NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1359090889|ref|NP_035349|]
View 

receptor-type tyrosine-protein phosphatase zeta isoform 1 precursor [Mus musculus]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 10123232)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
45-298 9.01e-110

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: 348.58  E-value: 9.01e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   45 NQKNWGKKYPICNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWEKASLEnTFIHNTGKTVEINLTN---DYYLSGGLSEK 119
Cdd:cd03122      1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  120 VFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEeAVKGKGRLRALSILFEVGVEENLDYKAIIDG 199
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  200 TESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234
                          250
                   ....*....|....*....
gi 1359090889  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
fn3 pfam00041
Fibronectin type III domain;
313-401 2.00e-09

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 2.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  313 SEPENVQADPENYTSLLVTWERPRVVyDAMIEKFAVLYQPLaGNDQAKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAVC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDG-NGPITGYEVEYRPK-NSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77

                   ....*....
gi 1359090889  393 SNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
 
Name Accession Description Interval E-value
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
45-298 9.01e-110

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: 348.58  E-value: 9.01e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   45 NQKNWGKKYPICNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWEKASLEnTFIHNTGKTVEINLTN---DYYLSGGLSEK 119
Cdd:cd03122      1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  120 VFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEeAVKGKGRLRALSILFEVGVEENLDYKAIIDG 199
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  200 TESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234
                          250
                   ....*....|....*....
gi 1359090889  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
38-295 3.81e-86

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: 281.51  E-value: 3.81e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889    38 WSYTGALNQKNWGKKYP-ICNSPKQSPINIDEDLTQVNVNLKKLKFQgWEKASleNTFIHNTGKTVEINL-TNDYYLSGG 115
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPpFCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   116 LSEKVFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADrfSSFEEAVKGKGRLRALSILFEVGVEENLDYKA 195
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   196 IIDGTESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSgyv 275
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230
                           250       260
                    ....*....|....*....|
gi 1359090889   276 mlmDYLQNNFREQQYKFSRQ 295
Cdd:smart01057  231 ---EPLVNNARPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
44-300 1.12e-82

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 271.83  E-value: 1.12e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   44 LNQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTfIHNTGKTVEINLTNDY--YLSGGLSEKVF 121
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDpsTISGGPLATRY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  122 KASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRfSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTE 201
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  202 SVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 281
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233
                          250
                   ....*....|....*....
gi 1359090889  282 QNNFREQQYKFSRQVFSSY 300
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
38-263 1.04e-32

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 128.08  E-value: 1.04e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   38 WSYTGALNQKNWGK---KYPICNS-PKQSPINIDedlTQVNVNLKKLKFQgWEKASLEntfIHNTGKTVEINLTNDYYLS 113
Cdd:COG3338     28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKFD-YKPTPLE---IVNNGHTIQVNVDPGSTLT 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  114 ggLSEKVFKASKITFHwgkcnvssEGSEHSLEGQKFPLEMQ-VYcfdadrfssfeeaVKGKGRLRALSILFEVGvEENLD 192
Cdd:COG3338    101 --VDGKRYELKQFHFH--------TPSEHTINGKSYPMEAHlVH-------------KDADGELAVVGVLFEEG-AENPA 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1359090889  193 YKAIID------GTESVSrfgkQAALDPfvlQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVF 263
Cdd:COG3338    157 LAKLWAnlpleaGEEVAL----DATIDL---NDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
fn3 pfam00041
Fibronectin type III domain;
313-401 2.00e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 2.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  313 SEPENVQADPENYTSLLVTWERPRVVyDAMIEKFAVLYQPLaGNDQAKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAVC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDG-NGPITGYEVEYRPK-NSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77

                   ....*....
gi 1359090889  393 SNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
PLN02179 PLN02179
carbonic anhydrase
49-253 8.95e-09

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 57.68  E-value: 8.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   49 WGKKYP---ICNSPK-QSPInideDLTQVNVNLkkLKFQGWEKA-SLENTFIHNTGKTVEINLTNDyylsgglsekvfkA 123
Cdd:PLN02179    50 WGKLNPqwkVCSTGKyQSPI----DLTDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD-------------A 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  124 SKITFHWG-----KCNVSSEgSEHSLEGQKFPLEMQVYCFDAdrfssfeeavkgKGRLRALSILFEVGvEENLDYKAIID 198
Cdd:PLN02179   111 GKITIHQTdyklvQCHWHSP-SEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLG-EPDEFLTKLLN 176
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1359090889  199 GTESVsrfGKQ----AALDPFVLQNllpnSTDKYYIYNGSLTSPPCTDTVEWIVFKDTV 253
Cdd:PLN02179   177 GIKGV---GKKeinlGIVDPRDIRF----ETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
313-406 8.50e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 45.95  E-value: 8.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  313 SEPENVQADPENYTSLLVTWERPRvVYDAMIEKFAVLYQPLAGNDQakHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVC 392
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDW--KEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                           90
                   ....*....|....
gi 1359090889  393 SNGlYGKYSDQLIV 406
Cdd:cd00063     79 GGG-ESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
313-395 2.90e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.14  E-value: 2.90e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   313 SEPENVQADPENYTSLLVTWERPRvvyDAMIEKFAVLYQPLAGNDQAKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVC 392
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ...
gi 1359090889   393 SNG 395
Cdd:smart00060   79 GAG 81
 
Name Accession Description Interval E-value
alpha_CARP_receptor_like cd03122
Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...
45-298 9.01e-110

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: 348.58  E-value: 9.01e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   45 NQKNWGKKYPICNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWEKASLEnTFIHNTGKTVEINLTN---DYYLSGGLSEK 119
Cdd:cd03122      1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  120 VFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEeAVKGKGRLRALSILFEVGVEENLDYKAIIDG 199
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  200 TESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 279
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234
                          250
                   ....*....|....*....
gi 1359090889  280 YLQNNFREQQYKFSRQVFS 298
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253
Carb_anhydrase smart01057
Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...
38-295 3.81e-86

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: 281.51  E-value: 3.81e-86
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889    38 WSYTGALNQKNWGKKYP-ICNSPKQSPINIDEDLTQVNVNLKKLKFQgWEKASleNTFIHNTGKTVEINL-TNDYYLSGG 115
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPpFCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   116 LSEKVFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADrfSSFEEAVKGKGRLRALSILFEVGVEENLDYKA 195
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   196 IIDGTESVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSgyv 275
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230
                           250       260
                    ....*....|....*....|
gi 1359090889   276 mlmDYLQNNFREQQYKFSRQ 295
Cdd:smart01057  231 ---EPLVNNARPLQPLNGRV 247
Carb_anhydrase pfam00194
Eukaryotic-type carbonic anhydrase;
44-300 1.12e-82

Eukaryotic-type carbonic anhydrase;


Pssm-ID: 459707 [Multi-domain]  Cd Length: 252  Bit Score: 271.83  E-value: 1.12e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   44 LNQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTfIHNTGKTVEINLTNDY--YLSGGLSEKVF 121
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDpsTISGGPLATRY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  122 KASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRfSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTE 201
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  202 SVSRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 281
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233
                          250
                   ....*....|....*....
gi 1359090889  282 QNNFREQQYKFSRQVFSSY 300
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252
alpha_CA cd00326
Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...
60-297 5.46e-73

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: 242.96  E-value: 5.46e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   60 KQSPINIDEDLTQVNVNLKKLKFQGWEKASLEntfIHNTGKTVEINL-TNDYYLSGGLSEKVFKASKITFHWGKCNvsSE 138
Cdd:cd00326      3 RQSPINIVTSAVVYDPSLPPLNFDYYPTTSLT---LVNNGHTVQVNFdDDGGTLSGGGLPGRYKLVQFHFHWGSEN--SP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  139 GSEHSLEGQKFPLEMQVYCFDADRFSSfeEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVSRFGKQAALDPFVLQ 218
Cdd:cd00326     78 GSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLS 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1359090889  219 NLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQqsgyvmlMDYLQNNFREQQYKFSRQVF 297
Cdd:cd00326    156 DLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDRE-------GKPLVNNYRPVQPLNGRVVY 227
alpha_CA_VI_IX_XII_XIV cd03123
Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...
46-300 1.37e-59

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: 205.62  E-value: 1.37e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   46 QKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNTGKTVEINLTNDYYLSGGLSEKvFKASK 125
Cdd:cd03123      2 EDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHIRGGPGTE-YTAAQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  126 ITFHWGKCNvSSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVSR 205
Cdd:cd03123     81 LHLHWGGRG-SLSGSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  206 FGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLavfcevLTMQQSgyvmLMDY----L 281
Cdd:cd03123    160 KGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQL------ETLENT----LMDThnktL 229
                          250
                   ....*....|....*....
gi 1359090889  282 QNNFREQQYKFSRQVFSSY 300
Cdd:cd03123    230 QNNYRATQPLNGRVVEASF 248
alpha_CA_XII_XIV cd03126
Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...
46-300 1.92e-52

Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the membrane proteins CA XII and XIV.


Pssm-ID: 239400  Cd Length: 249  Bit Score: 185.04  E-value: 1.92e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   46 QKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNTGKTVEINLTNDYYLsGGLSEKvFKASK 125
Cdd:cd03126      2 ENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHI-GGLPFK-YTASQ 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  126 ITFHWGKCNvSSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGvEENLDYKAIIDGTESVSR 205
Cdd:cd03126     80 LHLHWGQRG-SPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVG-PFNPSYEKIFSHLHEVKY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  206 FGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLavfcevLTMQQSGYVMLMD---YLQ 282
Cdd:cd03126    158 KDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQL------LALETALYSTEEDesrEMV 231
                          250
                   ....*....|....*...
gi 1359090889  283 NNFREQQYKFSRQVFSSY 300
Cdd:cd03126    232 NNYRQVQPFNERLVFASF 249
alpha_CA_IV_XV_like cd03117
Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...
59-298 7.47e-50

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: 177.08  E-value: 7.47e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   59 PKQSPINIDEDLTQVNVNLKKLKFQGWEKASLeNTFIHNTGKTVEINLTNDYYLSGG-LSEKvFKASKITFHWGkcNVSS 137
Cdd:cd03117      2 KRQSPINIVTKKVQYDENLTPFTFTGYDDTTT-NWTITNNGHTVQVTLPDGAKISGGgLPGT-YKALQFHFHWG--SNGS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  138 EGSEHSLEGQKFPLEMQVYCFDADrFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVSRFGKQAALDPFVL 217
Cdd:cd03117     78 PGSEHTIDGERYPMELHIVHIKES-YNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  218 QNLLP-NSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylqNNFREQQYKFSRQV 296
Cdd:cd03117    157 RSLLPsVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNGQPMV----NNFRPVQPLNGRVV 232

                   ..
gi 1359090889  297 FS 298
Cdd:cd03117    233 YA 234
alpha_CA_VI cd03125
Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
45-300 1.82e-40

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: 150.32  E-value: 1.82e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   45 NQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNtGKTVEINLTNDYYLSGGLSeKVFKAS 124
Cdd:cd03125      1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNN-GHTVQIDLPPTMSITTGDG-TVYTAV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  125 KITFHWGKCNVSSEGSEHSLEGQKFPLEMQVYCFDADrFSSFEEAVKGKGRLRALSILFEVG-VEENLDYKAIIDGTESV 203
Cdd:cd03125     79 QMHFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLYKVGhYAENTYYSDFISKLAKI 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  204 SRFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQlavfceVLTMQQSgyvmLMDY--- 280
Cdd:cd03125    158 KYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQ------IVKLENT----LMDHhnk 227
                          250       260
                   ....*....|....*....|.
gi 1359090889  281 -LQNNFREQQYKFSRQVFSSY 300
Cdd:cd03125    228 tIRNDYRRTQPLNHRVVEANF 248
alpha_CA_IX cd03150
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...
45-300 2.73e-38

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: 144.33  E-value: 2.73e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   45 NQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQGWEKASLENTFIHNTGKTVEINLTNDYYLSGGLsEKVFKAS 124
Cdd:cd03150      1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALGP-GQEYRAL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  125 KITFHWGKCNVSseGSEHSLEGQKFPLEMQVYCFDAdRFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTESVS 204
Cdd:cd03150     80 QLHLHWGAAGRP--GSEHTVDGHRFPAEIHVVHLST-AFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEIS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  205 RFGKQAALDPFVLQNLLPNSTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSgyvmlmDYLQNN 284
Cdd:cd03150    157 EEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHD------SRLQLN 230
                          250
                   ....*....|....*.
gi 1359090889  285 FREQQYKFSRQVFSSY 300
Cdd:cd03150    231 FRATQPLNGRKIEASF 246
alpha_CA_I_II_III_XIII cd03119
Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...
38-300 2.16e-35

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: 136.03  E-value: 2.16e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   38 WSYTGALNQKNWGKKYPICNSPKQSPINIDEDLTQVNVNLKKLKFQgWEKASLENtfIHNTGKTVEINLTNDY---YLSG 114
Cdd:cd03119      5 WGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVS-YDPATAKT--ILNNGHSFNVEFDDTDdrsVLRG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  115 GLSEKVFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDAdRFSSFEEAVKGKGRLRALSILFEVGvEENLDYK 194
Cdd:cd03119     82 GPLTGSYRLRQFHFHWGSSD--DHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVG-EANPELQ 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  195 AIIDGTESVSRFGKQAALDPFVLQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGY 274
Cdd:cd03119    158 KVLDALDSIKTKGKQAPFTNFDPSCLLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEP 236
                          250       260
                   ....*....|....*....|....*.
gi 1359090889  275 VMLMdylQNNFREQQYKFSRQVFSSY 300
Cdd:cd03119    237 PCPM---VDNWRPPQPLKGRKVRASF 259
alpha_CA_V cd03118
Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...
60-300 1.87e-33

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: 129.96  E-value: 1.87e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   60 KQSPINIDEDLTQVNVNLKKLKFQgWEKASLEntFIHNTGKTVEINL---TNDYYLSGGLSEKVFKASKITFHWGKCNvs 136
Cdd:cd03118      3 RQSPINIQWRDSVYDPQLAPLRVS-YDPATCL--YIWNNGYSFQVEFddsTDKSGISGGPLENHYRLKQFHFHWGANN-- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  137 SEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGVE-ENLdyKAIIDGTESVSRFGKQAALDPF 215
Cdd:cd03118     78 EWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHhEGL--QKLVDALPEVRHKDTVVEFNPF 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  216 VLQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTmqqSGYVMLMDYLQNNFREQQYKFSRQ 295
Cdd:cd03118    156 DPSCLLPACRD-YWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLF---TSRGEEEKVMVNNFRPLQPLMNRK 231

                   ....*
gi 1359090889  296 VFSSY 300
Cdd:cd03118    232 VRSSF 236
Cah COG3338
Carbonic anhydrase [Inorganic ion transport and metabolism];
38-263 1.04e-32

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 442567 [Multi-domain]  Cd Length: 247  Bit Score: 128.08  E-value: 1.04e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   38 WSYTGALNQKNWGK---KYPICNS-PKQSPINIDedlTQVNVNLKKLKFQgWEKASLEntfIHNTGKTVEINLTNDYYLS 113
Cdd:COG3338     28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKFD-YKPTPLE---IVNNGHTIQVNVDPGSTLT 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  114 ggLSEKVFKASKITFHwgkcnvssEGSEHSLEGQKFPLEMQ-VYcfdadrfssfeeaVKGKGRLRALSILFEVGvEENLD 192
Cdd:COG3338    101 --VDGKRYELKQFHFH--------TPSEHTINGKSYPMEAHlVH-------------KDADGELAVVGVLFEEG-AENPA 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1359090889  193 YKAIID------GTESVSrfgkQAALDPfvlQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVF 263
Cdd:COG3338    157 LAKLWAnlpleaGEEVAL----DATIDL---NDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225
alpha_CA_prokaryotic_like cd03124
Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...
45-263 1.69e-29

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: 117.76  E-value: 1.69e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   45 NQKNWG---KKYPICNS-PKQSPINIDEDLTQVNVnLKKLKFQgWEKASLEntfIHNTGKTVEINLTNDyylSGGLS--E 118
Cdd:cd03124      1 GPEHWGnldPEFALCATgKNQSPIDITTKAVVSDK-LPPLNYN-YKPTSAT---LVNNGHTIQVNFEGN---GGTLTidG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  119 KVFKASKITFHwgkcnvssEGSEHSLEGQKFPLEMQ-VYcfdadrfssfeeaVKGKGRLRALSILFEVGvEENLDYKAII 197
Cdd:cd03124     73 ETYQLLQFHFH--------SPSEHLINGKRYPLEAHlVH-------------KSKDGQLAVVAVLFEEG-KENPFLKKIL 130
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1359090889  198 DGTESvsRFGKQAALDPFV-LQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVF 263
Cdd:cd03124    131 DNMPK--KEGTEVNLPAILdPNELLPESRS-YYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKF 194
alpha_CA_VII cd03149
Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...
60-300 6.39e-29

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: 116.86  E-value: 6.39e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   60 KQSPINIDEDLTQVNVNLKKLKFQGWEKASLEntfIHNTGKTVEINLtNDY----YLSGGLSEKVFKASKITFHWGKCNv 135
Cdd:cd03149      3 RQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLS---ISNNGHSVMVEF-DDSddktVITGGPLENPYRLKQFHFHWGAKH- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  136 sSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGvEENLDYKAIIDGTESVSRFGKQAALDPF 215
Cdd:cd03149     78 -GSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETG-DEHPGLNRLTDALYMVRFKGTKAQFLDF 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  216 VLQNLLPNSTDkYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylQNNFREQQYKFSRQ 295
Cdd:cd03149    156 NPKCLLPKSLD-YWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHM---VNNFRPPQPLKGRT 231

                   ....*
gi 1359090889  296 VFSSY 300
Cdd:cd03149    232 VRASF 236
alpha_CARP_X_XI_like cd03121
Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...
49-296 1.70e-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: 115.97  E-value: 1.70e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   49 WGKKYP---ICNSPK-QSPINIDEDLTQVNVNLKKLKFQGWEKASLEntfIHNTGKTVEINLTNDY--YLSGGLSEKVFK 122
Cdd:cd03121      5 WGLVNSawnLCSKGRrQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGT---FYNTGRHVSFRPDKDPvvNISGGPLSYRYR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  123 ASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGVEENLDYKAIIDGTES 202
Cdd:cd03121     82 LEEIRLHFGRED--EQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRDTI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  203 VS-RFGKQAA-LDPFVLQNLLPNsTDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAvfcEVLTMQQSGYVMLMDY 280
Cdd:cd03121    160 TSiRYKGDAYfLQDLSIELLLPE-TDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMH---SLRLLSQNSPSQEKAP 235
                          250
                   ....*....|....*.
gi 1359090889  281 LQNNFREQQYKFSRQV 296
Cdd:cd03121    236 MSPNFRPVQPLNNRPV 251
alpha_CARP_VIII cd03120
Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...
49-289 6.80e-28

