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Conserved domains on  [gi|284015178|gb|ADB61129|]
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cytochrome c oxidase, subunit II [Haloterrigena turkmenica DSM 5511]

Protein Classification

CuRO_HCO_II_like_6 domain-containing protein( domain architecture ID 10195319)

CuRO_HCO_II_like_6 domain-containing protein

Graphical summary

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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; ...
 73-211 9.62e-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: 257.00  E-value: 9.62e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  73 GISAVIVISLVIWTYGMLLYVEDPQDEFDEEPVEIEVTGQGFAWYFEYANGVESISTMRIPADHPVAIEATSGDVWHTFG 152
Cdd:cd13918    1 GLSAIIVISLIVWTYGMLLYVEDPPDEADEDALEVEVEGFQFGWQFEYPNGVTTGNTLRVPADTPIALRVTSTDVFHTFG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 284015178 153 IPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNEWL 211
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; ...
 73-211 9.62e-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: 257.00  E-value: 9.62e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  73 GISAVIVISLVIWTYGMLLYVEDPQDEFDEEPVEIEVTGQGFAWYFEYANGVESISTMRIPADHPVAIEATSGDVWHTFG 152
Cdd:cd13918    1 GLSAIIVISLIVWTYGMLLYVEDPPDEADEDALEVEVEGFQFGWQFEYPNGVTTGNTLRVPADTPIALRVTSTDVFHTFG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 284015178 153 IPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNEWL 211
Cdd:cd13918   81 IPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
37-214 1.45e-55

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 180.41  E-value: 1.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  37 AYKYRDDGEPKDdeslptlgelPTGGKGGKKL-FLSFGISAVIVISLVIWTYGMLLYVEDPqdefDEEPVEIEVTGQGFA 115
Cdd:COG1622   58 AIRYRRRKGDAD----------PAQFHHNTKLeIVWTVIPIIIVIVLAVPTLRVLHALDDA----PEDPLTVEVTGYQWK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 116 WYFEYAN-GVESISTMRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTA 194
Cdd:COG1622  124 WLFRYPDqGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAG 203

                        170       180
                 ....*....|....*....|
gi 284015178 195 MTGNVQVMEEEAFNEWLNGQ 214
Cdd:COG1622  204 MRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 37-212 5.62e-49

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: 162.55  E-value: 5.62e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178   37 AYKYRDDGEPkddeslptlgELPTGGKGGKKLFLSFGIS-AVIVISLVIWTYGMLLYVEDPqdeFDEEPVEIEVTGQGFA 115
Cdd:TIGR02866  35 VWKFRRKGDE----------EKPSQIHGNRRLEYVWTVIpLIIVVGLFAATAKGLLYLERP---IPKDALKVKVTGYQWW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  116 WYFEYAN-GVESISTMRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTA 194
Cdd:TIGR02866 102 WDFEYPEsGFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSL 181

                         170
                  ....*....|....*...
gi 284015178  195 MTGNVQVMEEEAFNEWLN 212
Cdd:TIGR02866 182 MLFKVVVVPKEEFDAYVE 199
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
132-195 8.72e-15

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 69.75  E-value: 8.72e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 284015178  132 IPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAM 195
Cdd:pfam00116  50 LPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 83-214 1.11e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 69.42  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  83 VIWTY---GMLLYVEDPQ-------DEFDEEPVEIEVTGQGFAWYFEYAN-GVESI---STM------------------ 130
Cdd:MTH00051  65 IIWTLipaAILIFIAFPSlkllylmDEVIDPALTIKAIGHQWYWSYEYSDyGTDTIefdSYMiptsdlnsgdlrllevdn 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 131 --RIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFN 208
Cdd:MTH00051 145 rlIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYI 224


                 ....*.
gi 284015178 209 EWLNGQ 214
Cdd:MTH00051 225 NWVATQ 230
 
Name Accession Description Interval E-value
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 73-211 9.62e-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: 257.00  E-value: 9.62e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  73 GISAVIVISLVIWTYGMLLYVEDPQDEFDEEPVEIEVTGQGFAWYFEYANGVESISTMRIPADHPVAIEATSGDVWHTFG 152
Cdd:cd13918    1 GLSAIIVISLIVWTYGMLLYVEDPPDEADEDALEVEVEGFQFGWQFEYPNGVTTGNTLRVPADTPIALRVTSTDVFHTFG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 284015178 153 IPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNEWL 211
Cdd:cd13918   81 IPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
37-214 1.45e-55

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 180.41  E-value: 1.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  37 AYKYRDDGEPKDdeslptlgelPTGGKGGKKL-FLSFGISAVIVISLVIWTYGMLLYVEDPqdefDEEPVEIEVTGQGFA 115
Cdd:COG1622   58 AIRYRRRKGDAD----------PAQFHHNTKLeIVWTVIPIIIVIVLAVPTLRVLHALDDA----PEDPLTVEVTGYQWK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 116 WYFEYAN-GVESISTMRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTA 194
Cdd:COG1622  124 WLFRYPDqGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAG 203

                        170       180
                 ....*....|....*....|
gi 284015178 195 MTGNVQVMEEEAFNEWLNGQ 214
Cdd:COG1622  204 MRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 37-212 5.62e-49

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: 162.55  E-value: 5.62e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178   37 AYKYRDDGEPkddeslptlgELPTGGKGGKKLFLSFGIS-AVIVISLVIWTYGMLLYVEDPqdeFDEEPVEIEVTGQGFA 115
Cdd:TIGR02866  35 VWKFRRKGDE----------EKPSQIHGNRRLEYVWTVIpLIIVVGLFAATAKGLLYLERP---IPKDALKVKVTGYQWW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  116 WYFEYAN-GVESISTMRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTA 194
Cdd:TIGR02866 102 WDFEYPEsGFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSL 181

                         170
                  ....*....|....*...
gi 284015178  195 MTGNVQVMEEEAFNEWLN 212
Cdd:TIGR02866 182 MLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 106-201 7.16e-33

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: 117.34  E-value: 7.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 106 EIEVTGQGFAWYFEYANGVESISTMRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCF 185
Cdd:cd13915    3 EIQVTGRQWMWEFTYPNGKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCT 82

                         90
                 ....*....|....*.
gi 284015178 186 ELCGESHTAMTGNVQV 201
Cdd:cd13915   83 EYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 105-199 2.78e-31

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: 113.16  E-value: 2.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 105 VEIEVTGQGFAWYFEYANgVESISTMRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKC 184
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTIIC 79

                         90
                 ....*....|....*
gi 284015178 185 FELCGESHTAMTGNV 199
Cdd:cd13842   80 AEYCGLGHSYMLGKV 94
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 104-202 4.72e-31

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: 112.73  E-value: 4.72e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 104 PVEIEVTGQGFAWYFEYANG--------VESISTMRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMAD 175
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPGGdgklgtddDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPT 80

                         90       100
                 ....*....|....*....|....*..
gi 284015178 176 EPGEHEIKCFELCGESHTAMTGNVQVM 202
Cdd:cd13919   81 REGEYEVRCAELCGLGHYRMRATVKVV 107
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 105-211 7.01e-26

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: 99.40  E-value: 7.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 105 VEIEVTGQGFAWYFEYAN-GVESISTMRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIK 183
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPEaNVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLY 80

                         90       100
                 ....*....|....*....|....*...
gi 284015178 184 CFELCGESHTAMTGNVQVMEEEAFNEWL 211
Cdd:cd13914   81 CAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 104-202 3.54e-25

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: 97.31  E-value: 3.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 104 PVEIEVTGQGFAWYFEYAN----GVESISTMRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGE 179
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDepgrGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGV 80

                         90       100
                 ....*....|....*....|...
gi 284015178 180 HEIKCFELCGESHTAMTGNVQVM 202
Cdd:cd04213   81 YRGQCAEFCGASHALMRFKVIAL 103
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 107-210 4.03e-16

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: 73.76  E-value: 4.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 107 IEVTGQGFAWYFEYA--NGVESISTM-----------R---------IPADHPVAIEATSGDVWHTFGIPDLRVKADAIP 164
Cdd:cd13912    5 IKAIGHQWYWSYEYSdfNDLEFDSYMipeddlekgqlRllevdnrlvVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVP 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 284015178 165 GEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNEW 210
Cdd:cd13912   85 GRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
132-195 8.72e-15

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 69.75  E-value: 8.72e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 284015178  132 IPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAM 195
Cdd:pfam00116  50 LPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 105-201 9.47e-15

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: 68.95  E-value: 9.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 105 VEIEVTGQGFAWyfeyangveSISTMRIPADHPVAIEATSGDVWHTFGI--PDLRVKAD--AIPGEYDETWFMADEPGEH 180
Cdd:cd13916    1 QVVAVTGHQWYW---------ELSRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLLAQtqAMPGYTNVLRYTFDKPGTY 71

                         90       100
                 ....*....|....*....|.
gi 284015178 181 EIKCFELCGESHTAMTGNVQV 201
Cdd:cd13916   72 TILCLEYCGLAHHVMMAEFTV 92
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 83-214 1.11e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 69.42  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  83 VIWTY---GMLLYVEDPQ-------DEFDEEPVEIEVTGQGFAWYFEYAN-GVESI---STM------------------ 130
Cdd:MTH00051  65 IIWTLipaAILIFIAFPSlkllylmDEVIDPALTIKAIGHQWYWSYEYSDyGTDTIefdSYMiptsdlnsgdlrllevdn 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 131 --RIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFN 208
Cdd:MTH00051 145 rlIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYI 224


                 ....*.
gi 284015178 209 EWLNGQ 214
Cdd:MTH00051 225 NWVATQ 230
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 90-213 3.16e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 68.04  E-value: 3.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  90 LLYVEDPQdefdeEPVEIEVTGQGFAWYFEYA----NGVESISTMrIP-------------ADHPVAIEA--------TS 144
Cdd:MTH00140  83 LLYLLDET-----NNPLLTVKAIGHQWYWSYEysdfSVIEFDSYM-VPenelelgdfrlleVDNRLVLPYsvdtrvlvTS 156

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 284015178 145 GDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNEWLNG 213
Cdd:MTH00140 157 ADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 103-201 5.20e-13

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: 64.13  E-value: 5.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 103 EPVEIEVTGQGFAWYFEyangvesISTMRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEI 182
Cdd:cd13913    7 GPNEYEVYVVAQAFAFN-------PNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLI 79

                         90
                 ....*....|....*....
gi 284015178 183 KCFELCGESHTAMTGNVQV 201
Cdd:cd13913   80 ICNEYCGAGHHNMYGKIIV 98
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 90-211 7.63e-13

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 66.80  E-value: 7.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  90 LLYVedpQDEFDEEPVEIEVTGQGFAWYFEYAN--GVESISTMrIPA-------------DH----PVAIEA----TSGD 146
Cdd:MTH00008  83 LLYL---MDEVSNPSITLKTIGHQWYWSYEYSDfsNLEFDSYM-LPTsdlspgqfrllevDNravlPMQTEIrvlvTAAD 158

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284015178 147 VWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNEWL 211
Cdd:MTH00008 159 VIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 98-210 8.42e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 66.66  E-value: 8.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  98 DEFDEEPVEIEVTGQGFAWYFEYAN----GVES--IST----------------MRIPADHPVAIEATSGDVWHTFGIPD 155
Cdd:MTH00129  88 DEINDPHLTIKAMGHQWYWSYEYTDyedlGFDSymIPTqdltpgqfrlleadhrMVVPVESPIRVLVSAEDVLHSWAVPA 167

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 284015178 156 LRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNEW 210
Cdd:MTH00129 168 LGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 74-211 2.21e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 65.51  E-value: 2.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  74 ISAVIVISLVIWTYgMLLYVedpQDEFDEEPVEIEVTGQGFAWYFEYA--NGVESISTMrIP-------------ADHPV 138
Cdd:MTH00139  68 LPAFILLFLALPSL-RLLYL---MDEVSDPYLTFKAVGHQWYWSYEYSdfKNLSFDSYM-IPtedlssgefrlleVDNRL 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 139 A------IEA--TSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNEW 210
Cdd:MTH00139 143 VlpyksnIRAliTAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222


                 .
gi 284015178 211 L 211
Cdd:MTH00139 223 I 223
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 98-210 2.49e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 65.29  E-value: 2.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  98 DEFDEEPVEIEVTGQGFAWYFEYAN----GVESIST------------------MRIPADHPVAIEATSGDVWHTFGIPD 155
Cdd:MTH00185  88 DEINDPHLTIKAMGHQWYWSYEYTDyeqlEFDSYMTptqdltpgqfrlletdhrMVVPMESPIRVLITAEDVLHSWTVPA 167

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 284015178 156 LRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNEW 210
Cdd:MTH00185 168 LGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 98-216 7.51e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 64.03  E-value: 7.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  98 DEFDEEPVEIEVTGQGFAWYFEYANG----------------------VESISTMRIPADHPVAIEATSGDVWHTFGIPD 155
Cdd:MTH00076  88 DEINDPHLTVKAIGHQWYWSYEYTDYedlsfdsymiptqdltpgqfrlLEVDNRMVVPMESPIRMLITAEDVLHSWAVPS 167

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284015178 156 LRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNEWLNGQLT 216
Cdd:MTH00076 168 LGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 74-211 1.73e-11

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 63.23  E-value: 1.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  74 ISAVIVISLVIWTYgMLLYVedpQDEFDEEPVEIEVTGQGFAWYFEYANG------------------------VESIST 129
Cdd:MTH00023  77 IPAVILVFIALPSL-KLLYL---MDEVVSPALTIKAIGHQWYWSYEYSDYegetlefdsymvptsdlnsgdfrlLEVDNR 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 130 MRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNE 209
Cdd:MTH00023 153 LVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIN 232


                 ..
gi 284015178 210 WL 211
Cdd:MTH00023 233 WL 234
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 130-210 1.73e-11

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 62.81  E-value: 1.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 130 MRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNE 209
Cdd:MTH00098 142 VVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEK 221


                 .
gi 284015178 210 W 210
Cdd:MTH00098 222 W 222
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 74-216 2.34e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 62.80  E-value: 2.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  74 ISAVIVISLVIWTYGMLLYVedpqDEFDEEPVEIEVTGQGFAWYFEYA--NGVESISTM--------------------R 131
Cdd:MTH00038  68 VPAFILIFIALPSLQLLYLM----DEVNNPFLTIKAIGHQWYWSYEYTdyNDLEFDSYMvptsdlstglprllevdnrlV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 132 IPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNEWL 211
Cdd:MTH00038 144 LPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWV 223


                 ....*
gi 284015178 212 NGQLT 216
Cdd:MTH00038 224 SNFLE 228
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 86-195 3.18e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 61.51  E-value: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  86 TYGMLLYVEDPqdefdeepveIEVTGQGFAWYFEYANGVESISTM-----------RIPADHPVAIEATSGDVWHTFGIP 154
Cdd:MTH00047  73 TSDLDCFSSET----------IKVIGHQWYWSYEYSFGGSYDSFMtddifgvdkplRLVYGVPYHLLVTSSDVIHSFSVP 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 284015178 155 DLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAM 195
Cdd:MTH00047 143 DLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYM 183
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 74-211 7.33e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 61.58  E-value: 7.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  74 ISAVIVIsLVIWTYGMLLYVEDpQDEFDEEpVEIEVTGQGFAWYFEYANG------------------------VESIST 129
Cdd:MTH00027  99 IPAFILI-LIAFPSLRLLYIMD-ECGFSAN-ITIKVTGHQWYWSYSYEDYgekniefdsymiptadlefgdlrlLEVDNR 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 130 MRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNE 209
Cdd:MTH00027 176 LILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYID 255


                 ..
gi 284015178 210 WL 211
Cdd:MTH00027 256 WI 257
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 74-212 1.26e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 60.38  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  74 ISAVIVISLVIWTYGMLLYVedpqDEFDEEPVEIEVTGQGFAWYFEYA--NGVESISTMR-------------------- 131
Cdd:MTH00168  68 IPAFILISLALPSLRLLYLM----DEIDKPDLTIKAVGHQWYWSYEYTdyNDLEFDSYMVptqdlspgqfrllevdnrlv 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 132 IPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNEWL 211
Cdd:MTH00168 144 LPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223


                 .
gi 284015178 212 N 212
Cdd:MTH00168 224 D 224
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 130-212 2.74e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 59.54  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 130 MRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNE 209
Cdd:MTH00117 142 MVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFEN 221


                 ...
gi 284015178 210 WLN 212
Cdd:MTH00117 222 WSS 224
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 105-178 4.50e-09

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: 52.94  E-value: 4.50e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284015178 105 VEIEVTGQGFAWYFEYAN-GVESISTMRIPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPG 178
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEqGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPG 75
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 113-216 8.32e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 55.02  E-value: 8.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 113 GFAWYFEYA----NGVESISTMR--------------------IPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYD 168
Cdd:MTH00080 104 GHQWYWSYEfsdiPGLEFDSYMKsldqlrlgeprllevdnrcvLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILS 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 284015178 169 ETWFMADEPGEHEIKCFELCGESHTAMTGNVQVMEEEAFNEWLNGQLT 216
Cdd:MTH00080 184 TLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 132-195 5.63e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 52.52  E-value: 5.63e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 284015178 132 IPADHPVAIEATSGDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAM 195
Cdd:MTH00154 144 LPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFM 207
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 80-211 6.15e-08

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 53.26  E-value: 6.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178  80 ISLVIWTYGMLLYV------------EDPQDEF--DEEPVEIEVTGQGFAWYFEYAN-GVESISTMRIPADHPVAIEATS 144
Cdd:PRK10525  88 VEAVVWTVPILIIIflavltwktthaLEPSKPLahDEKPITIEVVSMDWKWFFIYPEqGIATVNEIAFPANVPVYFKVTS 167

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 284015178 145 GDVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMT-GNVQVMEEEAFNEWL 211
Cdd:PRK10525 168 NSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKfKAIATPDRAEFDQWV 235
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 143-207 1.94e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 44.04  E-value: 1.94e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 284015178 143 TSGDVWHTFGIPDLRVKADAIPGEYDE-TWFMADEpGEHEIKCFELCGESHTAMTGNVQVMEEEAF 207
Cdd:PTZ00047  88 TATDVIHSWSVPSLGIKADAIPGRLHKiNTFILRE-GVFYGQCSEMCGTLHGFMPIVVEAVSPEAY 152
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 146-201 3.34e-04

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: 39.14  E-value: 3.34e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 284015178 146 DVWHTFGIPDLRVKADAIPGEYDETWFMADEPGEHEIKCFELCGESHTAMTGNVQV 201
Cdd:cd04223   38 DITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLIV 93
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 143-201 6.00e-04

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: 38.12  E-value: 6.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178 143 TSGDVWHTFGIPDLRVKADAIPGeYDETWFMA-DEPGEHEIKCFELCGESHTAMTGNVQV 201
Cdd:cd13917   29 SSLDVQHGFSLQPKNINFQVLPG-YEWVITMTpNETGEFHIICNEYCGIGHHTMHGRIIV 87
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 79-184 5.69e-03

Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel.


Pssm-ID: 379208 [Multi-domain]  Cd Length: 104  Bit Score: 36.02  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284015178   79 VISLVIWtygmlLYVEDPQDEFDEEPVEIEVTgqgfawyfeyaNGVESISTMRIPADHPVAIEAT-SGDVWHTFGIPDLR 157
Cdd:pfam13473   2 IAALAVL-----FWLSKPAAAADDPTVEITVK-----------DGGFSPSRITVPAGTPVKLEFKnKDKTPAEFESPDLG 65

                          90       100
                  ....*....|....*....|....*..
gi 284015178  158 VKADAIPGEYDETWFMADEPGEHEIKC 184
Cdd:pfam13473  66 IEKVLAPGKTSTITIPPLKPGEYDFFC 92
 
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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