NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|442624335|ref|NP_611519|]
View 

carbonic anhydrase 14 [Drosophila melanogaster]

Protein Classification

carbonic anhydrase family protein( domain architecture ID 10123209)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
69-293 7.37e-109

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: 315.83  E-value: 7.37e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335  69 LAKQPSPITIPESNMIKRQLKMPLHWTYYEDLPMATVLENNGNTVIMRIYTaNNFMPQLSGAELLGRYQFVEAIFKWG-- 146
Cdd:cd03122   14 EGRQQSPIDIVEDTQVQRQGLQPLHFDGYEELTASTTLENTGKTVILRLEG-NSSDPFVSGGPLLGRYKFSEITFHWGtc 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335 147 -SLKSEHSIGKHNFCLELQALHRCAQ-------LNNNFEYLTLSYLFALSHVKNEHLKQVTDHLKWISQPGSSIELPPFH 218
Cdd:cd03122   93 nSDGSEHSIDGHKFPLEMQILHRNTDffdsfeaIKSPGGVLALAYLFELSHEDNPFLDPIIEGLRNVSRPGKEVELPPFP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335 219 LESLLQPFGSGYFSYEGTYDNGDVVLPTTWLINRKISVVDSRQLSEFEALYGRN------GNRNCKNGREKQPLGNRNVY 292
Cdd:cd03122  173 LSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRqdgvmsGDYLPNNGRPQQPLGSRTVF 252

                 .
gi 442624335 293 F 293
Cdd:cd03122  253 S 253
 
Name Accession Description Interval E-value
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
69-293 7.37e-109

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: 315.83  E-value: 7.37e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335  69 LAKQPSPITIPESNMIKRQLKMPLHWTYYEDLPMATVLENNGNTVIMRIYTaNNFMPQLSGAELLGRYQFVEAIFKWG-- 146
Cdd:cd03122   14 EGRQQSPIDIVEDTQVQRQGLQPLHFDGYEELTASTTLENTGKTVILRLEG-NSSDPFVSGGPLLGRYKFSEITFHWGtc 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335 147 -SLKSEHSIGKHNFCLELQALHRCAQ-------LNNNFEYLTLSYLFALSHVKNEHLKQVTDHLKWISQPGSSIELPPFH 218
Cdd:cd03122   93 nSDGSEHSIDGHKFPLEMQILHRNTDffdsfeaIKSPGGVLALAYLFELSHEDNPFLDPIIEGLRNVSRPGKEVELPPFP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335 219 LESLLQPFGSGYFSYEGTYDNGDVVLPTTWLINRKISVVDSRQLSEFEALYGRN------GNRNCKNGREKQPLGNRNVY 292
Cdd:cd03122  173 LSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRqdgvmsGDYLPNNGRPQQPLGSRTVF 252

                 .
gi 442624335 293 F 293
Cdd:cd03122  253 S 253
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
71-289 7.42e-54

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: 175.58  E-value: 7.42e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335    71 KQPSPITIPESNMIKRQLKMPLHWTYyeDLPMATVLENNGNTVIMRIytaNNFMPQLSGAELLGRYQFVEAIFKWGSLK- 149
Cdd:smart01057  23 KRQSPIDIVTAEAQYDPSLKPLKLSY--DQPTAKRILNNGHTVQVNF---DDDGSTLSGGPLPGRYRLKQFHFHWGGSDs 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335   150 --SEHSIGKHNFCLELQALHRCAQLNNNF------EYLTLSYLFALSHVKNEHLKQVTDHLKWISQPGSSIELPPFHLES 221
Cdd:smart01057  98 egSEHTIDGKRFPLELHLVHYNSKGSFSEavskpgGLAVVAVFFKVGAEENPALQAILDHLPLIKYKGQETELTPFDLSS 177
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442624335   222 LLQPFGSGYFSYEGTYDNGDVVLPTTWLINRKISVVDSRQLSEFEALYGRNGNRNCK-NGREKQPLGNR 289
Cdd:smart01057 178 LLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEPLVnNARPLQPLNGR 246
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
74-295 1.33e-33

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 123.15  E-value: 1.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335   74 SPITIPESNMIKRQLKMPLHWTYYEDLPMATVLENNGNTVIMRIYTANNfmPQLSGAELLGRYQFVEAIFKWGSLK---S 150
Cdd:pfam00194  19 SPINIDTRKVRYDPSLPPLTFQGYDVPPGKNTLTNNGHTVQVSLDDGDP--STISGGPLATRYRLVQFHFHWGSTDsrgS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335  151 EHSIGKHNFCLELQALHRCAQLNNNFEYLT-------LSYLFALSHVKNEHLKQVTDHLKWISQPGSSIELPPFHLESLL 223
Cdd:pfam00194  97 EHTIDGKRYPAELHIVHYNSKYKSFDEAAKhpdglavLGVFFEVGDENNPYLQPIVSALDNIKYKGKSVLLPPFDLSDLL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335  224 QPFGSGYFSYEGTydngdvvLPT-------TWLINRKISVVDSRQLSEFEALYGRNGNRNCK----NGREKQPLGNRNVY 292
Cdd:pfam00194 177 PEDLTSYYTYNGS-------LTTppcsesvTWIVFKEPISISEEQLEAFRTLLFSDGGEEPRplvnNFRPTQPLNGRVVF 249

