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Conserved domains on  [gi|47115606|sp|P61215|]
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RecName: Full=Carbonic anhydrase-related protein 10; AltName: Full=Carbonic anhydrase-related protein X; Short=CA-RP X; Short=CARP X

Protein Classification

carbonic anhydrase family protein( domain architecture ID 10123206)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
46-302 3.26e-172

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: 478.06  E-value: 3.26e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  46 VPSFWGLVNSAWNLCSVGKRQSPVNIETSHMIFDPFLTPLRINTGgRKVSGTMYNTGRHVSLRLDKEHLVNISGGPMTYS 125
Cdd:cd03121   1 GPSFWGLVNSAWNLCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTG-RKVSGTFYNTGRHVSFRPDKDPVVNISGGPLSYR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 126 HRLEEIRLHFGSEDSQGSEHLLNGQAFSGEVQLIHYNHELYTNVTEAAKSPNGLVVVSIFIKVSDSSNPFLNRMLNRDTI 205
Cdd:cd03121  80 YRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRDTI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 206 TRITYKNDAYLLQGLNIEELYPETSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLSQNQPSQIFLSMSDN 285
Cdd:cd03121 160 TSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEKAPMSPN 239
                       250
                ....*....|....*..
gi 47115606 286 FRPVQPLNNRCIRTNIN 302
Cdd:cd03121 240 FRPVQPLNNRPVRTNIN 256
 
Name Accession Description Interval E-value
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
46-302 3.26e-172

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: 478.06  E-value: 3.26e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  46 VPSFWGLVNSAWNLCSVGKRQSPVNIETSHMIFDPFLTPLRINTGgRKVSGTMYNTGRHVSLRLDKEHLVNISGGPMTYS 125
Cdd:cd03121   1 GPSFWGLVNSAWNLCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTG-RKVSGTFYNTGRHVSFRPDKDPVVNISGGPLSYR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 126 HRLEEIRLHFGSEDSQGSEHLLNGQAFSGEVQLIHYNHELYTNVTEAAKSPNGLVVVSIFIKVSDSSNPFLNRMLNRDTI 205
Cdd:cd03121  80 YRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRDTI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 206 TRITYKNDAYLLQGLNIEELYPETSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLSQNQPSQIFLSMSDN 285
Cdd:cd03121 160 TSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEKAPMSPN 239
                       250
                ....*....|....*..
gi 47115606 286 FRPVQPLNNRCIRTNIN 302
Cdd:cd03121 240 FRPVQPLNNRPVRTNIN 256
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
47-301 2.78e-83

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 252.19  E-value: 2.78e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606    47 PSFWGLVnsaWNLCSvGKRQSPVNIETSHMIFDPFLTPLRI-NTGGRKVSGTMYNTGRHVSLRLDKEHLVNISGGPMTYS 125
Cdd:pfam00194   3 PEHWGKV---YPSCG-GKRQSPINIDTRKVRYDPSLPPLTFqGYDVPPGKNTLTNNGHTVQVSLDDGDPSTISGGPLATR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606   126 HRLEEIRLHFGSEDSQGSEHLLNGQAFSGEVQLIHYNhELYTNVTEAAKSPNGLVVVSIFIKVSDSSNPFLNRMLnrDTI 205
Cdd:pfam00194  79 YRLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYN-SKYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIV--SAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606   206 TRITYKNDAYLLQGLNIEELYPE-TSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLSQNQPSQIFLSMSD 284
Cdd:pfam00194 156 DNIKYKGKSVLLPPFDLSDLLPEdLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEPRPLVN 235
                         250
                  ....*....|....*..
gi 47115606   285 NFRPVQPLNNRCIRTNI 301
Cdd:pfam00194 236 NFRPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
33-295 1.52e-78

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: 239.91  E-value: 1.52e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606     33 WAYKEVVQgsfvpvPSFWGLVNSAwnlCSVGKRQSPVNIETSHMIFDPFLTPLRINtGGRKVSGTMYNTGRHVSLRLDKE 112
Cdd:smart01057   1 WGYEGKNG------PEHWGKLDPP---FCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPTAKRILNNGHTVQVNFDDD 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606    113 HlVNISGGPMTYSHRLEEIRLHFGSEDSQGSEHLLNGQAFSGEVQLIHYNHElyTNVTEAAKSPNGLVVVSIFIKVSDSS 192
Cdd:smart01057  71 G-STLSGGPLPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEE 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606    193 NPFLNRMLnrDTITRITYKNDAYLLQGLNIEELYPE-TSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLS 271
Cdd:smart01057 148 NPALQAIL--DHLPLIKYKGQETELTPFDLSSLLPAsTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLL 225
                          250       260
                   ....*....|....*....|....
gi 47115606    272 QNQPSQiflSMSDNFRPVQPLNNR 295
Cdd:smart01057 226 PMEGNE---PLVNNARPLQPLNGR 246
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
47-295 2.58e-33

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 123.07  E-value: 2.58e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  47 PSFWGLVNSAWNLCSVGKRQSPVNIETSHmifDPFLTPLRINtgGRKVSGTMYNTGRHVSLRLDKEHLVNISGgpmtysH 126
Cdd:COG3338  36 PEHWGELSPEFATCATGKNQSPIDIRTAI---KADLPPLKFD--YKPTPLEIVNNGHTIQVNVDPGSTLTVDG------K 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 127 RLEEIRLHFGSedsqGSEHLLNGQAFSGEVQLIHynhelytnvteaaKSPNG-LVVVSIFIKVSDsSNPFLNRMLN---R 202
Cdd:COG3338 105 RYELKQFHFHT----PSEHTINGKSYPMEAHLVH-------------KDADGeLAVVGVLFEEGA-ENPALAKLWAnlpL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 203 DtitrityKNDAYLL-QGLNIEELYPETSSFITYDGSMTIPPCYETASWIIMNKPVYItrmqmhslrllSQNQPSQIFLS 281
Cdd:COG3338 167 E-------AGEEVALdATIDLNDLLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITV-----------SAEQIEAFARL 228
                       250
                ....*....|....
gi 47115606 282 MSDNFRPVQPLNNR 295
Cdd:COG3338 229 YPNNARPVQPLNGR 242
PLN02202 PLN02202
carbonate dehydratase
47-295 1.12e-14

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 73.17  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606   47 PSFWGLVNSAWNLCSVGKRQSPVNIETSHMIFDPfltplRINTGGRK---VSGTMYNTGRHVSLRLDKEhlvniSGGPMT 123
Cdd:PLN02202  39 PNQWGHLNPHFTKCAVGKLQSPIDIQRRQIFYNH-----KLESIHRDyyfTNATLVNHVCNVAMFFGEG-----AGDVII 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  124 YSHRLEEIRLHFGSEdsqgSEHLLNGQAFSGEVQLIHynhelytnvteAAKSPNGLVVVSIFiKVSdSSNPFLNRM---L 200
Cdd:PLN02202 109 DNKNYTLLQMHWHTP----SEHHLHGVQYAAELHMVH-----------QAKDGSFAVVASLF-KIG-TEEPFLSQMkdkL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  201 NRDTITRITYKNDAYLLQG-LNIEELYPETSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRllsqnqpSQIF 279
Cdd:PLN02202 172 VKLKEERFKGNHTAQVEVGkIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLR-------SPLD 244
                        250
                 ....*....|....*.
gi 47115606  280 LSMSDNFRPVQPLNNR 295
Cdd:PLN02202 245 KSFKNNSRPCQPLNGR 260
 
Name Accession Description Interval E-value
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
46-302 3.26e-172

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: 478.06  E-value: 3.26e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  46 VPSFWGLVNSAWNLCSVGKRQSPVNIETSHMIFDPFLTPLRINTGgRKVSGTMYNTGRHVSLRLDKEHLVNISGGPMTYS 125
Cdd:cd03121   1 GPSFWGLVNSAWNLCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTG-RKVSGTFYNTGRHVSFRPDKDPVVNISGGPLSYR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 126 HRLEEIRLHFGSEDSQGSEHLLNGQAFSGEVQLIHYNHELYTNVTEAAKSPNGLVVVSIFIKVSDSSNPFLNRMLNRDTI 205
Cdd:cd03121  80 YRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRDTI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 206 TRITYKNDAYLLQGLNIEELYPETSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLSQNQPSQIFLSMSDN 285
Cdd:cd03121 160 TSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEKAPMSPN 239
                       250
                ....*....|....*..
gi 47115606 286 FRPVQPLNNRCIRTNIN 302
Cdd:cd03121 240 FRPVQPLNNRPVRTNIN 256
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
63-298 2.82e-85

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: 256.44  E-value: 2.82e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  63 GKRQSPVNIETSHMIFDPFLTPLRINtGGRKVSGTMYNTGRHVSLRLDKEhLVNISGGPMTYSHRLEEIRLHFGSEDSQG 142
Cdd:cd00326   1 GKRQSPINIVTSAVVYDPSLPPLNFD-YYPTTSLTLVNNGHTVQVNFDDD-GGTLSGGGLPGRYKLVQFHFHWGSENSPG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 143 SEHLLNGQAFSGEVQLIHYNHELYTNvtEAAKSPNGLVVVSIFIKVSDSSNPFLNRMLnrDTITRITYKNDAYLLQGLNI 222
Cdd:cd00326  79 SEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKENPFLKKIL--DALPKIKYKGKETTLPPFDL 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47115606 223 EELYPE-TSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLSQNQPSqiflSMSDNFRPVQPLNNRCIR 298
Cdd:cd00326 155 SDLLPSsLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDREGK----PLVNNYRPVQPLNGRVVY 227
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
47-301 2.78e-83

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 252.19  E-value: 2.78e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606    47 PSFWGLVnsaWNLCSvGKRQSPVNIETSHMIFDPFLTPLRI-NTGGRKVSGTMYNTGRHVSLRLDKEHLVNISGGPMTYS 125
Cdd:pfam00194   3 PEHWGKV---YPSCG-GKRQSPINIDTRKVRYDPSLPPLTFqGYDVPPGKNTLTNNGHTVQVSLDDGDPSTISGGPLATR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606   126 HRLEEIRLHFGSEDSQGSEHLLNGQAFSGEVQLIHYNhELYTNVTEAAKSPNGLVVVSIFIKVSDSSNPFLNRMLnrDTI 205
Cdd:pfam00194  79 YRLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYN-SKYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIV--SAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606   206 TRITYKNDAYLLQGLNIEELYPE-TSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLSQNQPSQIFLSMSD 284
Cdd:pfam00194 156 DNIKYKGKSVLLPPFDLSDLLPEdLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEPRPLVN 235
                         250
                  ....*....|....*..
gi 47115606   285 NFRPVQPLNNRCIRTNI 301
Cdd:pfam00194 236 NFRPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
33-295 1.52e-78

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: 239.91  E-value: 1.52e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606     33 WAYKEVVQgsfvpvPSFWGLVNSAwnlCSVGKRQSPVNIETSHMIFDPFLTPLRINtGGRKVSGTMYNTGRHVSLRLDKE 112
Cdd:smart01057   1 WGYEGKNG------PEHWGKLDPP---FCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPTAKRILNNGHTVQVNFDDD 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606    113 HlVNISGGPMTYSHRLEEIRLHFGSEDSQGSEHLLNGQAFSGEVQLIHYNHElyTNVTEAAKSPNGLVVVSIFIKVSDSS 192
Cdd:smart01057  71 G-STLSGGPLPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEE 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606    193 NPFLNRMLnrDTITRITYKNDAYLLQGLNIEELYPE-TSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLS 271
Cdd:smart01057 148 NPALQAIL--DHLPLIKYKGQETELTPFDLSSLLPAsTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLL 225
                          250       260
                   ....*....|....*....|....
gi 47115606    272 QNQPSQiflSMSDNFRPVQPLNNR 295
Cdd:smart01057 226 PMEGNE---PLVNNARPLQPLNGR 246
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
63-298 7.62e-52

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: 171.85  E-value: 7.62e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  63 GKRQSPVNIETSHMIFDPFLTPLRI--NTGGRKvsgTMYNTGRhvSLRLDKEHLVNIS---GGPMTYSHRLEEIRLHFGS 137
Cdd:cd03119  25 GDRQSPIDIKTKDAKHDPSLKPLSVsyDPATAK---TILNNGH--SFNVEFDDTDDRSvlrGGPLTGSYRLRQFHFHWGS 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 138 EDSQGSEHLLNGQAFSGEVQLIHYNHElYTNVTEAAKSPNGLVVVSIFIKVSdSSNPFLNRMLnrDTITRITYKNDAYLL 217
Cdd:cd03119 100 SDDHGSEHTVDGVKYAAELHLVHWNSK-YGSFGEAAKQPDGLAVVGVFLKVG-EANPELQKVL--DALDSIKTKGKQAPF 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 218 QGLNIEELYPETSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLSQNQPSQIFLSMSDNFRPVQPLNNRCI 297
Cdd:cd03119 176 TNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEPPCPMVDNWRPPQPLKGRKV 255

                .
gi 47115606 298 R 298
Cdd:cd03119 256 R 256
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
63-298 1.42e-51

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: 170.40  E-value: 1.42e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  63 GKRQSPVNIETSHMIFDPFLTPLRINTGGrKVSGTMYNTGRHVSLRLDK--EHLVnISGGPMTYSHRLEEIRLHFGSEDS 140
Cdd:cd03149   1 GNRQSPIDIVSSEAVYDPKLKPLSLSYDP-CTSLSISNNGHSVMVEFDDsdDKTV-ITGGPLENPYRLKQFHFHWGAKHG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 141 QGSEHLLNGQAFSGEVQLIHYNHELYTNVTEAAKSPNGLVVVSIFIKVSDsSNPFLNRMlnRDTITRITYKNDAYLLQGL 220
Cdd:cd03149  79 SGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETGD-EHPGLNRL--TDALYMVRFKGTKAQFLDF 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47115606 221 NIEELYPETSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLSQNQPSQIFLSMSDNFRPVQPLNNRCIR 298
Cdd:cd03149 156 NPKCLLPKSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHMVNNFRPPQPLKGRTVR 233
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
63-300 3.48e-49

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: 164.79  E-value: 3.48e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  63 GKRQSPVNIETSHMIFDPFLTPLRINtgGRKVSG----TMYNTGRHVSLRLDKEhlVNISGGPMTySHRLEEIRLHFGSE 138
Cdd:cd03123  14 GKRQSPIDIQTDIVQFDPSLPPLELV--GYDLPGteefTLTNNGHTVQLSLPPT--MHIRGGPGT-EYTAAQLHLHWGGR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 139 DSQ-GSEHLLNGQAFSGEVQLIHYNHELYTNVTEAAKSPNGLVVVSIFIKVSDSSNPFLNRMLNRdtITRITYKNDAYLL 217
Cdd:cd03123  89 GSLsGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISH--LHEIKYKGQETTV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 218 QGLNIEELYPE-TSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLR--LLSQNQpsqifLSMSDNFRPVQPLNN 294
Cdd:cd03123 167 PGFNVRELLPEdLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLETLEntLMDTHN-----KTLQNNYRATQPLNG 241

                ....*.
gi 47115606 295 RCIRTN 300
Cdd:cd03123 242 RVVEAS 247
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
63-295 1.08e-48

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: 162.82  E-value: 1.08e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  63 GKRQSPVNIETSHMIFDPFLTPLR-INTGGRKVSGTMYNTGRHVSLRLDKehLVNISGG--PMTYshRLEEIRLHFGSED 139
Cdd:cd03117   1 GKRQSPINIVTKKVQYDENLTPFTfTGYDDTTTNWTITNNGHTVQVTLPD--GAKISGGglPGTY--KALQFHFHWGSNG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 140 SQGSEHLLNGQAFSGEVQLIHYNhELYTNVTEAAKSPNGLVVVSIFIKVSDSSNPFLNRMLNrdTITRITYKNDAYLLQG 219
Cdd:cd03117  77 SPGSEHTIDGERYPMELHIVHIK-ESYNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLIS--ALSNIPQKGGSTNLTP 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47115606 220 LNIEELYP--ETSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLSQNQPSQIFLsMSDNFRPVQPLNNR 295
Cdd:cd03117 154 FSLRSLLPsvLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNGQP-MVNNFRPVQPLNGR 230
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
63-297 1.72e-47

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: 160.39  E-value: 1.72e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  63 GKRQSPVNIETSHMIFDPFLTPLRINtgGRKVSGT----MYNTGRHVSLRLDKEhlVNISGGPMTYShrLEEIRLHFGSE 138
Cdd:cd03126  14 GVAQSPIDIHTDILQYDSSLPPLEFH--GYNVSGTeqftLTNNGHTVQLSLPPT--MHIGGLPFKYT--ASQLHLHWGQR 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 139 DSQ-GSEHLLNGQAFSGEVQLIHYNHELYTNVTEAAKSPNGLVVVSIFIKVSdSSNPFLNRMLNRdtITRITYKNDAYLL 217
Cdd:cd03126  88 GSPeGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVG-PFNPSYEKIFSH--LHEVKYKDQKVSV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 218 QGLNIEELYPE-TSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLSQNQPSQIFLSMSDNFRPVQPLNNRC 296
Cdd:cd03126 165 PGFNVQELLPKrLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALETALYSTEEDESREMVNNYRQVQPFNERL 244

                .
gi 47115606 297 I 297
Cdd:cd03126 245 V 245
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
63-300 1.55e-45

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: 155.00  E-value: 1.55e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  63 GKRQSPVNIETSHMIFDPFLTPLRINTGGRKVSgTMYNTGRHVSLRLDKE-HLVNISGGPMTYSHRLEEIRLHFGSEDSQ 141
Cdd:cd03118   1 GTRQSPINIQWRDSVYDPQLAPLRVSYDPATCL-YIWNNGYSFQVEFDDStDKSGISGGPLENHYRLKQFHFHWGANNEW 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 142 GSEHLLNGQAFSGEVQLIHYNHELYTNVTEAAKSPNGLVVVSIFIKVSdSSNPFLNRMLnrDTITRITYKNDAYLLQGLN 221
Cdd:cd03118  80 GSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLG-AHHEGLQKLV--DALPEVRHKDTVVEFNPFD 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47115606 222 IEELYPETSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLSQNQPSQIFLSMSDNFRPVQPLNNRCIRTN 300
Cdd:cd03118 157 PSCLLPACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLFTSRGEEEKVMVNNFRPLQPLMNRKVRSS 235
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
47-295 2.62e-44

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: 152.12  E-value: 2.62e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  47 PSFWGLVNSAwnlCSVGKRQSPVNIETSHMIFDPFLTPLRINTGGRKVSGT-MYNTGRHVSLRLDKEHLV-NISGGPMTY 124
Cdd:cd03122   2 PKHWAKKYPA---CGEGRQQSPIDIVEDTQVQRQGLQPLHFDGYEELTASTtLENTGKTVILRLEGNSSDpFVSGGPLLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 125 SHRLEEIRLHFGSEDSQGSEHLLNGQAFSGEVQLIHYNHELYTNVtEAAKSPNGLVVVSIFIKVSDSSNPFLNRMLnrDT 204
Cdd:cd03122  79 RYKFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDSF-EAIKSPGGVLALAYLFELSHEDNPFLDPII--EG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 205 ITRITYKN-----DAYLLQGLnieeLYPETSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLSQNQPSQIF 279
Cdd:cd03122 156 LRNVSRPGkevelPPFPLSDL----LPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDGVM 231
                       250
                ....*....|....*...
gi 47115606 280 L--SMSDNFRPVQPLNNR 295
Cdd:cd03122 232 SgdYLPNNGRPQQPLGSR 249
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
47-295 2.54e-40

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: 140.48  E-value: 2.54e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  47 PSFWGLVNSAWNLCSVGKRQSPVNIETSHMIFDPfLTPLRINtgGRKVSGTMYNTGRHVSLRLDKEhlvnisGGPMTY-S 125
Cdd:cd03124   2 PEHWGNLDPEFALCATGKNQSPIDITTKAVVSDK-LPPLNYN--YKPTSATLVNNGHTIQVNFEGN------GGTLTIdG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 126 HRLEEIRLHFGSedsqGSEHLLNGQAFSGEVQLIHYNHElytnvteaakspNGLVVVSIFIKVsDSSNPFLNRMLNRdti 205
Cdd:cd03124  73 ETYQLLQFHFHS----PSEHLINGKRYPLEAHLVHKSKD------------GQLAVVAVLFEE-GKENPFLKKILDN--- 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 206 TRITYKNDAYLLQGLNIEELYPETSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLlsqnqpsqifLSMSDN 285
Cdd:cd03124 133 MPKKEGTEVNLPAILDPNELLPESRSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRA----------AVYPNN 202
                       250
                ....*....|
gi 47115606 286 FRPVQPLNNR 295
Cdd:cd03124 203 ARPVQPLNGR 212
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
50-298 3.07e-38

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: 136.52  E-value: 3.07e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  50 WGLVNSAWNlcsvGKRQSPVNIETSHMIFDPFLTPLRINTG---GRKVSgtMYNTGRHVSLRLDKEHLVniSGGPMTYSH 126
Cdd:cd03120   4 WGLLFPEAN----GEYQSPINLNSREARYDPSLLEVRLSPNyvvCRDCE--VINDGHTIQIILKSKSVL--SGGPLPQGH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 127 RLE--EIRLHFGSEDSQGSEHLLNGQAFSGEVQLIHYNHELYTNVTEAAKSPNGLVVVSIFIKVSDSSnpfLNRMLNRDT 204
Cdd:cd03120  76 EFElaEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIGKEH---VGLKAVTEI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 205 ITRITYKNDAYLLQGLNIEELYPET--SSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLsQNQPSQIFLS- 281
Cdd:cd03120 153 LQDIQYKGKSKTIPCFNPNTLLPDPllRDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRL-RTHVKGAELVe 231
                       250       260
                ....*....|....*....|..
gi 47115606 282 -----MSDNFRPVQPLNNRCIR 298
Cdd:cd03120 232 gcdglLGDNFRPTQPLSDRVIR 253
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
63-300 4.11e-38

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: 135.85  E-value: 4.11e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  63 GKRQSPVNIETSHMIFDPFLTPLRINtgGRKVSG----TMYNTGRHVSLRLDKEhlVNISGGPmTYSHRLEEIRLHFGSE 138
Cdd:cd03150  14 GRFQSPVDIRPHLVAFCPALRPLELL--GFDLPPspslRLLNNGHTVQLSLPSG--LRMALGP-GQEYRALQLHLHWGAA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 139 DSQGSEHLLNGQAFSGEVQLIHYNHElYTNVTEAAKSPNGLVVVSIFIKVSDSSNPFLNRMLNRdtITRITYKNDAYLLQ 218
Cdd:cd03150  89 GRPGSEHTVDGHRFPAEIHVVHLSTA-FANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSR--LSEISEEESETVVP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 219 GLNIEELYPET-SSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRlLSQNQPSQIFLSMsdNFRPVQPLNNRCI 297
Cdd:cd03150 166 GLDVSALLPSDlSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLS-DSLWGPHDSRLQL--NFRATQPLNGRKI 242

                ...
gi 47115606 298 RTN 300
Cdd:cd03150 243 EAS 245
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
47-295 2.58e-33

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 123.07  E-value: 2.58e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  47 PSFWGLVNSAWNLCSVGKRQSPVNIETSHmifDPFLTPLRINtgGRKVSGTMYNTGRHVSLRLDKEHLVNISGgpmtysH 126
Cdd:COG3338  36 PEHWGELSPEFATCATGKNQSPIDIRTAI---KADLPPLKFD--YKPTPLEIVNNGHTIQVNVDPGSTLTVDG------K 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 127 RLEEIRLHFGSedsqGSEHLLNGQAFSGEVQLIHynhelytnvteaaKSPNG-LVVVSIFIKVSDsSNPFLNRMLN---R 202
Cdd:COG3338 105 RYELKQFHFHT----PSEHTINGKSYPMEAHLVH-------------KDADGeLAVVGVLFEEGA-ENPALAKLWAnlpL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 203 DtitrityKNDAYLL-QGLNIEELYPETSSFITYDGSMTIPPCYETASWIIMNKPVYItrmqmhslrllSQNQPSQIFLS 281
Cdd:COG3338 167 E-------AGEEVALdATIDLNDLLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITV-----------SAEQIEAFARL 228
                       250
                ....*....|....
gi 47115606 282 MSDNFRPVQPLNNR 295
Cdd:COG3338 229 YPNNARPVQPLNGR 242
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
63-300 7.86e-31

