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Conserved domains on  [gi|20130189|ref|NP_611525|]
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carbonic anhydrase 15 [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

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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 ...
82-325 2.49e-116

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: 336.25  E-value: 2.49e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  82 YNYDWDQ-GPHTWDtaCNNQSPINIDM-NCVEINYfDTPLIWSHYNSIPLGIRLENNGHTLILRAAFPERTPSIDGGDLL 159
Cdd:cd03122   1 NPKHWAKkYPACGE--GRQQSPIDIVEdTQVQRQG-LQPLHFDGYEELTASTTLENTGKTVILRLEGNSSDPFVSGGPLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 160 GRFDFREISFRWSWASSLGSEHTLDHHHSPLEMQCLHTDGDGCD---GCSSSQGVLMISYMFDLS-EHNPFLDVLIQHLA 235
Cdd:cd03122  78 GRYKFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDsfeAIKSPGGVLALAYLFELShEDNPFLDPIIEGLR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 236 AVEQAGQVVEVPPFPLSYLMSPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLRDRR------GSRIA 309
Cdd:cd03122 158 NVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRqdgvmsGDYLP 237
                       250
                ....*....|....*.
gi 20130189 310 RNARPVQPIGDRMVYL 325
Cdd:cd03122 238 NNGRPQQPLGSRTVFS 253
 
Name Accession Description Interval E-value
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
82-325 2.49e-116

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: 336.25  E-value: 2.49e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  82 YNYDWDQ-GPHTWDtaCNNQSPINIDM-NCVEINYfDTPLIWSHYNSIPLGIRLENNGHTLILRAAFPERTPSIDGGDLL 159
Cdd:cd03122   1 NPKHWAKkYPACGE--GRQQSPIDIVEdTQVQRQG-LQPLHFDGYEELTASTTLENTGKTVILRLEGNSSDPFVSGGPLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 160 GRFDFREISFRWSWASSLGSEHTLDHHHSPLEMQCLHTDGDGCD---GCSSSQGVLMISYMFDLS-EHNPFLDVLIQHLA 235
Cdd:cd03122  78 GRYKFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDsfeAIKSPGGVLALAYLFELShEDNPFLDPIIEGLR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 236 AVEQAGQVVEVPPFPLSYLMSPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLRDRR------GSRIA 309
Cdd:cd03122 158 NVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRqdgvmsGDYLP 237
                       250
                ....*....|....*.
gi 20130189 310 RNARPVQPIGDRMVYL 325
Cdd:cd03122 238 NNGRPQQPLGSRTVFS 253
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
82-322 5.54e-82

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: 248.77  E-value: 5.54e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189     82 YNYDWDQGPHTWDTAC------NNQSPINIDMNCVEINYFDTPLIWSHYNSIPLgiRLENNGHTLILRaaFPERTPSIDG 155
Cdd:smart01057   1 WGYEGKNGPEHWGKLDppfcggKRQSPIDIVTAEAQYDPSLKPLKLSYDQPTAK--RILNNGHTVQVN--FDDDGSTLSG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189    156 GDLLGRFDFREISFRWSWASSLGSEHTLDHHHSPLEMQCLHTDGDG--CDGCSSSQGVLMISYMFDLS-EHNPFLDVLIQ 232
Cdd:smart01057  77 GPLPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSKGsfSEAVSKPGGLAVVAVFFKVGaEENPALQAILD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189    233 HLAAVEQAGQVVEVPPFPLSYLMSPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLRDRRGSR-IARN 311
Cdd:smart01057 157 HLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEpLVNN 236
                          250
                   ....*....|.
gi 20130189    312 ARPVQPIGDRM 322
Cdd:smart01057 237 ARPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
89-327 1.77e-67

