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Conserved domains on  [gi|30581031|sp|O70354|]
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RecName: Full=Carbonic anhydrase-related protein 11; AltName: Full=CA-RP XI; Short=CA-XI; Short=CARP XI; AltName: Full=Carbonic anhydrase-related protein 2; Short=CA-RP II; Short=CARP-2; Flags: Precursor

Protein Classification

alpha_CARP_X_XI_like domain-containing protein( domain architecture ID 10123206)

alpha_CARP_X_XI_like domain-containing protein

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 ...
48-304 3.16e-151

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: 424.90  E-value: 3.16e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  48 GPPFWGLVNAAWSLCAVGKRQSPVDVELKRVLYDPFLPPLRLSTGgEKLRGTLYNTGRHVSFLPASRPVVNVSGGPLLYS 127
Cdd:cd03121   1 GPSFWGLVNSAWNLCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTG-RKVSGTFYNTGRHVSFRPDKDPVVNISGGPLSYR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 128 HRLSELRLLFGARDGAGSEHQINHEGFSAEVQLIHFNQELYGNLSAASRGPNGLAILSLFVNVAGSSNPFLSRLLNRDTI 207
Cdd:cd03121  80 YRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRDTI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 208 TRISYKNDAYFLQDLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQSLSGN 287
Cdd:cd03121 160 TSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEKAPMSPN 239
                       250
                ....*....|....*..
gi 30581031 288 GRPLQPLAHRALRGNRD 304
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 ...
48-304 3.16e-151

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: 424.90  E-value: 3.16e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  48 GPPFWGLVNAAWSLCAVGKRQSPVDVELKRVLYDPFLPPLRLSTGgEKLRGTLYNTGRHVSFLPASRPVVNVSGGPLLYS 127
Cdd:cd03121   1 GPSFWGLVNSAWNLCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTG-RKVSGTFYNTGRHVSFRPDKDPVVNISGGPLSYR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 128 HRLSELRLLFGARDGAGSEHQINHEGFSAEVQLIHFNQELYGNLSAASRGPNGLAILSLFVNVAGSSNPFLSRLLNRDTI 207
Cdd:cd03121  80 YRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRDTI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 208 TRISYKNDAYFLQDLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQSLSGN 287
Cdd:cd03121 160 TSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEKAPMSPN 239
                       250
                ....*....|....*..
gi 30581031 288 GRPLQPLAHRALRGNRD 304
Cdd:cd03121 240 FRPVQPLNNRPVRTNIN 256
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
48-300 1.24e-64

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 204.42  E-value: 1.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031    48 GPPFWGLVnaaWSLCAvGKRQSPVDVELKRVLYDPFLPPLRLSTGGEKLRG-TLYNTGRHVSFLPASRPVVNVSGGPLLY 126
Cdd:pfam00194   2 GPEHWGKV---YPSCG-GKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKnTLTNNGHTVQVSLDDGDPSTISGGPLAT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031   127 SHRLSELRLLFGARDGAGSEHQINHEGFSAEVQLIHFNQElYGNLSAASRGPNGLAILSLFVNVAGSSNPFLSRLLnrDT 206
Cdd:pfam00194  78 RYRLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNSK-YKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIV--SA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031   207 ITRISYKNDAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQSLS 285
Cdd:pfam00194 155 LDNIKYKGKSVLLPPFDLSDLLPEDLTsYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEPRPLV 234
                         250
                  ....*....|....*
gi 30581031   286 GNGRPLQPLAHRALR 300
Cdd:pfam00194 235 NNFRPTQPLNGRVVF 249
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
35-297 2.82e-63

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: 201.00  E-value: 2.82e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031     35 WSYKENLqgnfvpGPPFWGLVNAAwslCAVGKRQSPVDVELKRVLYDPFLPPLRLStGGEKLRGTLYNTGR--HVSFLPA 112
Cdd:smart01057   1 WGYEGKN------GPEHWGKLDPP---FCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPTAKRILNNGHtvQVNFDDD 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031    113 SrpvVNVSGGPLLYSHRLSELRLLFGARDGAGSEHQINHEGFSAEVQLIHFNQElyGNLSAASRGPNGLAILSLFVNVAG 192
Cdd:smart01057  71 G---STLSGGPLPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGA 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031    193 SSNPFLSRLLnrDTITRISYKNDAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRL 271
Cdd:smart01057 146 EENPALQAIL--DHLPLIKYKGQETELTPFDLSSLLPASTRhYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRT 223
                          250       260
                   ....*....|....*....|....*.
gi 30581031    272 LSQNPPSqifQSLSGNGRPLQPLAHR 297
Cdd:smart01057 224 LLPMEGN---EPLVNNARPLQPLNGR 246
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
4-297 2.22e-29

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 112.67  E-value: 2.22e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031   4 AARLSAPQALVLWAALGAAAHIGPApdpedwWSYkenlQGNFvpGPPFWGLVNAAWSLCAVGKRQSPVDVelkRVLYDPF 83
Cdd:COG3338   3 KRLLLALLLAAALPAAAAAAASAPH------WSY----EGET--GPEHWGELSPEFATCATGKNQSPIDI---RTAIKAD 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  84 LPPLRLS--TGGEKLRgtlyNTGR--HVSFLPASRpvVNVSGGP--LLYSHrlselrllFgardGAGSEHQINHEGFSAE 157
Cdd:COG3338  68 LPPLKFDykPTPLEIV----NNGHtiQVNVDPGST--LTVDGKRyeLKQFH--------F----HTPSEHTINGKSYPME 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 158 VQLIHfnqelygnlsaasRGPNG-LAILSLFVnVAGSSNPFLSRLLN---RDtitrisyKNDAYFLQD-LSLELLFPESF 232
Cdd:COG3338 130 AHLVH-------------KDADGeLAVVGVLF-EEGAENPALAKLWAnlpLE-------AGEEVALDAtIDLNDLLPEDR 188
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30581031 233 GFITYQGSLSTPPCSETVTWILIDRALNITSLQMhslrllsqnppsQIFQSL-SGNGRPLQPLAHR 297
Cdd:COG3338 189 SYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQI------------EAFARLyPNNARPVQPLNGR 242
PLN02202 PLN02202
carbonate dehydratase
48-314 6.80e-14

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 70.86  E-value: 6.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031   48 GPPFWGLVNAAWSLCAVGKRQSPVDVELKRVLYDPFLPPLRLSTggEKLRGTLYNTGRHVSFL---PASRPVVNVSGGPL 124
Cdd:PLN02202  38 GPNQWGHLNPHFTKCAVGKLQSPIDIQRRQIFYNHKLESIHRDY--YFTNATLVNHVCNVAMFfgeGAGDVIIDNKNYTL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  125 LYSHRLSElrllfgardgagSEHQINHEGFSAEVQLIHfnQELYGNLSAasrgpnglaILSLFVnvAGSSNPFLSRLLNR 204
Cdd:PLN02202 116 LQMHWHTP------------SEHHLHGVQYAAELHMVH--QAKDGSFAV---------VASLFK--IGTEEPFLSQMKDK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  205 DTITRISYKNDAYFLQ----DLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRllsqnppSQI 280
Cdd:PLN02202 171 LVKLKEERFKGNHTAQvevgKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLR-------SPL 243
                        250       260       270
                 ....*....|....*....|....*....|....
gi 30581031  281 FQSLSGNGRPLQPLAHRALRGNRDPRHPERRCRG 314
Cdd:PLN02202 244 DKSFKNNSRPCQPLNGRRVEMFHDHERVDKKDTG 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 ...
48-304 3.16e-151

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: 424.90  E-value: 3.16e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  48 GPPFWGLVNAAWSLCAVGKRQSPVDVELKRVLYDPFLPPLRLSTGgEKLRGTLYNTGRHVSFLPASRPVVNVSGGPLLYS 127
Cdd:cd03121   1 GPSFWGLVNSAWNLCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTG-RKVSGTFYNTGRHVSFRPDKDPVVNISGGPLSYR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 128 HRLSELRLLFGARDGAGSEHQINHEGFSAEVQLIHFNQELYGNLSAASRGPNGLAILSLFVNVAGSSNPFLSRLLNRDTI 207
Cdd:cd03121  80 YRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRDTI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 208 TRISYKNDAYFLQDLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQSLSGN 287
Cdd:cd03121 160 TSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEKAPMSPN 239
                       250
                ....*....|....*..
gi 30581031 288 GRPLQPLAHRALRGNRD 304
Cdd:cd03121 240 FRPVQPLNNRPVRTNIN 256
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
65-297 5.69e-70

