNTLTNNGHTVQVsLDDGDPSTISGGPLAT-RYRLVQFHFHWGSTDS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323   144 NGSEHTIGGVGYAGEMHLIHRNTRFATMADALKQPNGVIAIAVFLNESHDDNAVFSPLINLLPQVIYKGSECKLCSFDFQ 223
Cdd:pfam00194  94 RGSEHTIDGKRYPAELHIVHYNSKYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALDNIKYKGKSVLLPPFDLS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323   224 TFFPvaEKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVragRYDEEFSDKVPMKPL-RPIQNPSSRTI 302
Cdd:pfam00194 174 DLLP--EDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTL---LFSDGGEEPRPLVNNfRPTQPLNGRVV 248

                  ....
gi 17509323   303 QSSF 306
Cdd:pfam00194 249 FASF 252
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
63-305 2.56e-30

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 114.98  E-value: 2.56e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  63 SLGRTQSPIDIVPVITAFGEHLQnahfeVTYESTGeFKAVNDGNSIWL-MREGNSSELAisflpEEQYHLDAVNFHwatE 141
Cdd:COG3338  50 ATGKNQSPIDIRTAIKADLPPLK-----FDYKPTP-LEIVNNGHTIQVnVDPGSTLTVD-----GKRYELKQFHFH---T 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 142 PmngSEHTIGGVGYAGEMHLIHRNtrfatmadalkqPNGVIA-IAVFLNEShDDNAVFSPLINLLPQViyKGSECKL-CS 219
Cdd:COG3338 116 P---SEHTINGKSYPMEAHLVHKD------------ADGELAvVGVLFEEG-AENPALAKLWANLPLE--AGEEVALdAT 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 220 FDFQTFFPvaeKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVRAGRYdeefsdkvpmkplRPIQNPSS 299
Cdd:COG3338 178 IDLNDLLP---EDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARLYPNNA-------------RPVQPLNG 241

                ....*.
gi 17509323 300 RTIQSS 305
Cdd:COG3338 242 RLILES 247
PLN02202 PLN02202
carbonate dehydratase
63-291 3.77e-08

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 53.52  E-value: 3.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323   63 SLGRTQSPIDIVPVITAFGEHLQNAHFEVTYESTGEFKAVndGNSIWLMREGNSSELaisfLPEEQYHLdaVNFHWATEp 142
Cdd:PLN02202  53 AVGKLQSPIDIQRRQIFYNHKLESIHRDYYFTNATLVNHV--CNVAMFFGEGAGDVI----IDNKNYTL--LQMHWHTP- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  143 mngSEHTIGGVGYAGEMHLIH--RNTRFATMADALKqpngVIAIAVFLNESHDDnavfspLINLLPQViYKGSECKLCSF 220
Cdd:PLN02202 124 ---SEHHLHGVQYAAELHMVHqaKDGSFAVVASLFK----IGTEEPFLSQMKDK------LVKLKEER-FKGNHTAQVEV 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17509323  221 DFQTFFPVAEKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREvragRYDEEFSDKV-PMKPL 291
Cdd:PLN02202 190 GKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRS----PLDKSFKNNSrPCQPL 257
 
Name Accession Description Interval E-value
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
56-304 7.66e-118

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: 339.72  E-value: 7.66e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  56 GKVLNVPSLGRTQSPIDIVP--VITAFGehLQNAHFEVTYESTGEFKAVNDGNSIWLMREGNSSELAISFLP-EEQYHLD 132
Cdd:cd03122   6 AKKYPACGEGRQQSPIDIVEdtQVQRQG--LQPLHFDGYEELTASTTLENTGKTVILRLEGNSSDPFVSGGPlLGRYKFS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 133 AVNFHWATEPMNGSEHTIGGVGYAGEMHLIHRNTRFATMADALKQPNGVIAIAVFLNESHDDNAVFSPLINLLPQVIYKG 212
Cdd:cd03122  84 EITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEGLRNVSRPG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 213 SECKLCSFDFQTFFPVAekTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVRAGRYDEEFSDKVPMKPLR 292
Cdd:cd03122 164 KEVELPPFPLSDLLPPF--TDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDGVMSGDYLPNNGR 241
                       250
                ....*....|..
gi 17509323 293 PIQNPSSRTIQS 304
Cdd:cd03122 242 PQQPLGSRTVFS 253
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
65-302 3.06e-69

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: 215.22  E-value: 3.06e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  65 GRTQSPIDIVPVITAFGEHLQNAHFevTYESTGEFKAVNDGNSIWLMREGNSSelAISFLP-EEQYHLDAVNFHWATEPM 143
Cdd:cd00326   1 GKRQSPINIVTSAVVYDPSLPPLNF--DYYPTTSLTLVNNGHTVQVNFDDDGG--TLSGGGlPGRYKLVQFHFHWGSENS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 144 NGSEHTIGGVGYAGEMHLIHRNTRFATMaDALKQPNGVIAIAVFLNESHDDNAVFSPLINLLPQVIYKGSECKLCSFDFQ 223
Cdd:cd00326  77 PGSEHTIDGKRYPLELHLVHYNSDYYSS-EAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 224 TFFPvaEKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVRagrydeeFSDKVPMKP-LRPIQNPSSRTI 302
Cdd:cd00326 156 DLLP--SSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLL-------DREGKPLVNnYRPVQPLNGRVV 226
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
63-301 3.41e-68

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: 213.33  E-value: 3.41e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323     63 SLGRTQSPIDIVPVITAFGEHLQNAHFEvtYESTGEFKAVNDGNSIWLMREGNSSELAISFLPEEqYHLDAVNFHWATEP 142
Cdd:smart01057  20 CGGKRQSPIDIVTAEAQYDPSLKPLKLS--YDQPTAKRILNNGHTVQVNFDDDGSTLSGGPLPGR-YRLKQFHFHWGGSD 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323    143 MNGSEHTIGGVGYAGEMHLIHRNTRfATMADALKQPNGVIAIAVFLNESHDDNAVFSPLINLLPQVIYKGSECKLCSFDF 222
Cdd:smart01057  97 SEGSEHTIDGKRFPLELHLVHYNSK-GSFSEAVSKPGGLAVVAVFFKVGAEENPALQAILDHLPLIKYKGQETELTPFDL 175
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17509323    223 QTFFPvaEKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVRAGRYDEEFSDKVpmkplRPIQNPSSRT 301
Cdd:smart01057 176 SSLLP--ASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEPLVNNA-----RPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
65-306 5.05e-58

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 187.09  E-value: 5.05e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323    65 GRTQSPIDIVPVITAFGEHLQNAHFEVTYESTGEFKAVNDGNSIWL-MREGNSSELAISFLPEeQYHLDAVNFHWATEPM 143
Cdd:pfam00194  15 GKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNTLTNNGHTVQVsLDDGDPSTISGGPLAT-RYRLVQFHFHWGSTDS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323   144 NGSEHTIGGVGYAGEMHLIHRNTRFATMADALKQPNGVIAIAVFLNESHDDNAVFSPLINLLPQVIYKGSECKLCSFDFQ 223
Cdd:pfam00194  94 RGSEHTIDGKRYPAELHIVHYNSKYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALDNIKYKGKSVLLPPFDLS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323   224 TFFPvaEKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVragRYDEEFSDKVPMKPL-RPIQNPSSRTI 302
Cdd:pfam00194 174 DLLP--EDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTL---LFSDGGEEPRPLVNNfRPTQPLNGRVV 248

                  ....
gi 17509323   303 QSSF 306
Cdd:pfam00194 249 FASF 252
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
65-306 1.14e-40

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: 141.90  E-value: 1.14e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  65 GRTQSPIDIVPVITAFGEHLQNahFEVTYESTGEFKAVNDGNSIWLMREGNSSELAISFLP-EEQYHLDAVNFHWATEPM 143
Cdd:cd03149   1 GNRQSPIDIVSSEAVYDPKLKP--LSLSYDPCTSLSISNNGHSVMVEFDDSDDKTVITGGPlENPYRLKQFHFHWGAKHG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 144 NGSEHTIGGVGYAGEMHLIHRNTR-FATMADALKQPNGVIAIAVFLnESHDDNAVFSPLINLLPQVIYKGSECKLCSFDF 222
Cdd:cd03149  79 SGSEHTVDGKTFPSELHLVHWNAKkYKSFGEAAAAPDGLAVLGVFL-ETGDEHPGLNRLTDALYMVRFKGTKAQFLDFNP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 223 QTFFPvaeKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVragRYDEEFSDKVPM-KPLRPIQNPSSRT 301
Cdd:cd03149 158 KCLLP---KSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFREL---LFTSEEDQRNHMvNNFRPPQPLKGRT 231

                ....*
gi 17509323 302 IQSSF 306
Cdd:cd03149 232 VRASF 236
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
65-302 1.04e-39

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: 139.33  E-value: 1.04e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  65 GRTQSPIDIVPVITAFGEHLQNAHFEVTYESTGEFKAVNDGNSIwLMREGNSSELAISFLPEE----QYHldavnFHWAT 140
Cdd:cd03117   1 GKRQSPINIVTKKVQYDENLTPFTFTGYDDTTTNWTITNNGHTV-QVTLPDGAKISGGGLPGTykalQFH-----FHWGS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 141 EPMNGSEHTIGGVGYAGEMHLIHRNTRFATMADALKQPNGVIAIAVFLNESHDDNAVFSPLINLLPQVIYKGSECKLCSF 220
Cdd:cd03117  75 NGSPGSEHTIDGERYPMELHIVHIKESYNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 221 DFQTFFPVAEKTKeFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVragrydeEFSDKVPMKPL----RPIQN 296
Cdd:cd03117 155 SLRSLLPSVLLTK-YYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTV-------LFFDTDNGQPMvnnfRPVQP 226

                ....*.
gi 17509323 297 PSSRTI 302
Cdd:cd03117 227 LNGRVV 232
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
65-306 3.40e-39

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: 138.73  E-value: 3.40e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  65 GRTQSPIDIVPVITAFGEHLQnaHFEVTYESTGEFKAVNDGNSIWLMREG--NSSELAISFLPEeQYHLDAVNFHWATEP 142
Cdd:cd03119  25 GDRQSPIDIKTKDAKHDPSLK--PLSVSYDPATAKTILNNGHSFNVEFDDtdDRSVLRGGPLTG-SYRLRQFHFHWGSSD 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 143 MNGSEHTIGGVGYAGEMHLIHRNTRFATMADALKQPNGVIAIAVFLNESHdDNAVFSPLINLLPQVIYKGSECKLCSFDF 222
Cdd:cd03119 102 DHGSEHTVDGVKYAAELHLVHWNSKYGSFGEAAKQPDGLAVVGVFLKVGE-ANPELQKVLDALDSIKTKGKQAPFTNFDP 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 223 QTFFPvaeKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVRAGRYDEEfsdKVPM----KPLRPIQNps 298
Cdd:cd03119 181 SCLLP---ASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEP---PCPMvdnwRPPQPLKG-- 252

                ....*...
gi 17509323 299 sRTIQSSF 306
Cdd:cd03119 253 -RKVRASF 259
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
65-306 3.76e-38

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: 135.51  E-value: 3.76e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  65 GRTQSPIDIVPVITAFGEHLQNAHFeVTYE--STGEFKAVNDGNSIWLMRegnSSELAISFLPEEQYHLDAVNFHW-ATE 141
Cdd:cd03123  14 GKRQSPIDIQTDIVQFDPSLPPLEL-VGYDlpGTEEFTLTNNGHTVQLSL---PPTMHIRGGPGTEYTAAQLHLHWgGRG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 142 PMNGSEHTIGGVGYAGEMHLIHRNT-RFATMADALKQPNGVIAIAVFLNESHDDNAVFSPLINLLPQVIYKGSECKLCSF 220
Cdd:cd03123  90 SLSGSEHTIDGIRFAAELHIVHYNSdKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKYKGQETTVPGF 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 221 DFQTFFPvaEKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVragRYDEEfsDKVPMKPLRPIQNPSSR 300
Cdd:cd03123 170 NVRELLP--EDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLETLENT---LMDTH--NKTLQNNYRATQPLNGR 242

                ....*.
gi 17509323 301 TIQSSF 306
Cdd:cd03123 243 VVEASF 248
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
65-306 3.49e-36

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: 130.46  E-value: 3.49e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  65 GRTQSPIDIVPVITAFGEHLQNAHFeVTYESTG--EFKAVNDGNSIWLMRegnSSELAISFLPEEQYHLDAVNFHWATEP 142
Cdd:cd03150  14 GRFQSPVDIRPHLVAFCPALRPLEL-LGFDLPPspSLRLLNNGHTVQLSL---PSGLRMALGPGQEYRALQLHLHWGAAG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 143 MNGSEHTIGGVGYAGEMHLIHRNTRFATMADALKQPNGVIAIAVFLNESHDDNAVFSPLINLLPQVIYKGSECKLCSFDF 222
Cdd:cd03150  90 RPGSEHTVDGHRFPAEIHVVHLSTAFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEISEEESETVVPGLDV 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 223 QTFFPvaEKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVRAGRYDEEFSdkvpmKPLRPIQNPSSRTI 302
Cdd:cd03150 170 SALLP--SDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHDSRLQ-----LNFRATQPLNGRKI 242

                ....
gi 17509323 303 QSSF 306
Cdd:cd03150 243 EASF 246
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
63-302 4.96e-33

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: 122.52  E-value: 4.96e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  63 SLGRTQSPIDIVPVITAFGEHLQNAHFEVTYESTGEFkaVNDGNSIwLMREGNSSELAISFLP-EEQYHLDAVNFHWATE 141
Cdd:cd03121  16 SKGRRQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGTF--YNTGRHV-SFRPDKDPVVNISGGPlSYRYRLEEIRLHFGRE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 142 PMNGSEHTIGGVGYAGEMHLIHRNTR-FATMADALKQPNGVIAIAVFLNESHDDNAVFSPLINLL--PQVIYKGSECKLC 218
Cdd:cd03121  93 DEQGSEHTVNGQAFPGEVQLIHYNSElYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRDtiTSIRYKGDAYFLQ 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 219 SFDFQTFFPvaeKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVRAGRYDEEFsdkVPMKP-LRPIQNP 297
Cdd:cd03121 173 DLSIELLLP---ETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEK---APMSPnFRPVQPL 246

                ....*
gi 17509323 298 SSRTI 302
Cdd:cd03121 247 NNRPV 251
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
65-306 2.06e-32

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: 120.33  E-value: 2.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  65 GRTQSPIDIVPVITAFgeHLQNAHFEVTYESTGEFKAVNDGNSIWLMREGNSSELAISFLP-EEQYHLDAVNFHWATEPM 143
Cdd:cd03118   1 GTRQSPINIQWRDSVY--DPQLAPLRVSYDPATCLYIWNNGYSFQVEFDDSTDKSGISGGPlENHYRLKQFHFHWGANNE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 144 NGSEHTIGGVGYAGEMHLIHRN-TRFATMADALKQPNGVIAIAVFLNESHDDNAVfSPLINLLPQVIYKGSECKLCSFDF 222
Cdd:cd03118  79 WGSEHTVDGHTYPAELHLVHWNsVKYENFEEAVMEENGLAVIGVFLKLGAHHEGL-QKLVDALPEVRHKDTVVEFNPFDP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 223 QTFFPvaeKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVRAGRYDEEfsDKVPMKPLRPIQNPSSRTI 302
Cdd:cd03118 158 SCLLP---ACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLFTSRGEE--EKVMVNNFRPLQPLMNRKV 232

                ....
gi 17509323 303 QSSF 306
Cdd:cd03118 233 RSSF 236
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
65-306 6.75e-32

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: 119.58  E-value: 6.75e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  65 GRTQSPIDIVPVITAFGEHLQNAHFEVTYESTGEFKAVNDGNSIWLMREgNSSELAISFLPE-EQYHLDAVNFHWATEPM 143
Cdd:cd03120  13 GEYQSPINLNSREARYDPSLLEVRLSPNYVVCRDCEVINDGHTIQIILK-SKSVLSGGPLPQgHEFELAEVRFHWGRENQ 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 144 NGSEHTIGGVGYAGEMHLIHRN-TRFATMADALKQPNGVIAIAVFLnESHDDNAVFSPLINLLPQVIYKGSECKLCSFDF 222
Cdd:cd03120  92 RGSEHTVNFKAFPMELHLIHWNsTLYSSLEEAMGKPHGIAIIALFV-QIGKEHVGLKAVTEILQDIQYKGKSKTIPCFNP 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 223 QTFFPvAEKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVR---AGRYDEEFSDKVPMKPLRPIQNPSS 299
Cdd:cd03120 171 NTLLP-DPLLRDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLRthvKGAELVEGCDGLLGDNFRPTQPLSD 249

                ....*..
gi 17509323 300 RTIQSSF 306
Cdd:cd03120 250 RVIRAAF 256
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
63-305 2.56e-30

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 114.98  E-value: 2.56e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  63 SLGRTQSPIDIVPVITAFGEHLQnahfeVTYESTGeFKAVNDGNSIWL-MREGNSSELAisflpEEQYHLDAVNFHwatE 141
Cdd:COG3338  50 ATGKNQSPIDIRTAIKADLPPLK-----FDYKPTP-LEIVNNGHTIQVnVDPGSTLTVD-----GKRYELKQFHFH---T 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 142 PmngSEHTIGGVGYAGEMHLIHRNtrfatmadalkqPNGVIA-IAVFLNEShDDNAVFSPLINLLPQViyKGSECKL-CS 219
Cdd:COG3338 116 P---SEHTINGKSYPMEAHLVHKD------------ADGELAvVGVLFEEG-AENPALAKLWANLPLE--AGEEVALdAT 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 220 FDFQTFFPvaeKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVRAGRYdeefsdkvpmkplRPIQNPSS 299
Cdd:COG3338 178 IDLNDLLP---EDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARLYPNNA-------------RPVQPLNG 241

                ....*.
gi 17509323 300 RTIQSS 305
Cdd:COG3338 242 RLILES 247
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
65-270 4.75e-29

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: 111.80  E-value: 4.75e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  65 GRTQSPIDIVPVITAFGEHLQNAHFeVTYES-TGEFKAVNDGNSIWL-------MREGNSSElaisflpeeqYHLDAVNF 136
Cdd:cd03125  14 GKRQSPIDIQRREVRFNPSLLQLEL-VGYEKeQGEFTMTNNGHTVQIdlpptmsITTGDGTV----------YTAVQMHF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 137 HW--ATEPMNGSEHTIGGVGYAGEMHLIHRNTRFATMADALKQPNGVIAIAVFLNESHD-DNAVFSPLINLLPQVIYKGS 213
Cdd:cd03125  83 HWggRDSEISGSEHTIDGMRYVAELHIVHYNSKYKSYEEAKDKPDGLAVLAFLYKVGHYaENTYYSDFISKLAKIKYAGQ 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17509323 214 ECKLCSFDFQTFFPvaEKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKL 270
Cdd:cd03125 163 TTTLTSLDVRDMLP--ENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKL 217
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
65-306 9.83e-28

