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Conserved domains on  [gi|21358169|ref|NP_648555|]
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carbonic anhydrase 2, isoform A [Drosophila melanogaster]

Protein Classification

carbonic anhydrase family protein( domain architecture ID 11087199)

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
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
34-286 1.69e-111

Eukaryotic-type carbonic anhydrase;


:

Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 324.22  E-value: 1.69e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169    34 HGPEHWSEDYARCSGKHQSPINIDQVSAVEK-KFPKLEFFNFKVVPDNLQMTNNGHTVLVKMsyNEDEIPSVRGGPLAEK 112
Cdd:pfam00194   1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDpSLPPLTFQGYDVPPGKNTLTNNGHTVQVSL--DDGDPSTISGGPLATR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169   113 tplgYQFEQFHFHWGENDTIGSEDLINNRAYPAELHVVLRNLEYPDFASALDKDHGIAVMAFFFQVGDKSTGGYEGFTNL 192
Cdd:pfam00194  79 ----YRLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNSKYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169   193 LSQIDRKGKSVNMTnPLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFRLLTAND-----DHL 267
Cdd:pfam00194 155 LDNIKYKGKSVLLP-PFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDggeepRPL 233
                         250
                  ....*....|....*....
gi 21358169   268 KNNFRPIQPLNDRTLYKNY 286
Cdd:pfam00194 234 VNNFRPTQPLNGRVVFASF 252
 
Name Accession Description Interval E-value
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
34-286 1.69e-111

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 324.22  E-value: 1.69e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169    34 HGPEHWSEDYARCSGKHQSPINIDQVSAVEK-KFPKLEFFNFKVVPDNLQMTNNGHTVLVKMsyNEDEIPSVRGGPLAEK 112
Cdd:pfam00194   1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDpSLPPLTFQGYDVPPGKNTLTNNGHTVQVSL--DDGDPSTISGGPLATR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169   113 tplgYQFEQFHFHWGENDTIGSEDLINNRAYPAELHVVLRNLEYPDFASALDKDHGIAVMAFFFQVGDKSTGGYEGFTNL 192
Cdd:pfam00194  79 ----YRLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNSKYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169   193 LSQIDRKGKSVNMTnPLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFRLLTAND-----DHL 267
Cdd:pfam00194 155 LDNIKYKGKSVLLP-PFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDggeepRPL 233
                         250
                  ....*....|....*....
gi 21358169   268 KNNFRPIQPLNDRTLYKNY 286
Cdd:pfam00194 234 VNNFRPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
28-281 2.48e-97

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: 288.06  E-value: 2.48e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169     28 FGYEGRHGPEHWSE-DYARCSGKHQSPINIDQVSAV-EKKFPKLEFFNFKvvPDNLQMTNNGHTVLVKMSyneDEIPSVR 105
Cdd:smart01057   1 WGYEGKNGPEHWGKlDPPFCGGKRQSPIDIVTAEAQyDPSLKPLKLSYDQ--PTAKRILNNGHTVQVNFD---DDGSTLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169    106 GGPLAEKtplgYQFEQFHFHWGENDTIGSEDLINNRAYPAELHVVLRNlEYPDFASALDKDHGIAVMAFFFQVGDKSTGG 185
Cdd:smart01057  76 GGPLPGR----YRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYN-SKGSFSEAVSKPGGLAVVAVFFKVGAEENPA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169    186 YEGFTNLLSQIDRKGKSVNMTnPLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFRLL--TAN 263
Cdd:smart01057 151 LQAILDHLPLIKYKGQETELT-PFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLlpMEG 229
                          250
                   ....*....|....*...
gi 21358169    264 DDHLKNNFRPIQPLNDRT 281
Cdd:smart01057 230 NEPLVNNARPLQPLNGRV 247
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
48-283 2.76e-89