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: 116.81  E-value: 7.86e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  63 GKRQSPVNIETSHMIFDPFLTPLR-INTGGRKVSGTMYNTGRHVSLRLDKEHLVNISGGPMtysHRLEEIRLHFGSEDSQ 141
Cdd:cd03125  14 GKRQSPIDIQRREVRFNPSLLQLElVGYEKEQGEFTMTNNGHTVQIDLPPTMSITTGDGTV---YTAVQMHFHWGGRDSE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 142 --GSEHLLNGQAFSGEVQLIHYNHElYTNVTEAAKSPNGLVVVSIFIKVSDS-SNPFLNRMLNRdtITRITYKNDAYLLQ 218
Cdd:cd03125  91 isGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLYKVGHYaENTYYSDFISK--LAKIKYAGQTTTLT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606 219 GLNIEELYPET-SSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLR--LLSQNQPsqiflSMSDNFRPVQPLNNR 295
Cdd:cd03125 168 SLDVRDMLPENlHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLEntLMDHHNK-----TIRNDYRRTQPLNHR 242

                ....*
gi 47115606 296 CIRTN 300
Cdd:cd03125 243 VVEAN 247
PLN02202 PLN02202
carbonate dehydratase
47-295 1.12e-14

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 73.17  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606   47 PSFWGLVNSAWNLCSVGKRQSPVNIETSHMIFDPfltplRINTGGRK---VSGTMYNTGRHVSLRLDKEhlvniSGGPMT 123
Cdd:PLN02202  39 PNQWGHLNPHFTKCAVGKLQSPIDIQRRQIFYNH-----KLESIHRDyyfTNATLVNHVCNVAMFFGEG-----AGDVII 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  124 YSHRLEEIRLHFGSEdsqgSEHLLNGQAFSGEVQLIHynhelytnvteAAKSPNGLVVVSIFiKVSdSSNPFLNRM---L 200
Cdd:PLN02202 109 DNKNYTLLQMHWHTP----SEHHLHGVQYAAELHMVH-----------QAKDGSFAVVASLF-KIG-TEEPFLSQMkdkL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  201 NRDTITRITYKNDAYLLQG-LNIEELYPETSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRllsqnqpSQIF 279
Cdd:PLN02202 172 VKLKEERFKGNHTAQVEVGkIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLR-------SPLD 244
                        250
                 ....*....|....*.
gi 47115606  280 LSMSDNFRPVQPLNNR 295
Cdd:PLN02202 245 KSFKNNSRPCQPLNGR 260
PLN02179 PLN02179
carbonic anhydrase
47-258 6.77e-12

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 64.23  E-value: 6.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606   47 PSFWGLVNSAWNLCSVGKRQSPVNI--ETSHMIFDPFLTplrinTGGRKVSGTMYNTGRHVSLRLDKEhlvnisGGPMT- 123
Cdd:PLN02179  47 PAEWGKLNPQWKVCSTGKYQSPIDLtdERVSLIHDQALS-----RHYKPAPAVIQSRGHDVMVSWKGD------AGKITi 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47115606  124 YSHRLEEIRLHFGSEdsqgSEHLLNGQAFSGEVQLIHynhelytnvTEAAKSPnglVVVSIFIKVSDSsNPFLNRMLNrd 203
Cdd:PLN02179 116 HQTDYKLVQCHWHSP----SEHTINGTSYDLELHMVH---------TSASGKT---AVVGVLYKLGEP-DEFLTKLLN-- 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 47115606  204 TITRITYKNdaYLLQGLNIEELYPETSSFITYDGSMTIPPCYETASWIIMNKPVY 258
Cdd:PLN02179 177 GIKGVGKKE--INLGIVDPRDIRFETNNFYRYIGSLTIPPCTEGVIWTVVKRVVW 229
 
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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