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 212.13  E-value: 1.77e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189    89 GPHTWDT---ACN--NQSPINIDMNCVEINYFDTPLIWSHYNSIPLGIRLENNGHTLILRAAFPERtPSIDGGDLLGRFD 163
Cdd:pfam00194   2 GPEHWGKvypSCGgkRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNTLTNNGHTVQVSLDDGDP-STISGGPLATRYR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189   164 FREISFRWSWASSLGSEHTLDHHHSPLEMQCLH---TDGDGCDGCSSSQGVLMISYMFDL-SEHNPFLDVLIQHLAAVEQ 239
Cdd:pfam00194  81 LVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHynsKYKSFDEAAKHPDGLAVLGVFFEVgDENNPYLQPIVSALDNIKY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189   240 AGQVVEVPPFPLSYLMSPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLRDRRGS----RIARNARPV 315
Cdd:pfam00194 161 KGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGeeprPLVNNFRPT 240
                         250
                  ....*....|..
gi 20130189   316 QPIGDRMVYLNR 327
Cdd:pfam00194 241 QPLNGRVVFASF 252
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
84-324 1.18e-34

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 126.92  E-value: 1.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  84 YDWDQGPHTWDT------ACN---NQSPINIDMNC------VEINYFDTPLiwshynsiplgiRLENNGHTLilRAAFPE 148
Cdd:COG3338  30 YEGETGPEHWGElspefaTCAtgkNQSPIDIRTAIkadlppLKFDYKPTPL------------EIVNNGHTI--QVNVDP 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 149 R-TPSIDGGdllgRFDFREISFRwswassLGSEHTLDHHHSPLEMQCLHTDGDGcdgcsssqGVLMISYMFDLSEHNPFL 227
Cdd:COG3338  96 GsTLTVDGK----RYELKQFHFH------TPSEHTINGKSYPMEAHLVHKDADG--------ELAVVGVLFEEGAENPAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 228 DVLIQHLAAvEQAGQVVEVPPFPLSYLMSPfyDK-FYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLrdrrgs 306
Cdd:COG3338 158 AKLWANLPL-EAGEEVALDATIDLNDLLPE--DRsYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARL------ 228
                       250
                ....*....|....*...
gi 20130189 307 rIARNARPVQPIGDRMVY 324
Cdd:COG3338 229 -YPNNARPVQPLNGRLIL 245
PLN02179 PLN02179
carbonic anhydrase
79-282 8.33e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 52.29  E-value: 8.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189   79 PESYNYDWDQGPHTWDT------ACNN---QSPIniDMNCVEINYFDTPLIWSHYNSIPLGIrlENNGHTLILraafper 149
Cdd:PLN02179  36 LFTYKQKTEKGPAEWGKlnpqwkVCSTgkyQSPI--DLTDERVSLIHDQALSRHYKPAPAVI--QSRGHDVMV------- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  150 TPSIDGGDL-LGRFDFREISFRWSWASslgsEHTLDHHHSPLEMQCLHTdgdgcdgcSSSQGVLMISYMFDLSEHNPFLD 228
Cdd:PLN02179 105 SWKGDAGKItIHQTDYKLVQCHWHSPS----EHTINGTSYDLELHMVHT--------SASGKTAVVGVLYKLGEPDEFLT 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 20130189  229 VLIQHLAAV-EQAGQVVEVPPFPLSYLMspfyDKFYSYNGSLTEPPCHRGAEWLI 282
Cdd:PLN02179 173 KLLNGIKGVgKKEINLGIVDPRDIRFET----NNFYRYIGSLTIPPCTEGVIWTV 223
 
Name Accession Description Interval E-value
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
82-325 2.49e-116

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: 336.25  E-value: 2.49e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  82 YNYDWDQ-GPHTWDtaCNNQSPINIDM-NCVEINYfDTPLIWSHYNSIPLGIRLENNGHTLILRAAFPERTPSIDGGDLL 159
Cdd:cd03122   1 NPKHWAKkYPACGE--GRQQSPIDIVEdTQVQRQG-LQPLHFDGYEELTASTTLENTGKTVILRLEGNSSDPFVSGGPLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 160 GRFDFREISFRWSWASSLGSEHTLDHHHSPLEMQCLHTDGDGCD---GCSSSQGVLMISYMFDLS-EHNPFLDVLIQHLA 235
Cdd:cd03122  78 GRYKFSEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDsfeAIKSPGGVLALAYLFELShEDNPFLDPIIEGLR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 236 AVEQAGQVVEVPPFPLSYLMSPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLRDRR------GSRIA 309
Cdd:cd03122 158 NVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRqdgvmsGDYLP 237
                       250
                ....*....|....*.
gi 20130189 310 RNARPVQPIGDRMVYL 325
Cdd:cd03122 238 NNGRPQQPLGSRTVFS 253
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
82-322 5.54e-82

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: 248.77  E-value: 5.54e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189     82 YNYDWDQGPHTWDTAC------NNQSPINIDMNCVEINYFDTPLIWSHYNSIPLgiRLENNGHTLILRaaFPERTPSIDG 155
Cdd:smart01057   1 WGYEGKNGPEHWGKLDppfcggKRQSPIDIVTAEAQYDPSLKPLKLSYDQPTAK--RILNNGHTVQVN--FDDDGSTLSG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189    156 GDLLGRFDFREISFRWSWASSLGSEHTLDHHHSPLEMQCLHTDGDG--CDGCSSSQGVLMISYMFDLS-EHNPFLDVLIQ 232
Cdd:smart01057  77 GPLPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVHYNSKGsfSEAVSKPGGLAVVAVFFKVGaEENPALQAILD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189    233 HLAAVEQAGQVVEVPPFPLSYLMSPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLRDRRGSR-IARN 311
Cdd:smart01057 157 HLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEpLVNN 236
                          250
                   ....*....|.
gi 20130189    312 ARPVQPIGDRM 322
Cdd:smart01057 237 ARPLQPLNGRV 247
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
98-324 1.57e-79

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: 241.80  E-value: 1.57e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  98 NNQSPINIDMNCVEINYFDTPLIWSHYNSIPLgiRLENNGHTLILRaaFPERTPSIDGGDLLGRFDFREISFRWSWASSL 177
Cdd:cd00326   2 KRQSPINIVTSAVVYDPSLPPLNFDYYPTTSL--TLVNNGHTVQVN--FDDDGGTLSGGGLPGRYKLVQFHFHWGSENSP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 178 GSEHTLDHHHSPLEMQCLHTDGDGCD--GCSSSQGVLMISYMFDLS-EHNPFLDVLIQHLAAVEQAGQVVEVPPFPLSYL 254
Cdd:cd00326  78 GSEHTIDGKRYPLELHLVHYNSDYYSseAAKKPGGLAVLGVFFEVGeKENPFLKKILDALPKIKYKGKETTLPPFDLSDL 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 255 MSPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLRDRRGSRIARNARPVQPIGDRMVY 324
Cdd:cd00326 158 LPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDREGKPLVNNYRPVQPLNGRVVY 227
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
89-327 1.77e-67

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 212.13  E-value: 1.77e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189    89 GPHTWDT---ACN--NQSPINIDMNCVEINYFDTPLIWSHYNSIPLGIRLENNGHTLILRAAFPERtPSIDGGDLLGRFD 163
Cdd:pfam00194   2 GPEHWGKvypSCGgkRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNTLTNNGHTVQVSLDDGDP-STISGGPLATRYR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189   164 FREISFRWSWASSLGSEHTLDHHHSPLEMQCLH---TDGDGCDGCSSSQGVLMISYMFDL-SEHNPFLDVLIQHLAAVEQ 239
Cdd:pfam00194  81 LVQFHFHWGSTDSRGSEHTIDGKRYPAELHIVHynsKYKSFDEAAKHPDGLAVLGVFFEVgDENNPYLQPIVSALDNIKY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189   240 AGQVVEVPPFPLSYLMSPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLRDRRGS----RIARNARPV 315
Cdd:pfam00194 161 KGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGeeprPLVNNFRPT 240
                         250
                  ....*....|..
gi 20130189   316 QPIGDRMVYLNR 327
Cdd:pfam00194 241 QPLNGRVVFASF 252
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
98-324 5.69e-46

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: 155.89  E-value: 5.69e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  98 NNQSPINIDMNCVEINYFDTPLIWSHYNSIPLGIRLENNGHTLILRaaFPERtPSIDGGDLLGRFDFREISFRWSWASSL 177
Cdd:cd03117   2 KRQSPINIVTKKVQYDENLTPFTFTGYDDTTTNWTITNNGHTVQVT--LPDG-AKISGGGLPGTYKALQFHFHWGSNGSP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 178 GSEHTLDHHHSPLEMQCLHTD---GDGCDGCSSSQGVLMISYMFDLSE-HNPFLDVLIQHLAAVEQAGQVVEVPPFPLSY 253
Cdd:cd03117  79 GSEHTIDGERYPMELHIVHIKesyNSLLEALKDSDGLAVLGFFIEEGEeENTNFDPLISALSNIPQKGGSTNLTPFSLRS 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20130189 254 LMSPFY-DKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQL---RDRRGSRIARNARPVQPIGDRMVY 324
Cdd:cd03117 159 LLPSVLlTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVlffDTDNGQPMVNNFRPVQPLNGRVVY 233
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
89-325 4.87e-36

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: 129.70  E-value: 4.87e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  89 GPHTWD------TAC---NNQSPINIDMNCVEINYfDTPLiwsHYNSIPLGIRLENNGHTLILRAAFPERTPSIDGGdll 159
Cdd:cd03124   1 GPEHWGnldpefALCatgKNQSPIDITTKAVVSDK-LPPL---NYNYKPTSATLVNNGHTIQVNFEGNGGTLTIDGE--- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 160 gRFDFREISFRwswassLGSEHTLDHHHSPLEMQCLHTDGDGCdgcsssqgVLMISYMFDLSEHNPFLDVLIQHLAAVEQ 239
Cdd:cd03124  74 -TYQLLQFHFH------SPSEHLINGKRYPLEAHLVHKSKDGQ--------LAVVAVLFEEGKENPFLKKILDNMPKKEG 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 240 AGQVVEVPPFPLSYLmsPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLrdrrgsRIARNARPVQPIG 319
Cdd:cd03124 139 TEVNLPAILDPNELL--PESRSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAA------VYPNNARPVQPLN 210

                ....*.
gi 20130189 320 DRMVYL 325
Cdd:cd03124 211 GREVLL 216
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
84-324 1.18e-34

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 126.92  E-value: 1.18e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  84 YDWDQGPHTWDT------ACN---NQSPINIDMNC------VEINYFDTPLiwshynsiplgiRLENNGHTLilRAAFPE 148
Cdd:COG3338  30 YEGETGPEHWGElspefaTCAtgkNQSPIDIRTAIkadlppLKFDYKPTPL------------EIVNNGHTI--QVNVDP 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 149 R-TPSIDGGdllgRFDFREISFRwswassLGSEHTLDHHHSPLEMQCLHTDGDGcdgcsssqGVLMISYMFDLSEHNPFL 227
Cdd:COG3338  96 GsTLTVDGK----RYELKQFHFH------TPSEHTINGKSYPMEAHLVHKDADG--------ELAVVGVLFEEGAENPAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 228 DVLIQHLAAvEQAGQVVEVPPFPLSYLMSPfyDK-FYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLrdrrgs 306
Cdd:COG3338 158 AKLWANLPL-EAGEEVALDATIDLNDLLPE--DRsYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARL------ 228
                       250
                ....*....|....*...
gi 20130189 307 rIARNARPVQPIGDRMVY 324
Cdd:COG3338 229 -YPNNARPVQPLNGRLIL 245
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
89-324 1.07e-29

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: 113.78  E-value: 1.07e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  89 GPHTWDTA---CNN--QSPINIDMNCVEINYFDTPLIWSHYNSIPL-GIRLENNGHTLILRAAfpertPSIDGGDLLGRF 162
Cdd:cd03126   1 GENSWPKKypfCGGvaQSPIDIHTDILQYDSSLPPLEFHGYNVSGTeQFTLTNNGHTVQLSLP-----PTMHIGGLPFKY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 163 DFREISFRWSWASSL-GSEHTLDHHHSPLEMQCLHTDGDGCDGCSS----SQGVLMISYMFDLSEHNPFLDVLIQHLAAV 237
Cdd:cd03126  76 TASQLHLHWGQRGSPeGSEHTISGKHFAAELHIVHYNSDKYPDISTamnkSQGLAVLGILIEVGPFNPSYEKIFSHLHEV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 238 EQAGQVVEVPPFPLSYLMSPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQL---RDRRGSR-IARNAR 313
Cdd:cd03126 156 KYKDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALETAlysTEEDESReMVNNYR 235
                       250
                ....*....|.
gi 20130189 314 PVQPIGDRMVY 324
Cdd:cd03126 236 QVQPFNERLVF 246
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
100-326 1.41e-29

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: 113.56  E-value: 1.41e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 100 QSPINIDMNCVEINYFDTPLIWSHYNSIPLG-IRLENNGHTLILraAFPErTPSIDGGDLlGRFDFREISFRWSWASSL- 177
Cdd:cd03123  17 QSPIDIQTDIVQFDPSLPPLELVGYDLPGTEeFTLTNNGHTVQL--SLPP-TMHIRGGPG-TEYTAAQLHLHWGGRGSLs 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 178 GSEHTLDHHHSPLEMQCLHTDGDGCDGCSSSQG------VLMISYMFDLSEhNPFLDVLIQHLAAVEQAGQVVEVPPFPL 251
Cdd:cd03123  93 GSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADkpdglaVLAILIEVGYPE-NTYYEKIISHLHEIKYKGQETTVPGFNV 171
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20130189 252 SYLMSPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQ-LRDRRGSRIARNARPVQPIGDRMVYLN 326
Cdd:cd03123 172 RELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLETLENtLMDTHNKTLQNNYRATQPLNGRVVEAS 247
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
89-328 4.75e-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: 109.43  E-value: 4.75e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  89 GPHTWD------TACN---NQSPINIDMNCVeinYFDTPLIWSHYNSiPLGIR--LENNGHTLILRAAfPERTPSIDGGD 157
Cdd:cd03121   1 GPSFWGlvnsawNLCSkgrRQSPVDIEPSRL---LFDPFLTPLRIDT-GRKVSgtFYNTGRHVSFRPD-KDPVVNISGGP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 158 LLGRFDFREISFRWSWASSLGSEHTLDHHHSPLEMQCLHTDGDGCDGCS----SSQGVLMISYMFDLSE-HNPFLDVLIQ 232
Cdd:cd03121  76 LSYRYRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSELYPNFSeaskSPNGLVIVSLFVKIGEtSNPELRRLTN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 233 HLAA--VEQAGQVVEVPPFPLSYLMsPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLRDRRGSRI-- 308
Cdd:cd03121 156 RDTItsIRYKGDAYFLQDLSIELLL-PETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSLRLLSQNSPSQEka 234
                       250       260
                ....*....|....*....|..
gi 20130189 309 --ARNARPVQPIGDRMVYLNRY 328
Cdd:cd03121 235 pmSPNFRPVQPLNNRPVRTNIN 256
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
98-323 2.77e-25

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: 101.45  E-value: 2.77e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  98 NNQSPINIDMNCVEINYFDTPLIWSHYNSIPLGIrlENNGHTLILRAAFPERTPSIDGGDLLGRFDFREISFRWSWASSL 177
Cdd:cd03149   2 NRQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLSI--SNNGHSVMVEFDDSDDKTVITGGPLENPYRLKQFHFHWGAKHGS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 178 GSEHTLDHHHSPLEMQCLHTDGDG----CDGCSSSQGVLMISYMFDLSEHNPFLDVLIQHLAAVEQAGQVVEVPPFPLSY 253
Cdd:cd03149  80 GSEHTVDGKTFPSELHLVHWNAKKyksfGEAAAAPDGLAVLGVFLETGDEHPGLNRLTDALYMVRFKGTKAQFLDFNPKC 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20130189 254 LMsPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQL----RDRRGSRIARNARPVQPIGDRMV 323
Cdd:cd03149 160 LL-PKSLDYWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELlftsEEDQRNHMVNNFRPPQPLKGRTV 232
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
100-323 1.03e-24

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: 1.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 100 QSPINIDMNCVEINYFDTPLIWSHYNSIPL-GIRLENNGHTLILraAFPertPSIDGGDLLGRfDFR--EISFRWSWASS 176
Cdd:cd03150  17 QSPVDIRPHLVAFCPALRPLELLGFDLPPSpSLRLLNNGHTVQL--SLP---SGLRMALGPGQ-EYRalQLHLHWGAAGR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 177 LGSEHTLDHHHSPLEMQCLH--TDGDGCDGCSSSQGVLMI--SYMFDLSEHNPFLDVLIQHLAAVEQAGQVVEVPPFPLS 252
Cdd:cd03150  91 PGSEHTVDGHRFPAEIHVVHlsTAFANLDEALGRPGGLAVlaAFLAEGLHENSAYEQLLSRLSEISEEESETVVPGLDVS 170
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20130189 253 YLMSPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQ-LRDRRGSRIARNARPVQPIGDRMV 323
Cdd:cd03150 171 ALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDsLWGPHDSRLQLNFRATQPLNGRKI 242
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
100-324 8.01e-23

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: 94.91  E-value: 8.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 100 QSPINIDmncVEINYFDTPLIWSHYNSIPLGIR-LENNGHTLILRAAFPERTPSIDGGDLLGRFDFREISFRWSWASSLG 178
Cdd:cd03118   4 QSPINIQ---WRDSVYDPQLAPLRVSYDPATCLyIWNNGYSFQVEFDDSTDKSGISGGPLENHYRLKQFHFHWGANNEWG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 179 SEHTLDHHHSPLEMQCLHTDGDGC----DGCSSSQGVLMISYMFDLSEHNPFLDVLIQHLAAVEQAGQVVEVPPFPLSYL 254
Cdd:cd03118  81 SEHTVDGHTYPAELHLVHWNSVKYenfeEAVMEENGLAVIGVFLKLGAHHEGLQKLVDALPEVRHKDTVVEFNPFDPSCL 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20130189 255 MSPFYDkFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQL----RDRRGSRIARNARPVQPIGDRMVY 324
Cdd:cd03118 161 LPACRD-YWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLlftsRGEEEKVMVNNFRPLQPLMNRKVR 233
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
81-323 8.75e-22

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: 92.50  E-value: 8.75e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  81 SYNYDWDQGPHTWD-----TACNNQSPINIDMNcvEINYfDT---PLIWSHYNSIPLGIRleNNGHTLilRAAFPERTPS 152
Cdd:cd03119   4 HWGYDSHNGPEHWHelfpiAKGDRQSPIDIKTK--DAKH-DPslkPLSVSYDPATAKTIL--NNGHSF--NVEFDDTDDR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 153 --IDGGDLLGRFDFREISFRWSWASSLGSEHTLDHHHSPLEMQCLHTD---GDGCDGCSSSQGVLMISYMFDLSEHNPFL 227
Cdd:cd03119  77 svLRGGPLTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNskyGSFGEAAKQPDGLAVVGVFLKVGEANPEL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 228 DVLIQHLAAVEQAGQVVEVPPFPLSYLMSPFYDkFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQL----RDR 303
Cdd:cd03119 157 QKVLDALDSIKTKGKQAPFTNFDPSCLLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLlfnaEGE 235
                       250       260
                ....*....|....*....|
gi 20130189 304 RGSRIARNARPVQPIGDRMV 323
Cdd:cd03119 236 PPCPMVDNWRPPQPLKGRKV 255
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
100-323 1.76e-20

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: 89.14  E-value: 1.76e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 100 QSPINIdmNCVEINY----FDTPLIWSHynSIPLGIRLENNGHTLilRAAFPERtPSIDGGDLL--GRFDFREISFRWSW 173
Cdd:cd03120  16 QSPINL--NSREARYdpslLEVRLSPNY--VVCRDCEVINDGHTI--QIILKSK-SVLSGGPLPqgHEFELAEVRFHWGR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 174 ASSLGSEHTLDHHHSPLEMQCLH----TDGDGCDGCSSSQGVLMISYMFDLSEHNPFLDVLIQHLAAVEQAGQVVEVPPF 249
Cdd:cd03120  89 ENQRGSEHTVNFKAFPMELHLIHwnstLYSSLEEAMGKPHGIAIIALFVQIGKEHVGLKAVTEILQDIQYKGKSKTIPCF 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 250 -PLSYLMSPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLRDR-RGSRIAR--------NARPVQPIG 319
Cdd:cd03120 169 nPNTLLPDPLLRDYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRRLRTHvKGAELVEgcdgllgdNFRPTQPLS 248

                ....
gi 20130189 320 DRMV 323
Cdd:cd03120 249 DRVI 252
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
100-323 1.52e-16

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: 77.90  E-value: 1.52e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 100 QSPINIDMNCVEINYFDTPLIWSHYNSIPLGIRLENNGHTLilRAAFPErTPSIDGGDLlGRFDFREISFRW---SWASS 176
Cdd:cd03125  17 QSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNNGHTV--QIDLPP-TMSITTGDG-TVYTAVQMHFHWggrDSEIS 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189 177 lGSEHTLDHHHSPLEMQCLHTDG---------DGCDGCSssqgVLMISYMFDLSEHNPFLDVLIQHLAAVEQAGQVVEVP 247
Cdd:cd03125  93 -GSEHTIDGMRYVAELHIVHYNSkyksyeeakDKPDGLA----VLAFLYKVGHYAENTYYSDFISKLAKIKYAGQTTTLT 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20130189 248 PFPLSYLMSPFYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQ-LRDRRGSRIARNARPVQPIGDRMV 323
Cdd:cd03125 168 SLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLENtLMDHHNKTIRNDYRRTQPLNHRVV 244
PLN02179 PLN02179
carbonic anhydrase
79-282 8.33e-08

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 52.29  E-value: 8.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189   79 PESYNYDWDQGPHTWDT------ACNN---QSPIniDMNCVEINYFDTPLIWSHYNSIPLGIrlENNGHTLILraafper 149
Cdd:PLN02179  36 LFTYKQKTEKGPAEWGKlnpqwkVCSTgkyQSPI--DLTDERVSLIHDQALSRHYKPAPAVI--QSRGHDVMV------- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  150 TPSIDGGDL-LGRFDFREISFRWSWASslgsEHTLDHHHSPLEMQCLHTdgdgcdgcSSSQGVLMISYMFDLSEHNPFLD 228
Cdd:PLN02179 105 SWKGDAGKItIHQTDYKLVQCHWHSPS----EHTINGTSYDLELHMVHT--------SASGKTAVVGVLYKLGEPDEFLT 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 20130189  229 VLIQHLAAV-EQAGQVVEVPPFPLSYLMspfyDKFYSYNGSLTEPPCHRGAEWLI 282
Cdd:PLN02179 173 KLLNGIKGVgKKEINLGIVDPRDIRFET----NNFYRYIGSLTIPPCTEGVIWTV 223
PLN02202 PLN02202
carbonate dehydratase
179-323 5.97e-07

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 50.06  E-value: 5.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130189  179 SEHTLDHHHSPLEMQCLHTDGDGcdgcsssqGVLMISYMFDLSEHNPFLDVLIQHLAAVE-------QAGQVvEVPPFPL 251
Cdd:PLN02202 124 SEHHLHGVQYAAELHMVHQAKDG--------SFAVVASLFKIGTEEPFLSQMKDKLVKLKeerfkgnHTAQV-EVGKIDT 194
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20130189  252 SYLMSPfYDKFYSYNGSLTEPPCHRGAEWLIYPESLAISERQLNEFRQLRDRrgsRIARNARPVQPIGDRMV 323
Cdd:PLN02202 195 RHIERK-TRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRSPLDK---SFKNNSRPCQPLNGRRV 262
 
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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