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Conserved domains on  [gi|18858185|ref|NP_572581|]
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carbonic anhydrase-related protein B, isoform A [Drosophila melanogaster]

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 ...
37-298 9.44e-157

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: 438.77  E-value: 9.44e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  37 GPAFWGLINPEWSLCNKGRRQSPVNLEPQRLLFDPNLRPMHIDKHR-ISGLITNTGHSVIFTAGNDTVanydgmqtpVNI 115
Cdd:cd03121   1 GPSFWGLVNSAWNLCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTGRkVSGTFYNTGRHVSFRPDKDPV---------VNI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 116 SGGPLSYRYRFHEIHMHYGLNDQFGSEHSVEGYTFPAEIQIFGYNSQLYANFSDALNRAQGIVGVSILLQLGDLSNAELR 195
Cdd:cd03121  72 SGGPLSYRYRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 196 MLTDQLE--RIRYGGDEAFVKRLSIRGLLPDTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLMQGSPDH 273
Cdd:cd03121 152 RLTNRDTitSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQ 231
                       250       260
                ....*....|....*....|....*
gi 18858185 274 PKAPLGNNYRPPQPLLHRPIRTNID 298
Cdd:cd03121 232 EKAPMSPNFRPVQPLNNRPVRTNIN 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 ...
37-298 9.44e-157

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: 438.77  E-value: 9.44e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  37 GPAFWGLINPEWSLCNKGRRQSPVNLEPQRLLFDPNLRPMHIDKHR-ISGLITNTGHSVIFTAGNDTVanydgmqtpVNI 115
Cdd:cd03121   1 GPSFWGLVNSAWNLCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTGRkVSGTFYNTGRHVSFRPDKDPV---------VNI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 116 SGGPLSYRYRFHEIHMHYGLNDQFGSEHSVEGYTFPAEIQIFGYNSQLYANFSDALNRAQGIVGVSILLQLGDLSNAELR 195
Cdd:cd03121  72 SGGPLSYRYRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 196 MLTDQLE--RIRYGGDEAFVKRLSIRGLLPDTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLMQGSPDH 273
Cdd:cd03121 152 RLTNRDTitSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQ 231
                       250       260
                ....*....|....*....|....*
gi 18858185 274 PKAPLGNNYRPPQPLLHRPIRTNID 298
Cdd:cd03121 232 EKAPMSPNFRPVQPLNNRPVRTNIN 256
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
36-297 1.02e-93

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 278.77  E-value: 1.02e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185    36 SGPAFWGLINPEwslCNkGRRQSPVNLEPQRLLFDPNLRPMHI---DKHRISGLITNTGHSVIFTAGNdtvanydgmQTP 112
Cdd:pfam00194   1 LGPEHWGKVYPS---CG-GKRQSPINIDTRKVRYDPSLPPLTFqgyDVPPGKNTLTNNGHTVQVSLDD---------GDP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185   113 VNISGGPLSYRYRFHEIHMHYGLNDQFGSEHSVEGYTFPAEIQIFGYNSQlYANFSDALNRAQGIVGVSILLQLGDLSNA 192
Cdd:pfam00194  68 STISGGPLATRYRLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNSK-YKSFDEAAKHPDGLAVLGVFFEVGDENNP 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185   193 ELRMLTDQLERIRYGGDEAFVKRLSIRGLLP-DTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLMQGSP 271
Cdd:pfam00194 147 YLQPIVSALDNIKYKGKSVLLPPFDLSDLLPeDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDG 226
                         250       260
                  ....*....|....*....|....*.
gi 18858185   272 DHPKAPLGNNYRPPQPLLHRPIRTNI 297
Cdd:pfam00194 227 GEEPRPLVNNFRPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
30-292 7.03e-91

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: 271.49  E-value: 7.03e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185     30 WTYDGISGPAFWGLINPEWSlcnKGRRQSPVNLEPQRLLFDPNLRPMHIDKHRISGL-ITNTGHSVIFTAGNDTVanydg 108
Cdd:smart01057   1 WGYEGKNGPEHWGKLDPPFC---GGKRQSPIDIVTAEAQYDPSLKPLKLSYDQPTAKrILNNGHTVQVNFDDDGS----- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185    109 mqtpvNISGGPLSYRYRFHEIHMHYGLNDQFGSEHSVEGYTFPAEIQIFGYNSQlyANFSDALNRAQGIVGVSILLQLGD 188
Cdd:smart01057  73 -----TLSGGPLPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGA 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185    189 LSNAELRMLTDQLERIRYGGDEAFVKRLSIRGLLP-DTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLM 267
Cdd:smart01057 146 EENPALQAILDHLPLIKYKGQETELTPFDLSSLLPaSTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLL 225
                          250       260
                   ....*....|....*....|....*
gi 18858185    268 qgsPDHPKAPLGNNYRPPQPLLHRP 292
Cdd:smart01057 226 ---PMEGNEPLVNNARPLQPLNGRV 247
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
30-293 1.48e-41

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 144.64  E-value: 1.48e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  30 WTYDGISGPAFWGLINPEWSLCNKGRRQSPVNLEPQRllfDPNLRPMHIDKHRISGLITNTGHSVIFTAGNDTVANYDGM 109
Cdd:COG3338  28 WSYEGETGPEHWGELSPEFATCATGKNQSPIDIRTAI---KADLPPLKFDYKPTPLEIVNNGHTIQVNVDPGSTLTVDGK 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 110 qtpvnisggplsyRYRFHEIHMHYGlndqfgSEHSVEGYTFPAEIQIfgynsqLYANFSDALnraqGIVGVsiLLQLGDl 189
Cdd:COG3338 105 -------------RYELKQFHFHTP------SEHTINGKSYPMEAHL------VHKDADGEL----AVVGV--LFEEGA- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 190 SNAELRMLTDQL--ERiryGGDEAFVKRLSIRGLLPDTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLM 267
Cdd:COG3338 153 ENPALAKLWANLplEA---GEEVALDATIDLNDLLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARLY 229
                       250       260
                ....*....|....*....|....*.
gi 18858185 268 qgspdhpkaplGNNYRPPQPLLHRPI 293
Cdd:COG3338 230 -----------PNNARPVQPLNGRLI 244
PLN02202 PLN02202
carbonate dehydratase
32-293 3.64e-15

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 74.32  E-value: 3.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185   32 YDGISGPAFWGLINPEWSLCNKGRRQSPVNLEPQRLLFDPNLRPMHIDKHRISGLITNTGHSVIF----TAGNDTVANYD 107
Cdd:PLN02202  33 YKGKNGPNQWGHLNPHFTKCAVGKLQSPIDIQRRQIFYNHKLESIHRDYYFTNATLVNHVCNVAMffgeGAGDVIIDNKN 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  108 gmqtpvnisggplsyrYRFHEIHMHYglndqfGSEHSVEGYTFPAEIQIfgynsqlyanfsdaLNRAQ--GIVGVSILLQ 185
Cdd:PLN02202 113 ----------------YTLLQMHWHT------PSEHHLHGVQYAAELHM--------------VHQAKdgSFAVVASLFK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  186 LGD----LSNAELRMLTDQLERIRyGGDEAFVK--RLSIRGLLPDTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQ 259
Cdd:PLN02202 157 IGTeepfLSQMKDKLVKLKEERFK-GNHTAQVEvgKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQ 235
                        250       260       270
                 ....*....|....*....|....*....|....
gi 18858185  260 LHALRRLMQGSpdhpkapLGNNYRPPQPLLHRPI 293
Cdd:PLN02202 236 VELLRSPLDKS-------FKNNSRPCQPLNGRRV 262
 
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 ...
37-298 9.44e-157

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: 438.77  E-value: 9.44e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  37 GPAFWGLINPEWSLCNKGRRQSPVNLEPQRLLFDPNLRPMHIDKHR-ISGLITNTGHSVIFTAGNDTVanydgmqtpVNI 115
Cdd:cd03121   1 GPSFWGLVNSAWNLCSKGRRQSPVDIEPSRLLFDPFLTPLRIDTGRkVSGTFYNTGRHVSFRPDKDPV---------VNI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 116 SGGPLSYRYRFHEIHMHYGLNDQFGSEHSVEGYTFPAEIQIFGYNSQLYANFSDALNRAQGIVGVSILLQLGDLSNAELR 195
Cdd:cd03121  72 SGGPLSYRYRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 196 MLTDQLE--RIRYGGDEAFVKRLSIRGLLPDTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLMQGSPDH 273
Cdd:cd03121 152 RLTNRDTitSIRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQ 231
                       250       260
                ....*....|....*....|....*
gi 18858185 274 PKAPLGNNYRPPQPLLHRPIRTNID 298
Cdd:cd03121 232 EKAPMSPNFRPVQPLNNRPVRTNIN 256
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
36-297 1.02e-93

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 278.77  E-value: 1.02e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185    36 SGPAFWGLINPEwslCNkGRRQSPVNLEPQRLLFDPNLRPMHI---DKHRISGLITNTGHSVIFTAGNdtvanydgmQTP 112
Cdd:pfam00194   1 LGPEHWGKVYPS---CG-GKRQSPINIDTRKVRYDPSLPPLTFqgyDVPPGKNTLTNNGHTVQVSLDD---------GDP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185   113 VNISGGPLSYRYRFHEIHMHYGLNDQFGSEHSVEGYTFPAEIQIFGYNSQlYANFSDALNRAQGIVGVSILLQLGDLSNA 192
Cdd:pfam00194  68 STISGGPLATRYRLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNSK-YKSFDEAAKHPDGLAVLGVFFEVGDENNP 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185   193 ELRMLTDQLERIRYGGDEAFVKRLSIRGLLP-DTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLMQGSP 271
Cdd:pfam00194 147 YLQPIVSALDNIKYKGKSVLLPPFDLSDLLPeDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDG 226
                         250       260
                  ....*....|....*....|....*.
gi 18858185   272 DHPKAPLGNNYRPPQPLLHRPIRTNI 297
Cdd:pfam00194 227 GEEPRPLVNNFRPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
30-292 7.03e-91

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: 271.49  E-value: 7.03e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185     30 WTYDGISGPAFWGLINPEWSlcnKGRRQSPVNLEPQRLLFDPNLRPMHIDKHRISGL-ITNTGHSVIFTAGNDTVanydg 108
Cdd:smart01057   1 WGYEGKNGPEHWGKLDPPFC---GGKRQSPIDIVTAEAQYDPSLKPLKLSYDQPTAKrILNNGHTVQVNFDDDGS----- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185    109 mqtpvNISGGPLSYRYRFHEIHMHYGLNDQFGSEHSVEGYTFPAEIQIFGYNSQlyANFSDALNRAQGIVGVSILLQLGD 188
Cdd:smart01057  73 -----TLSGGPLPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGA 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185    189 LSNAELRMLTDQLERIRYGGDEAFVKRLSIRGLLP-DTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLM 267
Cdd:smart01057 146 EENPALQAILDHLPLIKYKGQETELTPFDLSSLLPaSTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLL 225
                          250       260
                   ....*....|....*....|....*
gi 18858185    268 qgsPDHPKAPLGNNYRPPQPLLHRP 292
Cdd:smart01057 226 ---PMEGNEPLVNNARPLQPLNGRV 247
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
54-294 3.19e-84

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: 253.74  E-value: 3.19e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  54 GRRQSPVNLEPQRLLFDPNLRPMHIDKH-RISGLITNTGHSVIFTAGNDtvanydgmqtPVNISGGPLSYRYRFHEIHMH 132
Cdd:cd00326   1 GKRQSPINIVTSAVVYDPSLPPLNFDYYpTTSLTLVNNGHTVQVNFDDD----------GGTLSGGGLPGRYKLVQFHFH 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 133 YGLNDQFGSEHSVEGYTFPAEIQIFGYNSQLYAnfSDALNRAQGIVGVSILLQLGDLSNAELRMLTDQLERIRYGGDEAF 212
Cdd:cd00326  71 WGSENSPGSEHTIDGKRYPLELHLVHYNSDYYS--SEAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETT 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 213 VKRLSIRGLLP-DTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLMQGSPDhpkaPLGNNYRPPQPLLHR 291
Cdd:cd00326 149 LPPFDLSDLLPsSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDREGK----PLVNNYRPVQPLNGR 224

                ...
gi 18858185 292 PIR 294
Cdd:cd00326 225 VVY 227
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
54-294 1.30e-59

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: 191.20  E-value: 1.30e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  54 GRRQSPVNLEPQRLLFDPNLRPMHIDKHRISGL-ITNTGHSViftagndtVANYDGMQTPVNISGGPLSYRYRFHEIHMH 132
Cdd:cd03149   1 GNRQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLsISNNGHSV--------MVEFDDSDDKTVITGGPLENPYRLKQFHFH 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 133 YGLNDQFGSEHSVEGYTFPAEIQIFGYNSQLYANFSDALNRAQGIVGVSILLQLGDlSNAELRMLTDQLERIRYGGDEAF 212
Cdd:cd03149  73 WGAKHGSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETGD-EHPGLNRLTDALYMVRFKGTKAQ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 213 VKRLSIRGLLPDTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLMQGSPDHPKAPLGNNYRPPQPLLHRP 292
Cdd:cd03149 152 FLDFNPKCLLPKSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHMVNNFRPPQPLKGRT 231

                ..
gi 18858185 293 IR 294
Cdd:cd03149 232 VR 233
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
30-294 6.16e-59

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: 189.96  E-value: 6.16e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  30 WTYDGISGPAFWGLINPewslCNKGRRQSPVNLEPQRLLFDPNLRPMHIDKHRISGL-ITNTGHS--VIFTAGNDTVAny 106
Cdd:cd03119   5 WGYDSHNGPEHWHELFP----IAKGDRQSPIDIKTKDAKHDPSLKPLSVSYDPATAKtILNNGHSfnVEFDDTDDRSV-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 107 dgmqtpvnISGGPLSYRYRFHEIHMHYGLNDQFGSEHSVEGYTFPAEIQIFGYNSQlYANFSDALNRAQGIVGVSILLQL 186
Cdd:cd03119  79 --------LRGGPLTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNSK-YGSFGEAAKQPDGLAVVGVFLKV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 187 GDlSNAELRMLTDQLERIRYGGDEAFVKRLSIRGLLPDTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRL 266
Cdd:cd03119 150 GE-ANPELQKVLDALDSIKTKGKQAPFTNFDPSCLLPASLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSL 228
                       250       260
                ....*....|....*....|....*...
gi 18858185 267 MQGSPDHPKAPLGNNYRPPQPLLHRPIR 294
Cdd:cd03119 229 LFNAEGEPPCPMVDNWRPPQPLKGRKVR 256
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
54-296 5.89e-56

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: 182.12  E-value: 5.89e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  54 GRRQSPVNLEPQRLLFDPNLRPMHIDKHRISGL----ITNTGHSVIFTAGNdtvanydGMQtpvnISGGPlSYRYRFHEI 129
Cdd:cd03123  14 GKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTeeftLTNNGHTVQLSLPP-------TMH----IRGGP-GTEYTAAQL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 130 HMHYG-LNDQFGSEHSVEGYTFPAEIQIFGYNSQLYANFSDALNRAQGIVGVSILLQLGDLSNAELRMLTDQLERIRYGG 208
Cdd:cd03123  82 HLHWGgRGSLSGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKYKG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 209 DEAFVKRLSIRGLLP-DTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRR-LMqgspDHPKAPLGNNYRPPQ 286
Cdd:cd03123 162 QETTVPGFNVRELLPeDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLETLENtLM----DTHNKTLQNNYRATQ 237
                       250
                ....*....|
gi 18858185 287 PLLHRPIRTN 296
Cdd:cd03123 238 PLNGRVVEAS 247
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
37-291 1.95e-51

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: 170.61  E-value: 1.95e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  37 GPAFWGLINPEwslCNKGRRQSPVNLEPQRLLFDPNLRPMHIDK-HRISG--LITNTGHSVIFTAgndtvanYDGMQTPv 113
Cdd:cd03122   1 NPKHWAKKYPA---CGEGRQQSPIDIVEDTQVQRQGLQPLHFDGyEELTAstTLENTGKTVILRL-------EGNSSDP- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 114 NISGGPLSYRYRFHEIHMHYGLNDQFGSEHSVEGYTFPAEIQIFGYNSQLYANFsDALNRAQGIVGVSILLQLGDLSNAE 193
Cdd:cd03122  70 FVSGGPLLGRYKFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDSF-EAIKSPGGVLALAYLFELSHEDNPF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 194 LRMLTDQLERIRYGGDEAFVKRLSIRGLLPD-TDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLMQGSPD 272
Cdd:cd03122 149 LDPIIEGLRNVSRPGKEVELPPFPLSDLLPPfTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQD 228
                       250       260
                ....*....|....*....|.
gi 18858185 273 HPKA--PLGNNYRPPQPLLHR 291
Cdd:cd03122 229 GVMSgdYLPNNGRPQQPLGSR 249
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
54-296 1.08e-49

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: 165.40  E-value: 1.08e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  54 GRRQSPVNLEPQRLLFDPNLRPMHIDKHRISGL-ITNTGHSVIftagndtvANYDGMQTPVNISGGPLSYRYRFHEIHMH 132
Cdd:cd03118   1 GTRQSPINIQWRDSVYDPQLAPLRVSYDPATCLyIWNNGYSFQ--------VEFDDSTDKSGISGGPLENHYRLKQFHFH 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 133 YGLNDQFGSEHSVEGYTFPAEIQIFGYNSQLYANFSDALNRAQGIVGVSILLQLGDLSNAeLRMLTDQLERIRYGGDEAF 212
Cdd:cd03118  73 WGANNEWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHHEG-LQKLVDALPEVRHKDTVVE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 213 VKRLSIRGLLPDTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLMQGSPDHPKAPLGNNYRPPQPLLHRP 292
Cdd:cd03118 152 FNPFDPSCLLPACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLFTSRGEEEKVMVNNFRPLQPLMNRK 231

                ....
gi 18858185 293 IRTN 296
Cdd:cd03118 232 VRSS 235
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
54-293 2.84e-49

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: 164.36  E-value: 2.84e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  54 GRRQSPVNLEPQRLLFDPNLRPMHIDKH---RISGLITNTGHSVIFTAGNdtvanydgmqtPVNISGGPLSYRYRFHEIH 130
Cdd:cd03117   1 GKRQSPINIVTKKVQYDENLTPFTFTGYddtTTNWTITNNGHTVQVTLPD-----------GAKISGGGLPGTYKALQFH 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 131 MHYGLNDQFGSEHSVEGYTFPAEIQIFGYNSQLYANfSDALNRAQGIVGVSILLQLGDLSNAELRMLTDQLERIRYGGDE 210
Cdd:cd03117  70 FHWGSNGSPGSEHTIDGERYPMELHIVHIKESYNSL-LEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 211 AFVKRLSIRGLLPDTD--HYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLMQGSPDHPKaPLGNNYRPPQPL 288
Cdd:cd03117 149 TNLTPFSLRSLLPSVLltKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNGQ-PMVNNFRPVQPL 227

                ....*
gi 18858185 289 LHRPI 293
Cdd:cd03117 228 NGRVV 232
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
54-293 2.95e-48

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: 162.31  E-value: 2.95e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  54 GRRQSPVNLEPQRLLFDPNLRPMHIDKHRISG----LITNTGHSViftagndtvanydGMQTPVNISGGPLSYRYRFHEI 129
Cdd:cd03126  14 GVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGteqfTLTNNGHTV-------------QLSLPPTMHIGGLPFKYTASQL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 130 HMHYG-LNDQFGSEHSVEGYTFPAEIQIFGYNSQLYANFSDALNRAQGIVGVSILLQLGDLSNAELRMLTdQLERIRYGG 208
Cdd:cd03126  81 HLHWGqRGSPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVGPFNPSYEKIFS-HLHEVKYKD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 209 DEAFVKRLSIRGLLPD-TDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLMQGSPDHPKAPLGNNYRPPQP 287
Cdd:cd03126 160 QKVSVPGFNVQELLPKrLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALETALYSTEEDESREMVNNYRQVQP 239

                ....*.
gi 18858185 288 LLHRPI 293
Cdd:cd03126 240 FNERLV 245
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
37-293 8.43e-47

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: 157.43  E-value: 8.43e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  37 GPAFWGLINPEWSLCNKGRRQSPVNLEPQRLLFDPnLRPMHIDKHRISGLITNTGHSV-IFTAGNDTVANYDGMqtpvni 115
Cdd:cd03124   1 GPEHWGNLDPEFALCATGKNQSPIDITTKAVVSDK-LPPLNYNYKPTSATLVNNGHTIqVNFEGNGGTLTIDGE------ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 116 sggplsyRYRFHEIHMHyglndqFGSEHSVEGYTFPAEIQIFGYNSQlyanfsdalnraQGIVGVSILLQLGDlSNAELR 195
Cdd:cd03124  74 -------TYQLLQFHFH------SPSEHLINGKRYPLEAHLVHKSKD------------GQLAVVAVLFEEGK-ENPFLK 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 196 MLTDQLERiRYGGDEAFVKRLSIRGLLPDTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLMqgspdhpk 275
Cdd:cd03124 128 KILDNMPK-KEGTEVNLPAILDPNELLPESRSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAAV-------- 198
                       250
                ....*....|....*...
gi 18858185 276 apLGNNYRPPQPLLHRPI 293
Cdd:cd03124 199 --YPNNARPVQPLNGREV 214
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
54-296 9.40e-46

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: 155.88  E-value: 9.40e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  54 GRRQSPVNLEPQRLLFDPNLRPMHIDKHRISGL----ITNTGHSVIFTagndtvanydgMQTPVNISGGPlSYRYRFHEI 129
Cdd:cd03150  14 GRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSpslrLLNNGHTVQLS-----------LPSGLRMALGP-GQEYRALQL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 130 HMHYGLNDQFGSEHSVEGYTFPAEIQIFGYNSQlYANFSDALNRAQGIVGVSILLQLGDLSNAELRMLTDQLERIRYGGD 209
Cdd:cd03150  82 HLHWGAAGRPGSEHTVDGHRFPAEIHVVHLSTA-FANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEISEEES 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 210 EAFVKRLSIRGLLP-DTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLMQGSPDhpkAPLGNNYRPPQPL 288
Cdd:cd03150 161 ETVVPGLDVSALLPsDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHD---SRLQLNFRATQPL 237

                ....*...
gi 18858185 289 LHRPIRTN 296
Cdd:cd03150 238 NGRKIEAS 245
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
30-293 1.48e-41

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 144.64  E-value: 1.48e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  30 WTYDGISGPAFWGLINPEWSLCNKGRRQSPVNLEPQRllfDPNLRPMHIDKHRISGLITNTGHSVIFTAGNDTVANYDGM 109
Cdd:COG3338  28 WSYEGETGPEHWGELSPEFATCATGKNQSPIDIRTAI---KADLPPLKFDYKPTPLEIVNNGHTIQVNVDPGSTLTVDGK 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 110 qtpvnisggplsyRYRFHEIHMHYGlndqfgSEHSVEGYTFPAEIQIfgynsqLYANFSDALnraqGIVGVsiLLQLGDl 189
Cdd:COG3338 105 -------------RYELKQFHFHTP------SEHTINGKSYPMEAHL------VHKDADGEL----AVVGV--LFEEGA- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 190 SNAELRMLTDQL--ERiryGGDEAFVKRLSIRGLLPDTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRLM 267
Cdd:COG3338 153 ENPALAKLWANLplEA---GEEVALDATIDLNDLLPEDRSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARLY 229
                       250       260
                ....*....|....*....|....*.
gi 18858185 268 qgspdhpkaplGNNYRPPQPLLHRPI 293
Cdd:COG3338 230 -----------PNNARPVQPLNGRLI 244
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
41-294 5.63e-39

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: 138.45  E-value: 5.63e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  41 WGLINPEwslcNKGRRQSPVNLEPQRLLFDPNLRPMHIDKHRI---SGLITNTGHSVIFTAGNDTVanydgmqtpvnISG 117
Cdd:cd03120   4 WGLLFPE----ANGEYQSPINLNSREARYDPSLLEVRLSPNYVvcrDCEVINDGHTIQIILKSKSV-----------LSG 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 118 GPL--SYRYRFHEIHMHYGLNDQFGSEHSVEGYTFPAEIQIFGYNSQLYANFSDALNRAQGIVGVSILLQLGDlSNAELR 195
Cdd:cd03120  69 GPLpqGHEFELAEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIGK-EHVGLK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 196 MLTDQLERIRYGGDEAFVKRLSIRGLLPDT--DHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQLHALRRL---MQG- 269
Cdd:cd03120 148 AVTEILQDIQYKGKSKTIPCFNPNTLLPDPllRDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLrthVKGa 227
                       250       260
                ....*....|....*....|....*.
gi 18858185 270 -SPDHPKAPLGNNYRPPQPLLHRPIR 294
Cdd:cd03120 228 eLVEGCDGLLGDNFRPTQPLSDRVIR 253
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
54-296 4.12e-35

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: 127.98  E-value: 4.12e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  54 GRRQSPVNLEPQRLLFDPNLRPMHI---DKHRISGLITNTGHSVIFTAGNdTVANYDGMQTPvnisggplsyrYRFHEIH 130
Cdd:cd03125  14 GKRQSPIDIQRREVRFNPSLLQLELvgyEKEQGEFTMTNNGHTVQIDLPP-TMSITTGDGTV-----------YTAVQMH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 131 MHYGLNDQ--FGSEHSVEGYTFPAEIQIFGYNSQlYANFSDALNRAQGIVGVSILLQLGD-LSNAELRMLTDQLERIRYG 207
Cdd:cd03125  82 FHWGGRDSeiSGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLYKVGHyAENTYYSDFISKLAKIKYA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185 208 GDEAFVKRLSIRGLLP-DTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQlhaLRRLMQGSPDHPKAPLGNNYRPPQ 286
Cdd:cd03125 161 GQTTTLTSLDVRDMLPeNLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQ---IVKLENTLMDHHNKTIRNDYRRTQ 237
                       250
                ....*....|
gi 18858185 287 PLLHRPIRTN 296
Cdd:cd03125 238 PLNHRVVEAN 247
PLN02202 PLN02202
carbonate dehydratase
32-293 3.64e-15

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 74.32  E-value: 3.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185   32 YDGISGPAFWGLINPEWSLCNKGRRQSPVNLEPQRLLFDPNLRPMHIDKHRISGLITNTGHSVIF----TAGNDTVANYD 107
Cdd:PLN02202  33 YKGKNGPNQWGHLNPHFTKCAVGKLQSPIDIQRRQIFYNHKLESIHRDYYFTNATLVNHVCNVAMffgeGAGDVIIDNKN 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  108 gmqtpvnisggplsyrYRFHEIHMHYglndqfGSEHSVEGYTFPAEIQIfgynsqlyanfsdaLNRAQ--GIVGVSILLQ 185
Cdd:PLN02202 113 ----------------YTLLQMHWHT------PSEHHLHGVQYAAELHM--------------VHQAKdgSFAVVASLFK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  186 LGD----LSNAELRMLTDQLERIRyGGDEAFVK--RLSIRGLLPDTDHYMTYDGSTTAPACHETVTWVVLNKPIYITKQQ 259
Cdd:PLN02202 157 IGTeepfLSQMKDKLVKLKEERFK-GNHTAQVEvgKIDTRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQ 235
                        250       260       270
                 ....*....|....*....|....*....|....
gi 18858185  260 LHALRRLMQGSpdhpkapLGNNYRPPQPLLHRPI 293
Cdd:PLN02202 236 VELLRSPLDKS-------FKNNSRPCQPLNGRRV 262
PLN02179 PLN02179
carbonic anhydrase
37-254 2.74e-14

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 71.17  E-value: 2.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185   37 GPAFWGLINPEWSLCNKGRRQSPVNLEPQR--LLFDpnlRPMHIDKHRISGLITNTGHSVIFT----AGNDTVANYDgmq 110
Cdd:PLN02179  46 GPAEWGKLNPQWKVCSTGKYQSPIDLTDERvsLIHD---QALSRHYKPAPAVIQSRGHDVMVSwkgdAGKITIHQTD--- 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858185  111 tpvnisggplsyrYRFHEIHMHYglndqfGSEHSVEGYTfpaeiqifgYNSQLYANFSDALNRAqGIVGVsiLLQLGDLS 190
Cdd:PLN02179 120 -------------YKLVQCHWHS------PSEHTINGTS---------YDLELHMVHTSASGKT-AVVGV--LYKLGEPD 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18858185  191 naelRMLTDQLERIR-YGGDEAFVKRLSIRGLLPDTDHYMTYDGSTTAPACHETVTWVVLNKPIY 254
Cdd:PLN02179 169 ----EFLTKLLNGIKgVGKKEINLGIVDPRDIRFETNNFYRYIGSLTIPPCTEGVIWTVVKRVVW 229
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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