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Conserved domains on  [gi|395132471|ref|NP_001257430|]
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carbonic anhydrase 6 isoform 3 precursor [Homo sapiens]

Protein Classification

carbonic anhydrase family protein( domain architecture ID 275)

carbonic anhydrase family protein similar to carbonic anhydrase, which catalyzes the reversible hydration of gaseous carbon dioxide to carbonic acid

CATH:  3.10.200.10
Gene Ontology:  GO:0004089|GO:0008270|GO:0006730
PubMed:  10978542|18336305
SCOP:  4002732

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
alpha_CA super family cl00012
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 25-219 1.01e-133

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.


The actual alignment was detected with superfamily member cd03125:

Pssm-ID: 469577  Cd Length: 249  Bit Score: 376.82  E-value: 1.01e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  25 YSVQISLPSTMRMTVADGTVYIAQQMHFHWGGASSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAA 104
Cdd:cd03125   55 HTVQIDLPPTMSITTGDGTVYTAVQMHFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSKYKSYEEAKDKPDGLAVLAF 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 105 FVEVKNYPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQV 184
Cdd:cd03125  135 LYKVGHYAENTYYSDFISKLAKIKYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQI 214

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 395132471 185 WKLENSLLDHRNKTIHNDYRRTQPLNHRVVESNFP 219
Cdd:cd03125  215 VKLENTLMDHHNKTIRNDYRRTQPLNHRVVEANFL 249
 
Name Accession Description Interval E-value
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 25-219 1.01e-133

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: 376.82  E-value: 1.01e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  25 YSVQISLPSTMRMTVADGTVYIAQQMHFHWGGASSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAA 104
Cdd:cd03125   55 HTVQIDLPPTMSITTGDGTVYTAVQMHFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSKYKSYEEAKDKPDGLAVLAF 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 105 FVEVKNYPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQV 184
Cdd:cd03125  135 LYKVGHYAENTYYSDFISKLAKIKYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQI 214

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 395132471 185 WKLENSLLDHRNKTIHNDYRRTQPLNHRVVESNFP 219
Cdd:cd03125  215 VKLENTLMDHHNKTIRNDYRRTQPLNHRVVEANFL 249
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
25-218 1.35e-87

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 259.89  E-value: 1.35e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471   25 YSVQISLPSTMRMTVADG---TVYIAQQMHFHWGgaSSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAV 101
Cdd:pfam00194  56 HTVQVSLDDGDPSTISGGplaTRYRLVQFHFHWG--STDSRGSEHTIDGKRYPAELHIVHYNSKYKSFDEAAKHPDGLAV 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  102 LAAFVEVkNYPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSR 181
Cdd:pfam00194 134 LGVFFEV-GDENNPYLQPIVSALDNIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISE 212

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 395132471  182 TQVWKLENSLLDHRNKT---IHNDYRRTQPLNHRVVESNF 218
Cdd:pfam00194 213 EQLEAFRTLLFSDGGEEprpLVNNFRPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 25-213 1.53e-73

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: 224.12  E-value: 1.53e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471    25 YSVQISLPSTMrMTVADG---TVYIAQQMHFHWGGASSEisGSEHTVDGIRHVIEIHIVHYNSKyKSYDIAQDAPDGLAV 101
Cdd:smart01057  61 HTVQVNFDDDG-STLSGGplpGRYRLKQFHFHWGGSDSE--GSEHTIDGKRFPLELHLVHYNSK-GSFSEAVSKPGGLAV 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471   102 LAAFVEVKNyPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSR 181
Cdd:smart01057 137 VAVFFKVGA-EENPALQAILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITIST 215

                          170       180       190
                   ....*....|....*....|....*....|..
gi 395132471   182 TQVWKLENSLLDHRNKTIHNDYRRTQPLNHRV 213
Cdd:smart01057 216 EQLEKFRTLLPMEGNEPLVNNARPLQPLNGRV 247
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
26-214 1.19e-39

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 137.32  E-value: 1.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  26 SVQISLPSTMRMTVaDGTVYIAQQMHFHwggasseiSGSEHTVDGIRHVIEIHIVHynskyksydiaQDAPDGLAVLAAF 105
Cdd:COG3338   88 TIQVNVDPGSTLTV-DGKRYELKQFHFH--------TPSEHTINGKSYPMEAHLVH-----------KDADGELAVVGVL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 106 VEVKNypENTYYSNFISHLAniKYPGQRTTL-TGLDVQDMLPRNLqHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQV 184
Cdd:COG3338  148 FEEGA--ENPALAKLWANLP--LEAGEEVALdATIDLNDLLPEDR-SYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQI 222

                        170       180       190
                 ....*....|....*....|....*....|
gi 395132471 185 WKLEnslldhrnKTIHNDYRRTQPLNHRVV 214
Cdd:COG3338  223 EAFA--------RLYPNNARPVQPLNGRLI 244
PLN02202 PLN02202
carbonate dehydratase
 39-215 1.26e-15

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 74.32  E-value: 1.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  39 VADGTVYIAQQMHFHwggasseiSGSEHTVDGIRHVIEIHIVHynskyksydiaqDAPDG-LAVLAAFVEVKNypENTYY 117
Cdd:PLN02202 107 IIDNKNYTLLQMHWH--------TPSEHHLHGVQYAAELHMVH------------QAKDGsFAVVASLFKIGT--EEPFL 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 118 SNFISHLANIK---YPGQRTTLTGLDVQDM--LPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLl 192
Cdd:PLN02202 165 SQMKDKLVKLKeerFKGNHTAQVEVGKIDTrhIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPL- 243

                        170       180
                 ....*....|....*....|...
gi 395132471 193 dhrNKTIHNDYRRTQPLNHRVVE 215
Cdd:PLN02202 244 ---DKSFKNNSRPCQPLNGRRVE 263
 
Name Accession Description Interval E-value
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 25-219 1.01e-133

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: 376.82  E-value: 1.01e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  25 YSVQISLPSTMRMTVADGTVYIAQQMHFHWGGASSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAA 104
Cdd:cd03125   55 HTVQIDLPPTMSITTGDGTVYTAVQMHFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSKYKSYEEAKDKPDGLAVLAF 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 105 FVEVKNYPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQV 184
Cdd:cd03125  135 LYKVGHYAENTYYSDFISKLAKIKYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQI 214

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 395132471 185 WKLENSLLDHRNKTIHNDYRRTQPLNHRVVESNFP 219
Cdd:cd03125  215 VKLENTLMDHHNKTIRNDYRRTQPLNHRVVEANFL 249
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
 25-218 1.10e-122

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: 348.91  E-value: 1.10e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  25 YSVQISLPSTMRMTVADGTVYIAQQMHFHWGGASSeISGSEHTVDGIRHVIEIHIVHYNS-KYKSYDIAQDAPDGLAVLA 103
Cdd:cd03123   56 HTVQLSLPPTMHIRGGPGTEYTAAQLHLHWGGRGS-LSGSEHTIDGIRFAAELHIVHYNSdKYSSFDEAADKPDGLAVLA 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 104 AFVEVKnYPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQ 183
Cdd:cd03123  135 ILIEVG-YPENTYYEKIISHLHEIKYKGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQ 213

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 395132471 184 VWKLENSLLDHRNKTIHNDYRRTQPLNHRVVESNF 218
Cdd:cd03123  214 LETLENTLMDTHNKTLQNNYRATQPLNGRVVEASF 248
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
25-218 1.35e-87

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 259.89  E-value: 1.35e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471   25 YSVQISLPSTMRMTVADG---TVYIAQQMHFHWGgaSSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAV 101
Cdd:pfam00194  56 HTVQVSLDDGDPSTISGGplaTRYRLVQFHFHWG--STDSRGSEHTIDGKRYPAELHIVHYNSKYKSFDEAAKHPDGLAV 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  102 LAAFVEVkNYPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSR 181
Cdd:pfam00194 134 LGVFFEV-GDENNPYLQPIVSALDNIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISE 212

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 395132471  182 TQVWKLENSLLDHRNKT---IHNDYRRTQPLNHRVVESNF 218
Cdd:pfam00194 213 EQLEAFRTLLFSDGGEEprpLVNNFRPTQPLNGRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 25-213 1.53e-73

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: 224.12  E-value: 1.53e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471    25 YSVQISLPSTMrMTVADG---TVYIAQQMHFHWGGASSEisGSEHTVDGIRHVIEIHIVHYNSKyKSYDIAQDAPDGLAV 101
Cdd:smart01057  61 HTVQVNFDDDG-STLSGGplpGRYRLKQFHFHWGGSDSE--GSEHTIDGKRFPLELHLVHYNSK-GSFSEAVSKPGGLAV 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471   102 LAAFVEVKNyPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSR 181
Cdd:smart01057 137 VAVFFKVGA-EENPALQAILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITIST 215

                          170       180       190
                   ....*....|....*....|....*....|..
gi 395132471   182 TQVWKLENSLLDHRNKTIHNDYRRTQPLNHRV 213
Cdd:smart01057 216 EQLEKFRTLLPMEGNEPLVNNARPLQPLNGRV 247
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 25-215 9.85e-72

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: 218.69  E-value: 9.85e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  25 YSVQISLPSTM-RMTVAD-GTVYIAQQMHFHWGGASSEisGSEHTVDGIRHVIEIHIVHYNSKYKSYDiAQDAPDGLAVL 102
Cdd:cd00326   40 HTVQVNFDDDGgTLSGGGlPGRYKLVQFHFHWGSENSP--GSEHTIDGKRYPLELHLVHYNSDYYSSE-AAKKPGGLAVL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 103 AAFVEVKNyPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRT 182
Cdd:cd00326  117 GVFFEVGE-KENPFLKKILDALPKIKYKGKETTLPPFDLSDLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKE 195

                        170       180       190
                 ....*....|....*....|....*....|...
gi 395132471 183 QVWKLENsLLDHRNKTIHNDYRRTQPLNHRVVE 215
Cdd:cd00326  196 QLEAFRS-LLDREGKPLVNNYRPVQPLNGRVVY 227
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 25-219 3.14e-67

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: 208.27  E-value: 3.14e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  25 YSVQISLPSTMRMTVADGTVYIAQQMHFHWGGAssEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAA 104
Cdd:cd03150   56 HTVQLSLPSGLRMALGPGQEYRALQLHLHWGAA--GRPGSEHTVDGHRFPAEIHVVHLSTAFANLDEALGRPGGLAVLAA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 105 FVEVKNYpENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQV 184
Cdd:cd03150  134 FLAEGLH-ENSAYEQLLSRLSEISEEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQL 212

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 395132471 185 WKLENSLLDHRNKTIHNDYRRTQPLNHRVVESNFP 219
Cdd:cd03150  213 HTLSDSLWGPHDSRLQLNFRATQPLNGRKIEASFP 247
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
 26-214 5.86e-59

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: 186.32  E-value: 5.86e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  26 SVQISLPSTMRMTVAD-GTVYIAQQMHFHWGGASSEisGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAA 104
Cdd:cd03117   43 TVQVTLPDGAKISGGGlPGTYKALQFHFHWGSNGSP--GSEHTIDGERYPMELHIVHIKESYNSLLEALKDSDGLAVLGF 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 105 FVEVKNyPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLP-RNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQ 183
Cdd:cd03117  121 FIEEGE-EENTNFDPLISALSNIPQKGGSTNLTPFSLRSLLPsVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQ 199

                        170       180       190
                 ....*....|....*....|....*....|...
gi 395132471 184 VWKLENSLLDHR--NKTIHNDYRRTQPLNHRVV 214
Cdd:cd03117  200 LDAFSTVLFFDTdnGQPMVNNFRPVQPLNGRVV 232
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
 25-218 1.26e-52

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: 170.79  E-value: 1.26e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  25 YSVQISLPSTMRMTVADGTvYIAQQMHFHWGGASSEiSGSEHTVDGIRHVIEIHIVHYNS-KYKSYDIAQDAPDGLAVLA 103
Cdd:cd03126   56 HTVQLSLPPTMHIGGLPFK-YTASQLHLHWGQRGSP-EGSEHTISGKHFAAELHIVHYNSdKYPDISTAMNKSQGLAVLG 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 104 AFVEVKnyPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQ 183
Cdd:cd03126  134 ILIEVG--PFNPSYEKIFSHLHEVKYKDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQ 211

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 395132471 184 VWKLENSLL-DHRN--KTIHNDYRRTQPLNHRVVESNF 218
Cdd:cd03126  212 LLALETALYsTEEDesREMVNNYRQVQPFNERLVFASF 249
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
 44-218 1.28e-45

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: 152.98  E-value: 1.28e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  44 VYIAQQMHFHWGgaSSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNypENTYYSNFISH 123
Cdd:cd03119   87 SYRLRQFHFHWG--SSDDHGSEHTVDGVKYAAELHLVHWNSKYGSFGEAAKQPDGLAVVGVFLKVGE--ANPELQKVLDA 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 124 LANIKYPGQRTTLTGLDVQDMLPRNLQhYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRNKT----I 199
Cdd:cd03119  163 LDSIKTKGKQAPFTNFDPSCLLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEPpcpmV 241

                        170
                 ....*....|....*....
gi 395132471 200 HNdYRRTQPLNHRVVESNF 218
Cdd:cd03119  242 DN-WRPPQPLKGRKVRASF 259
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
 25-218 5.75e-42

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: 143.05  E-value: 5.75e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  25 YSVQISLPSTMRMTVADG----TVYIAQQMHFHWGGASSeiSGSEHTVDGIRHVIEIHIVHYNS-KYKSYDIAQDAPDGL 99
Cdd:cd03149   40 HSVMVEFDDSDDKTVITGgpleNPYRLKQFHFHWGAKHG--SGSEHTVDGKTFPSELHLVHWNAkKYKSFGEAAAAPDGL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 100 AVLAAFVEVKNypENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLqHYYTYHGSLTTPPCTENVHWFVLADFVKL 179
Cdd:cd03149  118 AVLGVFLETGD--EHPGLNRLTDALYMVRFKGTKAQFLDFNPKCLLPKSL-DYWTYPGSLTTPPLNESVTWIVLKEPIPV 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 395132471 180 SRTQVWKLENSLL----DHRNKTIhNDYRRTQPLNHRVVESNF 218
Cdd:cd03149  195 SEKQMGKFRELLFtseeDQRNHMV-NNFRPPQPLKGRTVRASF 236
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
26-214 1.19e-39

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 137.32  E-value: 1.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  26 SVQISLPSTMRMTVaDGTVYIAQQMHFHwggasseiSGSEHTVDGIRHVIEIHIVHynskyksydiaQDAPDGLAVLAAF 105
Cdd:COG3338   88 TIQVNVDPGSTLTV-DGKRYELKQFHFH--------TPSEHTINGKSYPMEAHLVH-----------KDADGELAVVGVL 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 106 VEVKNypENTYYSNFISHLAniKYPGQRTTL-TGLDVQDMLPRNLqHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQV 184
Cdd:COG3338  148 FEEGA--ENPALAKLWANLP--LEAGEEVALdATIDLNDLLPEDR-SYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQI 222

                        170       180       190
                 ....*....|....*....|....*....|
gi 395132471 185 WKLEnslldhrnKTIHNDYRRTQPLNHRVV 214
Cdd:COG3338  223 EAFA--------RLYPNNARPVQPLNGRLI 244
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 45-216 8.77e-38

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: 132.48  E-value: 8.77e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  45 YIAQQMHFHWGGASSEisGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNyPENTYYSNFISHL 124
Cdd:cd03122   80 YKFSEITFHWGTCNSD--GSEHSIDGHKFPLEMQILHRNTDFFDSFEAIKSPGGVLALAYLFELSH-EDNPFLDPIIEGL 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 125 ANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLeNSLLDHRN------KT 198
Cdd:cd03122  157 RNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAF-RELLTRRQdgvmsgDY 235

                        170
                 ....*....|....*...
gi 395132471 199 IHNDYRRTQPLNHRVVES 216
Cdd:cd03122  236 LPNNGRPQQPLGSRTVFS 253
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
 41-216 2.25e-37

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: 130.47  E-value: 2.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  41 DGTVYIAQQMHFHwggasseiSGSEHTVDGIRHVIEIHIVHynskyksydiaQDAPDGLAVLAAFVEVknYPENTyysnF 120
Cdd:cd03124   71 DGETYQLLQFHFH--------SPSEHLINGKRYPLEAHLVH-----------KSKDGQLAVVAVLFEE--GKENP----F 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 121 ISHLAN--IKYPGQRTTLT-GLDVQDMLPRNLqHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLenslldhRNK 197
Cdd:cd03124  126 LKKILDnmPKKEGTEVNLPaILDPNELLPESR-SYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKF-------RAA 197

                        170
                 ....*....|....*....
gi 395132471 198 TIHNDYRRTQPLNHRVVES 216
Cdd:cd03124  198 VYPNNARPVQPLNGREVLL 216
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
 18-218 2.56e-31

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: 115.33  E-value: 2.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  18 QHVSDWTYSVQISLP-STMRMTVADGTV---YIAQQMHFHWGgASSEiSGSEHTVDGIRHVIEIHIVHYNS-KYKSYDIA 92
Cdd:cd03118   33 LYIWNNGYSFQVEFDdSTDKSGISGGPLenhYRLKQFHFHWG-ANNE-WGSEHTVDGHTYPAELHLVHWNSvKYENFEEA 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  93 QDAPDGLAVLAAFVEVKNYPENtyYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQhYYTYHGSLTTPPCTENVHWFV 172
Cdd:cd03118  111 VMEENGLAVIGVFLKLGAHHEG--LQKLVDALPEVRHKDTVVEFNPFDPSCLLPACRD-YWTYPGSLTTPPLTESVTWII 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 395132471 173 LADFVKLSRTQVWKLENSLLDHR---NKTIHNDYRRTQPLNHRVVESNF 218
Cdd:cd03118  188 QKQPIEVSPSQLSVFRTLLFTSRgeeEKVMVNNFRPLQPLMNRKVRSSF 236
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
 45-217 1.09e-28

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: 109.04  E-value: 1.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  45 YIAQQMHFHWGGASSEisGSEHTVDGIRHVIEIHIVHYNSK-YKSYDIAQDAPDGLAVLAAFVEVKNYPentyySNFISH 123
Cdd:cd03121   80 YRLEEIRLHFGREDEQ--GSEHTVNGQAFPGEVQLIHYNSElYPNFSEASKSPNGLVIVSLFVKIGETS-----NPELRR 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 124 LAN------IKYPGQRTTLTGLDVQDMLPrNLQHYYTYHGSLTTPPCTENVHWFVLADFV---KLSRTQVWKLENSLLDH 194
Cdd:cd03121  153 LTNrdtitsIRYKGDAYFLQDLSIELLLP-ETDHYITYEGSLTSPGCHETVTWIILNKPIyitKEQMHSLRLLSQNSPSQ 231

                        170       180
                 ....*....|....*....|...
gi 395132471 195 RNKTIHNDYRRTQPLNHRVVESN 217
Cdd:cd03121  232 EKAPMSPNFRPVQPLNNRPVRTN 254
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
 25-218 3.63e-25

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: 99.55  E-value: 3.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  25 YSVQISLPSTMRMT---VADGTVYIAQQMHFHWGGASSEisGSEHTVDGIRHVIEIHIVHYNSK-YKSYDIAQDAPDGLA 100
Cdd:cd03120   54 HTIQIILKSKSVLSggpLPQGHEFELAEVRFHWGRENQR--GSEHTVNFKAFPMELHLIHWNSTlYSSLEEAMGKPHGIA 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 101 VLAAFVEVKNypENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRN-LQHYYTYHGSLTTPPCTENVHWFVLADFVKL 179
Cdd:cd03120  132 IIALFVQIGK--EHVGLKAVTEILQDIQYKGKSKTIPCFNPNTLLPDPlLRDYWVYEGSLTTPPCSEGVTWILFRYPLTI 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 395132471 180 SRTQV---WKLEN-----SLLDHRNKTIHNDYRRTQPLNHRVVESNF 218
Cdd:cd03120  210 SQSQIeefRRLRThvkgaELVEGCDGLLGDNFRPTQPLSDRVIRAAF 256
PLN02202 PLN02202
carbonate dehydratase
 39-215 1.26e-15

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 74.32  E-value: 1.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  39 VADGTVYIAQQMHFHwggasseiSGSEHTVDGIRHVIEIHIVHynskyksydiaqDAPDG-LAVLAAFVEVKNypENTYY 117
Cdd:PLN02202 107 IIDNKNYTLLQMHWH--------TPSEHHLHGVQYAAELHMVH------------QAKDGsFAVVASLFKIGT--EEPFL 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471 118 SNFISHLANIK---YPGQRTTLTGLDVQDM--LPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLl 192
Cdd:PLN02202 165 SQMKDKLVKLKeerFKGNHTAQVEVGKIDTrhIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPL- 243

                        170       180
                 ....*....|....*....|...
gi 395132471 193 dhrNKTIHNDYRRTQPLNHRVVE 215
Cdd:PLN02202 244 ---DKSFKNNSRPCQPLNGRRVE 263
PLN02179 PLN02179
carbonic anhydrase
 43-172 6.28e-09

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 54.60  E-value: 6.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 395132471  43 TVYIAQQMHFHwggasseiSGSEHTVDGIRHVIEIHIVHYNSKYKSydiaqdapdglAVLAAFVEVKNYPEntyysnFIS 122
Cdd:PLN02179 118 TDYKLVQCHWH--------SPSEHTINGTSYDLELHMVHTSASGKT-----------AVVGVLYKLGEPDE------FLT 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 395132471 123 HLAN-IKYPGQRTTLTGLdvqdMLPRNLQ----HYYTYHGSLTTPPCTENVHWFV 172
Cdd:PLN02179 173 KLLNgIKGVGKKEINLGI----VDPRDIRfetnNFYRYIGSLTIPPCTEGVIWTV 223
 
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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