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: 114.57  E-value: 6.80e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   49 WGKKYPICNSPKQSPINI-------DEDLTQVNVNLKKLKFQGWEkaslentfIHNTGKTVEINLTNDYYLSGGL--SEK 119
Cdd:cd03120      4 WGLLFPEANGEYQSPINLnsrearyDPSLLEVRLSPNYVVCRDCE--------VINDGHTIQIILKSKSVLSGGPlpQGH 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  120 VFKASKITFHWGKCNvsSEGSEHSLEGQKFPLEMQVYCFDADRFSSFEEAVKGKGRLRALSILFEVGvEENLDYKAIIDG 199
Cdd:cd03120     76 EFELAEVRFHWGREN--QRGSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIG-KEHVGLKAVTEI 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  200 TESVSRFGKQAALDPFVLQNLLPNSTDK-YYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVFCEvLTMQQSGYVMLM 278
Cdd:cd03120    153 LQDIQYKGKSKTIPCFNPNTLLPDPLLRdYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRR-LRTHVKGAELVE 231
                          250
                   ....*....|....
gi 1359090889  279 --DY-LQNNFREQQ 289
Cdd:cd03120    232 gcDGlLGDNFRPTQ 245
fn3 pfam00041
Fibronectin type III domain;
313-401 2.00e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.88  E-value: 2.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  313 SEPENVQADPENYTSLLVTWERPRVVyDAMIEKFAVLYQPLaGNDQAKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAVC 392
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDG-NGPITGYEVEYRPK-NSGEPWNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77

                   ....*....
gi 1359090889  393 SNGlYGKYS 401
Cdd:pfam00041   78 GGG-EGPPS 85
PLN02179 PLN02179
carbonic anhydrase
49-253 8.95e-09

carbonic anhydrase


Pssm-ID: 177835  Cd Length: 235  Bit Score: 57.68  E-value: 8.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   49 WGKKYP---ICNSPK-QSPInideDLTQVNVNLkkLKFQGWEKA-SLENTFIHNTGKTVEINLTNDyylsgglsekvfkA 123
Cdd:PLN02179    50 WGKLNPqwkVCSTGKyQSPI----DLTDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD-------------A 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  124 SKITFHWG-----KCNVSSEgSEHSLEGQKFPLEMQVYCFDAdrfssfeeavkgKGRLRALSILFEVGvEENLDYKAIID 198
Cdd:PLN02179   111 GKITIHQTdyklvQCHWHSP-SEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLG-EPDEFLTKLLN 176
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1359090889  199 GTESVsrfGKQ----AALDPFVLQNllpnSTDKYYIYNGSLTSPPCTDTVEWIVFKDTV 253
Cdd:PLN02179   177 GIKGV---GKKeinlGIVDPRDIRF----ETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
313-406 8.50e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 45.95  E-value: 8.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889  313 SEPENVQADPENYTSLLVTWERPRvVYDAMIEKFAVLYQPLAGNDQakHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVC 392
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDW--KEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78
                           90
                   ....*....|....
gi 1359090889  393 SNGlYGKYSDQLIV 406
Cdd:cd00063     79 GGG-ESPPSESVTV 91
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
313-395 2.90e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 44.14  E-value: 2.90e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359090889   313 SEPENVQADPENYTSLLVTWERPRvvyDAMIEKFAVLYQPLAGNDQAKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAVC 392
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

                    ...
gi 1359090889   393 SNG 395
Cdd:smart00060   79 GAG 81
PLN02202 PLN02202
carbonate dehydratase
225-263 1.71e-03

carbonate dehydratase


Pssm-ID: 177853 [Multi-domain]  Cd Length: 284  Bit Score: 42.35  E-value: 1.71e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1359090889  225 TDKYYIYNGSLTSPPCTDTVEWIVFKDTVSISESQLAVF 263
Cdd:PLN02202   201 TRKYFRYIGSLTTPPCSENVSWTILGKVRSMSKEQVELL 239
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH