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Conserved domains on  [gi|1622895669|ref|XP_028695079|]
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carbonic anhydrase-related protein 11 isoform X3 [Macaca mulatta]

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 ...
7-268 1.80e-148

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: 419.13  E-value: 1.80e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   7 PPFWGLVNAAWSLCAVGKRQSPVDVELKRVLYDPFLPPLRLSTGgekllplPQLRGTLYNTGRHVSFLPAPRPVVNVSGG 86
Cdd:cd03121     2 PSFWGLVNSAWNLCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTG-------RKVSGTFYNTGRHVSFRPDKDPVVNISGG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  87 PLLYSHRLSELRLLFGARDGAGSEHQINHQGFSAEVQLIHFNQELYGNFSAASRSPNGLAILSLFVNVAGSSNPFLSRLL 166
Cdd:cd03121    75 PLSYRYRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 167 NRDTITRISYKNDAYFLQDLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQ 246
Cdd:cd03121   155 NRDTITSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEKA 234
                         250       260
                  ....*....|....*....|..
gi 1622895669 247 SLSGNGRPLQPLAHRALRGNRD 268
Cdd:cd03121   235 PMSPNFRPVQPLNNRPVRTNIN 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 ...
7-268 1.80e-148

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: 419.13  E-value: 1.80e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   7 PPFWGLVNAAWSLCAVGKRQSPVDVELKRVLYDPFLPPLRLSTGgekllplPQLRGTLYNTGRHVSFLPAPRPVVNVSGG 86
Cdd:cd03121     2 PSFWGLVNSAWNLCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTG-------RKVSGTFYNTGRHVSFRPDKDPVVNISGG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  87 PLLYSHRLSELRLLFGARDGAGSEHQINHQGFSAEVQLIHFNQELYGNFSAASRSPNGLAILSLFVNVAGSSNPFLSRLL 166
Cdd:cd03121    75 PLSYRYRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 167 NRDTITRISYKNDAYFLQDLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQ 246
Cdd:cd03121   155 NRDTITSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEKA 234
                         250       260
                  ....*....|....*....|..
gi 1622895669 247 SLSGNGRPLQPLAHRALRGNRD 268
Cdd:cd03121   235 PMSPNFRPVQPLNNRPVRTNIN 256
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
7-264 1.89e-63

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 202.50  E-value: 1.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   7 PPFWGLVnaaWSLCAvGKRQSPVDVELKRVLYDPFLPPLRLStggekLLPLPQLRGTLYNTGRHVSFLPAPRPVVNVSGG 86
Cdd:pfam00194   3 PEHWGKV---YPSCG-GKRQSPINIDTRKVRYDPSLPPLTFQ-----GYDVPPGKNTLTNNGHTVQVSLDDGDPSTISGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  87 PLLYSHRLSELRLLFGARDGAGSEHQINHQGFSAEVQLIHFNQElYGNFSAASRSPNGLAILSLFVNVAGSSNPFLSRLL 166
Cdd:pfam00194  74 PLATRYRLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNSK-YKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 167 nrDTITRISYKNDAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIF 245
Cdd:pfam00194 153 --SALDNIKYKGKSVLLPPFDLSDLLPEDLTsYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEP 230
                         250
                  ....*....|....*....
gi 1622895669 246 QSLSGNGRPLQPLAHRALR 264
Cdd:pfam00194 231 RPLVNNFRPTQPLNGRVVF 249
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
7-261 5.52e-60

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: 193.30  E-value: 5.52e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669    7 PPFWGLVNAAwslCAVGKRQSPVDVELKRVLYDPFLPPLRLSTGgekllplPQLRGTLYNTGRHVSF-LPAPRPVVnvSG 85
Cdd:smart01057   9 PEHWGKLDPP---FCGGKRQSPIDIVTAEAQYDPSLKPLKLSYD-------QPTAKRILNNGHTVQVnFDDDGSTL--SG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   86 GPLLYSHRLSELRLLFGARDGAGSEHQINHQGFSAEVQLIHFNQElyGNFSAASRSPNGLAILSLFVNVAGSSNPFLSRL 165
Cdd:smart01057  77 GPLPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQAI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  166 LnrDTITRISYKNDAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSqi 244
Cdd:smart01057 155 L--DHLPLIKYKGQETELTPFDLSSLLPASTRhYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN-- 230
                          250
                   ....*....|....*..
gi 1622895669  245 fQSLSGNGRPLQPLAHR 261
Cdd:smart01057 231 -EPLVNNARPLQPLNGR 246
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
7-261 7.28e-26

