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Conserved domains on  [gi|530364503|ref|XP_005245116|]
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carbonic anhydrase 14 isoform X1 [Homo sapiens]

Protein Classification

carbonic anhydrase family protein; carbonic anhydrase( domain architecture ID 10123249)

carbonic anhydrase family protein similar to carbonic anhydrase, which catalyzes the reversible hydration of gaseous carbon dioxide to carbonic acid; carbonic anhydrase (CA) catalyzes the zinc-dependent reversible hydration of carbon dioxide into bicarbonate and a proton

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
29-278 4.21e-177

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: 490.50  E-value: 4.21e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  29 GQDHWPASYPECGNNAQSPIDIQTDSVTFDPDLPALQPHGYDQPGTEPLDLHNNGHTVQLSLPSTLYLGGLPRKYVAAQL 108
Cdd:cd03126    1 GENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHIGGLPFKYTASQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 109 HLHWGQKGSPGGSEHQINSEATFAELHIVHYDSDSYDSLSEAAERPQGLAVLGILIEVGEtKNIAYEHILSHLHEVRHKD 188
Cdd:cd03126   81 HLHWGQRGSPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVGP-FNPSYEKIFSHLHEVKYKD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 189 QKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEEEPSKLLVQNYRALQP 268
Cdd:cd03126  160 QKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALETALYSTEEDESREMVNNYRQVQP 239
                        250
                 ....*....|
gi 530364503 269 LNQRMVFASF 278
Cdd:cd03126  240 FNERLVFASF 249
 
Name Accession Description Interval E-value
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
29-278 4.21e-177

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: 490.50  E-value: 4.21e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  29 GQDHWPASYPECGNNAQSPIDIQTDSVTFDPDLPALQPHGYDQPGTEPLDLHNNGHTVQLSLPSTLYLGGLPRKYVAAQL 108
Cdd:cd03126    1 GENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHIGGLPFKYTASQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 109 HLHWGQKGSPGGSEHQINSEATFAELHIVHYDSDSYDSLSEAAERPQGLAVLGILIEVGEtKNIAYEHILSHLHEVRHKD 188
Cdd:cd03126   81 HLHWGQRGSPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVGP-FNPSYEKIFSHLHEVKYKD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 189 QKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEEEPSKLLVQNYRALQP 268
Cdd:cd03126  160 QKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALETALYSTEEDESREMVNNYRQVQP 239
                        250
                 ....*....|
gi 530364503 269 LNQRMVFASF 278
Cdd:cd03126  240 FNERLVFASF 249
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
28-278 2.99e-120

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 346.56  E-value: 2.99e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503   28 HGQDHWPASYPECGNNAQSPIDIQTDSVTFDPDLPALQPHGYDQPGTEPlDLHNNGHTVQLSL----PSTLYLGGLPRKY 103
Cdd:pfam00194   1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKN-TLTNNGHTVQVSLddgdPSTISGGPLATRY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  104 VAAQLHLHWGQKGSPGgSEHQINSEATFAELHIVHYDSDsYDSLSEAAERPQGLAVLGILIEVGETKNIAYEHILSHLHE 183
Cdd:pfam00194  80 RLVQFHFHWGSTDSRG-SEHTIDGKRYPAELHIVHYNSK-YKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALDN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  184 VRHKDQKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEEEPSKLLVQNY 263
Cdd:pfam00194 158 IKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEPRPLVNNF 237
                         250
                  ....*....|....*
gi 530364503  264 RALQPLNQRMVFASF 278
Cdd:pfam00194 238 RPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
22-273 1.17e-106

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: 311.94  E-value: 1.17e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503    22 WTYEGPHGQDHWPASYPECGN-NAQSPIDIQTDSVTFDPDLPALQPHgYDQPGtePLDLHNNGHTVQLSLP---STLYLG 97
Cdd:smart01057   1 WGYEGKNGPEHWGKLDPPFCGgKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPT--AKRILNNGHTVQVNFDddgSTLSGG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503    98 GLPRKYVAAQLHLHWGQKGSPGgSEHQINSEATFAELHIVHYDSDSydSLSEAAERPQGLAVLGILIEVGETKNIAYEHI 177
Cdd:smart01057  78 PLPGRYRLKQFHFHWGGSDSEG-SEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEENPALQAI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503   178 LSHLHEVRHKDQKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQgTLFSTEEEPSk 257
Cdd:smart01057 155 LDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFR-TLLPMEGNEP- 232
                          250
                   ....*....|....*.
gi 530364503   258 lLVQNYRALQPLNQRM 273
Cdd:smart01057 233 -LVNNARPLQPLNGRV 247
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
15-277 7.26e-60

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 192.41  E-value: 7.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  15 AADGGQHWTYEGPHGQDHWP---ASYPECGN-NAQSPIDIQTdsvTFDPDLPALQPHgYdqpGTEPLDLHNNGHTVQLSL 90
Cdd:COG3338   21 AAASAPHWSYEGETGPEHWGelsPEFATCATgKNQSPIDIRT---AIKADLPPLKFD-Y---KPTPLEIVNNGHTIQVNV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  91 P--STLYLGGlpRKYVAAQLHLHwgqkgSPggSEHQINSEATFAELHIVHYDSDSydslseaaerpqGLAVLGILIEVGE 168
Cdd:COG3338   94 DpgSTLTVDG--KRYELKQFHFH-----TP--SEHTINGKSYPMEAHLVHKDADG------------ELAVVGVLFEEGA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 169 TkNIAYEHILSHLHEVRHkDQKTSVPPFNLRELLPKQLGqYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQgtl 248
Cdd:COG3338  153 E-NPALAKLWANLPLEAG-EEVALDATIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFA--- 226
                        250       260
                 ....*....|....*....|....*....
gi 530364503 249 fsteeepsKLLVQNYRALQPLNQRMVFAS 277
Cdd:COG3338  227 --------RLYPNNARPVQPLNGRLILES 247
PLN02202 PLN02202
carbonate dehydratase
24-274 6.73e-15

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 73.94  E-value: 6.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  24 YEGPHGQDHWPASYPECGNNA----QSPIDIQTDSVTFDPDLPALQPHGYDQPGTepldLHNngHTVQLSLPSTLYLGGL 99
Cdd:PLN02202  33 YKGKNGPNQWGHLNPHFTKCAvgklQSPIDIQRRQIFYNHKLESIHRDYYFTNAT----LVN--HVCNVAMFFGEGAGDV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 100 ---PRKYVAAQLHLHwgqkgSPggSEHQINSEATFAELHIVHYDSDSydslseaaerpqGLAVLGILIEVGETKNI--AY 174
Cdd:PLN02202 107 iidNKNYTLLQMHWH-----TP--SEHHLHGVQYAAELHMVHQAKDG------------SFAVVASLFKIGTEEPFlsQM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 175 EHILSHLHEVRHKDQKTS---VPPFNLRELlPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLfst 251
Cdd:PLN02202 168 KDKLVKLKEERFKGNHTAqveVGKIDTRHI-ERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPL--- 243
                        250       260
                 ....*....|....*....|...
gi 530364503 252 eeepSKLLVQNYRALQPLNQRMV 274
Cdd:PLN02202 244 ----DKSFKNNSRPCQPLNGRRV 262
 
Name Accession Description Interval E-value
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
29-278 4.21e-177

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: 490.50  E-value: 4.21e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  29 GQDHWPASYPECGNNAQSPIDIQTDSVTFDPDLPALQPHGYDQPGTEPLDLHNNGHTVQLSLPSTLYLGGLPRKYVAAQL 108
Cdd:cd03126    1 GENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHIGGLPFKYTASQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 109 HLHWGQKGSPGGSEHQINSEATFAELHIVHYDSDSYDSLSEAAERPQGLAVLGILIEVGEtKNIAYEHILSHLHEVRHKD 188
Cdd:cd03126   81 HLHWGQRGSPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVGP-FNPSYEKIFSHLHEVKYKD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 189 QKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEEEPSKLLVQNYRALQP 268
Cdd:cd03126  160 QKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALETALYSTEEDESREMVNNYRQVQP 239
                        250
                 ....*....|
gi 530364503 269 LNQRMVFASF 278
Cdd:cd03126  240 FNERLVFASF 249
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
29-278 3.77e-158

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: 442.13  E-value: 3.77e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  29 GQDHWPASYPECGNNAQSPIDIQTDSVTFDPDLPALQPHGYDQPGTEPLDLHNNGHTVQLSLPSTLYLGGLP-RKYVAAQ 107
Cdd:cd03123    1 GEDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHIRGGPgTEYTAAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 108 LHLHWGQKGSPGGSEHQINSEATFAELHIVHYDSDSYDSLSEAAERPQGLAVLGILIEVGETKNIAYEHILSHLHEVRHK 187
Cdd:cd03123   81 LHLHWGGRGSLSGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKYK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 188 DQKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEeepSKLLVQNYRALQ 267
Cdd:cd03123  161 GQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLETLENTLMDTH---NKTLQNNYRATQ 237
                        250
                 ....*....|.
gi 530364503 268 PLNQRMVFASF 278
Cdd:cd03123  238 PLNGRVVEASF 248
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
28-278 2.99e-120

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 346.56  E-value: 2.99e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503   28 HGQDHWPASYPECGNNAQSPIDIQTDSVTFDPDLPALQPHGYDQPGTEPlDLHNNGHTVQLSL----PSTLYLGGLPRKY 103
Cdd:pfam00194   1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKN-TLTNNGHTVQVSLddgdPSTISGGPLATRY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  104 VAAQLHLHWGQKGSPGgSEHQINSEATFAELHIVHYDSDsYDSLSEAAERPQGLAVLGILIEVGETKNIAYEHILSHLHE 183
Cdd:pfam00194  80 RLVQFHFHWGSTDSRG-SEHTIDGKRYPAELHIVHYNSK-YKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALDN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  184 VRHKDQKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEEEPSKLLVQNY 263
Cdd:pfam00194 158 IKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEPRPLVNNF 237
                         250
                  ....*....|....*
gi 530364503  264 RALQPLNQRMVFASF 278
Cdd:pfam00194 238 RPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
22-273 1.17e-106

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: 311.94  E-value: 1.17e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503    22 WTYEGPHGQDHWPASYPECGN-NAQSPIDIQTDSVTFDPDLPALQPHgYDQPGtePLDLHNNGHTVQLSLP---STLYLG 97
Cdd:smart01057   1 WGYEGKNGPEHWGKLDPPFCGgKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPT--AKRILNNGHTVQVNFDddgSTLSGG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503    98 GLPRKYVAAQLHLHWGQKGSPGgSEHQINSEATFAELHIVHYDSDSydSLSEAAERPQGLAVLGILIEVGETKNIAYEHI 177
Cdd:smart01057  78 PLPGRYRLKQFHFHWGGSDSEG-SEHTIDGKRFPLELHLVHYNSKG--SFSEAVSKPGGLAVVAVFFKVGAEENPALQAI 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503   178 LSHLHEVRHKDQKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQgTLFSTEEEPSk 257
Cdd:smart01057 155 LDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFR-TLLPMEGNEP- 232
                          250
                   ....*....|....*.
gi 530364503   258 lLVQNYRALQPLNQRM 273
Cdd:smart01057 233 -LVNNARPLQPLNGRV 247
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
45-275 4.18e-96

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: 284.18  E-value: 4.18e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  45 QSPIDIQTDSVTFDPDLPALQPHGYDqpgTEPLDLHNNGHTVQLSLP---STLYLGGLPRKYVAAQLHLHWGQKGSPGgS 121
Cdd:cd00326    4 QSPINIVTSAVVYDPSLPPLNFDYYP---TTSLTLVNNGHTVQVNFDddgGTLSGGGLPGRYKLVQFHFHWGSENSPG-S 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 122 EHQINSEATFAELHIVHYDSDSYDSlsEAAERPQGLAVLGILIEVGETKNIAYEHILSHLHEVRHKDQKTSVPPFNLREL 201
Cdd:cd00326   80 EHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLSDL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530364503 202 LPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTeeepSKLLVQNYRALQPLNQRMVF 275
Cdd:cd00326  158 LPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDRE----GKPLVNNYRPVQPLNGRVVY 227
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
43-276 6.20e-91

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: 271.45  E-value: 6.20e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  43 NAQSPIDIQTDSVTFDPDLPALQPHGYDQPgTEPLDLHNNGHTVQLSLPSTLYL--GGLPRKYVAAQLHLHWGQKGSPGg 120
Cdd:cd03117    2 KRQSPINIVTKKVQYDENLTPFTFTGYDDT-TTNWTITNNGHTVQVTLPDGAKIsgGGLPGTYKALQFHFHWGSNGSPG- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 121 SEHQINSEATFAELHIVHYDSdSYDSLSEAAERPQGLAVLGILIEVGETKNIAYEHILSHLHEVRHKDQKTSVPPFNLRE 200
Cdd:cd03117   80 SEHTIDGERYPMELHIVHIKE-SYNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSLRS 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530364503 201 LLPKQ-LGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEEEpSKLLVQNYRALQPLNQRMVFA 276
Cdd:cd03117  159 LLPSVlLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDN-GQPMVNNFRPVQPLNGRVVYA 234
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
29-278 6.17e-87

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: 261.81  E-value: 6.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  29 GQDHWPASYPECGNNAQSPIDIQTDSVTFDPDLPALQPHGYDQPGTEPLDLHNNGHTVQLSLPSTLYLG-GLPRKYVAAQ 107
Cdd:cd03150    1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMAlGPGQEYRALQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 108 LHLHWGQKGSPGgSEHQINSEATFAELHIVHYDSdSYDSLSEAAERPQGLAVLGILIEVGETKNIAYEHILSHLHEVRHK 187
Cdd:cd03150   81 LHLHWGAAGRPG-SEHTVDGHRFPAEIHVVHLST-AFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEISEE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 188 DQKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSteeEPSKLLVQNYRALQ 267
Cdd:cd03150  159 ESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWG---PHDSRLQLNFRATQ 235
                        250
                 ....*....|.
gi 530364503 268 PLNQRMVFASF 278
Cdd:cd03150  236 PLNGRKIEASF 246
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
29-278 2.98e-79

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: 242.00  E-value: 2.98e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  29 GQDHWPASYPECGNNAQSPIDIQTDSVTFDPDLPALQPHGYDQPGTEpLDLHNNGHTVQLSLPSTLYLG-GLPRKYVAAQ 107
Cdd:cd03125    1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGE-FTMTNNGHTVQIDLPPTMSITtGDGTVYTAVQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 108 LHLHWGQKGSP-GGSEHQINSEATFAELHIVHYDSDsYDSLSEAAERPQGLAVLGILIEVGE-TKNIAYEHILSHLHEVR 185
Cdd:cd03125   80 MHFHWGGRDSEiSGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLYKVGHyAENTYYSDFISKLAKIK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 186 HKDQKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEeepSKLLVQNYRA 265
Cdd:cd03125  159 YAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLENTLMDHH---NKTIRNDYRR 235
                        250
                 ....*....|...
gi 530364503 266 LQPLNQRMVFASF 278
Cdd:cd03125  236 TQPLNHRVVEANF 248
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
21-278 3.05e-64

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: 204.21  E-value: 3.05e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  21 HWTYEGPHGQDHWPASYPECGNNAQSPIDIQTDSVTFDPdlpALQP--HGYDqPGTEPLDLhNNGHTVQLSL-----PST 93
Cdd:cd03119    4 HWGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDP---SLKPlsVSYD-PATAKTIL-NNGHSFNVEFddtddRSV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  94 LYLGGLPRKYVAAQLHLHWGQkgSPG-GSEHQINSEATFAELHIVHYDSdSYDSLSEAAERPQGLAVLGILIEVGETKNi 172
Cdd:cd03119   79 LRGGPLTGSYRLRQFHFHWGS--SDDhGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVGEANP- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 173 AYEHILSHLHEVRHKDQKTSVPPFNLRELLPKQLgQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTE 252
Cdd:cd03119  155 ELQKVLDALDSIKTKGKQAPFTNFDPSCLLPASL-DYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAE 233
                        250       260
                 ....*....|....*....|....*.
gi 530364503 253 EEPSKLLVQNYRALQPLNQRMVFASF 278
Cdd:cd03119  234 GEPPCPMVDNWRPPQPLKGRKVRASF 259
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
15-277 7.26e-60

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 192.41  E-value: 7.26e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  15 AADGGQHWTYEGPHGQDHWP---ASYPECGN-NAQSPIDIQTdsvTFDPDLPALQPHgYdqpGTEPLDLHNNGHTVQLSL 90
Cdd:COG3338   21 AAASAPHWSYEGETGPEHWGelsPEFATCATgKNQSPIDIRT---AIKADLPPLKFD-Y---KPTPLEIVNNGHTIQVNV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  91 P--STLYLGGlpRKYVAAQLHLHwgqkgSPggSEHQINSEATFAELHIVHYDSDSydslseaaerpqGLAVLGILIEVGE 168
Cdd:COG3338   94 DpgSTLTVDG--KRYELKQFHFH-----TP--SEHTINGKSYPMEAHLVHKDADG------------ELAVVGVLFEEGA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 169 TkNIAYEHILSHLHEVRHkDQKTSVPPFNLRELLPKQLGqYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQgtl 248
Cdd:COG3338  153 E-NPALAKLWANLPLEAG-EEVALDATIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFA--- 226
                        250       260
                 ....*....|....*....|....*....
gi 530364503 249 fsteeepsKLLVQNYRALQPLNQRMVFAS 277
Cdd:COG3338  227 --------RLYPNNARPVQPLNGRLILES 247
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
43-278 1.00e-58

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: 189.28  E-value: 1.00e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  43 NAQSPIDIQTDSVTFDPdlpALQPHGYDQPGTEPLDLHNNGHTVQLSL----PSTLYLGG-LPRKYVAAQLHLHWGQKGS 117
Cdd:cd03149    2 NRQSPIDIVSSEAVYDP---KLKPLSLSYDPCTSLSISNNGHSVMVEFddsdDKTVITGGpLENPYRLKQFHFHWGAKHG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 118 pGGSEHQINSEATFAELHIVHYDSDSYDSLSEAAERPQGLAVLGILIEVGEtKNIAYEHILSHLHEVRHKDQKTSVPPFN 197
Cdd:cd03149   79 -SGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETGD-EHPGLNRLTDALYMVRFKGTKAQFLDFN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 198 LRELLPKQLgQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEEEPSKLLVQNYRALQPLNQRMVFAS 277
Cdd:cd03149  157 PKCLLPKSL-DYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHMVNNFRPPQPLKGRTVRAS 235

                 .
gi 530364503 278 F 278
Cdd:cd03149  236 F 236
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
29-276 1.81e-58

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: 189.10  E-value: 1.81e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  29 GQDHWPASYPECGNNA-QSPIDIQTDSVTFDPDLPALQPHGYDQPgTEPLDLHNNGHTVQLSL---PSTLYL--GGLPRK 102
Cdd:cd03122    1 NPKHWAKKYPACGEGRqQSPIDIVEDTQVQRQGLQPLHFDGYEEL-TASTTLENTGKTVILRLegnSSDPFVsgGPLLGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 103 YVAAQLHLHWGQKGSpGGSEHQINSEATFAELHIVHYDSDSYDSLsEAAERPQGLAVLGILIEVGETKNIAYEHILSHLH 182
Cdd:cd03122   80 YKFSEITFHWGTCNS-DGSEHSIDGHKFPLEMQILHRNTDFFDSF-EAIKSPGGVLALAYLFELSHEDNPFLDPIIEGLR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 183 EVRHKDQKTSVPPFNLRELLPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLqGTLFSTEEEPSKL---L 259
Cdd:cd03122  158 NVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAF-RELLTRRQDGVMSgdyL 236
                        250
                 ....*....|....*..
gi 530364503 260 VQNYRALQPLNQRMVFA 276
Cdd:cd03122  237 PNNGRPQQPLGSRTVFS 253
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
29-274 2.06e-52

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: 172.07  E-value: 2.06e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  29 GQDHWPASYPE---CGN-NAQSPIDIQTDSVTFDPdLPALQPhgydQPGTEPLDLHNNGHTVQLSLP---STLYLGGlpR 101
Cdd:cd03124    1 GPEHWGNLDPEfalCATgKNQSPIDITTKAVVSDK-LPPLNY----NYKPTSATLVNNGHTIQVNFEgngGTLTIDG--E 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 102 KYVAAQLHLHwgqkgSPggSEHQINSEATFAELHIVHYDSDsydslseaaerpQGLAVLGILIEVGETkNIAYEHILSHL 181
Cdd:cd03124   74 TYQLLQFHFH-----SP--SEHLINGKRYPLEAHLVHKSKD------------GQLAVVAVLFEEGKE-NPFLKKILDNM 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 182 HEVrhKDQKTSVPPF-NLRELLPKQLGqYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTeeepskllv 260
Cdd:cd03124  134 PKK--EGTEVNLPAIlDPNELLPESRS-YYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAAVYPN--------- 201
                        250
                 ....*....|....
gi 530364503 261 qNYRALQPLNQRMV 274
Cdd:cd03124  202 -NARPVQPLNGREV 214
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
45-278 5.26e-50

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: 166.56  E-value: 5.26e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  45 QSPIDIQTDSVTFDPDLPALQPHgYDqPGTePLDLHNNGHTVQLSL-----PSTLYLGGLPRKYVAAQLHLHWGQKGSpG 119
Cdd:cd03118    4 QSPINIQWRDSVYDPQLAPLRVS-YD-PAT-CLYIWNNGYSFQVEFddstdKSGISGGPLENHYRLKQFHFHWGANNE-W 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 120 GSEHQINSEATFAELHIVHYDSDSYDSLSEAAERPQGLAVLGILIEVGEtKNIAYEHILSHLHEVRHKDQKTSVPPFNLR 199
Cdd:cd03118   80 GSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGA-HHEGLQKLVDALPEVRHKDTVVEFNPFDPS 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530364503 200 ELLPkQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLFSTEEEPSKLLVQNYRALQPLNQRMVFASF 278
Cdd:cd03118  159 CLLP-ACRDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLFTSRGEEEKVMVNNFRPLQPLMNRKVRSSF 236
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
45-274 2.62e-44

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: 152.57  E-value: 2.62e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  45 QSPIDIQTDSVTFDPDLPALQPHGYDQPGTEpldLHNNGHTVQLSL---PSTLYLGG-LPRKYVAAQLHLHWGQKGSpGG 120
Cdd:cd03121   21 QSPVDIEPSRLLFDPFLTPLRIDTGRKVSGT---FYNTGRHVSFRPdkdPVVNISGGpLSYRYRLEEIRLHFGREDE-QG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 121 SEHQINSEATFAELHIVHYDSDSYDSLSEAAERPQGLAVLGILIEVGETKNIAYEHIL--SHLHEVRHKDQKTSVPPFNL 198
Cdd:cd03121   97 SEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTnrDTITSIRYKGDAYFLQDLSI 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530364503 199 RELLPKQLGqYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLqGTLFSTEEEPSKL-LVQNYRALQPLNQRMV 274
Cdd:cd03121  177 ELLLPETDH-YITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSL-RLLSQNSPSQEKApMSPNFRPVQPLNNRPV 251
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
33-278 7.56e-43

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: 148.85  E-value: 7.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  33 WPASYPECGNNAQSPIDIQTDSVTFDPDLpalqphgyDQPGTEP-------LDLHNNGHTVQLSLPSTLYLGG--LPR-- 101
Cdd:cd03120    4 WGLLFPEANGEYQSPINLNSREARYDPSL--------LEVRLSPnyvvcrdCEVINDGHTIQIILKSKSVLSGgpLPQgh 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 102 KYVAAQLHLHWGQKGSPGgSEHQINSEATFAELHIVHYDSDSYDSLSEAAERPQGLAVLGILIEVGEtKNIAYEHILSHL 181
Cdd:cd03120   76 EFELAEVRFHWGRENQRG-SEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIGK-EHVGLKAVTEIL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 182 HEVRHKDQKTSVPPFNLRELLPK-QLGQYFRYNGSLTTPPCYQSVLWTVF---YRRSQISMEQLEKLQGTLFSTE--EEP 255
Cdd:cd03120  154 QDIQYKGKSKTIPCFNPNTLLPDpLLRDYWVYEGSLTTPPCSEGVTWILFrypLTISQSQIEEFRRLRTHVKGAElvEGC 233
                        250       260
                 ....*....|....*....|...
gi 530364503 256 SKLLVQNYRALQPLNQRMVFASF 278
Cdd:cd03120  234 DGLLGDNFRPTQPLSDRVIRAAF 256
PLN02202 PLN02202
carbonate dehydratase
24-274 6.73e-15

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 73.94  E-value: 6.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  24 YEGPHGQDHWPASYPECGNNA----QSPIDIQTDSVTFDPDLPALQPHGYDQPGTepldLHNngHTVQLSLPSTLYLGGL 99
Cdd:PLN02202  33 YKGKNGPNQWGHLNPHFTKCAvgklQSPIDIQRRQIFYNHKLESIHRDYYFTNAT----LVN--HVCNVAMFFGEGAGDV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 100 ---PRKYVAAQLHLHwgqkgSPggSEHQINSEATFAELHIVHYDSDSydslseaaerpqGLAVLGILIEVGETKNI--AY 174
Cdd:PLN02202 107 iidNKNYTLLQMHWH-----TP--SEHHLHGVQYAAELHMVHQAKDG------------SFAVVASLFKIGTEEPFlsQM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503 175 EHILSHLHEVRHKDQKTS---VPPFNLRELlPKQLGQYFRYNGSLTTPPCYQSVLWTVFYRRSQISMEQLEKLQGTLfst 251
Cdd:PLN02202 168 KDKLVKLKEERFKGNHTAqveVGKIDTRHI-ERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPL--- 243
                        250       260
                 ....*....|....*....|...
gi 530364503 252 eeepSKLLVQNYRALQPLNQRMV 274
Cdd:PLN02202 244 ----DKSFKNNSRPCQPLNGRRV 262
PLN02179 PLN02179
carbonic anhydrase
23-232 1.54e-11

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 63.46  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  23 TYEGPHGQDHWPASYPECGNNA-QSPIDIQTDSVTFDPDlPALQPHGYDQPGTepldLHNNGHTVQLSLPS-----TLYl 96
Cdd:PLN02179  43 TEKGPAEWGKLNPQWKVCSTGKyQSPIDLTDERVSLIHD-QALSRHYKPAPAV----IQSRGHDVMVSWKGdagkiTIH- 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530364503  97 gglPRKYVAAQLHLHwgqkgSPggSEHQINSEATFAELHIVHydsdsydslSEAAERPqglAVLGILIEVGETKNIAYEh 176
Cdd:PLN02179 117 ---QTDYKLVQCHWH-----SP--SEHTINGTSYDLELHMVH---------TSASGKT---AVVGVLYKLGEPDEFLTK- 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530364503 177 ILSHLHEVRHKDQKTS-VPPFNLRellpKQLGQYFRYNGSLTTPPCYQSVLWTVFYR 232
Cdd:PLN02179 174 LLNGIKGVGKKEINLGiVDPRDIR----FETNNFYRYIGSLTIPPCTEGVIWTVVKR 226
 
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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