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: 108.39  E-value: 9.83e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  65 GRTQSPIDIVPVITAFGEHLQNAHFE-VTYESTGEFKAVNDGNSIWLMRegnSSELAISFLPEE----QYHLdavnfHWA 139
Cdd:cd03126  14 GVAQSPIDIHTDILQYDSSLPPLEFHgYNVSGTEQFTLTNNGHTVQLSL---PPTMHIGGLPFKytasQLHL-----HWG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 140 TE-PMNGSEHTIGGVGYAGEMHLIHRNT-RFATMADALKQPNGVIAIAVFLnESHDDNAVFSPLINLLPQVIYKGSECKL 217
Cdd:cd03126  86 QRgSPEGSEHTISGKHFAAELHIVHYNSdKYPDISTAMNKSQGLAVLGILI-EVGPFNPSYEKIFSHLHEVKYKDQKVSV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 218 CSFDFQTFFPvaEKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREVragRYDEEFSDKVPM-KPLRPIQN 296
Cdd:cd03126 165 PGFNVQELLP--KRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALETA---LYSTEEDESREMvNNYRQVQP 239
                       250
                ....*....|
gi 17509323 297 PSSRTIQSSF 306
Cdd:cd03126 240 FNERLVFASF 249
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
65-273 3.12e-23

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: 95.42  E-value: 3.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  65 GRTQSPIDIVPvITAFGEHLQNAHFEVTYEStgeFKAVNDGNSIWLMREGNSSELAIsflPEEQYHLdaVNFHWATepmn 144
Cdd:cd03124  18 GKNQSPIDITT-KAVVSDKLPPLNYNYKPTS---ATLVNNGHTIQVNFEGNGGTLTI---DGETYQL--LQFHFHS---- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323 145 GSEHTIGGVGYAGEMHLIHRNTrfatmadalkqpNGVIA-IAVFLNEShDDNAVFSPLINLLPQViyKGSECKLCSF-DF 222
Cdd:cd03124  85 PSEHLINGKRYPLEAHLVHKSK------------DGQLAvVAVLFEEG-KENPFLKKILDNMPKK--EGTEVNLPAIlDP 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 17509323 223 QTFFPvaeKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREV 273
Cdd:cd03124 150 NELLP---ESRSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAA 197
PLN02202 PLN02202
carbonate dehydratase
63-291 3.77e-08

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 53.52  E-value: 3.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323   63 SLGRTQSPIDIVPVITAFGEHLQNAHFEVTYESTGEFKAVndGNSIWLMREGNSSELaisfLPEEQYHLdaVNFHWATEp 142
Cdd:PLN02202  53 AVGKLQSPIDIQRRQIFYNHKLESIHRDYYFTNATLVNHV--CNVAMFFGEGAGDVI----IDNKNYTL--LQMHWHTP- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  143 mngSEHTIGGVGYAGEMHLIH--RNTRFATMADALKqpngVIAIAVFLNESHDDnavfspLINLLPQViYKGSECKLCSF 220
Cdd:PLN02202 124 ---SEHHLHGVQYAAELHMVHqaKDGSFAVVASLFK----IGTEEPFLSQMKDK------LVKLKEER-FKGNHTAQVEV 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17509323  221 DFQTFFPVAEKTKEFWMYEGSETTDPFRETVNWIVIRAALPISSHQLDKLREvragRYDEEFSDKV-PMKPL 291
Cdd:PLN02202 190 GKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRS----PLDKSFKNNSrPCQPL 257
PLN02179 PLN02179
carbonic anhydrase
51-260 1.67e-06

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 48.44  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323   51 KLDSLGKVLNVpslGRTQSPIDI----VPVI--TAFGEHLQNAHFEVTyestgefkavNDGNSIWLMREGNSSELAIsfl 124
Cdd:PLN02179  52 KLNPQWKVCST---GKYQSPIDLtderVSLIhdQALSRHYKPAPAVIQ----------SRGHDVMVSWKGDAGKITI--- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509323  125 peEQYHLDAVNFHWATEpmngSEHTIGGVGYAGEMHLIHRNTRFATmadalkqpnGVIAIAVFLNEShddNAVFSPLINL 204
Cdd:PLN02179 116 --HQTDYKLVQCHWHSP----SEHTINGTSYDLELHMVHTSASGKT---------AVVGVLYKLGEP---DEFLTKLLNG 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17509323  205 LPQVIYKgsECKLCSFDFQTffpVAEKTKEFWMYEGSETTDPFRETVNWIVIRAAL 260
Cdd:PLN02179 178 IKGVGKK--EINLGIVDPRD---IRFETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH