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Conserved domains on  [gi|169636420|ref|NP_001207|]
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carbonic anhydrase 9 precursor [Homo sapiens]

Protein Classification

carbonic anhydrase family protein( domain architecture ID 10123557)

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_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
145-391 6.57e-170

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: 477.14  E-value: 6.57e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 145 GDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLPELRLRNNGHSVQLTLPPGLEMALGPGREYRALQ 224
Cdd:cd03150    1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALGPGQEYRALQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 225 LHLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGS 304
Cdd:cd03150   81 LHLHWGAAGRPGSEHTVDGHRFPAEIHVVHLSTAFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEISEEES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 305 ETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSRLQLNFRATQPLNGR 384
Cdd:cd03150  161 ETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHDSRLQLNFRATQPLNGR 240

                 ....*..
gi 169636420 385 VIEASFP 391
Cdd:cd03150  241 KIEASFP 247
PHA03169 super family cl27451
hypothetical protein; Provisional
44-148 1.69e-04

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA03169:

Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.81  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420  44 QEDSPLGGGSSGEDDPLGEEDLPSE-------EDSPREEDPPGEEDLPGEEDLPGEEDLPEVKPKSEEEGSLKLEDLPTV 116
Cdd:PHA03169 116 SGLSPENTSGSSPESPASHSPPPSPpshpgphEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQS 195
                         90       100       110
                 ....*....|....*....|....*....|..
gi 169636420 117 EAPGDPQEPQNNAhrDKEGDDQSHWRYGGDPP 148
Cdd:PHA03169 196 ETPTSSPPPQSPP--DEPGEPQSPTPQQAPSP 225
 
Name Accession Description Interval E-value
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
145-391 6.57e-170

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: 477.14  E-value: 6.57e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 145 GDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLPELRLRNNGHSVQLTLPPGLEMALGPGREYRALQ 224
Cdd:cd03150    1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALGPGQEYRALQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 225 LHLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGS 304
Cdd:cd03150   81 LHLHWGAAGRPGSEHTVDGHRFPAEIHVVHLSTAFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEISEEES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 305 ETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSRLQLNFRATQPLNGR 384
Cdd:cd03150  161 ETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHDSRLQLNFRATQPLNGR 240

                 ....*..
gi 169636420 385 VIEASFP 391
Cdd:cd03150  241 KIEASFP 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
149-390 9.12e-104

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 309.20  E-value: 9.12e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420  149 WPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPlPELRLRNNGHSVQLTLPPG--LEMALGP-GREYRALQL 225
Cdd:pfam00194   6 WGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPP-GKNTLTNNGHTVQVSLDDGdpSTISGGPlATRYRLVQF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420  226 HLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGSE 305
Cdd:pfam00194  85 HFHWGSTDSRGSEHTIDGKRYPAELHIVHYNSKYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALDNIKYKGKS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420  306 TQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSR---LQLNFRATQPLN 382
Cdd:pfam00194 165 VLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEprpLVNNFRPTQPLN 244

                  ....*...
gi 169636420  383 GRVIEASF 390
Cdd:pfam00194 245 GRVVFASF 252
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
141-385 6.57e-91

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: 276.12  E-value: 6.57e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420   141 WRYGGD---PPWPRVSPACA-GRFQSPVDIRPQLAAFCPALRPLEllgFQLPPLPELRLRNNGHSVQLTLPPG-LEMALG 215
Cdd:smart01057   1 WGYEGKngpEHWGKLDPPFCgGKRQSPIDIVTAEAQYDPSLKPLK---LSYDQPTAKRILNNGHTVQVNFDDDgSTLSGG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420   216 P-GREYRALQLHLHWGAAGRPGSEHTVEGHRFPAEIHVVHlSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLS 294
Cdd:smart01057  78 PlPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVH-YNSKGSFSEAVSKPGGLAVVAVFFKVGAEENPALQAILD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420   295 RLEEIAEEGSETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSRLQLN 374
Cdd:smart01057 157 HLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEPLVNN 236
                          250
                   ....*....|.
gi 169636420   375 FRATQPLNGRV 385
Cdd:smart01057 237 ARPLQPLNGRV 247
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
133-389 1.52e-59

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 195.49  E-value: 1.52e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 133 KEGDDQSHWRYGGD--PP-WPRVSP---ACA-GRFQSPVDIRPQLAAfcpalrPLELLGFQLPPLPeLRLRNNGHSVQLT 205
Cdd:COG3338   20 AAAASAPHWSYEGEtgPEhWGELSPefaTCAtGKNQSPIDIRTAIKA------DLPPLKFDYKPTP-LEIVNNGHTIQVN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 206 LPPGLEMALGpGREYRALQLHLHwgaagRPgSEHTVEGHRFPAEIHVVHLSTAfarvdealgrpGGLAVLAAFLEEGpEE 285
Cdd:COG3338   93 VDPGSTLTVD-GKRYELKQFHFH-----TP-SEHTINGKSYPMEAHLVHKDAD-----------GELAVVGVLFEEG-AE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 286 NSAYEQLLSRLEeiAEEGSETQVP-GLDISALLPSDfSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTlw 364
Cdd:COG3338  154 NPALAKLWANLP--LEAGEEVALDaTIDLNDLLPED-RSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARL-- 228
                        250       260
                 ....*....|....*....|....*
gi 169636420 365 gpgdsrLQLNFRATQPLNGRVIEAS 389
Cdd:COG3338  229 ------YPNNARPVQPLNGRLILES 247
PLN02202 PLN02202
carbonate dehydratase
145-387 8.86e-20

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 89.35  E-value: 8.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 145 GDPPWPRVSP---ACA-GRFQSPVDIRPQLAAFCPALRPLELLGFqlppLPELRLRNNGHSVQLTLPPGLEMALGPGREY 220
Cdd:PLN02202  38 GPNQWGHLNPhftKCAvGKLQSPIDIQRRQIFYNHKLESIHRDYY----FTNATLVNHVCNVAMFFGEGAGDVIIDNKNY 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 221 RALQLHLHwgaagrPGSEHTVEGHRFPAEIHVVHLStafarvdealgRPGGLAVLAAFLEEGPEEN--SAYEQLLSRLEE 298
Cdd:PLN02202 114 TLLQMHWH------TPSEHHLHGVQYAAELHMVHQA-----------KDGSFAVVASLFKIGTEEPflSQMKDKLVKLKE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 299 IAEEGSET---QVPGLDiSALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDtlwgPGDSRLQLNF 375
Cdd:PLN02202 177 ERFKGNHTaqvEVGKID-TRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRS----PLDKSFKNNS 251
                        250
                 ....*....|..
gi 169636420 376 RATQPLNGRVIE 387
Cdd:PLN02202 252 RPCQPLNGRRVE 263
PHA03169 PHA03169
hypothetical protein; Provisional
44-148 1.69e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.81  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420  44 QEDSPLGGGSSGEDDPLGEEDLPSE-------EDSPREEDPPGEEDLPGEEDLPGEEDLPEVKPKSEEEGSLKLEDLPTV 116
Cdd:PHA03169 116 SGLSPENTSGSSPESPASHSPPPSPpshpgphEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQS 195
                         90       100       110
                 ....*....|....*....|....*....|..
gi 169636420 117 EAPGDPQEPQNNAhrDKEGDDQSHWRYGGDPP 148
Cdd:PHA03169 196 ETPTSSPPPQSPP--DEPGEPQSPTPQQAPSP 225
CobT2 COG4547
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
41-137 9.37e-03

Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 443611 [Multi-domain]  Cd Length: 608  Bit Score: 38.24  E-value: 9.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420  41 PRMQEDSPLGGGSsgEDDPLGEEDLPSEEDSPREEDPPGEEDLPGEEDLPGEEDLPEVKPKSEEEGslklEDLPTVEAPG 120
Cdd:COG4547  214 DEDEEDEDDEDDS--GEQEEDEEDGEDEDEESDEGAEAEDAEASGDDAEEGESEAAEAESDEMAEE----AEGEDSEEPG 287
                         90
                 ....*....|....*..
gi 169636420 121 DPQEPQNNAHRDKEGDD 137
Cdd:COG4547  288 EPWRPNAPPPDDPADPD 304
 
Name Accession Description Interval E-value
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
145-391 6.57e-170

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: 477.14  E-value: 6.57e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 145 GDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLPELRLRNNGHSVQLTLPPGLEMALGPGREYRALQ 224
Cdd:cd03150    1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALGPGQEYRALQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 225 LHLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGS 304
Cdd:cd03150   81 LHLHWGAAGRPGSEHTVDGHRFPAEIHVVHLSTAFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEISEEES 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 305 ETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSRLQLNFRATQPLNGR 384
Cdd:cd03150  161 ETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHDSRLQLNFRATQPLNGR 240

                 ....*..
gi 169636420 385 VIEASFP 391
Cdd:cd03150  241 KIEASFP 247
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
145-390 1.15e-150

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: 428.26  E-value: 1.15e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 145 GDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLPELRLRNNGHSVQLTLPPGLEMALGPGREYRALQ 224
Cdd:cd03123    1 GEDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHIRGGPGTEYTAAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 225 LHLHWGAAG-RPGSEHTVEGHRFPAEIHVVHL-STAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEE 302
Cdd:cd03123   81 LHLHWGGRGsLSGSEHTIDGIRFAAELHIVHYnSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKYK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 303 GSETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSRLQLNFRATQPLN 382
Cdd:cd03123  161 GQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQLETLENTLMDTHNKTLQNNYRATQPLN 240

                 ....*...
gi 169636420 383 GRVIEASF 390
Cdd:cd03123  241 GRVVEASF 248
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
149-390 9.12e-104

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 309.20  E-value: 9.12e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420  149 WPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPlPELRLRNNGHSVQLTLPPG--LEMALGP-GREYRALQL 225
Cdd:pfam00194   6 WGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPP-GKNTLTNNGHTVQVSLDDGdpSTISGGPlATRYRLVQF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420  226 HLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGSE 305
Cdd:pfam00194  85 HFHWGSTDSRGSEHTIDGKRYPAELHIVHYNSKYKSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALDNIKYKGKS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420  306 TQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSR---LQLNFRATQPLN 382
Cdd:pfam00194 165 VLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEEprpLVNNFRPTQPLN 244

                  ....*...
gi 169636420  383 GRVIEASF 390
Cdd:pfam00194 245 GRVVFASF 252
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
158-387 4.10e-92

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: 278.40  E-value: 4.10e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 158 GRFQSPVDIRPQLAAFCPALRPLELLGFqlpPLPELRLRNNGHSVQLTLPPGLEMALGPG--REYRALQLHLHWGAAGRP 235
Cdd:cd00326    1 GKRQSPINIVTSAVVYDPSLPPLNFDYY---PTTSLTLVNNGHTVQVNFDDDGGTLSGGGlpGRYKLVQFHFHWGSENSP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 236 GSEHTVEGHRFPAEIHVVHLSTAFARvDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGSETQVPGLDISA 315
Cdd:cd00326   78 GSEHTIDGKRYPLELHLVHYNSDYYS-SEAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLSD 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169636420 316 LLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDsRLQLNFRATQPLNGRVIE 387
Cdd:cd00326  157 LLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDREGK-PLVNNYRPVQPLNGRVVY 227
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
141-385 6.57e-91

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: 276.12  E-value: 6.57e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420   141 WRYGGD---PPWPRVSPACA-GRFQSPVDIRPQLAAFCPALRPLEllgFQLPPLPELRLRNNGHSVQLTLPPG-LEMALG 215
Cdd:smart01057   1 WGYEGKngpEHWGKLDPPFCgGKRQSPIDIVTAEAQYDPSLKPLK---LSYDQPTAKRILNNGHTVQVNFDDDgSTLSGG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420   216 P-GREYRALQLHLHWGAAGRPGSEHTVEGHRFPAEIHVVHlSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLS 294
Cdd:smart01057  78 PlPGRYRLKQFHFHWGGSDSEGSEHTIDGKRFPLELHLVH-YNSKGSFSEAVSKPGGLAVVAVFFKVGAEENPALQAILD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420   295 RLEEIAEEGSETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSRLQLN 374
Cdd:smart01057 157 HLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGNEPLVNN 236
                          250
                   ....*....|.
gi 169636420   375 FRATQPLNGRV 385
Cdd:smart01057 237 ARPLQPLNGRV 247
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
137-391 2.99e-81

