NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1906202172|ref|WP_188975180|]
View 

cytochrome c oxidase subunit II [Haloarcula sebkhae]

Protein Classification

cupredoxin domain-containing protein; multicopper oxidase( domain architecture ID 10195319)

cupredoxin domain-containing protein may contain a type I copper center and be involved in inter-molecular electron transfer reactions; multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which may contain three cupredoxin domains that include one mononuclear and one trinuclear copper center; similar to Pleurotus ostreatus laccase-2 that may be involved in lignin degradation and detoxification of lignin-derived products

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-230 2.93e-87

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


:

Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 255.46  E-value: 2.93e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  93 SISAIIVVSLIAWTYSQLLYIEQGPDPAQEEALEIDVEGYRFGWDFVYPNG-HTTNTLRVPQDRVVRLQVTSTDVFHNFG 171
Cdd:cd13918     1 GLSAIIVISLIVWTYGMLLYVEDPPDEADEDALEVEVEGFQFGWQFEYPNGvTTGNTLRVPADTPIALRVTSTDVFHTFG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1906202172 172 IPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEYEEWY 230
Cdd:cd13918    81 IPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
 
Name Accession Description Interval E-value
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-230 2.93e-87

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 255.46  E-value: 2.93e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  93 SISAIIVVSLIAWTYSQLLYIEQGPDPAQEEALEIDVEGYRFGWDFVYPNG-HTTNTLRVPQDRVVRLQVTSTDVFHNFG 171
Cdd:cd13918     1 GLSAIIVISLIVWTYGMLLYVEDPPDEADEDALEVEVEGFQFGWQFEYPNGvTTGNTLRVPADTPIALRVTSTDVFHTFG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1906202172 172 IPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEYEEWY 230
Cdd:cd13918    81 IPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 22-231 7.76e-81

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 241.52  E-value: 7.76e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  22 APSAVFDQIFEVFLLL---GTAVGVVVVAYTMYHALKYRDDGGEtdpyadkverpemgEMPTGGTGGRKVFYSFSIS-AI 97
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVlavSTLISLLVAALLAYVVWKFRRKGDE--------------EKPSQIHGNRRLEYVWTVIpLI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  98 IVVSLIAWTYSQLLYIEQGPDPaqeEALEIDVEGYRFGWDFVYPNG--HTTNTLRVPQDRVVRLQVTSTDVFHNFGIPAL 175
Cdd:TIGR02866  67 IVVGLFAATAKGLLYLERPIPK---DALKVKVTGYQWWWDFEYPESgfTTVNELVLPAGTPVELQVTSKDVIHSFWVPEL 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1906202172 176 RVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEYEEWYA 231
Cdd:TIGR02866 144 GGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-239 1.51e-62

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 195.82  E-value: 1.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172   2 AVSLITYATVVFPMHGGDVrapSAVFDQIFEVFLLLGTAVGVVVVAYTMYHALKYRDDGGETDP----YADKVErpemge 77
Cdd:COG1622    10 LLALLLSGQLSLPDPAGPI---AEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPaqfhHNTKLE------ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  78 mpTGGTGgrkvfysfsISAIIVVSLIAWTYSQLLYIEQGPDPAqeeaLEIDVEGYRFGWDFVYPNGH--TTNTLRVPQDR 155
Cdd:COG1622    81 --IVWTV---------IPIIIVIVLAVPTLRVLHALDDAPEDP----LTVEVTGYQWKWLFRYPDQGiaTVNELVLPVGR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 156 VVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEYEEWYAETNG 235
Cdd:COG1622   146 PVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKA 225


                  ....
gi 1906202172 236 TAAS 239
Cdd:COG1622   226 SAAT 229
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
125-214 7.58e-21

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 84.77  E-value: 7.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 125 LEIDVEGYRFGWDFVYPN------------------GH-----TTNTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDA 181
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDfgdlefdsymiptedleeGQlrlleVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1906202172 182 VPGQYTSAWFTANETGTYTAKCYELCGSGHSLM 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 94-229 4.17e-19

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 83.26  E-value: 4.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  94 ISAIIVVsLIAWTYSQLLYIEqgpDPAQEEALEIDVEGYRFGWDFVYPNGH-------------------------TTNT 148
Cdd:MTH00023   77 IPAVILV-FIALPSLKLLYLM---DEVVSPALTIKAIGHQWYWSYEYSDYEgetlefdsymvptsdlnsgdfrlleVDNR 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 149 LRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEYEE 228
Cdd:MTH00023  153 LVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIN 232


                  .
gi 1906202172 229 W 229
Cdd:MTH00023  233 W 233
 
Name Accession Description Interval E-value
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-230 2.93e-87

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 255.46  E-value: 2.93e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  93 SISAIIVVSLIAWTYSQLLYIEQGPDPAQEEALEIDVEGYRFGWDFVYPNG-HTTNTLRVPQDRVVRLQVTSTDVFHNFG 171
Cdd:cd13918     1 GLSAIIVISLIVWTYGMLLYVEDPPDEADEDALEVEVEGFQFGWQFEYPNGvTTGNTLRVPADTPIALRVTSTDVFHTFG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1906202172 172 IPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEYEEWY 230
Cdd:cd13918    81 IPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 22-231 7.76e-81

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 241.52  E-value: 7.76e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  22 APSAVFDQIFEVFLLL---GTAVGVVVVAYTMYHALKYRDDGGEtdpyadkverpemgEMPTGGTGGRKVFYSFSIS-AI 97
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVlavSTLISLLVAALLAYVVWKFRRKGDE--------------EKPSQIHGNRRLEYVWTVIpLI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  98 IVVSLIAWTYSQLLYIEQGPDPaqeEALEIDVEGYRFGWDFVYPNG--HTTNTLRVPQDRVVRLQVTSTDVFHNFGIPAL 175
Cdd:TIGR02866  67 IVVGLFAATAKGLLYLERPIPK---DALKVKVTGYQWWWDFEYPESgfTTVNELVLPAGTPVELQVTSKDVIHSFWVPEL 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1906202172 176 RVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEYEEWYA 231
Cdd:TIGR02866 144 GGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-239 1.51e-62

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 195.82  E-value: 1.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172   2 AVSLITYATVVFPMHGGDVrapSAVFDQIFEVFLLLGTAVGVVVVAYTMYHALKYRDDGGETDP----YADKVErpemge 77
Cdd:COG1622    10 LLALLLSGQLSLPDPAGPI---AEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPaqfhHNTKLE------ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  78 mpTGGTGgrkvfysfsISAIIVVSLIAWTYSQLLYIEQGPDPAqeeaLEIDVEGYRFGWDFVYPNGH--TTNTLRVPQDR 155
Cdd:COG1622    81 --IVWTV---------IPIIIVIVLAVPTLRVLHALDDAPEDP----LTVEVTGYQWKWLFRYPDQGiaTVNELVLPVGR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 156 VVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEYEEWYAETNG 235
Cdd:COG1622   146 PVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKA 225


                  ....
gi 1906202172 236 TAAS 239
Cdd:COG1622   226 SAAT 229
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 124-220 5.89e-42

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 138.92  E-value: 5.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 124 ALEIDVEGYRFGWDFVYPNGHTT-NTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAK 202
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKREiNELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLF 80

                          90
                  ....*....|....*...
gi 1906202172 203 CYELCGSGHSLMTTDVVV 220
Cdd:cd13915    81 CTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 124-221 7.89e-37

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 125.83  E-value: 7.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 124 ALEIDVEGYRFGWDFVYPNGH---------TTNTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTAN 194
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGGDgklgtdddvTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPT 80

                          90       100
                  ....*....|....*....|....*..
gi 1906202172 195 ETGTYTAKCYELCGSGHSLMTTDVVVM 221
Cdd:cd13919    81 REGEYEVRCAELCGLGHYRMRATVKVV 107
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 126-229 1.87e-36

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 125.21  E-value: 1.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 126 EIDVEGYRFGWDFVYP--NGHTTNTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKC 203
Cdd:cd13914     2 EIEVEAYQWGWEFSYPeaNVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYC 81

                          90       100
                  ....*....|....*....|....*.
gi 1906202172 204 YELCGSGHSLMTTDVVVMPQDEYEEW 229
Cdd:cd13914    82 AEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 125-219 8.72e-34

Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 117.78  E-value: 8.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 125 LEIDVEGYRFGWDFVYPNGHTTNTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCY 204
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTIICA 80

                          90
                  ....*....|....*
gi 1906202172 205 ELCGSGHSLMTTDVV 219
Cdd:cd13842    81 EYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 124-221 6.38e-31

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 110.40  E-value: 6.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 124 ALEIDVEGYRFGWDFVYPNGH-----TTNTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGT 198
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPgrgivTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGV 80

                          90       100
                  ....*....|....*....|...
gi 1906202172 199 YTAKCYELCGSGHSLMTTDVVVM 221
Cdd:cd04213    81 YRGQCAEFCGASHALMRFKVIAL 103
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 145-229 2.25e-26

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 99.57  E-value: 2.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 145 TTNTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQD 224
Cdd:cd13912    46 VDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLE 125


                  ....*
gi 1906202172 225 EYEEW 229
Cdd:cd13912   126 DFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
125-214 7.58e-21

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 84.77  E-value: 7.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 125 LEIDVEGYRFGWDFVYPN------------------GH-----TTNTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDA 181
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDfgdlefdsymiptedleeGQlrlleVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1906202172 182 VPGQYTSAWFTANETGTYTAKCYELCGSGHSLM 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 94-229 4.17e-19

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 83.26  E-value: 4.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  94 ISAIIVVsLIAWTYSQLLYIEqgpDPAQEEALEIDVEGYRFGWDFVYPNGH-------------------------TTNT 148
Cdd:MTH00023   77 IPAVILV-FIALPSLKLLYLM---DEVVSPALTIKAIGHQWYWSYEYSDYEgetlefdsymvptsdlnsgdfrlleVDNR 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 149 LRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEYEE 228
Cdd:MTH00023  153 LVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIN 232


                  .
gi 1906202172 229 W 229
Cdd:MTH00023  233 W 233
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 147-229 7.35e-19

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 82.29  E-value: 7.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 147 NTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00140  140 NRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDF 219


                  ...
gi 1906202172 227 EEW 229
Cdd:MTH00140  220 VKW 222
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 94-232 2.53e-18

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 80.90  E-value: 2.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  94 ISAIIVVsLIAWTYSQLLY-IEQGPDPAqeeaLEIDVEGYRFGWDFVYPNGHTT-----------------------NTL 149
Cdd:MTH00038   68 VPAFILI-FIALPSLQLLYlMDEVNNPF----LTIKAIGHQWYWSYEYTDYNDLefdsymvptsdlstglprllevdNRL 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 150 RVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEYEEW 229
Cdd:MTH00038  143 VLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENW 222


                  ...
gi 1906202172 230 YAE 232
Cdd:MTH00038  223 VSN 225
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 94-231 9.16e-18

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 79.44  E-value: 9.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  94 ISAIIVVsLIAWTYSQLLYIEqgpDPAQEEALEIDVEGYRFGWDFVYPN-GHTT------------------------NT 148
Cdd:MTH00051   70 IPAAILI-FIAFPSLKLLYLM---DEVIDPALTIKAIGHQWYWSYEYSDyGTDTiefdsymiptsdlnsgdlrllevdNR 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 149 LRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEYEE 228
Cdd:MTH00051  146 LIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYIN 225


                  ...
gi 1906202172 229 WYA 231
Cdd:MTH00051  226 WVA 228
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 92-229 1.17e-17

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 79.16  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  92 FSISAIIVVSLIAWTYSQLLYIEqgpDPAQEEALEIDVEGYRFGWDFVYPNGHT---------TNTLR------------ 150
Cdd:MTH00185   65 WTILPAIILIMIALPSLRILYLM---DEINDPHLTIKAMGHQWYWSYEYTDYEQlefdsymtpTQDLTpgqfrlletdhr 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 151 --VPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEYEE 228
Cdd:MTH00185  142 mvVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFEN 221


                  .
gi 1906202172 229 W 229
Cdd:MTH00185  222 W 222
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 145-220 2.76e-17

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 74.91  E-value: 2.76e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1906202172 145 TTNTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVV 220
Cdd:cd13913    23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIV 98
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 147-229 1.98e-16

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 75.91  E-value: 1.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 147 NTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00098  140 NRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYF 219


                  ...
gi 1906202172 227 EEW 229
Cdd:MTH00098  220 EKW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 147-229 2.64e-16

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 75.59  E-value: 2.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 147 NTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00076  140 NRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNF 219


                  ...
gi 1906202172 227 EEW 229
Cdd:MTH00076  220 LNW 222
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 141-229 2.94e-16

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 75.34  E-value: 2.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 141 PNGH-----TTNTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMT 215
Cdd:MTH00117  129 PNGHfrlleVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMP 208

                          90
                  ....*....|....
gi 1906202172 216 TDVVVMPQDEYEEW 229
Cdd:MTH00117  209 IVVESVPLKHFENW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 145-229 1.56e-15

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 73.59  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 145 TTNTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQD 224
Cdd:MTH00129  138 ADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLE 217


                  ....*
gi 1906202172 225 EYEEW 229
Cdd:MTH00129  218 HFENW 222
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 147-229 5.27e-15

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 71.94  E-value: 5.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 147 NTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00168  140 NRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETF 219


                  ...
gi 1906202172 227 EEW 229
Cdd:MTH00168  220 ENW 222
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 147-229 8.64e-15

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 71.29  E-value: 8.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 147 NTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00139  140 NRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFF 219


                  ...
gi 1906202172 227 EEW 229
Cdd:MTH00139  220 LEW 222
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 126-220 1.61e-14

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 67.41  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 126 EIDVEGYRFGWDFvypnghTTNTLRVPQdrVVRLQVTSTDVFHNFGI--PALRV--KTDAVPGQYTSAWFTANETGTYTA 201
Cdd:cd13916     2 VVAVTGHQWYWEL------SRTEIPAGK--PVEFRVTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFDKPGTYTI 73

                          90
                  ....*....|....*....
gi 1906202172 202 KCYELCGSGHSLMTTDVVV 220
Cdd:cd13916    74 LCLEYCGLAHHVMMAEFTV 92
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 145-214 8.41e-14

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 68.70  E-value: 8.41e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 145 TTNTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLM 214
Cdd:MTH00154  138 VDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFM 207
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 147-229 9.74e-14

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 68.34  E-value: 9.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 147 NTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00008  140 NRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSF 219


                  ...
gi 1906202172 227 EEW 229
Cdd:MTH00008  220 MKW 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 94-229 1.46e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 68.51  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  94 ISAIIVVsLIAWTYSQLLYI-EQGPDPAQeeaLEIDVEGYRFGWDFVYPNG-------------------------HTTN 147
Cdd:MTH00027   99 IPAFILI-LIAFPSLRLLYImDECGFSAN---ITIKVTGHQWYWSYSYEDYgekniefdsymiptadlefgdlrllEVDN 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 148 TLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEYE 227
Cdd:MTH00027  175 RLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYI 254


                  ..
gi 1906202172 228 EW 229
Cdd:MTH00027  255 DW 256
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 127-222 1.95e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 66.90  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 127 IDVEGYRFGWDFVYPNG------------HTTNTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTAN 194
Cdd:MTH00047   84 IKVIGHQWYWSYEYSFGgsydsfmtddifGVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPD 163

                          90       100
                  ....*....|....*....|....*....
gi 1906202172 195 ETGTYTAKCYELCGSGHSLMTTDV-VVMP 222
Cdd:MTH00047  164 RHGVFVGYCSELCGVGHSYMPIVIeVVDV 192
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 125-221 4.36e-13

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 63.72  E-value: 4.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 125 LEIDVEGYRFGWDFVYPNGH--TTNTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAK 202
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQGiaTVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80

                          90
                  ....*....|....*....
gi 1906202172 203 CYELCGSGHSLMTTDVVVM 221
Cdd:cd04212    81 SANYSGEGFSDMKFKVLAV 99
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 147-229 4.07e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 61.18  E-value: 4.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 147 NTLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00080  143 NRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNF 222


                  ...
gi 1906202172 227 EEW 229
Cdd:MTH00080  223 KEW 225
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 149-232 8.39e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 59.06  E-value: 8.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 149 LRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMPQDEY-- 226
Cdd:PTZ00047   75 LTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVSPEAYaa 154


                  ....*...
gi 1906202172 227 --EEWYAE 232
Cdd:PTZ00047  155 haKKYYKD 162
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 129-220 3.04e-10

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 55.46  E-value: 3.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 129 VEGYRFGWDFVypnghttntLRVPQDRVVRLQVTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCG 208
Cdd:cd13917     5 LVARAWQWRPV---------LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCG 75

                          90
                  ....*....|..
gi 1906202172 209 SGHSLMTTDVVV 220
Cdd:cd13917    76 IGHHTMHGRIIV 87
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 88-243 5.30e-09

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 55.58  E-value: 5.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172  88 VFYSFSISAIIVVSLIAWTYSQLLyieqgpDP-----AQEEALEIDVEGYRFGWDFVYPNG--HTTNTLRVPQDRVVRLQ 160
Cdd:PRK10525   91 VVWTVPILIIIFLAVLTWKTTHAL------EPskplaHDEKPITIEVVSMDWKWFFIYPEQgiATVNEIAFPANVPVYFK 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 161 VTSTDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVVMP-QDEYEEWYAETNGTAAS 239
Cdd:PRK10525  165 VTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPdRAEFDQWVAKAKQSPNT 244


                  ....
gi 1906202172 240 GNET 243
Cdd:PRK10525  245 MNDM 248
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 145-222 2.35e-05

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 42.22  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906202172 145 TTNTLRVPQDRVVRLQVT----STDVFHNFGIPALRVKTDAVPGQYTSAWFTANETGTYTAKCYELCGSGHSLMTTDVVV 220
Cdd:cd04223    14 TPDIIEVKEGDEVTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLIV 93


                  ..
gi 1906202172 221 MP 222
Cdd:cd04223    94 EP 95
 
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