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: 266.84  E-value: 2.76e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  48 GKHQSPINIDQVSAVekKFPKLEFFNFKVVP-DNLQMTNNGHTVLVKMsynEDEIPSVRGGPLAEKtplgYQFEQFHFHW 126
Cdd:cd00326   1 GKRQSPINIVTSAVV--YDPSLPPLNFDYYPtTSLTLVNNGHTVQVNF---DDDGGTLSGGGLPGR----YKLVQFHFHW 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 127 GENDTIGSEDLINNRAYPAELHVVLRNLEYPDFAsALDKDHGIAVMAFFFQVGDKSTGGYEGFTNLLSQIDRKGKSVNMT 206
Cdd:cd00326  72 GSENSPGSEHTIDGKRYPLELHLVHYNSDYYSSE-AAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLP 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21358169 207 nPLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFR-LLTANDDHLKNNFRPIQPLNDRTLY 283
Cdd:cd00326 151 -PFDLSDLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRsLLDREGKPLVNNYRPVQPLNGRVVY 227
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
1-284 1.69e-62

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 198.95  E-value: 1.69e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169   1 MRRCRNTPFAIVIAPILICASLVLAQDFGYEGRHGPEHW---SEDYARCS-GKHQSPINIDQvsAVEKKFPKLEFfNFKV 76
Cdd:COG3338   1 MKKRLLLALLLAAALPAAAAAAASAPHWSYEGETGPEHWgelSPEFATCAtGKNQSPIDIRT--AIKADLPPLKF-DYKP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  77 VPdnLQMTNNGHTVLVkmsyNEDEIPSVRggpLAEKTplgYQFEQFHFHwgendtIGSEDLINNRAYPAELHVVLRnley 156
Cdd:COG3338  78 TP--LEIVNNGHTIQV----NVDPGSTLT---VDGKR---YELKQFHFH------TPSEHTINGKSYPMEAHLVHK---- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 157 pdfasalDKDHGIAVMAFFFQVGDKStggyEGFTNLLSQI-DRKGKSVNMTNPLPLGEYISKSvESYFSYTGSLTTPPCS 235
Cdd:COG3338 136 -------DADGELAVVGVLFEEGAEN----PALAKLWANLpLEAGEEVALDATIDLNDLLPED-RSYYRYSGSLTTPPCS 203
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 21358169 236 EEVTWIDFTTPIDITEKQLNAFRLLTAnddhlkNNFRPIQPLNDRTLYK 284
Cdd:COG3338 204 EGVLWIVLKQPITVSAEQIEAFARLYP------NNARPVQPLNGRLILE 246
PLN02202 PLN02202
carbonate dehydratase
17-280 7.28e-20

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 87.80  E-value: 7.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169   17 LICASLVLAQD----FGYEGRHGPEHWSE---DYARCS-GKHQSPINIDQVSAVEKKfpKLEFFNFKVVPDNLQMTNngH 88
Cdd:PLN02202  16 LICIAPADAQTegvvFGYKGKNGPNQWGHlnpHFTKCAvGKLQSPIDIQRRQIFYNH--KLESIHRDYYFTNATLVN--H 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169   89 TVLVKMSYNEDEipsvrGGPLAEKTplGYQFEQFHFHwgendtIGSEDLINNRAYPAELHVVLRNleypdfasaldKDHG 168
Cdd:PLN02202  92 VCNVAMFFGEGA-----GDVIIDNK--NYTLLQMHWH------TPSEHHLHGVQYAAELHMVHQA-----------KDGS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  169 IAVMAFFFQVGDKSTGGYEGFTNLLSQIDRKGKSvNMTNPLPLGE----YISKSVESYFSYTGSLTTPPCSEEVTWIDFT 244
Cdd:PLN02202 148 FAVVASLFKIGTEEPFLSQMKDKLVKLKEERFKG-NHTAQVEVGKidtrHIERKTRKYFRYIGSLTTPPCSENVSWTILG 226
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 21358169  245 TPIDITEKQLNAFRllTANDDHLKNNFRPIQPLNDR 280
Cdd:PLN02202 227 KVRSMSKEQVELLR--SPLDKSFKNNSRPCQPLNGR 260
 
Name Accession Description Interval E-value
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
34-286 1.69e-111

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 324.22  E-value: 1.69e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169    34 HGPEHWSEDYARCSGKHQSPINIDQVSAVEK-KFPKLEFFNFKVVPDNLQMTNNGHTVLVKMsyNEDEIPSVRGGPLAEK 112
Cdd:pfam00194   1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDpSLPPLTFQGYDVPPGKNTLTNNGHTVQVSL--DDGDPSTISGGPLATR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169   113 tplgYQFEQFHFHWGENDTIGSEDLINNRAYPAELHVVLRNLEYPDFASALDKDHGIAVMAFFFQVGDKSTGGYEGFTNL 192
Cdd:pfam00194  79 ----YRLVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNSKYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169   193 LSQIDRKGKSVNMTnPLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFRLLTAND-----DHL 267
Cdd:pfam00194 155 LDNIKYKGKSVLLP-PFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDggeepRPL 233
                         250
                  ....*....|....*....
gi 21358169   268 KNNFRPIQPLNDRTLYKNY 286
Cdd:pfam00194 234 VNNFRPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
28-281 2.48e-97

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: 288.06  E-value: 2.48e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169     28 FGYEGRHGPEHWSE-DYARCSGKHQSPINIDQVSAV-EKKFPKLEFFNFKvvPDNLQMTNNGHTVLVKMSyneDEIPSVR 105
Cdd:smart01057   1 WGYEGKNGPEHWGKlDPPFCGGKRQSPIDIVTAEAQyDPSLKPLKLSYDQ--PTAKRILNNGHTVQVNFD---DDGSTLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169    106 GGPLAEKtplgYQFEQFHFHWGENDTIGSEDLINNRAYPAELHVVLRNlEYPDFASALDKDHGIAVMAFFFQVGDKSTGG 185
Cdd:smart01057  76 GGPLPGR----YRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYN-SKGSFSEAVSKPGGLAVVAVFFKVGAEENPA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169    186 YEGFTNLLSQIDRKGKSVNMTnPLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFRLL--TAN 263
Cdd:smart01057 151 LQAILDHLPLIKYKGQETELT-PFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLlpMEG 229
                          250
                   ....*....|....*...
gi 21358169    264 DDHLKNNFRPIQPLNDRT 281
Cdd:smart01057 230 NEPLVNNARPLQPLNGRV 247
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
48-283 2.76e-89

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: 266.84  E-value: 2.76e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  48 GKHQSPINIDQVSAVekKFPKLEFFNFKVVP-DNLQMTNNGHTVLVKMsynEDEIPSVRGGPLAEKtplgYQFEQFHFHW 126
Cdd:cd00326   1 GKRQSPINIVTSAVV--YDPSLPPLNFDYYPtTSLTLVNNGHTVQVNF---DDDGGTLSGGGLPGR----YKLVQFHFHW 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 127 GENDTIGSEDLINNRAYPAELHVVLRNLEYPDFAsALDKDHGIAVMAFFFQVGDKSTGGYEGFTNLLSQIDRKGKSVNMT 206
Cdd:cd00326  72 GSENSPGSEHTIDGKRYPLELHLVHYNSDYYSSE-AAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLP 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21358169 207 nPLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFR-LLTANDDHLKNNFRPIQPLNDRTLY 283
Cdd:cd00326 151 -PFDLSDLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRsLLDREGKPLVNNYRPVQPLNGRVVY 227
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
48-284 3.26e-71

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: 220.99  E-value: 3.26e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  48 GKHQSPINIdqVSAVEKKFPKLEFFNFK---VVPDNLQMTNNGHTVLVKMsyneDEIPSVRGGPLAEKtplgYQFEQFHF 124
Cdd:cd03117   1 GKRQSPINI--VTKKVQYDENLTPFTFTgydDTTTNWTITNNGHTVQVTL----PDGAKISGGGLPGT----YKALQFHF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 125 HWGENDTIGSEDLINNRAYPAELHVVLRNLEYPDFASALDKDHGIAVMAFFFQVGDKSTGGYEGFTNLLSQIDRKGKSVN 204
Cdd:cd03117  71 HWGSNGSPGSEHTIDGERYPMELHIVHIKESYNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTN 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 205 MTNP----LPLGEYISKsvesYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFRLL----TANDDHLKNNFRPIQP 276
Cdd:cd03117 151 LTPFslrsLLPSVLLTK----YYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVlffdTDNGQPMVNNFRPVQP 226

                ....*...
gi 21358169 277 LNDRTLYK 284
Cdd:cd03117 227 LNGRVVYA 234
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
35-286 1.12e-63

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: 202.15  E-value: 1.12e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  35 GPEHWSEDYARCSGKHQSPINIDQVSAV-EKKFPKLEFFNFKVVP-DNLQMTNNGHTVlvKMSynedeIPS---VRGGPL 109
Cdd:cd03123   1 GEDHWPKKYPACGGKRQSPIDIQTDIVQfDPSLPPLELVGYDLPGtEEFTLTNNGHTV--QLS-----LPPtmhIRGGPG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 110 AEktplgYQFEQFHFHWGENDTI-GSEDLINNRAYPAELHVVLRN-LEYPDFASALDKDHGIAVMAFFFQVGDKSTGGYE 187
Cdd:cd03123  74 TE-----YTAAQLHLHWGGRGSLsGSEHTIDGIRFAAELHIVHYNsDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYE 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 188 GFTNLLSQIDRKGKSVNMTnPLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFR--LLTANDD 265
Cdd:cd03123 149 KIISHLHEIKYKGQETTVP-GFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLETLEntLMDTHNK 227
                       250       260
                ....*....|....*....|.
gi 21358169 266 HLKNNFRPIQPLNDRTLYKNY 286
Cdd:cd03123 228 TLQNNYRATQPLNGRVVEASF 248
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
35-284 4.71e-63

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: 200.66  E-value: 4.71e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  35 GPEHWSEDYARC-SGKHQSPINIDQVSAVEK-KFPKLEFFNFKVVPDNLQMTNNGHTVLVkMSYNEDEIPSVRGGPLAEK 112
Cdd:cd03122   1 NPKHWAKKYPACgEGRQQSPIDIVEDTQVQRqGLQPLHFDGYEELTASTTLENTGKTVIL-RLEGNSSDPFVSGGPLLGR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 113 tplgYQFEQFHFHWGENDTIGSEDLINNRAYPAELHVVLRNLEYPDFASALDKDHGIAVMAFFFQVGDKSTGGYEGFTNL 192
Cdd:cd03122  80 ----YKFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 193 LSQIDRKGKSVNMtNPLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFRLL-------TANDD 265
Cdd:cd03122 156 LRNVSRPGKEVEL-PPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELltrrqdgVMSGD 234
                       250
                ....*....|....*....
gi 21358169 266 HLKNNFRPIQPLNDRTLYK 284
Cdd:cd03122 235 YLPNNGRPQQPLGSRTVFS 253
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
1-284 1.69e-62

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 198.95  E-value: 1.69e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169   1 MRRCRNTPFAIVIAPILICASLVLAQDFGYEGRHGPEHW---SEDYARCS-GKHQSPINIDQvsAVEKKFPKLEFfNFKV 76
Cdd:COG3338   1 MKKRLLLALLLAAALPAAAAAAASAPHWSYEGETGPEHWgelSPEFATCAtGKNQSPIDIRT--AIKADLPPLKF-DYKP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  77 VPdnLQMTNNGHTVLVkmsyNEDEIPSVRggpLAEKTplgYQFEQFHFHwgendtIGSEDLINNRAYPAELHVVLRnley 156
Cdd:COG3338  78 TP--LEIVNNGHTIQV----NVDPGSTLT---VDGKR---YELKQFHFH------TPSEHTINGKSYPMEAHLVHK---- 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 157 pdfasalDKDHGIAVMAFFFQVGDKStggyEGFTNLLSQI-DRKGKSVNMTNPLPLGEYISKSvESYFSYTGSLTTPPCS 235
Cdd:COG3338 136 -------DADGELAVVGVLFEEGAEN----PALAKLWANLpLEAGEEVALDATIDLNDLLPED-RSYYRYSGSLTTPPCS 203
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 21358169 236 EEVTWIDFTTPIDITEKQLNAFRLLTAnddhlkNNFRPIQPLNDRTLYK 284
Cdd:COG3338 204 EGVLWIVLKQPITVSAEQIEAFARLYP------NNARPVQPLNGRLILE 246
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
24-282 9.51e-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: 9.51e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  24 LAQDFGYEGRHGPEHWSEDYARCSGKHQSPINIDQVSAveKKFPKLEFFNFKVVPDN-LQMTNNGHTVLVKMSYNEDEip 102
Cdd:cd03119   1 MSHHWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDA--KHDPSLKPLSVSYDPATaKTILNNGHSFNVEFDDTDDR-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 103 SV-RGGPLaektPLGYQFEQFHFHWGENDTIGSEDLINNRAYPAELHVVLRNLEYPDFASALDKDHGIAVMAFFFQVGdK 181
Cdd:cd03119  77 SVlRGGPL----TGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNSKYGSFGEAAKQPDGLAVVGVFLKVG-E 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 182 STGGYEGFTNLLSQIDRKGKSVNMTNPLPLGeYISKSVEsYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFRLLT 261
Cdd:cd03119 152 ANPELQKVLDALDSIKTKGKQAPFTNFDPSC-LLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLL 229
                       250       260
                ....*....|....*....|....*.
gi 21358169 262 ANDDH-----LKNNFRPIQPLNDRTL 282
Cdd:cd03119 230 FNAEGeppcpMVDNWRPPQPLKGRKV 255
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
35-284 3.13e-56

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: 182.09  E-value: 3.13e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  35 GPEHW---SEDYARCS-GKHQSPINIDQVSAVEKKFPKLeffNFKVVPDNLQMTNNGHTVLVKMsynEDEIPSVRggpLA 110
Cdd:cd03124   1 GPEHWgnlDPEFALCAtGKNQSPIDITTKAVVSDKLPPL---NYNYKPTSATLVNNGHTIQVNF---EGNGGTLT---ID 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 111 EKTplgYQFEQFHFHwgendtIGSEDLINNRAYPAELHVVLRNleypdfasaldKDHGIAVMAFFFQVGDKStggyEGFT 190
Cdd:cd03124  72 GET---YQLLQFHFH------SPSEHLINGKRYPLEAHLVHKS-----------KDGQLAVVAVLFEEGKEN----PFLK 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 191 NLLSQI-DRKGKSVNMTNPLPLGEYISKSvESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFRLLTanddhLKN 269
Cdd:cd03124 128 KILDNMpKKEGTEVNLPAILDPNELLPES-RSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAAV-----YPN 201
                       250
                ....*....|....*
gi 21358169 270 NFRPIQPLNDRTLYK 284
Cdd:cd03124 202 NARPVQPLNGREVLL 216
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
35-282 3.35e-50

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: 167.44  E-value: 3.35e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  35 GPEHWSEDYARCSGKHQSPINID-QVSAVEKKFPKLEFFNFKVVPD-NLQMTNNGHTVLVKMsynedeiPS---VRGGPL 109
Cdd:cd03150   1 GQPPWPSVSPACAGRFQSPVDIRpHLVAFCPALRPLELLGFDLPPSpSLRLLNNGHTVQLSL-------PSglrMALGPG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 110 AEktplgYQFEQFHFHWGENDTIGSEDLINNRAYPAELHVVLRNLEYPDFASALDKDHGIAVMAFFFQVGDKSTGGYEGF 189
Cdd:cd03150  74 QE-----YRALQLHLHWGAAGRPGSEHTVDGHRFPAEIHVVHLSTAFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 190 TNLLSQIDRKGkSVNMTNPLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFR--LLTANDDHL 267
Cdd:cd03150 149 LSRLSEISEEE-SETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSdsLWGPHDSRL 227
                       250
                ....*....|....*
gi 21358169 268 KNNFRPIQPLNDRTL 282
Cdd:cd03150 228 QLNFRATQPLNGRKI 242
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
35-286 8.09e-50

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: 166.50  E-value: 8.09e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  35 GPEHWSEDYARCSGKHQSPINIDQVSAV-EKKFPKLEFFNFKVVPDNLQMTNNGHTVLVkmsyneDEIPSVRggpLAEKT 113
Cdd:cd03125   1 DESHWPEKYPACGGKRQSPIDIQRREVRfNPSLLQLELVGYEKEQGEFTMTNNGHTVQI------DLPPTMS---ITTGD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 114 PLGYQFEQFHFHWG--ENDTIGSEDLINNRAYPAELHVVLRNLEYPDFASALDKDHGIAVMAFFFQVGDKSTGG-YEGFT 190
Cdd:cd03125  72 GTVYTAVQMHFHWGgrDSEISGSEHTIDGMRYVAELHIVHYNSKYKSYEEAKDKPDGLAVLAFLYKVGHYAENTyYSDFI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 191 NLLSQIDRKGKSVNMTNpLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFR--LLTANDDHLK 268
Cdd:cd03125 152 SKLAKIKYAGQTTTLTS-LDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLEntLMDHHNKTIR 230
                       250
                ....*....|....*...
gi 21358169 269 NNFRPIQPLNDRTLYKNY 286
Cdd:cd03125 231 NDYRRTQPLNHRVVEANF 248
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
48-282 2.07e-49

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: 165.01  E-value: 2.07e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  48 GKHQSPINIDQVSAVEKkfPKLEFFNFKVVP-DNLQMTNNGHTVLVKMSyNEDEIPSVRGGPLaektPLGYQFEQFHFHW 126
Cdd:cd03149   1 GNRQSPIDIVSSEAVYD--PKLKPLSLSYDPcTSLSISNNGHSVMVEFD-DSDDKTVITGGPL----ENPYRLKQFHFHW 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 127 GENDTIGSEDLINNRAYPAELHVVLRNL-EYPDFASALDKDHGIAVMAFFFQVGDKSTGgYEGFTNLLSQIDRKGKSVNM 205
Cdd:cd03149  74 GAKHGSGSEHTVDGKTFPSELHLVHWNAkKYKSFGEAAAAPDGLAVLGVFLETGDEHPG-LNRLTDALYMVRFKGTKAQF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 206 T--NPLPLgeyISKSVEsYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFR--LLTANDD---HLKNNFRPIQPLN 278
Cdd:cd03149 153 LdfNPKCL---LPKSLD-YWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRelLFTSEEDqrnHMVNNFRPPQPLK 228

                ....
gi 21358169 279 DRTL 282
Cdd:cd03149 229 GRTV 232
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
35-286 4.82e-49

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: 164.63  E-value: 4.82e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  35 GPEHWSEDYARCSGKHQSPINIDQVSAV-EKKFPKLEFFNFKVVP-DNLQMTNNGHTVlvKMSYnedeIPSVRGGPLaek 112
Cdd:cd03126   1 GENSWPKKYPFCGGVAQSPIDIHTDILQyDSSLPPLEFHGYNVSGtEQFTLTNNGHTV--QLSL----PPTMHIGGL--- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 113 tPLGYQFEQFHFHWGE-NDTIGSEDLINNRAYPAELHVVLRNLE-YPDFASALDKDHGIAVMAFFFQVGDKSTGgYEGFT 190
Cdd:cd03126  72 -PFKYTASQLHLHWGQrGSPEGSEHTISGKHFAAELHIVHYNSDkYPDISTAMNKSQGLAVLGILIEVGPFNPS-YEKIF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 191 NLLSQIDRKGKSVNMTnPLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFR--LLTANDD--- 265
Cdd:cd03126 150 SHLHEVKYKDQKVSVP-GFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALEtaLYSTEEDesr 228
                       250       260
                ....*....|....*....|.
gi 21358169 266 HLKNNFRPIQPLNDRTLYKNY 286
Cdd:cd03126 229 EMVNNYRQVQPFNERLVFASF 249
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
48-286 4.59e-47

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: 158.85  E-value: 4.59e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  48 GKHQSPINIDQVSAVEKkfPKLEFFNFKVVPDN-LQMTNNGHTVLVKMSYNEDEiPSVRGGPLAEKtplgYQFEQFHFHW 126
Cdd:cd03118   1 GTRQSPINIQWRDSVYD--PQLAPLRVSYDPATcLYIWNNGYSFQVEFDDSTDK-SGISGGPLENH----YRLKQFHFHW 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 127 GENDTIGSEDLINNRAYPAELHVVLRN-LEYPDFASALDKDHGIAVMAFFFQVGdKSTGGYEGFTNLLSQIDRKGKSVNM 205
Cdd:cd03118  74 GANNEWGSEHTVDGHTYPAELHLVHWNsVKYENFEEAVMEENGLAVIGVFLKLG-AHHEGLQKLVDALPEVRHKDTVVEF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 206 TNPLPlgEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFR--LLTA---NDDHLKNNFRPIQPLNDR 280
Cdd:cd03118 153 NPFDP--SCLLPACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRtlLFTSrgeEEKVMVNNFRPLQPLMNR 230

                ....*.
gi 21358169 281 TLYKNY 286
Cdd:cd03118 231 KVRSSF 236
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
39-282 7.12e-46

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: 156.55  E-value: 7.12e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  39 WSEDYARCSGKHQSPINIDQVSAVEKKF---PKLEFfNFKVVPDnLQMTNNGHTVLVKMSYNedeiPSVRGGPLaektPL 115
Cdd:cd03120   4 WGLLFPEANGEYQSPINLNSREARYDPSlleVRLSP-NYVVCRD-CEVINDGHTIQIILKSK----SVLSGGPL----PQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 116 GYQFE--QFHFHWGENDTIGSEDLINNRAYPAELHVVLRNLE-YPDFASALDKDHGIAVMAFFFQVGdKSTGGYEGFTNL 192
Cdd:cd03120  74 GHEFElaEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTlYSSLEEAMGKPHGIAIIALFVQIG-KEHVGLKAVTEI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 193 LSQIDRKGKSVNMTNPLPLGEYISKSVESYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFRLLT----------A 262
Cdd:cd03120 153 LQDIQYKGKSKTIPCFNPNTLLPDPLLRDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLRthvkgaelveG 232
                       250       260
                ....*....|....*....|
gi 21358169 263 NDDHLKNNFRPIQPLNDRTL 282
Cdd:cd03120 233 CDGLLGDNFRPTQPLSDRVI 252
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
35-285 1.12e-43

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: 150.64  E-value: 1.12e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  35 GPEHW---SEDYARCS-GKHQSPINIDQVSAVEKKF-PKLEFFNFKVVpdNLQMTNNGHTVLVKMSYneDEIPSVRGGPL 109
Cdd:cd03121   1 GPSFWglvNSAWNLCSkGRRQSPVDIEPSRLLFDPFlTPLRIDTGRKV--SGTFYNTGRHVSFRPDK--DPVVNISGGPL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 110 AEKtplgYQFEQFHFHWGENDTIGSEDLINNRAYPAELHVVLRNLE-YPDFASALDKDHGIAVMAFFFQVGDKSTGGYEG 188
Cdd:cd03121  77 SYR----YRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSElYPNFSEASKSPNGLVIVSLFVKIGETSNPELRR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169 189 FTNLL--SQIDRKGKSVNMTNPLPLGEYISKSveSYFSYTGSLTTPPCSEEVTWIDFTTPIDITEKQLNAFRLLTANDDH 266
Cdd:cd03121 153 LTNRDtiTSIRYKGDAYFLQDLSIELLLPETD--HYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPS 230
                       250       260
                ....*....|....*....|....
gi 21358169 267 -----LKNNFRPIQPLNDRTLYKN 285
Cdd:cd03121 231 qekapMSPNFRPVQPLNNRPVRTN 254
PLN02202 PLN02202
carbonate dehydratase
17-280 7.28e-20

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 87.80  E-value: 7.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169   17 LICASLVLAQD----FGYEGRHGPEHWSE---DYARCS-GKHQSPINIDQVSAVEKKfpKLEFFNFKVVPDNLQMTNngH 88
Cdd:PLN02202  16 LICIAPADAQTegvvFGYKGKNGPNQWGHlnpHFTKCAvGKLQSPIDIQRRQIFYNH--KLESIHRDYYFTNATLVN--H 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169   89 TVLVKMSYNEDEipsvrGGPLAEKTplGYQFEQFHFHwgendtIGSEDLINNRAYPAELHVVLRNleypdfasaldKDHG 168
Cdd:PLN02202  92 VCNVAMFFGEGA-----GDVIIDNK--NYTLLQMHWH------TPSEHHLHGVQYAAELHMVHQA-----------KDGS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  169 IAVMAFFFQVGDKSTGGYEGFTNLLSQIDRKGKSvNMTNPLPLGE----YISKSVESYFSYTGSLTTPPCSEEVTWIDFT 244
Cdd:PLN02202 148 FAVVASLFKIGTEEPFLSQMKDKLVKLKEERFKG-NHTAQVEVGKidtrHIERKTRKYFRYIGSLTTPPCSENVSWTILG 226
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 21358169  245 TPIDITEKQLNAFRllTANDDHLKNNFRPIQPLNDR 280
Cdd:PLN02202 227 KVRSMSKEQVELLR--SPLDKSFKNNSRPCQPLNGR 260
PLN02179 PLN02179
carbonic anhydrase
28-240 3.78e-11

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 62.31  E-value: 3.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169   28 FGYEGR--HGPEHWSE---DYARCS-GKHQSPINI--DQVSAVEKKFPKLEFfnfkvVPDNLQMTNNGHTVLVkmSYNED 99
Cdd:PLN02179  37 FTYKQKteKGPAEWGKlnpQWKVCStGKYQSPIDLtdERVSLIHDQALSRHY-----KPAPAVIQSRGHDVMV--SWKGD 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358169  100 eipsvrGGPLA-EKTplGYQFEQFHFHwgendtIGSEDLINNRAYPAELHVVlrnleypdFASALDKdhgIAVMAFFFQV 178
Cdd:PLN02179 110 ------AGKITiHQT--DYKLVQCHWH------SPSEHTINGTSYDLELHMV--------HTSASGK---TAVVGVLYKL 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21358169  179 GDKStggyEGFTNLLSQIDRKGK---SVNMTNPlplgEYISKSVESYFSYTGSLTTPPCSEEVTW 240
Cdd:PLN02179 165 GEPD----EFLTKLLNGIKGVGKkeiNLGIVDP----RDIRFETNNFYRYIGSLTIPPCTEGVIW 221
 
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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