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Conserved domains on  [gi|1958775066|ref|XP_038965331|]
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carbonic anhydrase-related protein isoform X1 [Rattus norvegicus]

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 ...
 35-175 1.36e-103

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 cd03120:

Pssm-ID: 469577  Cd Length: 256  Bit Score: 297.92  E-value: 1.36e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  35 VEWGLVFPDANGEYQSPINLNSREARYDPSLLDVRLSPNYVVCRDCEVTNDGHTIQVILKSKSVLSGGPLPQGQEFELYE 114
Cdd:cd03120     2 VEWGLLFPEANGEYQSPINLNSREARYDPSLLEVRLSPNYVVCRDCEVINDGHTIQIILKSKSVLSGGPLPQGHEFELAE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958775066 115 VRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLFGSIDEAVGKPHGIVIIALFVQCIEE 175
Cdd:cd03120    82 VRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIGKE 142
 
Name Accession Description Interval E-value
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
 35-175 1.36e-103

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: 297.92  E-value: 1.36e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  35 VEWGLVFPDANGEYQSPINLNSREARYDPSLLDVRLSPNYVVCRDCEVTNDGHTIQVILKSKSVLSGGPLPQGQEFELYE 114
Cdd:cd03120     2 VEWGLLFPEANGEYQSPINLNSREARYDPSLLEVRLSPNYVVCRDCEVINDGHTIQIILKSKSVLSGGPLPQGHEFELAE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958775066 115 VRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLFGSIDEAVGKPHGIVIIALFVQCIEE 175
Cdd:cd03120    82 VRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIGKE 142
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
37-171 1.17e-52

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 168.21  E-value: 1.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  37 WGLVFPDANGEYQSPINLNSREARYDPSLLDVRLSPNYVVCRDCEVTNDGHTIQVILK--SKSVLSGGPLPqgQEFELYE 114
Cdd:pfam00194   6 WGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNTLTNNGHTVQVSLDdgDPSTISGGPLA--TRYRLVQ 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958775066 115 VRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLfGSIDEAVGKPHGIVIIALFVQ 171
Cdd:pfam00194  84 FHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFE 139
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 36-171 2.84e-49

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: 159.40  E-value: 2.84e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066   36 EWGLVFPD-ANGEYQSPINLNSREARYDPSLldVRLSPNYVVCRDCEVTNDGHTIQVILK-SKSVLSGGPLPQgqEFELY 113
Cdd:smart01057  11 HWGKLDPPfCGGKRQSPIDIVTAEAQYDPSL--KPLKLSYDQPTAKRILNNGHTVQVNFDdDGSTLSGGPLPG--RYRLK 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958775066  114 EVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTlfGSIDEAVGKPHGIVIIALFVQ 171
Cdd:smart01057  87 QFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFK 142
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
37-144 4.70e-17

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 75.69  E-value: 4.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  37 WGLVFPD----ANGEYQSPINL-NSREARYDPSLLDVRLSPNYVVcrdcevtNDGHTIQVILKSKSVLSGGplpqGQEFE 111
Cdd:COG3338    39 WGELSPEfatcATGKNQSPIDIrTAIKADLPPLKFDYKPTPLEIV-------NNGHTIQVNVDPGSTLTVD----GKRYE 107

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958775066 112 LYEVRFHwgrenqRGSEHTVNFKAFPMELHLIH 144
Cdd:COG3338   108 LKQFHFH------TPSEHTINGKSYPMEAHLVH 134
PLN02179 PLN02179
carbonic anhydrase
 36-144 7.16e-07

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 47.67  E-value: 7.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  36 EWGLVFPD----ANGEYQSPINL-NSREARYDPSLLDVRLSPNYVVcrdceVTNDGHTIQVILKSksvlSGGPLPQGQ-E 109
Cdd:PLN02179   49 EWGKLNPQwkvcSTGKYQSPIDLtDERVSLIHDQALSRHYKPAPAV-----IQSRGHDVMVSWKG----DAGKITIHQtD 119

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958775066 110 FELyeVRFHWgrenQRGSEHTVNFKAFPMELHLIH 144
Cdd:PLN02179  120 YKL--VQCHW----HSPSEHTINGTSYDLELHMVH 148
 
Name Accession Description Interval E-value
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
 35-175 1.36e-103

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: 297.92  E-value: 1.36e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  35 VEWGLVFPDANGEYQSPINLNSREARYDPSLLDVRLSPNYVVCRDCEVTNDGHTIQVILKSKSVLSGGPLPQGQEFELYE 114
Cdd:cd03120     2 VEWGLLFPEANGEYQSPINLNSREARYDPSLLEVRLSPNYVVCRDCEVINDGHTIQIILKSKSVLSGGPLPQGHEFELAE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958775066 115 VRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLFGSIDEAVGKPHGIVIIALFVQCIEE 175
Cdd:cd03120    82 VRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIGKE 142
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
37-171 1.17e-52

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 168.21  E-value: 1.17e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  37 WGLVFPDANGEYQSPINLNSREARYDPSLLDVRLSPNYVVCRDCEVTNDGHTIQVILK--SKSVLSGGPLPqgQEFELYE 114
Cdd:pfam00194   6 WGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNTLTNNGHTVQVSLDdgDPSTISGGPLA--TRYRLVQ 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958775066 115 VRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLfGSIDEAVGKPHGIVIIALFVQ 171
Cdd:pfam00194  84 FHFHWGSTDSRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFE 139
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
 36-171 2.84e-49

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: 159.40  E-value: 2.84e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066   36 EWGLVFPD-ANGEYQSPINLNSREARYDPSLldVRLSPNYVVCRDCEVTNDGHTIQVILK-SKSVLSGGPLPQgqEFELY 113
Cdd:smart01057  11 HWGKLDPPfCGGKRQSPIDIVTAEAQYDPSL--KPLKLSYDQPTAKRILNNGHTVQVNFDdDGSTLSGGPLPG--RYRLK 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958775066  114 EVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTlfGSIDEAVGKPHGIVIIALFVQ 171
Cdd:smart01057  87 QFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFK 142
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
 46-171 4.36e-48

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: 155.90  E-value: 4.36e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  46 GEYQSPINLNSREARYDPSLLDVRLSPNYvvCRDCEVTNDGHTIQVILKS-KSVLSGGPLPQgqEFELYEVRFHWGRENQ 124
Cdd:cd00326     1 GKRQSPINIVTSAVVYDPSLPPLNFDYYP--TTSLTLVNNGHTVQVNFDDdGGTLSGGGLPG--RYKLVQFHFHWGSENS 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958775066 125 RGSEHTVNFKAFPMELHLIHWNSTLFGSidEAVGKPHGIVIIALFVQ 171
Cdd:cd00326    77 PGSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFE 121
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
 37-171 5.02e-37

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: 128.19  E-value: 5.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  37 WGLVFPDANGEYQSPINLNSREARYDPSLLDVRLSpNYVV--CRDCEVTNDGHTIQVILKSKSVLSGGPlpqGQEFELYE 114
Cdd:cd03123     5 WPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELV-GYDLpgTEEFTLTNNGHTVQLSLPPTMHIRGGP---GTEYTAAQ 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958775066 115 VRFHWG-RENQRGSEHTVNFKAFPMELHLIHWNSTLFGSIDEAVGKPHGIVIIALFVQ 171
Cdd:cd03123    81 LHLHWGgRGSLSGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIE 138
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
 37-171 4.42e-36

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: 126.01  E-value: 4.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  37 WGLVFPDANGEYQSPINLNSREARYDPSLLDvrLSPNYVVCRDCEVTNDGHTIQVIL---KSKSVLSGGPLPQgqEFELY 113
Cdd:cd03119    16 WHELFPIAKGDRQSPIDIKTKDAKHDPSLKP--LSVSYDPATAKTILNNGHSFNVEFddtDDRSVLRGGPLTG--SYRLR 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958775066 114 EVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTlFGSIDEAVGKPHGIVIIALFVQ 171
Cdd:cd03119    92 QFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNSK-YGSFGEAAKQPDGLAVVGVFLK 148
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
 46-171 3.86e-35