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: 217.15  E-value: 5.69e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  65 GKRQSPVDVELKRVLYDPFLPPLRLStGGEKLRGTLYNTGRHVSFLPASRPVVnVSGGPLLYSHRLSELRLLFGARDGAG 144
Cdd:cd00326   1 GKRQSPINIVTSAVVYDPSLPPLNFD-YYPTTSLTLVNNGHTVQVNFDDDGGT-LSGGGLPGRYKLVQFHFHWGSENSPG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 145 SEHQINHEGFSAEVQLIHFNQELYGnlSAASRGPNGLAILSLFVNVAGSSNPFLSRLLnrDTITRISYKNDAYFLQDLSL 224
Cdd:cd00326  79 SEHTIDGKRYPLELHLVHYNSDYYS--SEAAKKPGGLAVLGVFFEVGEKENPFLKKIL--DALPKIKYKGKETTLPPFDL 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30581031 225 ELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPsqifQSLSGNGRPLQPLAHR 297
Cdd:cd00326 155 SDLLPSSLRdYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDREG----KPLVNNYRPVQPLNGR 224
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
48-300 1.24e-64

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 204.42  E-value: 1.24e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031    48 GPPFWGLVnaaWSLCAvGKRQSPVDVELKRVLYDPFLPPLRLSTGGEKLRG-TLYNTGRHVSFLPASRPVVNVSGGPLLY 126
Cdd:pfam00194   2 GPEHWGKV---YPSCG-GKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKnTLTNNGHTVQVSLDDGDPSTISGGPLAT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031   127 SHRLSELRLLFGARDGAGSEHQINHEGFSAEVQLIHFNQElYGNLSAASRGPNGLAILSLFVNVAGSSNPFLSRLLnrDT 206
Cdd:pfam00194  78 RYRLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNSK-YKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIV--SA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031   207 ITRISYKNDAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQSLS 285
Cdd:pfam00194 155 LDNIKYKGKSVLLPPFDLSDLLPEDLTsYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEPRPLV 234
                         250
                  ....*....|....*
gi 30581031   286 GNGRPLQPLAHRALR 300
Cdd:pfam00194 235 NNFRPTQPLNGRVVF 249
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
35-297 2.82e-63

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: 201.00  E-value: 2.82e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031     35 WSYKENLqgnfvpGPPFWGLVNAAwslCAVGKRQSPVDVELKRVLYDPFLPPLRLStGGEKLRGTLYNTGR--HVSFLPA 112
Cdd:smart01057   1 WGYEGKN------GPEHWGKLDPP---FCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPTAKRILNNGHtvQVNFDDD 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031    113 SrpvVNVSGGPLLYSHRLSELRLLFGARDGAGSEHQINHEGFSAEVQLIHFNQElyGNLSAASRGPNGLAILSLFVNVAG 192
Cdd:smart01057  71 G---STLSGGPLPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGA 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031    193 SSNPFLSRLLnrDTITRISYKNDAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRL 271
Cdd:smart01057 146 EENPALQAIL--DHLPLIKYKGQETELTPFDLSSLLPASTRhYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRT 223
                          250       260
                   ....*....|....*....|....*.
gi 30581031    272 LSQNPPSqifQSLSGNGRPLQPLAHR 297
Cdd:smart01057 224 LLPMEGN---EPLVNNARPLQPLNGR 246
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
63-300 2.15e-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: 160.30  E-value: 2.15e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  63 AVGKRQSPVDVELKRVLYDPFLPPLRLSTGGEKLRgTLYNTGR--HVSFLPASRPVVnVSGGPLLYSHRLSELRLLFGAR 140
Cdd:cd03119  23 AKGDRQSPIDIKTKDAKHDPSLKPLSVSYDPATAK-TILNNGHsfNVEFDDTDDRSV-LRGGPLTGSYRLRQFHFHWGSS 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 141 DGAGSEHQINHEGFSAEVQLIHFNQElYGNLSAASRGPNGLAILSLFVNVaGSSNPFLSRLLnrDTITRISYKNDAYFLQ 220
Cdd:cd03119 101 DDHGSEHTVDGVKYAAELHLVHWNSK-YGSFGEAAKQPDGLAVVGVFLKV-GEANPELQKVL--DALDSIKTKGKQAPFT 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 221 DLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQSLSGNGRPLQPLAHRALR 300
Cdd:cd03119 177 NFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEPPCPMVDNWRPPQPLKGRKVR 256
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
48-297 5.55e-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: 151.31  E-value: 5.55e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  48 GPPFWGLVNAAwslCAvGKRQSPVDVELKRVLYDPFLPPLRLS----TGGEKLrgTLYNTGRHVSF-LPasrPVVNVSGG 122
Cdd:cd03123   1 GEDHWPKKYPA---CG-GKRQSPIDIQTDIVQFDPSLPPLELVgydlPGTEEF--TLTNNGHTVQLsLP---PTMHIRGG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 123 P-LLYshRLSELRLLFGARDGA-GSEHQINHEGFSAEVQLIHFNQELYGNLSAASRGPNGLAILSLFVNVAGSSNP---- 196
Cdd:cd03123  72 PgTEY--TAAQLHLHWGGRGSLsGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTyyek 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 197 FLSRLLNrdtitrISYKNDAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLR--LLS 273
Cdd:cd03123 150 IISHLHE------IKYKGQETTVPGFNVRELLPEDLShYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLETLEntLMD 223
                       250       260
                ....*....|....*....|....
gi 30581031 274 QNPpsqifQSLSGNGRPLQPLAHR 297
Cdd:cd03123 224 THN-----KTLQNNYRATQPLNGR 242
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
65-300 5.24e-41

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: 143.06  E-value: 5.24e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  65 GKRQSPVDVELKRVLYDPFLPPLRLSTGGEKLRgTLYNTGRhvSFLPA---SRPVVNVSGGPLLYSHRLSELRLLFGARD 141
Cdd:cd03118   1 GTRQSPINIQWRDSVYDPQLAPLRVSYDPATCL-YIWNNGY--SFQVEfddSTDKSGISGGPLENHYRLKQFHFHWGANN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 142 GAGSEHQINHEGFSAEVQLIHFNQELYGNLSAASRGPNGLAILSLFVNVaGSSNPFLSRLLnrDTITRISYKNDAYFLQD 221
Cdd:cd03118  78 EWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKL-GAHHEGLQKLV--DALPEVRHKDTVVEFNP 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30581031 222 LSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQSLSGNGRPLQPLAHRALR 300
Cdd:cd03118 155 FDPSCLLPACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLFTSRGEEEKVMVNNFRPLQPLMNRKVR 233
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
65-300 1.85e-39

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: 139.20  E-value: 1.85e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  65 GKRQSPVDVELKRVLYDPFLPPLRLSTGgEKLRGTLYNTGRHVS--FLPASRPVVnVSGGPLLYSHRLSELRLLFGARDG 142
Cdd:cd03149   1 GNRQSPIDIVSSEAVYDPKLKPLSLSYD-PCTSLSISNNGHSVMveFDDSDDKTV-ITGGPLENPYRLKQFHFHWGAKHG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 143 AGSEHQINHEGFSAEVQLIHFNQELYGNLSAASRGPNGLAILSLFVNvAGSSNPFLSRLlnRDTITRISYKNDAYFLQDL 222
Cdd:cd03149  79 SGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLE-TGDEHPGLNRL--TDALYMVRFKGTKAQFLDF 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30581031 223 SLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIFQSLSGNGRPLQPLAHRALR 300
Cdd:cd03149 156 NPKCLLPKSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHMVNNFRPPQPLKGRTVR 233
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
65-297 9.05e-38

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: 134.96  E-value: 9.05e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  65 GKRQSPVDVELKRVLYDPFLPPLRLS----TGGEKLrgTLYNTGRHVSF-LPasrPVVNVSGGPLLYShrLSELRLLFGA 139
Cdd:cd03126  14 GVAQSPIDIHTDILQYDSSLPPLEFHgynvSGTEQF--TLTNNGHTVQLsLP---PTMHIGGLPFKYT--ASQLHLHWGQ 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 140 R-DGAGSEHQINHEGFSAEVQLIHFNQELYGNLSAASRGPNGLAILSLFVNVaGSSNPFLSRLLNRdtITRISYKNDAYF 218
Cdd:cd03126  87 RgSPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEV-GPFNPSYEKIFSH--LHEVKYKDQKVS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 219 LQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLR--LLS--QNPPSQIFQslsgNGRPLQP 293
Cdd:cd03126 164 VPGFNVQELLPKRLDeYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALEtaLYSteEDESREMVN----NYRQVQP 239

                ....
gi 30581031 294 LAHR 297
Cdd:cd03126 240 FNER 243
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
65-297 6.55e-37

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: 132.39  E-value: 6.55e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  65 GKRQSPVDVELKRVLYDPFLPPLRLS-TGGEKLRGTLYNTGRHVSF-LPasrPVVNVSGGPLLYSHRLSELRLLFGARDG 142
Cdd:cd03117   1 GKRQSPINIVTKKVQYDENLTPFTFTgYDDTTTNWTITNNGHTVQVtLP---DGAKISGGGLPGTYKALQFHFHWGSNGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 143 AGSEHQINHEGFSAEVQLIHFNQElYGNLSAASRGPNGLAILSLFVNVAGSSNPFLSRLLNrdTITRISYKNDAYFLQDL 222
Cdd:cd03117  78 PGSEHTIDGERYPMELHIVHIKES-YNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLIS--ALSNIPQKGGSTNLTPF 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30581031 223 SLELLFP--ESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQiFQSLSGNGRPLQPLAHR 297
Cdd:cd03117 155 SLRSLLPsvLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDN-GQPMVNNFRPVQPLNGR 230
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
48-297 2.95e-36

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: 130.94  E-value: 2.95e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  48 GPPFWGLVNAAwslCAVGKRQSPVDVELKRVLYDPFLPPLRLS-TGGEKLRGTLYNTGRHVSFLPASRPVV-NVSGGPLL 125
Cdd:cd03122   1 NPKHWAKKYPA---CGEGRQQSPIDIVEDTQVQRQGLQPLHFDgYEELTASTTLENTGKTVILRLEGNSSDpFVSGGPLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 126 YSHRLSELRLLFGARDGAGSEHQINHEGFSAEVQLIHFNQELYGNLSAASrGPNGLAILSLFVNVAGSSNPFLSRLLnrD 205
Cdd:cd03122  78 GRYKFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDSFEAIK-SPGGVLALAYLFELSHEDNPFLDPII--E 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 206 TITRISYKNDAYFLQDLSLELLFPESF-GFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLL--SQNPPSQIFQ 282
Cdd:cd03122 155 GLRNVSRPGKEVELPPFPLSDLLPPFTdKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELltRRQDGVMSGD 234
                       250
                ....*....|....*
gi 30581031 283 SLSGNGRPLQPLAHR 297
Cdd:cd03122 235 YLPNNGRPQQPLGSR 249
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
52-301 1.27e-35

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: 129.59  E-value: 1.27e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  52 WGLVNAAwslcAVGKRQSPVDVELKRVLYDPFLPPLRLSTGGEKLRGT-LYNTGRHVSFLPASRPVVnvSGGPLLYSHR- 129
Cdd:cd03120   4 WGLLFPE----ANGEYQSPINLNSREARYDPSLLEVRLSPNYVVCRDCeVINDGHTIQIILKSKSVL--SGGPLPQGHEf 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 130 -LSELRLLFGARDGAGSEHQINHEGFSAEVQLIHFNQELYGNLSAASRGPNGLAILSLFVNVaGSSNPFLSRLlnRDTIT 208
Cdd:cd03120  78 eLAEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQI-GKEHVGLKAV--TEILQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 209 RISYKNDAYFLQDLSLELLFPESF--GFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQN-PPSQIFQSLS 285
Cdd:cd03120 155 DIQYKGKSKTIPCFNPNTLLPDPLlrDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLRTHvKGAELVEGCD 234
                       250       260
                ....*....|....*....|
gi 30581031 286 G----NGRPLQPLAHRALRG 301
Cdd:cd03120 235 GllgdNFRPTQPLSDRVIRA 254
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
48-297 5.57e-33

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: 121.22  E-value: 5.57e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  48 GPPFWGLVNAAWSLCAVGKRQSPVDVELKRVLYDPfLPPLRLSTGGEKLrgTLYNTG--RHVSFLP-ASRPVVNvsggpl 124
Cdd:cd03124   1 GPEHWGNLDPEFALCATGKNQSPIDITTKAVVSDK-LPPLNYNYKPTSA--TLVNNGhtIQVNFEGnGGTLTID------ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 125 lySHRLSELRLLFGArdgaGSEHQINHEGFSAEVQLIHFNQElygnlsaasrgpNGLAILSLFVnVAGSSNPFLSRLLNR 204
Cdd:cd03124  72 --GETYQLLQFHFHS----PSEHLINGKRYPLEAHLVHKSKD------------GQLAVVAVLF-EEGKENPFLKKILDN 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 205 dtitRISYKNDAYFLQD-LSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLsqnppsqifqS 283
Cdd:cd03124 133 ----MPKKEGTEVNLPAiLDPNELLPESRSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAA----------V 198
                       250
                ....*....|....
gi 30581031 284 LSGNGRPLQPLAHR 297
Cdd:cd03124 199 YPNNARPVQPLNGR 212
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
52-302 1.77e-29

Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the secreted CA VI, which is found in saliva.


Pssm-ID: 239399  Cd Length: 249  Bit Score: 112.96  E-value: 1.77e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  52 WGLVNAAwslCAvGKRQSPVDVELKRVLYDPFLPPLRLST-GGEKLRGTLYNTGRHVSF-LPASRPVVNVSGGPllysHR 129
Cdd:cd03125   5 WPEKYPA---CG-GKRQSPIDIQRREVRFNPSLLQLELVGyEKEQGEFTMTNNGHTVQIdLPPTMSITTGDGTV----YT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 130 LSELRLLFGARDG--AGSEHQINHEGFSAEVQLIHFNQElYGNLSAASRGPNGLAILSLFVNVA-GSSNPFLSRLLNRdt 206
Cdd:cd03125  77 AVQMHFHWGGRDSeiSGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLYKVGhYAENTYYSDFISK-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 207 ITRISYKNDAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLR--LLSQNPpsqifQS 283
Cdd:cd03125 154 LAKIKYAGQTTTLTSLDVRDMLPENLHhYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLEntLMDHHN-----KT 228
                       250
                ....*....|....*....
gi 30581031 284 LSGNGRPLQPLAHRALRGN 302
Cdd:cd03125 229 IRNDYRRTQPLNHRVVEAN 247
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
4-297 2.22e-29

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 112.67  E-value: 2.22e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031   4 AARLSAPQALVLWAALGAAAHIGPApdpedwWSYkenlQGNFvpGPPFWGLVNAAWSLCAVGKRQSPVDVelkRVLYDPF 83
Cdd:COG3338   3 KRLLLALLLAAALPAAAAAAASAPH------WSY----EGET--GPEHWGELSPEFATCATGKNQSPIDI---RTAIKAD 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  84 LPPLRLS--TGGEKLRgtlyNTGR--HVSFLPASRpvVNVSGGP--LLYSHrlselrllFgardGAGSEHQINHEGFSAE 157
Cdd:COG3338  68 LPPLKFDykPTPLEIV----NNGHtiQVNVDPGST--LTVDGKRyeLKQFH--------F----HTPSEHTINGKSYPME 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 158 VQLIHfnqelygnlsaasRGPNG-LAILSLFVnVAGSSNPFLSRLLN---RDtitrisyKNDAYFLQD-LSLELLFPESF 232
Cdd:COG3338 130 AHLVH-------------KDADGeLAVVGVLF-EEGAENPALAKLWAnlpLE-------AGEEVALDAtIDLNDLLPEDR 188
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30581031 233 GFITYQGSLSTPPCSETVTWILIDRALNITSLQMhslrllsqnppsQIFQSL-SGNGRPLQPLAHR 297
Cdd:COG3338 189 SYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQI------------EAFARLyPNNARPVQPLNGR 242
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
48-300 4.57e-29

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: 111.97  E-value: 4.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  48 GPPFWGLVNAAwslCAvGKRQSPVDVELKRVLYDPFLPPLRLS----TGGEKLRgtLYNTGRHVSF-LPASrpvVNVSGG 122
Cdd:cd03150   1 GQPPWPSVSPA---CA-GRFQSPVDIRPHLVAFCPALRPLELLgfdlPPSPSLR--LLNNGHTVQLsLPSG---LRMALG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 123 PLlYSHRLSELRLLFGARDGAGSEHQINHEGFSAEVQLIHFNQElYGNLSAASRGPNGLAILSLFVNVAGSSNPFLSRLL 202
Cdd:cd03150  72 PG-QEYRALQLHLHWGAAGRPGSEHTVDGHRFPAEIHVVHLSTA-FANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031 203 NRdtITRISYKNDAYFLQDLSLELLFPESFG-FITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRLLSQNPPSQIf 281
Cdd:cd03150 150 SR--LSEISEEESETVVPGLDVSALLPSDLSrYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHDSR- 226
                       250
                ....*....|....*....
gi 30581031 282 qsLSGNGRPLQPLAHRALR 300
Cdd:cd03150 227 --LQLNFRATQPLNGRKIE 243
PLN02202 PLN02202
carbonate dehydratase
48-314 6.80e-14

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 70.86  E-value: 6.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031   48 GPPFWGLVNAAWSLCAVGKRQSPVDVELKRVLYDPFLPPLRLSTggEKLRGTLYNTGRHVSFL---PASRPVVNVSGGPL 124
Cdd:PLN02202  38 GPNQWGHLNPHFTKCAVGKLQSPIDIQRRQIFYNHKLESIHRDY--YFTNATLVNHVCNVAMFfgeGAGDVIIDNKNYTL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  125 LYSHRLSElrllfgardgagSEHQINHEGFSAEVQLIHfnQELYGNLSAasrgpnglaILSLFVnvAGSSNPFLSRLLNR 204
Cdd:PLN02202 116 LQMHWHTP------------SEHHLHGVQYAAELHMVH--QAKDGSFAV---------VASLFK--IGTEEPFLSQMKDK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  205 DTITRISYKNDAYFLQ----DLSLELLFPESFGFITYQGSLSTPPCSETVTWILIDRALNITSLQMHSLRllsqnppSQI 280
Cdd:PLN02202 171 LVKLKEERFKGNHTAQvevgKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLR-------SPL 243
                        250       260       270
                 ....*....|....*....|....*....|....
gi 30581031  281 FQSLSGNGRPLQPLAHRALRGNRDPRHPERRCRG 314
Cdd:PLN02202 244 DKSFKNNSRPCQPLNGRRVEMFHDHERVDKKDTG 277
PLN02179 PLN02179
carbonic anhydrase
30-259 3.00e-11

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 62.31  E-value: 3.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031   30 DPEDWWSYKENLQgnfvPGPPFWGLVNAAWSLCAVGKRQSPVDVELKRVlydpflpplrlstggeklrGTLYNTGRHVSF 109
Cdd:PLN02179  32 GNKPLFTYKQKTE----KGPAEWGKLNPQWKVCSTGKYQSPIDLTDERV-------------------SLIHDQALSRHY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  110 LPASrPVVNVSGGPLLYSHRLSELRLLFGARD--------GAGSEHQINHEGFSAEVQLIHfnqelygnLSAASRgpngL 181
Cdd:PLN02179  89 KPAP-AVIQSRGHDVMVSWKGDAGKITIHQTDyklvqchwHSPSEHTINGTSYDLELHMVH--------TSASGK----T 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581031  182 AILSLFVNVaGSSNPFLSRLLNrdTITRISYKndayflqDLSLELLFP-----ESFGFITYQGSLSTPPCSETVTWILID 256
Cdd:PLN02179 156 AVVGVLYKL-GEPDEFLTKLLN--GIKGVGKK-------EINLGIVDPrdirfETNNFYRYIGSLTIPPCTEGVIWTVVK 225

                 ...
gi 30581031  257 RAL 259
Cdd:PLN02179 226 RVV 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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