                  ...
gi 442624335  293 FNI 295
Cdd:pfam00194 250 ASF 252
 
Name Accession Description Interval E-value
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
69-293 7.37e-109

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: 315.83  E-value: 7.37e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335  69 LAKQPSPITIPESNMIKRQLKMPLHWTYYEDLPMATVLENNGNTVIMRIYTaNNFMPQLSGAELLGRYQFVEAIFKWG-- 146
Cdd:cd03122   14 EGRQQSPIDIVEDTQVQRQGLQPLHFDGYEELTASTTLENTGKTVILRLEG-NSSDPFVSGGPLLGRYKFSEITFHWGtc 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335 147 -SLKSEHSIGKHNFCLELQALHRCAQ-------LNNNFEYLTLSYLFALSHVKNEHLKQVTDHLKWISQPGSSIELPPFH 218
Cdd:cd03122   93 nSDGSEHSIDGHKFPLEMQILHRNTDffdsfeaIKSPGGVLALAYLFELSHEDNPFLDPIIEGLRNVSRPGKEVELPPFP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335 219 LESLLQPFGSGYFSYEGTYDNGDVVLPTTWLINRKISVVDSRQLSEFEALYGRN------GNRNCKNGREKQPLGNRNVY 292
Cdd:cd03122  173 LSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRqdgvmsGDYLPNNGRPQQPLGSRTVF 252

                 .
gi 442624335 293 F 293
Cdd:cd03122  253 S 253
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
71-289 7.42e-54

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: 175.58  E-value: 7.42e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335    71 KQPSPITIPESNMIKRQLKMPLHWTYyeDLPMATVLENNGNTVIMRIytaNNFMPQLSGAELLGRYQFVEAIFKWGSLK- 149
Cdd:smart01057  23 KRQSPIDIVTAEAQYDPSLKPLKLSY--DQPTAKRILNNGHTVQVNF---DDDGSTLSGGPLPGRYRLKQFHFHWGGSDs 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335   150 --SEHSIGKHNFCLELQALHRCAQLNNNF------EYLTLSYLFALSHVKNEHLKQVTDHLKWISQPGSSIELPPFHLES 221
Cdd:smart01057  98 egSEHTIDGKRFPLELHLVHYNSKGSFSEavskpgGLAVVAVFFKVGAEENPALQAILDHLPLIKYKGQETELTPFDLSS 177
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442624335   222 LLQPFGSGYFSYEGTYDNGDVVLPTTWLINRKISVVDSRQLSEFEALYGRNGNRNCK-NGREKQPLGNR 289
Cdd:smart01057 178 LLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEPLVnNARPLQPLNGR 246
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
74-295 1.33e-33

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 123.15  E-value: 1.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335   74 SPITIPESNMIKRQLKMPLHWTYYEDLPMATVLENNGNTVIMRIYTANNfmPQLSGAELLGRYQFVEAIFKWGSLK---S 150
Cdd:pfam00194  19 SPINIDTRKVRYDPSLPPLTFQGYDVPPGKNTLTNNGHTVQVSLDDGDP--STISGGPLATRYRLVQFHFHWGSTDsrgS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335  151 EHSIGKHNFCLELQALHRCAQLNNNFEYLT-------LSYLFALSHVKNEHLKQVTDHLKWISQPGSSIELPPFHLESLL 223
Cdd:pfam00194  97 EHTIDGKRYPAELHIVHYNSKYKSFDEAAKhpdglavLGVFFEVGDENNPYLQPIVSALDNIKYKGKSVLLPPFDLSDLL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335  224 QPFGSGYFSYEGTydngdvvLPT-------TWLINRKISVVDSRQLSEFEALYGRNGNRNCK----NGREKQPLGNRNVY 292
Cdd:pfam00194 177 PEDLTSYYTYNGS-------LTTppcsesvTWIVFKEPISISEEQLEAFRTLLFSDGGEEPRplvnNFRPTQPLNGRVVF 249

                  ...
gi 442624335  293 FNI 295
Cdd:pfam00194 250 ASF 252
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
71-292 8.30e-21

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: 88.48  E-value: 8.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335  71 KQPSPITIPESNMIKRQLKMPLHWTYYEDLPMATVLENNGNTVIMRIytaNNFMpQLSGAELLGRYQFVEAIFKWGSLK- 149
Cdd:cd03117    2 KRQSPINIVTKKVQYDENLTPFTFTGYDDTTTNWTITNNGHTVQVTL---PDGA-KISGGGLPGTYKALQFHFHWGSNGs 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335 150 --SEHSIGKHNFCLELQALHRCAQLNNNFEYLT-------LSYLFALSHVKNEHLKQVTDHLKWISQPGSSIELPPFHLE 220
Cdd:cd03117   78 pgSEHTIDGERYPMELHIVHIKESYNSLLEALKdsdglavLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSLR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442624335 221 SLLQP-FGSGYFSYEG---TYDNGDVVLpttWLINRKISVVDSRQLSEFEALYGRNGNRNCK---NGREKQPLGNRNVY 292
Cdd:cd03117  158 SLLPSvLLTKYYRYNGsltTPGCNEAVI---WTVFEEPIPISRAQLDAFSTVLFFDTDNGQPmvnNFRPVQPLNGRVVY 233
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
71-291 9.75e-12

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: 63.82  E-value: 9.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335  71 KQPSPITI-PESNMIKRQLKmPLHWTYYEDLPMATV-LENNGNTVIMriytanNFMPQLSGAELLGR-YQFVEAIFKWGS 147
Cdd:cd03150   15 RFQSPVDIrPHLVAFCPALR-PLELLGFDLPPSPSLrLLNNGHTVQL------SLPSGLRMALGPGQeYRALQLHLHWGA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335 148 LK---SEHSIGKHNFCLELQALHrcaqLNNNFEYLT-----------LSYLFALSHVKNEHLKQVTDHLKWISQPGSSIE 213
Cdd:cd03150   88 AGrpgSEHTVDGHRFPAEIHVVH----LSTAFANLDealgrpgglavLAAFLAEGLHENSAYEQLLSRLSEISEEESETV 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442624335 214 LPPFHLESLLQPFGSGYFSYEGTYDNGDVVLPTTWLINRKISVVDSRQLSEF-EALYGRNGNRNCKNGREKQPLGNRNV 291
Cdd:cd03150  164 VPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLsDSLWGPHDSRLQLNFRATQPLNGRKI 242
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
71-295 2.27e-11

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: 62.82  E-value: 2.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335  71 KQPSPITIPESNMIKRQLKMPLHWTYYEDLpmATVLENNGNTVIMRIYTANnfMPQLSGAELLGRYQFVEAIFKWGSLK- 149
Cdd:cd03121   19 RRQSPVDIEPSRLLFDPFLTPLRIDTGRKV--SGTFYNTGRHVSFRPDKDP--VVNISGGPLSYRYRLEEIRLHFGREDe 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335 150 --SEHSIGKHNFCLELQALHRCAQLNNNFE--------YLTLSYLFALSHVKNEHLKQVTDHLKW--ISQPGSSIELPPF 217
Cdd:cd03121   95 qgSEHTVNGQAFPGEVQLIHYNSELYPNFSeaskspngLVIVSLFVKIGETSNPELRRLTNRDTItsIRYKGDAYFLQDL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335 218 HLESLLqPFGSGYFSYEGTYDNGDVVLPTTWLINRKISVVDSRQLSEFEALYgRNGNRNCK-----NGREKQPLGNRNVY 292
Cdd:cd03121  175 SIELLL-PETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLS-QNSPSQEKapmspNFRPVQPLNNRPVR 252

                 ...
gi 442624335 293 FNI 295
Cdd:cd03121  253 TNI 255
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
74-292 3.62e-07

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: 50.22  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335  74 SPITIPESNMIKRQLKMPLHWTYYEDLPMATV-LENNGNTVIMriytanNFMPQLSGAELLGRYQFVEAIFKWG---SLK 149
Cdd:cd03126   18 SPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFtLTNNGHTVQL------SLPPTMHIGGLPFKYTASQLHLHWGqrgSPE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335 150 -SEHSIGKHNFCLELQALHRCAQLNNNF-----EYLTLSYLFALSHV--KNEHLKQVTDHLKWISQPGSSIELPPFHLES 221
Cdd:cd03126   92 gSEHTISGKHFAAELHIVHYNSDKYPDIstamnKSQGLAVLGILIEVgpFNPSYEKIFSHLHEVKYKDQKVSVPGFNVQE 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442624335 222 LLQPFGSGYFSYEGTYDNGDVVLPTTWLINRKISVVDSRQLSEFE-ALYGRNGNRN---CKNGREKQPLGNRNVY 292
Cdd:cd03126  172 LLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALEtALYSTEEDESremVNNYRQVQPFNERLVF 246
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
70-291 1.70e-06

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: 48.24  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335  70 AKQPSPITIPESNMIKRQLKMPLHWTYYEDLPMATVLENNGNTVIMriytanNFMPQLSGAELLGR-YQFVEAIFKWGSL 148
Cdd:cd03125   14 GKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNNGHTVQI------DLPPTMSITTGDGTvYTAVQMHFHWGGR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335 149 K-----SEHSIGKHNFCLELQALHRcaqlnnNFEYLT-------------LSYLFALSHV-KNEHLKQVTDHLKWISQPG 209
Cdd:cd03125   88 DseisgSEHTIDGMRYVAELHIVHY------NSKYKSyeeakdkpdglavLAFLYKVGHYaENTYYSDFISKLAKIKYAG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624335 210 SSIELPPFHLESLLQPFGSGYFSYEGTYDNGDVVLPTTWLINRKISVVDSRQLSEFEALYGRNGNRNCKNG-REKQPLGN 288
Cdd:cd03125  162 QTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLENTLMDHHNKTIRNDyRRTQPLNH 241

                 ...
gi 442624335 289 RNV 291
Cdd:cd03125  242 RVV 244
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH