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Conserved domains on  [gi|55231715|gb|AAV47134|]
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cytochrome C oxidase subunit II membrane domain [Haloarcula marismortui ATCC 43049]

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

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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; ...
 93-230 3.84e-89

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: 260.85  E-value: 3.84e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  93 SISAIIVVSLIAWTYSQLLYIEQGPDPAQEEALEIDVEGYRFGWDFIYPNG-HTANTLRVPQDRVVRLQVTSTDVFHNFG 171
Cdd:cd13918   1 GLSAIIVISLIVWTYGMLLYVEDPPDEADEDALEVEVEGFQFGWQFEYPNGvTTGNTLRVPADTPIALRVTSTDVFHTFG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 55231715 172 IPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYEAWY 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 3.84e-89

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: 260.85  E-value: 3.84e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  93 SISAIIVVSLIAWTYSQLLYIEQGPDPAQEEALEIDVEGYRFGWDFIYPNG-HTANTLRVPQDRVVRLQVTSTDVFHNFG 171
Cdd:cd13918   1 GLSAIIVISLIVWTYGMLLYVEDPPDEADEDALEVEVEGFQFGWQFEYPNGvTTGNTLRVPADTPIALRVTSTDVFHTFG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 55231715 172 IPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYEAWY 230
Cdd:cd13918  81 IPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 22-231 7.28e-85

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: 251.92  E-value: 7.28e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715    22 APSAVFEQIFEVFLLL---GTAVGVVVVAYTMYHALKYRDDGSGtdpyadkverpemgELPTGGTGGRKVFYSFSIS-AI 97
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVlavSTLISLLVAALLAYVVWKFRRKGDE--------------EKPSQIHGNRRLEYVWTVIpLI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715    98 IVVSLIAWTYSQLLYIEQGPDPaqeEALEIDVEGYRFGWDFIYPNG--HTANTLRVPQDRVVRLQVTSTDVFHNFGIPEL 175
Cdd:TIGR02866  67 IVVGLFAATAKGLLYLERPIPK---DALKVKVTGYQWWWDFEYPESgfTTVNELVLPAGTPVELQVTSKDVIHSFWVPEL 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 55231715   176 RVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYEAWYN 231
Cdd:TIGR02866 144 GGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-237 6.85e-62

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 194.66  E-value: 6.85e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715   1 MATSLITYATVVFPLhGGDVRAPSAV------FEQIFEVFLLLGTAVGVVVVAYTMYHALKYRDDGSGTDP----YADKV 70
Cdd:COG1622   1 MKRLLLALLLLALLL-SGQLSLPDPAgpiaeeIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPaqfhHNTKL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  71 ErpemgelpTGGTGgrkvfysfsISAIIVVSLIAWTYSQLLYIEQGPDPAqeeaLEIDVEGYRFGWDFIYPNGH--TANT 148
Cdd:COG1622  80 E--------IVWTV---------IPIIIVIVLAVPTLRVLHALDDAPEDP----LTVEVTGYQWKWLFRYPDQGiaTVNE 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715 149 LRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYEA 228
Cdd:COG1622 139 LVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDA 218


                ....*....
gi 55231715 229 WYNGTEGSA 237
Cdd:COG1622 219 WLAEQKASA 227
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
145-214 4.14e-20

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 83.23  E-value: 4.14e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715   145 TANTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLM 214
Cdd:pfam00116  44 VDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 147-235 1.51e-19

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 84.61  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  147 NTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00140 140 NRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDF 219


                 ....*....
gi 55231715  227 EAWYNGTEG 235
Cdd:MTH00140 220 VKWLELMSE 228
 
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 3.84e-89

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: 260.85  E-value: 3.84e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  93 SISAIIVVSLIAWTYSQLLYIEQGPDPAQEEALEIDVEGYRFGWDFIYPNG-HTANTLRVPQDRVVRLQVTSTDVFHNFG 171
Cdd:cd13918   1 GLSAIIVISLIVWTYGMLLYVEDPPDEADEDALEVEVEGFQFGWQFEYPNGvTTGNTLRVPADTPIALRVTSTDVFHTFG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 55231715 172 IPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYEAWY 230
Cdd:cd13918  81 IPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 22-231 7.28e-85

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: 251.92  E-value: 7.28e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715    22 APSAVFEQIFEVFLLL---GTAVGVVVVAYTMYHALKYRDDGSGtdpyadkverpemgELPTGGTGGRKVFYSFSIS-AI 97
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVlavSTLISLLVAALLAYVVWKFRRKGDE--------------EKPSQIHGNRRLEYVWTVIpLI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715    98 IVVSLIAWTYSQLLYIEQGPDPaqeEALEIDVEGYRFGWDFIYPNG--HTANTLRVPQDRVVRLQVTSTDVFHNFGIPEL 175
Cdd:TIGR02866  67 IVVGLFAATAKGLLYLERPIPK---DALKVKVTGYQWWWDFEYPESgfTTVNELVLPAGTPVELQVTSKDVIHSFWVPEL 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 55231715   176 RVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYEAWYN 231
Cdd:TIGR02866 144 GGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-237 6.85e-62

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 194.66  E-value: 6.85e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715   1 MATSLITYATVVFPLhGGDVRAPSAV------FEQIFEVFLLLGTAVGVVVVAYTMYHALKYRDDGSGTDP----YADKV 70
Cdd:COG1622   1 MKRLLLALLLLALLL-SGQLSLPDPAgpiaeeIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPaqfhHNTKL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  71 ErpemgelpTGGTGgrkvfysfsISAIIVVSLIAWTYSQLLYIEQGPDPAqeeaLEIDVEGYRFGWDFIYPNGH--TANT 148
Cdd:COG1622  80 E--------IVWTV---------IPIIIVIVLAVPTLRVLHALDDAPEDP----LTVEVTGYQWKWLFRYPDQGiaTVNE 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715 149 LRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYEA 228
Cdd:COG1622 139 LVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDA 218


                ....*....
gi 55231715 229 WYNGTEGSA 237
Cdd:COG1622 219 WLAEQKASA 227
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 124-220 1.17e-41

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: 138.53  E-value: 1.17e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715 124 ALEIDVEGYRFGWDFIYPNGHTA-NTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAK 202
Cdd:cd13915   1 ALEIQVTGRQWMWEFTYPNGKREiNELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLF 80

                        90
                ....*....|....*...
gi 55231715 203 CYELCGSGHSLMTTDVVV 220
Cdd:cd13915  81 CTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 126-229 2.28e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 127.91  E-value: 2.28e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715 126 EIDVEGYRFGWDFIYP--NGHTANTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKC 203
Cdd:cd13914   2 EIEVEAYQWGWEFSYPeaNVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYC 81

                        90       100
                ....*....|....*....|....*.
gi 55231715 204 YELCGSGHSLMTTDVVVMPQDEYEAW 229
Cdd:cd13914  82 AEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 124-221 3.08e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 124.68  E-value: 3.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715 124 ALEIDVEGYRFGWDFIYPNGH---------TANTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTAN 194
Cdd:cd13919   1 ALVVEVTAQQWAWTFRYPGGDgklgtdddvTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPT 80

                        90       100
                ....*....|....*....|....*..
gi 55231715 195 ETGTYAAKCYELCGSGHSLMTTDVVVM 221
Cdd:cd13919  81 REGEYEVRCAELCGLGHYRMRATVKVV 107
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 125-219 7.29e-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: 118.17  E-value: 7.29e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715 125 LEIDVEGYRFGWDFIYPNGHTANTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCY 204
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPNVRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTIICA 80

                        90
                ....*....|....*
gi 55231715 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 1.24e-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: 112.71  E-value: 1.24e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715 124 ALEIDVEGYRFGWDFIYPNGH-----TANTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGT 198
Cdd:cd04213   1 ALTIEVTGHQWWWEFRYPDEPgrgivTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGV 80

                        90       100
                ....*....|....*....|...
gi 55231715 199 YAAKCYELCGSGHSLMTTDVVVM 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 ...
 147-229 2.22e-25

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: 97.26  E-value: 2.22e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715 147 NTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:cd13912  48 NRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDF 127


                ...
gi 55231715 227 EAW 229
Cdd:cd13912 128 LSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
145-214 4.14e-20

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 83.23  E-value: 4.14e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715   145 TANTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLM 214
Cdd:pfam00116  44 VDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 147-235 1.51e-19

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 84.61  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  147 NTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00140 140 NRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDF 219


                 ....*....
gi 55231715  227 EAWYNGTEG 235
Cdd:MTH00140 220 VKWLELMSE 228
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 94-229 3.21e-18

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 81.34  E-value: 3.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715   94 ISAIIVVsLIAWTYSQLLYIEqgpDPAQEEALEIDVEGYRFGWDFIYPNGHTA-------------------------NT 148
Cdd:MTH00023  77 IPAVILV-FIALPSLKLLYLM---DEVVSPALTIKAIGHQWYWSYEYSDYEGEtlefdsymvptsdlnsgdfrllevdNR 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  149 LRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYEA 228
Cdd:MTH00023 153 LVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIN 232


                 .
gi 55231715  229 W 229
Cdd:MTH00023 233 W 233
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 94-231 7.34e-18

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 80.13  E-value: 7.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715   94 ISAIIVVsLIAWTYSQLLY-IEQGPDPAqeeaLEIDVEGYRFGWDFIYPNGH-----------------------TANTL 149
Cdd:MTH00038  68 VPAFILI-FIALPSLQLLYlMDEVNNPF----LTIKAIGHQWYWSYEYTDYNdlefdsymvptsdlstglprlleVDNRL 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  150 RVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYEAW 229
Cdd:MTH00038 143 VLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENW 222


                 ..
gi 55231715  230 YN 231
Cdd:MTH00038 223 VS 224
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 92-229 6.49e-17

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 77.62  E-value: 6.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715   92 FSISAIIVVSLIAWTYSQLLYIEqgpDPAQEEALEIDVEGYRFGWDFIYPNGHTAN-----------------------T 148
Cdd:MTH00185  65 WTILPAIILIMIALPSLRILYLM---DEINDPHLTIKAMGHQWYWSYEYTDYEQLEfdsymtptqdltpgqfrlletdhR 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  149 LRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYEA 228
Cdd:MTH00185 142 MVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFEN 221


                 .
gi 55231715  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 7.39e-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: 73.76  E-value: 7.39e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55231715 145 TANTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVV 220
Cdd:cd13913  23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIV 98
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 94-229 1.45e-16

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 76.74  E-value: 1.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715   94 ISAIIVVsLIAWTYSQLLYIEqgpDPAQEEALEIDVEGYRFGWDFIYPNGHTA-------------------------NT 148
Cdd:MTH00051  70 IPAAILI-FIAFPSLKLLYLM---DEVIDPALTIKAIGHQWYWSYEYSDYGTDtiefdsymiptsdlnsgdlrllevdNR 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  149 LRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYEA 228
Cdd:MTH00051 146 LIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYIN 225


                 .
gi 55231715  229 W 229
Cdd:MTH00051 226 W 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 147-229 7.22e-16

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 74.43  E-value: 7.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  147 NTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00076 140 NRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNF 219


                 ...
gi 55231715  227 EAW 229
Cdd:MTH00076 220 LNW 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 147-229 8.88e-16

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 74.37  E-value: 8.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  147 NTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00098 140 NRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYF 219


                 ...
gi 55231715  227 EAW 229
Cdd:MTH00098 220 EKW 222
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 141-229 1.43e-15

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 73.79  E-value: 1.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  141 PNGH-----TANTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMT 215
Cdd:MTH00117 129 PNGHfrlleVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMP 208

                         90
                 ....*....|....
gi 55231715  216 TDVVVMPQDEYEAW 229
Cdd:MTH00117 209 IVVESVPLKHFENW 222
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 147-229 1.11e-14

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 71.16  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  147 NTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00168 140 NRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETF 219


                 ...
gi 55231715  227 EAW 229
Cdd:MTH00168 220 ENW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 151-229 1.34e-14

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 70.90  E-value: 1.34e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55231715  151 VPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYEAW 229
Cdd:MTH00129 144 VPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 126-220 2.53e-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: 67.02  E-value: 2.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715 126 EIDVEGYRFGWdfiypnghTANTLRVPQDRVVRLQVTSTDVFHNFGI--PELRV--KTDAVPGQYTSAWFTANETGTYAA 201
Cdd:cd13916   2 VVAVTGHQWYW--------ELSRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFDKPGTYTI 73

                        90
                ....*....|....*....
gi 55231715 202 KCYELCGSGHSLMTTDVVV 220
Cdd:cd13916  74 LCLEYCGLAHHVMMAEFTV 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 125-221 3.26e-14

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: 66.80  E-value: 3.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715 125 LEIDVEGYRFGWDFIYPNGHTA--NTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAK 202
Cdd:cd04212   1 LEIQVVSLDWKWLFIYPEQGIAtvNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80

                        90
                ....*....|....*....
gi 55231715 203 CYELCGSGHSLMTTDVVVM 221
Cdd:cd04212  81 SANYSGEGFSDMKFKVLAV 99
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 158-222 8.87e-14

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 68.06  E-value: 8.87e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55231715  158 RLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDV-VVMP 222
Cdd:MTH00047 127 HLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIeVVDV 192
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 147-229 2.34e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 67.43  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  147 NTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00139 140 NRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFF 219


                 ...
gi 55231715  227 EAW 229
Cdd:MTH00139 220 LEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 147-229 3.83e-13

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 66.80  E-value: 3.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  147 NTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEY 226
Cdd:MTH00008 140 NRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSF 219


                 ...
gi 55231715  227 EAW 229
Cdd:MTH00008 220 MKW 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 94-229 9.10e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 66.59  E-value: 9.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715   94 ISAIIVVsLIAWTYSQLLYI-EQGPDPAQeeaLEIDVEGYRFGWDFIYPNG-------------------------HTAN 147
Cdd:MTH00027  99 IPAFILI-LIAFPSLRLLYImDECGFSAN---ITIKVTGHQWYWSYSYEDYgekniefdsymiptadlefgdlrllEVDN 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  148 TLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYE 227
Cdd:MTH00027 175 RLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYI 254


                 ..
gi 55231715  228 AW 229
Cdd:MTH00027 255 DW 256
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 147-214 9.37e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 66.01  E-value: 9.37e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55231715  147 NTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLM 214
Cdd:MTH00154 140 NRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFM 207
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 149-230 1.84e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 58.29  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  149 LRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMPQDEYEA 228
Cdd:PTZ00047  75 LTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVSPEAYAA 154


                 ....*.
gi 55231715  229 ----WY 230
Cdd:PTZ00047 155 hakkYY 160
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 147-214 2.32e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 59.25  E-value: 2.32e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55231715  147 NTLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLM 214
Cdd:MTH00080 143 NRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFM 210
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 129-220 2.33e-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: 55.84  E-value: 2.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715 129 VEGYRFGWDFIypnghtantLRVPQDRVVRLQVTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCG 208
Cdd:cd13917   5 LVARAWQWRPV---------LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCG 75

                        90
                ....*....|..
gi 55231715 209 SGHSLMTTDVVV 220
Cdd:cd13917  76 IGHHTMHGRIIV 87
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 88-229 4.31e-09

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 56.35  E-value: 4.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715   88 VFYSFSISAIIVVSLIAWTYSQLLyieqgpDP-----AQEEALEIDVEGYRFGWDFIYPNG--HTANTLRVPQDRVVRLQ 160
Cdd:PRK10525  91 VVWTVPILIIIFLAVLTWKTTHAL------EPskplaHDEKPITIEVVSMDWKWFFIYPEQgiATVNEIAFPANVPVYFK 164

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715  161 VTSTDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVVMP-QDEYEAW 229
Cdd:PRK10525 165 VTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPdRAEFDQW 234
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 145-222 2.19e-06

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: 44.92  E-value: 2.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55231715 145 TANTLRVPQDRVVRLQVT----STDVFHNFGIPELRVKTDAVPGQYTSAWFTANETGTYAAKCYELCGSGHSLMTTDVVV 220
Cdd:cd04223  14 TPDIIEVKEGDEVTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLIV 93


                ..
gi 55231715 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.
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