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: 123.02  E-value: 3.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  46 GEYQSPINLNSREARYDPSLLDVRLSpnYVVCRDCEVTNDGHTIQVILK---SKSVLSGGPLPQgqEFELYEVRFHWGRE 122
Cdd:cd03149     1 GNRQSPIDIVSSEAVYDPKLKPLSLS--YDPCTSLSISNNGHSVMVEFDdsdDKTVITGGPLEN--PYRLKQFHFHWGAK 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958775066 123 NQRGSEHTVNFKAFPMELHLIHWNSTLFGSIDEAVGKPHGIVIIALFVQ 171
Cdd:cd03149    77 HGSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLE 125
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
 37-171 2.57e-34

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: 121.37  E-value: 2.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  37 WGLVFPDAN----GEYQSPINLNSREARYDPSLLDVRLSPNYVVcrDCEVTNDGHTIQVILKSKSV--LSGGPLpqGQEF 110
Cdd:cd03121     5 WGLVNSAWNlcskGRRQSPVDIEPSRLLFDPFLTPLRIDTGRKV--SGTFYNTGRHVSFRPDKDPVvnISGGPL--SYRY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958775066 111 ELYEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLFGSIDEAVGKPHGIVIIALFVQ 171
Cdd:cd03121    81 RLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVK 141
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
 46-171 4.50e-32

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: 114.94  E-value: 4.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  46 GEYQSPINLNSREARYDPSLLDVRLSPNYVVCRdcEVTNDGHTIQVILK---SKSVLSGGPLpqGQEFELYEVRFHWGRE 122
Cdd:cd03118     1 GTRQSPINIQWRDSVYDPQLAPLRVSYDPATCL--YIWNNGYSFQVEFDdstDKSGISGGPL--ENHYRLKQFHFHWGAN 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958775066 123 NQRGSEHTVNFKAFPMELHLIHWNSTLFGSIDEAVGKPHGIVIIALFVQ 171
Cdd:cd03118    77 NEWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLK 125
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
 46-171 3.02e-30

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: 110.05  E-value: 3.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  46 GEYQSPINLNSREARYDPSLLDVRLSpNYVVCRD-CEVTNDGHTIQVILKSKSVLSGGPLPQgqEFELYEVRFHWGRENQ 124
Cdd:cd03117     1 GKRQSPINIVTKKVQYDENLTPFTFT-GYDDTTTnWTITNNGHTVQVTLPDGAKISGGGLPG--TYKALQFHFHWGSNGS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958775066 125 RGSEHTVNFKAFPMELHLIHWNSTlFGSIDEAVGKPHGIVIIALFVQ 171
Cdd:cd03117    78 PGSEHTIDGERYPMELHIVHIKES-YNSLLEALKDSDGLAVLGFFIE 123
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 37-170 6.75e-27

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: 101.79  E-value: 6.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  37 WGLVFPDANGEYQSPINLNSREARYDPSLLDVRLSPNYVVCRDCEVTNDGHTIQVILKSKSVLSGGplpQGQEFELYEVR 116
Cdd:cd03125     5 WPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNNGHTVQIDLPPTMSITTG---DGTVYTAVQMH 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958775066 117 FHWG-RENQ-RGSEHTVNFKAFPMELHLIHWNSTlFGSIDEAVGKPHGIVIIALFV 170
Cdd:cd03125    82 FHWGgRDSEiSGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLY 136
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
 37-171 2.49e-26

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: 100.42  E-value: 2.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  37 WGLVFPDANGEYQSPINLNSREARYDPSLLDVRL-------SPNYVVCrdcevtNDGHTIQVILKSKSVLSGGPlpqGQE 109
Cdd:cd03150     5 WPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELlgfdlppSPSLRLL------NNGHTVQLSLPSGLRMALGP---GQE 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958775066 110 FELYEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTlFGSIDEAVGKPHGIVIIALFVQ 171
Cdd:cd03150    76 YRALQLHLHWGAAGRPGSEHTVDGHRFPAEIHVVHLSTA-FANLDEALGRPGGLAVLAAFLA 136
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
 37-171 8.42e-25

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: 96.45  E-value: 8.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  37 WGLVFPDANGEYQSPINLNSREARYDPSLLDVRLSP-NYVVCRDCEVTNDGHTIQVILKSKSVLSGGPlpqgQEFELYEV 115
Cdd:cd03126     5 WPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGyNVSGTEQFTLTNNGHTVQLSLPPTMHIGGLP----FKYTASQL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958775066 116 RFHWGREN-QRGSEHTVNFKAFPMELHLIHWNSTLFGSIDEAVGKPHGIVIIALFVQ 171
Cdd:cd03126    81 HLHWGQRGsPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIE 137
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
 37-171 2.70e-21

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: 87.03  E-value: 2.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  37 WGLVFPDAN-GEYQSPIN-LNSREAR---YDPSLLDV-RLSPNYVVcrdceVTNDGHTIQVILKSKSV---LSGGPLPQg 107
Cdd:cd03122     5 WAKKYPACGeGRQQSPIDiVEDTQVQrqgLQPLHFDGyEELTASTT-----LENTGKTVILRLEGNSSdpfVSGGPLLG- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958775066 108 qEFELYEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNsTLFGSIDEAVGKPHGIVIIALFVQ 171
Cdd:cd03122    79 -RYKFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRN-TDFFDSFEAIKSPGGVLALAYLFE 140
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
 37-144 4.23e-19

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: 80.39  E-value: 4.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  37 WGLVFPD----ANGEYQSPINLNSREARYDpSLLDVRLSPNyvvCRDCEVTNDGHTIQVILKSKSvlsGGPLPQGQEFEL 112
Cdd:cd03124     5 WGNLDPEfalcATGKNQSPIDITTKAVVSD-KLPPLNYNYK---PTSATLVNNGHTIQVNFEGNG---GTLTIDGETYQL 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958775066 113 yeVRFHWgrenQRGSEHTVNFKAFPMELHLIH 144
Cdd:cd03124    78 --LQFHF----HSPSEHLINGKRYPLEAHLVH 103
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
37-144 4.70e-17

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 75.69  E-value: 4.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  37 WGLVFPD----ANGEYQSPINL-NSREARYDPSLLDVRLSPNYVVcrdcevtNDGHTIQVILKSKSVLSGGplpqGQEFE 111
Cdd:COG3338    39 WGELSPEfatcATGKNQSPIDIrTAIKADLPPLKFDYKPTPLEIV-------NNGHTIQVNVDPGSTLTVD----GKRYE 107

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958775066 112 LYEVRFHwgrenqRGSEHTVNFKAFPMELHLIH 144
Cdd:COG3338   108 LKQFHFH------TPSEHTINGKSYPMEAHLVH 134
PLN02179 PLN02179
carbonic anhydrase
 36-144 7.16e-07

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 47.67  E-value: 7.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775066  36 EWGLVFPD----ANGEYQSPINL-NSREARYDPSLLDVRLSPNYVVcrdceVTNDGHTIQVILKSksvlSGGPLPQGQ-E 109
Cdd:PLN02179   49 EWGKLNPQwkvcSTGKYQSPIDLtDERVSLIHDQALSRHYKPAPAV-----IQSRGHDVMVSWKG----DAGKITIHQtD 119

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958775066 110 FELyeVRFHWgrenQRGSEHTVNFKAFPMELHLIH 144
Cdd:PLN02179  120 YKL--VQCHW----HSPSEHTINGTSYDLELHMVH 148
 
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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