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 103.81  E-value: 7.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   7 PPFWGLVNAAWSLCAVGKRQSPVDVelkRVLYDPFLPPLRLS--TGGEKLLplpqlrgtlyNTGRHVSFLPAPRPVVNVS 84
Cdd:COG3338    36 PEHWGELSPEFATCATGKNQSPIDI---RTAIKADLPPLKFDykPTPLEIV----------NNGHTIQVNVDPGSTLTVD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  85 GGP--LLYSHrlselrllFGArdgaGSEHQINHQGFSAEVQLIHfnqelygnfsaasRSPNG-LAILSLFVnVAGSSNPF 161
Cdd:COG3338   103 GKRyeLKQFH--------FHT----PSEHTINGKSYPMEAHLVH-------------KDADGeLAVVGVLF-EEGAENPA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 162 LSRLLN---RDtitrisyKNDAYFLQD-LSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMhslrlls 237
Cdd:COG3338   157 LAKLWAnlpLE-------AGEEVALDAtIDLNDLLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQI------- 222
                         250       260
                  ....*....|....*....|....*
gi 1622895669 238 qnppsQIFQSL-SGNGRPLQPLAHR 261
Cdd:COG3338   223 -----EAFARLyPNNARPVQPLNGR 242
PLN02202 PLN02202
carbonate dehydratase
7-278 2.36e-12

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 66.62  E-value: 2.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   7 PPFWGLVNAAWSLCAVGKRQSPVDVELKRVLYDPFLPPLRLSTGGEKllplpqlrGTLYNTGRHVSFL---PAPRPVVNV 83
Cdd:PLN02202   39 PNQWGHLNPHFTKCAVGKLQSPIDIQRRQIFYNHKLESIHRDYYFTN--------ATLVNHVCNVAMFfgeGAGDVIIDN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  84 SGGPLLYSHRLSElrllfgardgagSEHQINHQGFSAEVQLIHfnQELYGNFSAasrspnglaILSLFVnvAGSSNPFLS 163
Cdd:PLN02202  111 KNYTLLQMHWHTP------------SEHHLHGVQYAAELHMVH--QAKDGSFAV---------VASLFK--IGTEEPFLS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 164 RLLNRDTITRISYKNDAYFLQ----DLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRllsqn 239
Cdd:PLN02202  166 QMKDKLVKLKEERFKGNHTAQvevgKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLR----- 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1622895669 240 ppSQIFQSLSGNGRPLQPLAHRALRGNRDPRHPERRCRG 278
Cdd:PLN02202  241 --SPLDKSFKNNSRPCQPLNGRRVEMFHDHERVDKKDTG 277
 
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 ...
7-268 1.80e-148

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: 419.13  E-value: 1.80e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   7 PPFWGLVNAAWSLCAVGKRQSPVDVELKRVLYDPFLPPLRLSTGgekllplPQLRGTLYNTGRHVSFLPAPRPVVNVSGG 86
Cdd:cd03121     2 PSFWGLVNSAWNLCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTG-------RKVSGTFYNTGRHVSFRPDKDPVVNISGG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  87 PLLYSHRLSELRLLFGARDGAGSEHQINHQGFSAEVQLIHFNQELYGNFSAASRSPNGLAILSLFVNVAGSSNPFLSRLL 166
Cdd:cd03121    75 PLSYRYRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 167 NRDTITRISYKNDAYFLQDLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQ 246
Cdd:cd03121   155 NRDTITSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEKA 234
                         250       260
                  ....*....|....*....|..
gi 1622895669 247 SLSGNGRPLQPLAHRALRGNRD 268
Cdd:cd03121   235 PMSPNFRPVQPLNNRPVRTNIN 256
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
23-261 6.31e-68

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: 213.30  E-value: 6.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  23 GKRQSPVDVELKRVLYDPFLPPLRLStggekllPLPQLRGTLYNTGRHVSFLPAPRPVVnVSGGPLLYSHRLSELRLLFG 102
Cdd:cd00326     1 GKRQSPINIVTSAVVYDPSLPPLNFD-------YYPTTSLTLVNNGHTVQVNFDDDGGT-LSGGGLPGRYKLVQFHFHWG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 103 ARDGAGSEHQINHQGFSAEVQLIHFNQELYGnfSAASRSPNGLAILSLFVNVAGSSNPFLSRLLnrDTITRISYKNDAYF 182
Cdd:cd00326    73 SENSPGSEHTIDGKRYPLELHLVHYNSDYYS--SEAAKKPGGLAVLGVFFEVGEKENPFLKKIL--DALPKIKYKGKETT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 183 LQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPsqifQSLSGNGRPLQPLAHR 261
Cdd:cd00326   149 LPPFDLSDLLPSSLRdYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDREG----KPLVNNYRPVQPLNGR 224
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
7-264 1.89e-63

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 202.50  E-value: 1.89e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   7 PPFWGLVnaaWSLCAvGKRQSPVDVELKRVLYDPFLPPLRLStggekLLPLPQLRGTLYNTGRHVSFLPAPRPVVNVSGG 86
Cdd:pfam00194   3 PEHWGKV---YPSCG-GKRQSPINIDTRKVRYDPSLPPLTFQ-----GYDVPPGKNTLTNNGHTVQVSLDDGDPSTISGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  87 PLLYSHRLSELRLLFGARDGAGSEHQINHQGFSAEVQLIHFNQElYGNFSAASRSPNGLAILSLFVNVAGSSNPFLSRLL 166
Cdd:pfam00194  74 PLATRYRLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNSK-YKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 167 nrDTITRISYKNDAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIF 245
Cdd:pfam00194 153 --SALDNIKYKGKSVLLPPFDLSDLLPEDLTsYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEP 230
                         250
                  ....*....|....*....
gi 1622895669 246 QSLSGNGRPLQPLAHRALR 264
Cdd:pfam00194 231 RPLVNNFRPTQPLNGRVVF 249
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
7-261 5.52e-60

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: 193.30  E-value: 5.52e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669    7 PPFWGLVNAAwslCAVGKRQSPVDVELKRVLYDPFLPPLRLSTGgekllplPQLRGTLYNTGRHVSF-LPAPRPVVnvSG 85
Cdd:smart01057   9 PEHWGKLDPP---FCGGKRQSPIDIVTAEAQYDPSLKPLKLSYD-------QPTAKRILNNGHTVQVnFDDDGSTL--SG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   86 GPLLYSHRLSELRLLFGARDGAGSEHQINHQGFSAEVQLIHFNQElyGNFSAASRSPNGLAILSLFVNVAGSSNPFLSRL 165
Cdd:smart01057  77 GPLPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQAI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  166 LnrDTITRISYKNDAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSqi 244
Cdd:smart01057 155 L--DHLPLIKYKGQETELTPFDLSSLLPASTRhYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN-- 230
                          250
                   ....*....|....*..
gi 1622895669  245 fQSLSGNGRPLQPLAHR 261
Cdd:smart01057 231 -EPLVNNARPLQPLNGR 246
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
21-264 2.70e-47

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: 161.07  E-value: 2.70e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  21 AVGKRQSPVDVELKRVLYDPFLPPLRLSTGgekllplPQLRGTLYNTGR--HVSFLPAPRPVVnVSGGPLLYSHRLSELR 98
Cdd:cd03119    23 AKGDRQSPIDIKTKDAKHDPSLKPLSVSYD-------PATAKTILNNGHsfNVEFDDTDDRSV-LRGGPLTGSYRLRQFH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  99 LLFGARDGAGSEHQINHQGFSAEVQLIHFNQElYGNFSAASRSPNGLAILSLFVNVaGSSNPFLSRLLnrDTITRISYKN 178
Cdd:cd03119    95 FHWGSSDDHGSEHTVDGVKYAAELHLVHWNSK-YGSFGEAAKQPDGLAVVGVFLKV-GEANPELQKVL--DALDSIKTKG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 179 DAYFLQDLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQSLSGNGRPLQPL 258
Cdd:cd03119   171 KQAPFTNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEPPCPMVDNWRPPQPL 250

                  ....*.
gi 1622895669 259 AHRALR 264
Cdd:cd03119   251 KGRKVR 256
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
20-261 5.47e-44

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: 152.08  E-value: 5.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  20 CAvGKRQSPVDVELKRVLYDPFLPPLRLStgGEKLLPLPQLrgTLYNTGRHVSF-LPaprPVVNVSGGP-LLYshRLSEL 97
Cdd:cd03123    12 CG-GKRQSPIDIQTDIVQFDPSLPPLELV--GYDLPGTEEF--TLTNNGHTVQLsLP---PTMHIRGGPgTEY--TAAQL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  98 RLLFGARDGA-GSEHQINHQGFSAEVQLIHFNQELYGNFSAASRSPNGLAILSLFVNVAGSSNP----FLSRLLNrdtit 172
Cdd:cd03123    82 HLHWGGRGSLsGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTyyekIISHLHE----- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 173 rISYKNDAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLR--LLSQNPpsqifQSLS 249
Cdd:cd03123   157 -IKYKGQETTVPGFNVRELLPEDLShYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLETLEntLMDTHN-----KTLQ 230
                         250
                  ....*....|..
gi 1622895669 250 GNGRPLQPLAHR 261
Cdd:cd03123   231 NNYRATQPLNGR 242
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
23-264 4.55e-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: 141.51  E-value: 4.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  23 GKRQSPVDVELKRVLYDPFLPPLRLSTGGEKLLplpqlrgTLYNTGRHVS--FLPAPRPVVnVSGGPLLYSHRLSELRLL 100
Cdd:cd03149     1 GNRQSPIDIVSSEAVYDPKLKPLSLSYDPCTSL-------SISNNGHSVMveFDDSDDKTV-ITGGPLENPYRLKQFHFH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 101 FGARDGAGSEHQINHQGFSAEVQLIHFNQELYGNFSAASRSPNGLAILSLFVNvAGSSNPFLSRLlnRDTITRISYKNDA 180
Cdd:cd03149    73 WGAKHGSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLE-TGDEHPGLNRL--TDALYMVRFKGTK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 181 YFLQDLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQSLSGNGRPLQPLAH 260
Cdd:cd03149   150 AQFLDFNPKCLLPKSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHMVNNFRPPQPLKG 229

                  ....
gi 1622895669 261 RALR 264
Cdd:cd03149   230 RTVR 233
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
23-264 1.23e-39

Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme V. CA V is the mitochondrial isozyme, which may play a role in gluconeogenesis and ureagenesis and possibly also in lipogenesis.


Pssm-ID: 239392  Cd Length: 236  Bit Score: 140.36  E-value: 1.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  23 GKRQSPVDVELKRVLYDPFLPPLRLSTGGEKLLplpqlrgTLYNTGR--HVSFLPAPRPVVnVSGGPLLYSHRLSELRLL 100
Cdd:cd03118     1 GTRQSPINIQWRDSVYDPQLAPLRVSYDPATCL-------YIWNNGYsfQVEFDDSTDKSG-ISGGPLENHYRLKQFHFH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 101 FGARDGAGSEHQINHQGFSAEVQLIHFNQELYGNFSAASRSPNGLAILSLFVNVaGSSNPFLSRLLnrDTITRISYKNDA 180
Cdd:cd03118    73 WGANNEWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKL-GAHHEGLQKLV--DALPEVRHKDTV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 181 YFLQDLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQSLSGNGRPLQPLAH 260
Cdd:cd03118   150 VEFNPFDPSCLLPACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLFTSRGEEEKVMVNNFRPLQPLMN 229

                  ....
gi 1622895669 261 RALR 264
Cdd:cd03118   230 RKVR 233
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
7-261 2.97e-37

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: 134.40  E-value: 2.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   7 PPFWGLVNAAwslCAVGKRQSPVDVELKRVLYDPFLPPLRLSTggeklLPLPQLRGTLYNTGRHVSFLPAPRPVV-NVSG 85
Cdd:cd03122     2 PKHWAKKYPA---CGEGRQQSPIDIVEDTQVQRQGLQPLHFDG-----YEELTASTTLENTGKTVILRLEGNSSDpFVSG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  86 GPLLYSHRLSELRLLFGARDGAGSEHQINHQGFSAEVQLIHFNQELYGNFSAASrSPNGLAILSLFVNVAGSSNPFLSRL 165
Cdd:cd03122    74 GPLLGRYKFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDSFEAIK-SPGGVLALAYLFELSHEDNPFLDPI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 166 LnrDTITRISYKNDAYFLQDLSLELLFPESF-GFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLL--SQNPPS 242
Cdd:cd03122   153 I--EGLRNVSRPGKEVELPPFPLSDLLPPFTdKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELltRRQDGV 230
                         250
                  ....*....|....*....
gi 1622895669 243 QIFQSLSGNGRPLQPLAHR 261
Cdd:cd03122   231 MSGDYLPNNGRPQQPLGSR 249
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
23-261 2.96e-36

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: 131.88  E-value: 2.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  23 GKRQSPVDVELKRVLYDPFLPPLRLStgGEKLLPLPQLrgTLYNTGRHVSF-LPaprPVVNVSGGPLLYShrLSELRLLF 101
Cdd:cd03126    14 GVAQSPIDIHTDILQYDSSLPPLEFH--GYNVSGTEQF--TLTNNGHTVQLsLP---PTMHIGGLPFKYT--ASQLHLHW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 102 GAR-DGAGSEHQINHQGFSAEVQLIHFNQELYGNFSAASRSPNGLAILSLFVNVaGSSNPFLSRLLNRdtITRISYKNDA 180
Cdd:cd03126    85 GQRgSPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEV-GPFNPSYEKIFSH--LHEVKYKDQK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 181 YFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLR--LLS--QNPPSQIFQslsgNGRPL 255
Cdd:cd03126   162 VSVPGFNVQELLPKRLDeYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALEtaLYSteEDESREMVN----NYRQV 237

                  ....*.
gi 1622895669 256 QPLAHR 261
Cdd:cd03126   238 QPFNER 243
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
23-261 1.65e-33

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: 123.92  E-value: 1.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  23 GKRQSPVDVELKRVLYDPFLPPLRLSTGGEkllplPQLRGTLYNTGRHVSF-LPaprPVVNVSGGPLLYSHRLSELRLLF 101
Cdd:cd03117     1 GKRQSPINIVTKKVQYDENLTPFTFTGYDD-----TTTNWTITNNGHTVQVtLP---DGAKISGGGLPGTYKALQFHFHW 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 102 GARDGAGSEHQINHQGFSAEVQLIHFNQElYGNFSAASRSPNGLAILSLFVNVAGSSNPFLSRLLNrdTITRISYKNDAY 181
Cdd:cd03117    73 GSNGSPGSEHTIDGERYPMELHIVHIKES-YNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLIS--ALSNIPQKGGST 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 182 FLQDLSLELLFP--ESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQiFQSLSGNGRPLQPLA 259
Cdd:cd03117   150 NLTPFSLRSLLPsvLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDN-GQPMVNNFRPVQPLN 228

                  ..
gi 1622895669 260 HR 261
Cdd:cd03117   229 GR 230
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
10-265 1.78e-31

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: 119.19  E-value: 1.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  10 WGLVNAAwslcAVGKRQSPVDVELKRVLYDPFLPPLRLSTGgekllpLPQLRGT-LYNTGRHVSFLPAPRPVVnvSGGPL 88
Cdd:cd03120     4 WGLLFPE----ANGEYQSPINLNSREARYDPSLLEVRLSPN------YVVCRDCeVINDGHTIQIILKSKSVL--SGGPL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  89 LYSHR--LSELRLLFGARDGAGSEHQINHQGFSAEVQLIHFNQELYGNFSAASRSPNGLAILSLFVNVaGSSNPFLSRLl 166
Cdd:cd03120    72 PQGHEfeLAEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQI-GKEHVGLKAV- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 167 nRDTITRISYKNDAYFLQDLSLELLFPESF--GFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQN-PPSQ 243
Cdd:cd03120   150 -TEILQDIQYKGKSKTIPCFNPNTLLPDPLlrDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLRTHvKGAE 228
                         250       260
                  ....*....|....*....|....*.
gi 1622895669 244 IFQSLSG----NGRPLQPLAHRALRG 265
Cdd:cd03120   229 LVEGCDGllgdNFRPTQPLSDRVIRA 254
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
7-261 9.15e-31

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: 116.22  E-value: 9.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   7 PPFWGLVNAAWSLCAVGKRQSPVDVELKRVLYDPfLPPLRLSTGGEKLlplpqlrgTLYNTG--RHVSFLP-APRPVVNv 83
Cdd:cd03124     2 PEHWGNLDPEFALCATGKNQSPIDITTKAVVSDK-LPPLNYNYKPTSA--------TLVNNGhtIQVNFEGnGGTLTID- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  84 sggpllySHRLSELRLLFGArdgaGSEHQINHQGFSAEVQLIHFNQElygnfsaasrspNGLAILSLFVnVAGSSNPFLS 163
Cdd:cd03124    72 -------GETYQLLQFHFHS----PSEHLINGKRYPLEAHLVHKSKD------------GQLAVVAVLF-EEGKENPFLK 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 164 RLLNRdtitRISYKNDAYFLQD-LSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLsqnpps 242
Cdd:cd03124   128 KILDN----MPKKEGTEVNLPAiLDPNELLPESRSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAA------ 197
                         250
                  ....*....|....*....
gi 1622895669 243 qifqSLSGNGRPLQPLAHR 261
Cdd:cd03124   198 ----VYPNNARPVQPLNGR 212
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
20-266 4.79e-30

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: 115.27  E-value: 4.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  20 CAvGKRQSPVDVELKRVLYDPFLPPLRLStGGEKllplPQLRGTLYNTGRHVSFLPAPRPVVNVSGGPLlysHRLSELRL 99
Cdd:cd03125    12 CG-GKRQSPIDIQRREVRFNPSLLQLELV-GYEK----EQGEFTMTNNGHTVQIDLPPTMSITTGDGTV---YTAVQMHF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 100 LFGARDG--AGSEHQINHQGFSAEVQLIHFNQElYGNFSAASRSPNGLAILSLFVNVA-GSSNPFLSRLLNRdtITRISY 176
Cdd:cd03125    83 HWGGRDSeiSGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLYKVGhYAENTYYSDFISK--LAKIKY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 177 KNDAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLR--LLSQNPpsqifQSLSGNGR 253
Cdd:cd03125   160 AGQTTTLTSLDVRDMLPENLHhYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLEntLMDHHN-----KTIRNDYR 234
                         250
                  ....*....|...
gi 1622895669 254 PLQPLAHRALRGN 266
Cdd:cd03125   235 RTQPLNHRVVEAN 247
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
20-264 4.95e-30

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: 115.05  E-value: 4.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  20 CAvGKRQSPVDVELKRVLYDPFLPPLRLStgGEKLLPLPQLRgtLYNTGRHVSF-LPaprPVVNVSGGPLlYSHRLSELR 98
Cdd:cd03150    12 CA-GRFQSPVDIRPHLVAFCPALRPLELL--GFDLPPSPSLR--LLNNGHTVQLsLP---SGLRMALGPG-QEYRALQLH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  99 LLFGARDGAGSEHQINHQGFSAEVQLIHFNQElYGNFSAASRSPNGLAILSLFVNVAGSSNPFLSRLLNRdtITRISYKN 178
Cdd:cd03150    83 LHWGAAGRPGSEHTVDGHRFPAEIHVVHLSTA-FANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSR--LSEISEEE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 179 DAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIfqsLSGNGRPLQP 257
Cdd:cd03150   160 SETVVPGLDVSALLPSDLSrYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHDSR---LQLNFRATQP 236

                  ....*..
gi 1622895669 258 LAHRALR 264
Cdd:cd03150   237 LNGRKIE 243
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
7-261 7.28e-26

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 103.81  E-value: 7.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   7 PPFWGLVNAAWSLCAVGKRQSPVDVelkRVLYDPFLPPLRLS--TGGEKLLplpqlrgtlyNTGRHVSFLPAPRPVVNVS 84
Cdd:COG3338    36 PEHWGELSPEFATCATGKNQSPIDI---RTAIKADLPPLKFDykPTPLEIV----------NNGHTIQVNVDPGSTLTVD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  85 GGP--LLYSHrlselrllFGArdgaGSEHQINHQGFSAEVQLIHfnqelygnfsaasRSPNG-LAILSLFVnVAGSSNPF 161
Cdd:COG3338   103 GKRyeLKQFH--------FHT----PSEHTINGKSYPMEAHLVH-------------KDADGeLAVVGVLF-EEGAENPA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 162 LSRLLN---RDtitrisyKNDAYFLQD-LSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMhslrlls 237
Cdd:COG3338   157 LAKLWAnlpLE-------AGEEVALDAtIDLNDLLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQI------- 222
                         250       260
                  ....*....|....*....|....*
gi 1622895669 238 qnppsQIFQSL-SGNGRPLQPLAHR 261
Cdd:COG3338   223 -----EAFARLyPNNARPVQPLNGR 242
PLN02202 PLN02202
carbonate dehydratase
7-278 2.36e-12

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 66.62  E-value: 2.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   7 PPFWGLVNAAWSLCAVGKRQSPVDVELKRVLYDPFLPPLRLSTGGEKllplpqlrGTLYNTGRHVSFL---PAPRPVVNV 83
Cdd:PLN02202   39 PNQWGHLNPHFTKCAVGKLQSPIDIQRRQIFYNHKLESIHRDYYFTN--------ATLVNHVCNVAMFfgeGAGDVIIDN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  84 SGGPLLYSHRLSElrllfgardgagSEHQINHQGFSAEVQLIHfnQELYGNFSAasrspnglaILSLFVnvAGSSNPFLS 163
Cdd:PLN02202  111 KNYTLLQMHWHTP------------SEHHLHGVQYAAELHMVH--QAKDGSFAV---------VASLFK--IGTEEPFLS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 164 RLLNRDTITRISYKNDAYFLQ----DLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRllsqn 239
Cdd:PLN02202  166 QMKDKLVKLKEERFKGNHTAQvevgKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLR----- 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1622895669 240 ppSQIFQSLSGNGRPLQPLAHRALRGNRDPRHPERRCRG 278
Cdd:PLN02202  241 --SPLDKSFKNNSRPCQPLNGRRVEMFHDHERVDKKDTG 277
PLN02179 PLN02179
carbonic anhydrase
7-223 3.44e-10

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 59.61  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669   7 PPFWGLVNAAWSLCAVGKRQSPVDVELKRVlydpflpplrlstggekllplpqlrGTLYNTGRHVSFLPAPrPVVNVSGG 86
Cdd:PLN02179   47 PAEWGKLNPQWKVCSTGKYQSPIDLTDERV-------------------------SLIHDQALSRHYKPAP-AVIQSRGH 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669  87 PLLYSHRLSELRLLFGARD--------GAGSEHQINHQGFSAEVQLIHFnqelygnfSAASRSpnglAILSLFVNVaGSS 158
Cdd:PLN02179  101 DVMVSWKGDAGKITIHQTDyklvqchwHSPSEHTINGTSYDLELHMVHT--------SASGKT----AVVGVLYKL-GEP 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895669 159 NPFLSRLLNrdTITRISYKndayflqDLSLELLFP-----ESFGFITYQGSLSTPPCSETVTWILIDRAL 223
Cdd:PLN02179  168 DEFLTKLLN--GIKGVGKK-------EINLGIVDPrdirfETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 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.
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