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: 251.63  E-value: 2.99e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 137 DQSHWryggdppwPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLpELRLRNNGHSVQLTLPPGLEMALGP 216
Cdd:cd03125    1 DESHW--------PEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQG-EFTMTNNGHTVQIDLPPTMSITTGD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 217 GREYRALQLHLHWGAAGR--PGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEG-PEENSAYEQLL 293
Cdd:cd03125   72 GTVYTAVQMHFHWGGRDSeiSGSEHTIDGMRYVAELHIVHYNSKYKSYEEAKDKPDGLAVLAFLYKVGhYAENTYYSDFI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 294 SRLEEIAEEGSETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSRLQL 373
Cdd:cd03125  152 SKLAKIKYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQIVKLENTLMDHHNKTIRN 231
                        250
                 ....*....|....*...
gi 169636420 374 NFRATQPLNGRVIEASFP 391
Cdd:cd03125  232 DYRRTQPLNHRVVEANFL 249
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
145-390 4.33e-80

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: 248.60  E-value: 4.33e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 145 GDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLPELRLRNNGHSVQLTLPPGLEMALGPgREYRALQ 224
Cdd:cd03126    1 GENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHIGGLP-FKYTASQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 225 LHLHWGAAGRP-GSEHTVEGHRFPAEIHVVHL-STAFARVDEALGRPGGLAVLAAFLEEGPEeNSAYEQLLSRLEEIAEE 302
Cdd:cd03126   80 LHLHWGQRGSPeGSEHTISGKHFAAELHIVHYnSDKYPDISTAMNKSQGLAVLGILIEVGPF-NPSYEKIFSHLHEVKYK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 303 GSETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGP-GDSRLQL--NFRATQ 379
Cdd:cd03126  159 DQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQLLALETALYSTeEDESREMvnNYRQVQ 238
                        250
                 ....*....|.
gi 169636420 380 PLNGRVIEASF 390
Cdd:cd03126  239 PFNERLVFASF 249
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
158-386 1.88e-77

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: 241.02  E-value: 1.88e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 158 GRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLPeLRLRNNGHSVQLTLPPGLEMALG--PGReYRALQLHLHWGAAGRP 235
Cdd:cd03117    1 GKRQSPINIVTKKVQYDENLTPFTFTGYDDTTTN-WTITNNGHTVQVTLPDGAKISGGglPGT-YKALQFHFHWGSNGSP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 236 GSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGSETQVPGLDISA 315
Cdd:cd03117   79 GSEHTIDGERYPMELHIVHIKESYNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSLRS 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169636420 316 LLPS-DFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTL--WGPGDSRLQLNFRATQPLNGRVI 386
Cdd:cd03117  159 LLPSvLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLffDTDNGQPMVNNFRPVQPLNGRVV 232
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
133-389 1.52e-59

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 195.49  E-value: 1.52e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 133 KEGDDQSHWRYGGD--PP-WPRVSP---ACA-GRFQSPVDIRPQLAAfcpalrPLELLGFQLPPLPeLRLRNNGHSVQLT 205
Cdd:COG3338   20 AAAASAPHWSYEGEtgPEhWGELSPefaTCAtGKNQSPIDIRTAIKA------DLPPLKFDYKPTP-LEIVNNGHTIQVN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 206 LPPGLEMALGpGREYRALQLHLHwgaagRPgSEHTVEGHRFPAEIHVVHLSTAfarvdealgrpGGLAVLAAFLEEGpEE 285
Cdd:COG3338   93 VDPGSTLTVD-GKRYELKQFHFH-----TP-SEHTINGKSYPMEAHLVHKDAD-----------GELAVVGVLFEEG-AE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 286 NSAYEQLLSRLEeiAEEGSETQVP-GLDISALLPSDfSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTlw 364
Cdd:COG3338  154 NPALAKLWANLP--LEAGEEVALDaTIDLNDLLPED-RSYYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAFARL-- 228
                        250       260
                 ....*....|....*....|....*
gi 169636420 365 gpgdsrLQLNFRATQPLNGRVIEAS 389
Cdd:COG3338  229 ------YPNNARPVQPLNGRLILES 247
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
149-386 1.84e-56

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: 187.56  E-value: 1.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 149 WPRVSPAC-AGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLpELRLRNNGHSVQLTL-PPGLEMALG----PGReYRA 222
Cdd:cd03122    5 WAKKYPACgEGRQQSPIDIVEDTQVQRQGLQPLHFDGYEELTA-STTLENTGKTVILRLeGNSSDPFVSggplLGR-YKF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 223 LQLHLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEE 302
Cdd:cd03122   83 SEITFHWGTCNSDGSEHSIDGHKFPLEMQILHRNTDFFDSFEAIKSPGGVLALAYLFELSHEDNPFLDPIIEGLRNVSRP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 303 GSETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLS-----DTLWGPGDSRLQLNFRA 377
Cdd:cd03122  163 GKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRelltrRQDGVMSGDYLPNNGRP 242

                 ....*....
gi 169636420 378 TQPLNGRVI 386
Cdd:cd03122  243 QQPLGSRTV 251
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
149-387 2.65e-55

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: 183.24  E-value: 2.65e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 149 WPRVSP---ACA-GRFQSPVDIrPQLAAFCPALRPLELLGFQLPplpeLRLRNNGHSVQLTLPPGLEMALGPGREYRALQ 224
Cdd:cd03124    5 WGNLDPefaLCAtGKNQSPIDI-TTKAVVSDKLPPLNYNYKPTS----ATLVNNGHTIQVNFEGNGGTLTIDGETYQLLQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 225 LHLHwgaagRPgSEHTVEGHRFPAEIHVVHLSTAfarvdealgrpGGLAVLAAFLEEGpEENSAYEQLLSRLEEIAEEGs 304
Cdd:cd03124   80 FHFH-----SP-SEHLINGKRYPLEAHLVHKSKD-----------GQLAVVAVLFEEG-KENPFLKKILDNMPKKEGTE- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 305 ETQVPGLDISALLPSDfSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPgdsrlqlNFRATQPLNGR 384
Cdd:cd03124  141 VNLPAILDPNELLPES-RSYYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKFRAAVYPN-------NARPVQPLNGR 212

                 ...
gi 169636420 385 VIE 387
Cdd:cd03124  213 EVL 215
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
158-390 1.65e-52

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: 176.56  E-value: 1.65e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 158 GRFQSPVDIRPQLAAFCPALRPLELlgfQLPPLPELRLRNNGHSVQLTLPPGLEMAL---GP-GREYRALQLHLHWGAAG 233
Cdd:cd03149    1 GNRQSPIDIVSSEAVYDPKLKPLSL---SYDPCTSLSISNNGHSVMVEFDDSDDKTVitgGPlENPYRLKQFHFHWGAKH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 234 RPGSEHTVEGHRFPAEIHVVHL-STAFARVDEALGRPGGLAVLAAFLEEGpEENSAYEQLLSRLEEIAEEGSETQVPGLD 312
Cdd:cd03149   78 GSGSEHTVDGKTFPSELHLVHWnAKKYKSFGEAAAAPDGLAVLGVFLETG-DEHPGLNRLTDALYMVRFKGTKAQFLDFN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 313 ISALLPSDFSrYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLW-GPGDSRLQL--NFRATQPLNGRVIEAS 389
Cdd:cd03149  157 PKCLLPKSLD-YWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFtSEEDQRNHMvnNFRPPQPLKGRTVRAS 235

                 .
gi 169636420 390 F 390
Cdd:cd03149  236 F 236
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
138-390 2.10e-52

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: 177.25  E-value: 2.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 138 QSHWRYG---GDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPLEllgFQLPPLPELRLRNNGHSVQLTLPPGLEMAL 214
Cdd:cd03119    2 SHHWGYDshnGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLS---VSYDPATAKTILNNGHSFNVEFDDTDDRSV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 215 ---GP-GREYRALQLHLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGpEENSAYE 290
Cdd:cd03119   79 lrgGPlTGSYRLRQFHFHWGSSDDHGSEHTVDGVKYAAELHLVHWNSKYGSFGEAAKQPDGLAVVGVFLKVG-EANPELQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 291 QLLSRLEEIAEEGSETQVPGLDISALLPSdfSR-YFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQL---HTLSDTLWGP 366
Cdd:cd03119  158 KVLDALDSIKTKGKQAPFTNFDPSCLLPA--SLdYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMakfRSLLFNAEGE 235
                        250       260
                 ....*....|....*....|....
gi 169636420 367 GDSRLQLNFRATQPLNGRVIEASF 390
Cdd:cd03119  236 PPCPMVDNWRPPQPLKGRKVRASF 259
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
145-386 5.82e-43

Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup contains carbonic anhydrase related proteins (CARPs) X and XI, which have been implicated in various biological processes of the central nervous system. CARPs are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. CARP XI plays a role in the development of gastrointestinal stromal tumors.


Pssm-ID: 239395 [Multi-domain]  Cd Length: 256  Bit Score: 152.18  E-value: 5.82e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 145 GDPPWPRVSPA---CA-GRFQSPVDIRPQLAAFCPALRPLELLGfqlPPLPELRLRNNGHSVQLTLPPG--LEMALGP-G 217
Cdd:cd03121    1 GPSFWGLVNSAwnlCSkGRRQSPVDIEPSRLLFDPFLTPLRIDT---GRKVSGTFYNTGRHVSFRPDKDpvVNISGGPlS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 218 REYRALQLHLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTA-FARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRL 296
Cdd:cd03121   78 YRYRLEEIRLHFGREDEQGSEHTVNGQAFPGEVQLIHYNSElYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 297 E--EIAEEGSETQVPGLDISALLPsDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHT---LSDTLWGPGDSRL 371
Cdd:cd03121  158 TitSIRYKGDAYFLQDLSIELLLP-ETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMHSlrlLSQNSPSQEKAPM 236
                        250
                 ....*....|....*
gi 169636420 372 QLNFRATQPLNGRVI 386
Cdd:cd03121  237 SPNFRPVQPLNNRPV 251
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
158-390 1.41e-42

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: 150.38  E-value: 1.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 158 GRFQSPVDIRPQLAAFCPALRPLELlgfQLPPLPELRLRNNGHSVQLTLPPGLEMAL---GP-GREYRALQLHLHWGAAG 233
Cdd:cd03118    1 GTRQSPINIQWRDSVYDPQLAPLRV---SYDPATCLYIWNNGYSFQVEFDDSTDKSGisgGPlENHYRLKQFHFHWGANN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 234 RPGSEHTVEGHRFPAEIHVVHL-STAFARVDEALGRPGGLAVLAAFLEEGpEENSAYEQLLSRLEEIAEEGSETQVPGLD 312
Cdd:cd03118   78 EWGSEHTVDGHTYPAELHLVHWnSVKYENFEEAVMEENGLAVIGVFLKLG-AHHEGLQKLVDALPEVRHKDTVVEFNPFD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 313 ISALLPSDfSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQL---HTLSDTLWGPGDSRLQLNFRATQPLNGRVIEAS 389
Cdd:cd03118  157 PSCLLPAC-RDYWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLsvfRTLLFTSRGEEEKVMVNNFRPLQPLMNRKVRSS 235

                 .
gi 169636420 390 F 390
Cdd:cd03118  236 F 236
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
149-390 8.27e-39

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: 141.15  E-value: 8.27e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 149 WPRVSPACAGRFQSPVDIRPQLAAFCPALrplelLGFQLPP----LPELRLRNNGHSVQLTLPPGLEMALGP---GREYR 221
Cdd:cd03120    4 WGLLFPEANGEYQSPINLNSREARYDPSL-----LEVRLSPnyvvCRDCEVINDGHTIQIILKSKSVLSGGPlpqGHEFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 222 ALQLHLHWGAAGRPGSEHTVEGHRFPAEIHVVHL-STAFARVDEALGRPGGLAVLAAFLEEGpEENSAYEQLLSRLEEIA 300
Cdd:cd03120   79 LAEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWnSTLYSSLEEAMGKPHGIAIIALFVQIG-KEHVGLKAVTEILQDIQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 301 EEGSETQVPGLDISALLPSDFSR-YFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQL--------HTLSDTLWGPGDSRL 371
Cdd:cd03120  158 YKGKSKTIPCFNPNTLLPDPLLRdYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIeefrrlrtHVKGAELVEGCDGLL 237
                        250
                 ....*....|....*....
gi 169636420 372 QLNFRATQPLNGRVIEASF 390
Cdd:cd03120  238 GDNFRPTQPLSDRVIRAAF 256
PLN02202 PLN02202
carbonate dehydratase
145-387 8.86e-20

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 89.35  E-value: 8.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 145 GDPPWPRVSP---ACA-GRFQSPVDIRPQLAAFCPALRPLELLGFqlppLPELRLRNNGHSVQLTLPPGLEMALGPGREY 220
Cdd:PLN02202  38 GPNQWGHLNPhftKCAvGKLQSPIDIQRRQIFYNHKLESIHRDYY----FTNATLVNHVCNVAMFFGEGAGDVIIDNKNY 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 221 RALQLHLHwgaagrPGSEHTVEGHRFPAEIHVVHLStafarvdealgRPGGLAVLAAFLEEGPEEN--SAYEQLLSRLEE 298
Cdd:PLN02202 114 TLLQMHWH------TPSEHHLHGVQYAAELHMVHQA-----------KDGSFAVVASLFKIGTEEPflSQMKDKLVKLKE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 299 IAEEGSET---QVPGLDiSALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDtlwgPGDSRLQLNF 375
Cdd:PLN02202 177 ERFKGNHTaqvEVGKID-TRHIERKTRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELLRS----PLDKSFKNNS 251
                        250
                 ....*....|..
gi 169636420 376 RATQPLNGRVIE 387
Cdd:PLN02202 252 RPCQPLNGRRVE 263
PLN02179 PLN02179
carbonic anhydrase
145-349 5.00e-14

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 71.55  E-value: 5.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 145 GDPPWPRVSP---ACA-GRFQSPVDIRPQLAAfcpaLRPLELLGFQLPPLPELrLRNNGHSVQLTLPPGLEMALGPGREY 220
Cdd:PLN02179  46 GPAEWGKLNPqwkVCStGKYQSPIDLTDERVS----LIHDQALSRHYKPAPAV-IQSRGHDVMVSWKGDAGKITIHQTDY 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420 221 RALQLHLHwgaagrPGSEHTVEGHRFPAEIHVVHLSTAfarvdealgrpGGLAVLAAFLEEGpEENSAYEQLLSRLEEIA 300
Cdd:PLN02179 121 KLVQCHWH------SPSEHTINGTSYDLELHMVHTSAS-----------GKTAVVGVLYKLG-EPDEFLTKLLNGIKGVG 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169636420 301 EEGsetqvpgLDISALLPSDF----SRYFQYEGSLTTPPCAQGVIWTVFNQTV 349
Cdd:PLN02179 183 KKE-------INLGIVDPRDIrfetNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
PHA03169 PHA03169
hypothetical protein; Provisional
44-148 1.69e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.81  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420  44 QEDSPLGGGSSGEDDPLGEEDLPSE-------EDSPREEDPPGEEDLPGEEDLPGEEDLPEVKPKSEEEGSLKLEDLPTV 116
Cdd:PHA03169 116 SGLSPENTSGSSPESPASHSPPPSPpshpgphEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQS 195
                         90       100       110
                 ....*....|....*....|....*....|..
gi 169636420 117 EAPGDPQEPQNNAhrDKEGDDQSHWRYGGDPP 148
Cdd:PHA03169 196 ETPTSSPPPQSPP--DEPGEPQSPTPQQAPSP 225
CobT2 COG4547
Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; ...
41-137 9.37e-03

Cobalamin biosynthesis cobaltochelatase CobT subunit [Coenzyme transport and metabolism]; Cobalamin biosynthesis cobaltochelatase CobT subunit is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 443611 [Multi-domain]  Cd Length: 608  Bit Score: 38.24  E-value: 9.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636420  41 PRMQEDSPLGGGSsgEDDPLGEEDLPSEEDSPREEDPPGEEDLPGEEDLPGEEDLPEVKPKSEEEGslklEDLPTVEAPG 120
Cdd:COG4547  214 DEDEEDEDDEDDS--GEQEEDEEDGEDEDEESDEGAEAEDAEASGDDAEEGESEAAEAESDEMAEE----AEGEDSEEPG 287
                         90
                 ....*....|....*..
gi 169636420 121 DPQEPQNNAHRDKEGDD 137
Cdd:COG4547  288 EPWRPNAPPPDDPADPD 304
 
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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