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Conserved domains on  [gi|8569250|pdb|1EKJ|A]
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Chain A, BETA-CARBONIC ANHYDRASE

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03014 super family cl28979
carbonic anhydrase
2-221 4.58e-124

carbonic anhydrase


The actual alignment was detected with superfamily member PLN03014:

Pssm-ID: 178588 [Multi-domain]  Cd Length: 347  Bit Score: 355.20  E-value: 4.58e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A         2 TSSSDGIPKSEASERIKTGFLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVP 81
Cdd:PLN03014 117 TGTSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVP 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A        82 PYDQAKYAGTGAAIEYAVLHLKVSNIVVIGHSACGGIKGLLSFPFDGTYSTDFIEEWVKIGLPAKAKVKAQHGDAPFAEL 161
Cdd:PLN03014 197 PFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFPLDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQ 276
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       162 CTHCEKEAVNASLGNLLTYPFVREGLVNKTLALKGGYYDFVKGSFELWGLEFGLSSTFSV 221
Cdd:PLN03014 277 CGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGAFELWGLEFGLSETSSV 336
 
Name Accession Description Interval E-value
PLN03014 PLN03014
carbonic anhydrase
2-221 4.58e-124

carbonic anhydrase


Pssm-ID: 178588 [Multi-domain]  Cd Length: 347  Bit Score: 355.20  E-value: 4.58e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A         2 TSSSDGIPKSEASERIKTGFLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVP 81
Cdd:PLN03014 117 TGTSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVP 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A        82 PYDQAKYAGTGAAIEYAVLHLKVSNIVVIGHSACGGIKGLLSFPFDGTYSTDFIEEWVKIGLPAKAKVKAQHGDAPFAEL 161
Cdd:PLN03014 197 PFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFPLDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQ 276
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       162 CTHCEKEAVNASLGNLLTYPFVREGLVNKTLALKGGYYDFVKGSFELWGLEFGLSSTFSV 221
Cdd:PLN03014 277 CGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGAFELWGLEFGLSETSSV 336
beta_CA_cladeB cd00884
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
20-209 5.22e-105

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 238449  Cd Length: 190  Bit Score: 300.61  E-value: 5.22e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       20 GFLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDQ-AKYAGTGAAIEYA 98
Cdd:cd00884   1 GFRRFRKEYFPEERELFEKLAKGQSPKALFIACSDSRVVPALITQTQPGELFVVRNVGNLVPPYEPdGGFHGTSAAIEYA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       99 VLHLKVSNIVVIGHSACGGIKGLLSFPfDGTYSTDFIEEWVKIGLPAKAKVKAQHGDAPFAELCTHCEKEAVNASLGNLL 178
Cdd:cd00884  81 VAVLKVEHIVVCGHSDCGGIRALLSPE-DLLDKLPFIGKWLRIAEPAKEVVLAELSHADFDDQLRALEKENVLLSLENLL 159
                       170       180       190
                ....*....|....*....|....*....|.
1EKJ_A      179 TYPFVREGLVNKTLALKGGYYDFVKGSFELW 209
Cdd:cd00884 160 TYPFVRERLEAGTLSLHGWYYDIETGELYAY 190
CynT COG0288
Carbonic anhydrase [Inorganic ion transport and metabolism];
12-201 2.93e-68

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 440057  Cd Length: 204  Bit Score: 208.09  E-value: 2.93e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       12 EASERIKTGFLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDQakyaGT 91
Cdd:COG0288   2 EALKRLLEGNRRFVAGKFPQDPERFEELAKGQHPFALVIGCSDSRVPPELIFDQGPGDLFVVRNAGNVVPPYDP----GV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       92 GAAIEYAVLHLKVSNIVVIGHSACGGIKGLLSFPFDGtySTDFIEEWVKIGLPAKAKVKAQHGDAPFAELCTHCEKEAVN 171
Cdd:COG0288  78 LASIEYAVEVLGVKLIVVLGHSGCGAVKAALDGLELE--ELGLIGNWLRHIRPAVERVRAELPAADGEERLDRLVELNVR 155
                       170       180       190
                ....*....|....*....|....*....|
1EKJ_A      172 ASLGNLLTYPFVREGLVNKTLALKGGYYDF 201
Cdd:COG0288 156 EQVENLRTSPIVREAVAAGKLKVHGWVYDL 185
Pro_CA pfam00484
Carbonic anhydrase; This family includes carbonic anhydrases as well as a family of ...
48-204 3.50e-59

Carbonic anhydrase; This family includes carbonic anhydrases as well as a family of non-functional homologs related to YbcF.


Pssm-ID: 459828  Cd Length: 156  Bit Score: 183.09  E-value: 3.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A         48 MVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDQakyaGTGAAIEYAVLHLKVSNIVVIGHSACGGIKGLLSfPFD 127
Cdd:pfam00484   2 LIIGCSDSRVPPELIFDTGPGDLFVVRNAGNLVPPYDL----NVLASIEYAVEVLKVKHIVVCGHSGCGAVKAALD-AAG 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1EKJ_A        128 GTYSTDFIEEWVKIGLPAKAKVKAQHGDA-PFAELCTHCEKEAVNASLGNLLTYPFVREGLVNKTLALKGGYYDFVKG 204
Cdd:pfam00484  77 PAELPGFIDNWLRHIRPAVERVAEELESLdDPEERDDALEELNVREQVENLRTFPIVREAVAKGKLKIHGWVYDLETG 154
Pro_CA smart00947
Carbonic anhydrase; Carbonic anhydrases (CA) are zinc metalloenzymes which catalyze the ...
40-209 1.19e-55

Carbonic anhydrase; Carbonic anhydrases (CA) are zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. In Escherichia coli, CA (gene cynT) is involved in recycling carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (gene cynS). By this action, it prevents the depletion of cellular bicarbonate. In photosynthetic bacteria and plant chloroplast, CA is essential to inorganic carbon fixation. Prokaryotic and plant chloroplast CA are structurally and evolutionary related and form a family distinct from the one which groups the many different forms of eukaryotic CA's.


Pssm-ID: 214929 [Multi-domain]  Cd Length: 154  Bit Score: 174.23  E-value: 1.19e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A          40 AKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDqakyAGTGAAIEYAVLHLKVSNIVVIGHSACGGIK 119
Cdd:smart00947   1 AKGQHPKALIIGCSDSRVPPELIFGLGPGDLFVIRNAGNIVPPYD----DGVLASLEYAVEVLGVKEIVVCGHTDCGAVK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A         120 GLLSfPFDGtystdFIEEWVKIGLPAKAKVKAQHGDapfaelCTHCEKEAVNASLGNLLTYPFVREGLVNKTLALKGGYY 199
Cdd:smart00947  77 AALD-DEPG-----LIDNWLERIRPARERALEELGD------VDALEELNVRDQVENLRTSPAIREAVAKGKLKVHGWVY 144
                          170
                   ....*....|
1EKJ_A         200 DFVKGSFELW 209
Cdd:smart00947 145 DIETGKLEVL 154
 
Name Accession Description Interval E-value
PLN03014 PLN03014
carbonic anhydrase
2-221 4.58e-124

carbonic anhydrase


Pssm-ID: 178588 [Multi-domain]  Cd Length: 347  Bit Score: 355.20  E-value: 4.58e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A         2 TSSSDGIPKSEASERIKTGFLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVP 81
Cdd:PLN03014 117 TGTSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVP 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A        82 PYDQAKYAGTGAAIEYAVLHLKVSNIVVIGHSACGGIKGLLSFPFDGTYSTDFIEEWVKIGLPAKAKVKAQHGDAPFAEL 161
Cdd:PLN03014 197 PFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFPLDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQ 276
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       162 CTHCEKEAVNASLGNLLTYPFVREGLVNKTLALKGGYYDFVKGSFELWGLEFGLSSTFSV 221
Cdd:PLN03014 277 CGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGAFELWGLEFGLSETSSV 336
PLN00416 PLN00416
carbonate dehydratase
10-220 2.28e-119

carbonate dehydratase


Pssm-ID: 177809  Cd Length: 258  Bit Score: 339.70  E-value: 2.28e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A        10 KSEASERIKTGFLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDQAKYA 89
Cdd:PLN00416  45 NSDAIERIKTGFTQFKTEKYLKNSTLFNHLAKTQTPKFLVFACSDSRVCPSHILNFQPGEAFVVRNIANMVPPFDQKRHS 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A        90 GTGAAIEYAVLHLKVSNIVVIGHSACGGIKGLLSFPFDGTYS-TDFIEEWVKIGLPAKAKVKAQHGDAPFAELCTHCEKE 168
Cdd:PLN00416 125 GVGAAVEYAVVHLKVENILVIGHSCCGGIKGLMSIEDDAAPTqSDFIENWVKIGASARNKIKEEHKDLSYDDQCNKCEKE 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
1EKJ_A       169 AVNASLGNLLTYPFVREGLVNKTLALKGGYYDFVKGSFELWGLEFGLSSTFS 220
Cdd:PLN00416 205 AVNVSLGNLLSYPFVRAEVVKNTLAIRGGHYNFVKGTFDLWELDFKTTPAFA 256
beta_CA_cladeB cd00884
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
20-209 5.22e-105

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 238449  Cd Length: 190  Bit Score: 300.61  E-value: 5.22e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       20 GFLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDQ-AKYAGTGAAIEYA 98
Cdd:cd00884   1 GFRRFRKEYFPEERELFEKLAKGQSPKALFIACSDSRVVPALITQTQPGELFVVRNVGNLVPPYEPdGGFHGTSAAIEYA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       99 VLHLKVSNIVVIGHSACGGIKGLLSFPfDGTYSTDFIEEWVKIGLPAKAKVKAQHGDAPFAELCTHCEKEAVNASLGNLL 178
Cdd:cd00884  81 VAVLKVEHIVVCGHSDCGGIRALLSPE-DLLDKLPFIGKWLRIAEPAKEVVLAELSHADFDDQLRALEKENVLLSLENLL 159
                       170       180       190
                ....*....|....*....|....*....|.
1EKJ_A      179 TYPFVREGLVNKTLALKGGYYDFVKGSFELW 209
Cdd:cd00884 160 TYPFVRERLEAGTLSLHGWYYDIETGELYAY 190
PLN03019 PLN03019
carbonic anhydrase
3-221 2.18e-104

carbonic anhydrase


Pssm-ID: 166660  Cd Length: 330  Bit Score: 304.38  E-value: 2.18e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A         3 SSSDGiPKSEASERIKTGFLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPP 82
Cdd:PLN03019 114 SSSDS-KSFDPVERIKEGFVTFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFHPGDAFVVRNIANMVPP 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A        83 YDQAKYAGTGAAIEYAVLHLKVSNIVVIGHSACGGIKGLLSFPFDGTYSTDFIEEWVKIGLPAKAKVKAQHGDAPFAELC 162
Cdd:PLN03019 193 FDKVKYAGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFPLDGNNSTDFIEDWVKICLPAKSKVLAESESSAFEDQC 272
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
1EKJ_A       163 THCEKeAVNASLGNLLTYPFVREGLVNKTLALKGGYYDFVKGSFELWGLEFGLSSTFSV 221
Cdd:PLN03019 273 GRCER-AVNVSLANLLTYPFVREGVVKGTLALKGGYYDFVNGSFELWELQFGISPVHSI 330
CynT COG0288
Carbonic anhydrase [Inorganic ion transport and metabolism];
12-201 2.93e-68

Carbonic anhydrase [Inorganic ion transport and metabolism];


Pssm-ID: 440057  Cd Length: 204  Bit Score: 208.09  E-value: 2.93e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       12 EASERIKTGFLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDQakyaGT 91
Cdd:COG0288   2 EALKRLLEGNRRFVAGKFPQDPERFEELAKGQHPFALVIGCSDSRVPPELIFDQGPGDLFVVRNAGNVVPPYDP----GV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       92 GAAIEYAVLHLKVSNIVVIGHSACGGIKGLLSFPFDGtySTDFIEEWVKIGLPAKAKVKAQHGDAPFAELCTHCEKEAVN 171
Cdd:COG0288  78 LASIEYAVEVLGVKLIVVLGHSGCGAVKAALDGLELE--ELGLIGNWLRHIRPAVERVRAELPAADGEERLDRLVELNVR 155
                       170       180       190
                ....*....|....*....|....*....|
1EKJ_A      172 ASLGNLLTYPFVREGLVNKTLALKGGYYDF 201
Cdd:COG0288 156 EQVENLRTSPIVREAVAAGKLKVHGWVYDL 185
PLN03006 PLN03006
carbonate dehydratase
11-216 7.53e-63

carbonate dehydratase


Pssm-ID: 178583  Cd Length: 301  Bit Score: 197.66  E-value: 7.53e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A        11 SEASERIKTGFLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDQAKyAG 90
Cdd:PLN03006  79 TDVFDDMKQRFLAFKKLKYMDDFEHYKNLADAQAPKFLVIACADSRVCPSAVLGFQPGDAFTVRNIANLVPPYESGP-TE 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A        91 TGAAIEYAVLHLKVSNIVVIGHSACGGIKGLLSFPFDGTySTDFIEEWVKIGLPAKAKVKAQHGDAPFAELCTHCEKEAV 170
Cdd:PLN03006 158 TKAALEFSVNTLNVENILVIGHSRCGGIQALMKMEDEGD-SRSFIHNWVVVGKKAKESTKAVASNLHFDHQCQHCEKASI 236
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
1EKJ_A       171 NASLGNLLTYPFVREGLVNKTLALKGGYYDFVKGSFELWGLEFGLS 216
Cdd:PLN03006 237 NHSLERLLGYPWIEEKVRQGSLSLHGGYYNFVDCTFEKWTVDYAAS 282
Pro_CA pfam00484
Carbonic anhydrase; This family includes carbonic anhydrases as well as a family of ...
48-204 3.50e-59

Carbonic anhydrase; This family includes carbonic anhydrases as well as a family of non-functional homologs related to YbcF.


Pssm-ID: 459828  Cd Length: 156  Bit Score: 183.09  E-value: 3.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A         48 MVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDQakyaGTGAAIEYAVLHLKVSNIVVIGHSACGGIKGLLSfPFD 127
Cdd:pfam00484   2 LIIGCSDSRVPPELIFDTGPGDLFVVRNAGNLVPPYDL----NVLASIEYAVEVLKVKHIVVCGHSGCGAVKAALD-AAG 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1EKJ_A        128 GTYSTDFIEEWVKIGLPAKAKVKAQHGDA-PFAELCTHCEKEAVNASLGNLLTYPFVREGLVNKTLALKGGYYDFVKG 204
Cdd:pfam00484  77 PAELPGFIDNWLRHIRPAVERVAEELESLdDPEERDDALEELNVREQVENLRTFPIVREAVAKGKLKIHGWVYDLETG 154
Pro_CA smart00947
Carbonic anhydrase; Carbonic anhydrases (CA) are zinc metalloenzymes which catalyze the ...
40-209 1.19e-55

Carbonic anhydrase; Carbonic anhydrases (CA) are zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. In Escherichia coli, CA (gene cynT) is involved in recycling carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (gene cynS). By this action, it prevents the depletion of cellular bicarbonate. In photosynthetic bacteria and plant chloroplast, CA is essential to inorganic carbon fixation. Prokaryotic and plant chloroplast CA are structurally and evolutionary related and form a family distinct from the one which groups the many different forms of eukaryotic CA's.


Pssm-ID: 214929 [Multi-domain]  Cd Length: 154  Bit Score: 174.23  E-value: 1.19e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A          40 AKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDqakyAGTGAAIEYAVLHLKVSNIVVIGHSACGGIK 119
Cdd:smart00947   1 AKGQHPKALIIGCSDSRVPPELIFGLGPGDLFVIRNAGNIVPPYD----DGVLASLEYAVEVLGVKEIVVCGHTDCGAVK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A         120 GLLSfPFDGtystdFIEEWVKIGLPAKAKVKAQHGDapfaelCTHCEKEAVNASLGNLLTYPFVREGLVNKTLALKGGYY 199
Cdd:smart00947  77 AALD-DEPG-----LIDNWLERIRPARERALEELGD------VDALEELNVRDQVENLRTSPAIREAVAKGKLKVHGWVY 144
                          170
                   ....*....|
1EKJ_A         200 DFVKGSFELW 209
Cdd:smart00947 145 DIETGKLEVL 154
PLN02154 PLN02154
carbonic anhydrase
17-211 6.66e-51

carbonic anhydrase


Pssm-ID: 215111  Cd Length: 290  Bit Score: 166.85  E-value: 6.66e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A        17 IKTGFLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYdQAKYAGTGAAIE 96
Cdd:PLN02154  79 MRHRFLKFKRQKYLPEIEKFKALAIAQSPKVMVIGCADSRVCPSYVLGFQPGEAFTIRNVANLVTPV-QNGPTETNSALE 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A        97 YAVLHLKVSNIVVIGHSACGGIKGLLSFPFDGTYSTDFIEEWVKIGLPAKAKVKAQHGDAPFAELCTHCEKEAVNASLGN 176
Cdd:PLN02154 158 FAVTTLQVENIIVMGHSNCGGIAALMSHQNHQGQHSSLVERWVMNGKAAKLRTQLASSHLSFDEQCRNCEKESIKDSVMN 237
                        170       180       190
                 ....*....|....*....|....*....|....*
1EKJ_A       177 LLTYPFVREGLVNKTLALKGGYYDFVKGSFELWGL 211
Cdd:PLN02154 238 LITYSWIRDRVKRGEVKIHGCYYNLSDCSLEKWRL 272
beta_CA cd00382
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
43-209 5.79e-46

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 238224 [Multi-domain]  Cd Length: 119  Bit Score: 148.42  E-value: 5.79e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       43 QSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDqakyAGTGAAIEYAVLHLKVSNIVVIGHSACGGIKGll 122
Cdd:cd00382   1 QKPKALIIGCSDSRVPPELIFGLGPGDLFVVRNAGNLVPPYD----LDVLASLEYAVEVLGVKHIIVCGHTDCGAVKA-- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A      123 sfpfdgtystdfieewvkiglpakakvkaqhgdapfaelcthCEKEAVNASLGNLLTYPFVREGLVNKTLALKGGYYDFV 202
Cdd:cd00382  75 ------------------------------------------LVEENVREQVENLRSHPLIQEAVAPGELKVHGWVYDIE 112

                ....*..
1EKJ_A      203 KGSFELW 209
Cdd:cd00382 113 TGKLEVL 119
beta_CA_cladeA cd00883
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
26-119 2.18e-33

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 238448  Cd Length: 182  Bit Score: 118.44  E-value: 2.18e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       26 KEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDqakyAGTGAAIEYAVLHLKVS 105
Cdd:cd00883   6 EEKKAKDPDFFPRLAKGQTPEYLWIGCSDSRVPENTILGLLPGEVFVHRNIANLVSPTD----LNCLSVLQYAVDVLKVK 81
                        90
                ....*....|....
1EKJ_A      106 NIVVIGHSACGGIK 119
Cdd:cd00883  82 HIIVCGHYGCGGVK 95
beta_CA_cladeC cd03378
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
12-120 2.07e-23

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 239473 [Multi-domain]  Cd Length: 154  Bit Score: 91.43  E-value: 2.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       12 EASERIKTG---FLHFKKEKYDKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPydqaky 88
Cdd:cd03378   3 EALERLKEGnkrFVSGKPLHPDQDLARRRELAKGQKPFAVILSCSDSRVPPEIIFDQGLGDLFVVRVAGNIVDD------ 76
                        90       100       110
                ....*....|....*....|....*....|..
1EKJ_A       89 aGTGAAIEYAVLHLKVSNIVVIGHSACGGIKG 120
Cdd:cd03378  77 -DVLGSLEYAVEVLGVPLVVVLGHESCGAVAA 107
PRK10437 PRK10437
carbonic anhydrase; Provisional
30-125 3.59e-18

carbonic anhydrase; Provisional


Pssm-ID: 182460  Cd Length: 220  Bit Score: 79.59  E-value: 3.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A        30 DKNPALYGELAKGQSPPFMVFACSDSRVCPSHVLDFQPGEAFVVRNVANLVPPYDqakyAGTGAAIEYAVLHLKVSNIVV 109
Cdd:PRK10437  20 EEDPGFFEKLAQAQKPRFLWIGCSDSRVPAERLTGLEPGELFVHRNVANLVIHTD----LNCLSVVQYAVDVLEVEHIII 95
                         90
                 ....*....|....*.
1EKJ_A       110 IGHSACGGIKGLLSFP 125
Cdd:PRK10437  96 CGHYGCGGVQAAVENP 111
beta_CA_cladeD cd03379
Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of ...
49-205 9.01e-08

Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.


Pssm-ID: 239474  Cd Length: 142  Bit Score: 49.56  E-value: 9.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A       49 VFACSDSRVCPSHVLDFQPGEAFVVRNVANLVppydqakyagTGAAIEYAVL---HLKVSNIVVIGHSACGGIKgllsfp 125
Cdd:cd03379   7 IVTCMDARLDPEKALGLKLGDAKVIRNAGGRV----------TDDAIRSLVVsvyLLGTREIIVIHHTDCGMLT------ 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A      126 fdgtystdFIEEWVKIGLPAKAKVKAQHGDAPFAELCT-HCEKEAVNASLGNLLTYPFVReglvnKTLALKGGYYDFVKG 204
Cdd:cd03379  71 --------FTDEELKEKMKERGIAEAYGGIDKEFWFLGfDDLEESVREDVERIRNHPLIP-----DDVPVHGYVYDVKTG 137

                .
1EKJ_A      205 S 205
Cdd:cd03379 138 K 138
PRK15219 PRK15219
carbonic anhydrase; Provisional
1-120 1.96e-06

carbonic anhydrase; Provisional


Pssm-ID: 237927 [Multi-domain]  Cd Length: 245  Bit Score: 47.13  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EKJ_A         1 TTSSSDGIPKSEASERIKTGFLHFKKEKYDKNPALYGEL--AKGQSPPFMVFACSDSRVCPSHVLDFQPGEAF---VVRN 75
Cdd:PRK15219  44 TKEERDKMTPDQIIESLKQGNKRFRSGKPAQHDYLAQKRasAAGQYPAAVILSCIDSRAPAEIILDTGIGETFnsrVAGN 123
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
1EKJ_A        76 VAN--LVppydqakyagtgAAIEYA--VLHLKVsnIVVIGHSACGGIKG 120
Cdd:PRK15219 124 ISNddLL------------GSMEFAcaVAGAKV--VLVMGHTACGAVKG 158
 
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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