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Conserved domains on  [gi|2735944|gb|AAC61619|]
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cytochrome oxidase subunit 2 (mitochondrion) [Onchocerca volvulus]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475892)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-231 3.51e-118

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 336.21  E-value: 3.51e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944     1 MYLQNYVFPIPGNSYVFCCYYIHNYYSHIIFFGFFVMFLVSGGIYFFGNSFKFNLKRSDSRMIELILQVLIVNFLIMMAG 80
Cdd:MTH00080   1 NYFQGYNLNFSNSLFSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    81 PGFWLIQYQGRMFRQSELTLKVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSS 160
Cdd:MTH00080  81 PSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735944   161 DVIHSFAIPKCFIKMDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGWSVNYLL 231
Cdd:MTH00080 161 DVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
 
Name Accession Description Interval E-value
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-231 3.51e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 336.21  E-value: 3.51e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944     1 MYLQNYVFPIPGNSYVFCCYYIHNYYSHIIFFGFFVMFLVSGGIYFFGNSFKFNLKRSDSRMIELILQVLIVNFLIMMAG 80
Cdd:MTH00080   1 NYFQGYNLNFSNSLFSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    81 PGFWLIQYQGRMFRQSELTLKVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSS 160
Cdd:MTH00080  81 PSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735944   161 DVIHSFAIPKCFIKMDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGWSVNYLL 231
Cdd:MTH00080 161 DVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 96-225 4.24e-78

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: 230.92  E-value: 4.24e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   96 SELTLKVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKM 175
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 2735944  176 DALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGW 225
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
98-217 6.57e-55

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 171.82  E-value: 6.57e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944     98 LTLKVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDA 177
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2735944    178 LNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELT 217
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
29-225 1.19e-30

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 113.00  E-value: 1.19e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   29 IIFFGFFVMFLVsggIYFFgnsFKFNLKRSD--------SRMIELILQVLIVNFLIMMAGPGFWLIQYQGRMfRQSELTL 100
Cdd:COG1622  43 MLVIFVLVFGLL---LYFA---IRYRRRKGDadpaqfhhNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDA-PEDPLTV 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944  101 KVIGHQWYWSYEYGDSGKLcfdsfmkslddlslgdfrlfdVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNG 180
Cdd:COG1622 116 EVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPG 174

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 2735944  181 LLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGW 225
Cdd:COG1622 175 RVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 22-225 1.40e-29

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: 109.39  E-value: 1.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944     22 IHNYYSHIIFFGFFVMFLVSGG-IYFFgnsFKFNLKRSD--------SRMIELILQVLIVNFLIMMAGPGFWLIQYQGRM 92
Cdd:TIGR02866   9 IAFLFLFVLAVSTLISLLVAALlAYVV---WKFRRKGDEekpsqihgNRRLEYVWTVIPLIIVVGLFAATAKGLLYLERP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944     93 FRQSELTLKVIGHQWYWSYEYGDSGklcfdsfmkslddlslgdfrlFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCF 172
Cdd:TIGR02866  86 IPKDALKVKVTGYQWWWDFEYPESG---------------------FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELG 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2735944    173 IKMDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGW 225
Cdd:TIGR02866 145 GKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-231 3.51e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 336.21  E-value: 3.51e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944     1 MYLQNYVFPIPGNSYVFCCYYIHNYYSHIIFFGFFVMFLVSGGIYFFGNSFKFNLKRSDSRMIELILQVLIVNFLIMMAG 80
Cdd:MTH00080   1 NYFQGYNLNFSNSLFSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    81 PGFWLIQYQGRMFRQSELTLKVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSS 160
Cdd:MTH00080  81 PSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2735944   161 DVIHSFAIPKCFIKMDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGWSVNYLL 231
Cdd:MTH00080 161 DVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 96-225 4.24e-78

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: 230.92  E-value: 4.24e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   96 SELTLKVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKM 175
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 2735944  176 DALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGW 225
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 29-230 1.95e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 191.97  E-value: 1.95e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    29 IIFFGFFVMFLVsggIYFFGNSFkFNLKRSDSRMIELILQVLIVNFLIMMAGPGFWLIqYQGRMFRQSELTLKVIGHQWY 108
Cdd:MTH00154  31 LIMITILVGYMM---ISLLFNKF-TNRFLLEGQEIEIIWTILPAIILIFIALPSLRLL-YLLDEVNNPSITLKTIGHQWY 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   109 WSYEYGDSGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNGLLTKVTCS 188
Cdd:MTH00154 106 WSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFL 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 2735944   189 FSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGWSVNYL 230
Cdd:MTH00154 186 INRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 18-228 3.39e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 191.35  E-value: 3.39e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    18 CCYYIHNY----YSHIIFFGFFVMFLVSGGIYFfgnsfkfNLKRSDSRMIELILQVLIVNFLIMMAGPGFWLIQYQGRMF 93
Cdd:MTH00168  19 ELILFHDHalliLVLILTLVLYSLLVLVTSKYT-------NRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEID 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    94 RqSELTLKVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFI 173
Cdd:MTH00168  92 K-PDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGL 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 2735944   174 KMDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGWSVN 228
Cdd:MTH00168 171 KMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 29-228 8.46e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 190.54  E-value: 8.46e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    29 IIFFGF--FVMFLVSGGIYFFGNSFKFN----LKRSDSRMIELILQVLIVNFLIMMAGPGFWLIqYQGRMFRQSELTLKV 102
Cdd:MTH00140  21 IFFHDHamVVLVLIFSFVMYMLVLLLFNkfscRTILEAQKLETIWTIVPALILVFLALPSLRLL-YLLDETNNPLLTVKA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   103 IGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNGLL 182
Cdd:MTH00140 100 IGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRL 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 2735944   183 TKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGWSVN 228
Cdd:MTH00140 180 NQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 59-230 7.26e-59

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 185.31  E-value: 7.26e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    59 DSRMIELILQVLIVNFLIMMAGPGFwLIQYQGRMFRQSELTLKVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRL 138
Cdd:MTH00098  57 DAQEVETIWTILPAIILILIALPSL-RILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   139 FDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTS 218
Cdd:MTH00098 136 LEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVP 215

                        170
                 ....*....|..
gi 2735944   219 LECWKGWSVNYL 230
Cdd:MTH00098 216 LKYFEKWSASML 227
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 21-230 5.63e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 180.67  E-value: 5.63e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    21 YIHNYyshIIFFGFFVMFLVSGGIYFFGNSFKFNLKRSDSRMIELILQVLIVNFLIMMAGPGFWLIqYQGRMFRQSELTL 100
Cdd:MTH00038  22 YFHDY---ALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLL-YLMDEVNNPFLTI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   101 KVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNG 180
Cdd:MTH00038  98 KAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPG 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 2735944   181 LLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGWSVNYL 230
Cdd:MTH00038 178 RLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 59-226 3.39e-56

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 178.57  E-value: 3.39e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    59 DSRMIELILQVLIVNFLIMMAGPGFwLIQYQgrMFRQSE--LTLKVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDF 136
Cdd:MTH00117  57 DAQEVELIWTILPAIVLILLALPSL-RILYL--MDEINNphLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHF 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   137 RLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLEL 216
Cdd:MTH00117 134 RLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVES 213

                        170
                 ....*....|
gi 2735944   217 TSLECWKGWS 226
Cdd:MTH00117 214 VPLKHFENWS 223
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
98-217 6.57e-55

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 171.82  E-value: 6.57e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944     98 LTLKVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDA 177
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2735944    178 LNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELT 217
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 36-230 1.17e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 174.69  E-value: 1.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    36 VMFLVSGGIYFF---GNSFKFNLKRS-DSRMIELILQVLIVNFLIMMAGPGFwLIQYQGRMFRQSELTLKVIGHQWYWSY 111
Cdd:MTH00185  30 IVFLISTLVLYIivaMVTTKLTNKYIlDSQEIEIVWTILPAIILIMIALPSL-RILYLMDEINDPHLTIKAMGHQWYWSY 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   112 EYGDSGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNGLLTKVTCSFSC 191
Cdd:MTH00185 109 EYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISR 188

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 2735944   192 SGLFFGQCSEICGANHSFMPIVLELTSLECWKGWSVNYL 230
Cdd:MTH00185 189 PGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 25-229 4.74e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 172.98  E-value: 4.74e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    25 YYSHIIFFGFFVMFLVsGGIYFFGNSFKFnLKRS--DSRMIELILQVLIVNFLIMMAGPGFWLIqYQGRMFRQSELTLKV 102
Cdd:MTH00139  23 FHDHAMVILIMILSFV-GYISLSLMSNKF-TSRSllESQEVETIWTVLPAFILLFLALPSLRLL-YLMDEVSDPYLTFKA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   103 IGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNGLL 182
Cdd:MTH00139 100 VGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRL 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 2735944   183 TKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGWSVNY 229
Cdd:MTH00139 180 NQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 59-226 7.02e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 172.98  E-value: 7.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    59 DSRMIELILQVLIVNFLIMMAGPGFwLIQYQGRMFRQSELTLKVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRL 138
Cdd:MTH00129  57 DSQEIEIIWTVLPAVILILIALPSL-RILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   139 FDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTS 218
Cdd:MTH00129 136 LEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVP 215


                 ....*...
gi 2735944   219 LECWKGWS 226
Cdd:MTH00129 216 LEHFENWS 223
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 59-226 1.85e-53

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 171.50  E-value: 1.85e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    59 DSRMIELILQVLIVNFLIMMAGPGFwLIQYQGRMFRQSELTLKVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRL 138
Cdd:MTH00076  57 DAQEIEMVWTIMPAIILIVIALPSL-RILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   139 FDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTS 218
Cdd:MTH00076 136 LEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATP 215


                 ....*...
gi 2735944   219 LECWKGWS 226
Cdd:MTH00076 216 LNNFLNWS 223
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 59-225 4.81e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 165.72  E-value: 4.81e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    59 DSRMIELILQVLIVNFLIMMAGPGFWLIqYQGRMFRQSELTLKVIGHQWYWSYEYGDSGK--LCFDSFMKSLDDLSLGDF 136
Cdd:MTH00051  59 EGTLIEIIWTLIPAAILIFIAFPSLKLL-YLMDEVIDPALTIKAIGHQWYWSYEYSDYGTdtIEFDSYMIPTSDLNSGDL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   137 RLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLEL 216
Cdd:MTH00051 138 RLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEG 217


                 ....*....
gi 2735944   217 TSLECWKGW 225
Cdd:MTH00051 218 VSLDKYINW 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 59-229 1.82e-50

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 163.87  E-value: 1.82e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    59 DSRMIELILQVLIVNFLIMMAGPGFWLIqYQGRMFRQSELTLKVIGHQWYWSYEYGDSGKLCFDSFMKSLDDLSLGDFRL 138
Cdd:MTH00008  57 EAQQIETIWTILPALILLFLAFPSLRLL-YLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   139 FDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTS 218
Cdd:MTH00008 136 LEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVD 215

                        170
                 ....*....|.
gi 2735944   219 LECWKGWSVNY 229
Cdd:MTH00008 216 TKSFMKWVSSF 226
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 29-228 3.92e-50

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 163.38  E-value: 3.92e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    29 IIFFGFFVMFL----VSGGIYFFGNSFK---FNLKRSDSRMIELILQVLIVNFLIMMAGPGFWLIqYQGRMFRQSELTLK 101
Cdd:MTH00023  29 IIFFHDQIMFLliiiITVVLWLIVEALNgkfYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLL-YLMDEVVSPALTIK 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   102 VIGHQWYWSYEYGD--SGKLCFDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALN 179
Cdd:MTH00023 108 AIGHQWYWSYEYSDyeGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVP 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 2735944   180 GLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGWSVN 228
Cdd:MTH00023 188 GRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 44-225 2.15e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 152.10  E-value: 2.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    44 IYFFGNSFKFNLKRSDSRMIELILQVLIVNFLIMMAGPGFWLIQYQGRMFRQSELTLKVIGHQWYWSYEYGDSGK--LCF 121
Cdd:MTH00027  73 ILLGNNYYSYYWNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGFSANITIKVTGHQWYWSYSYEDYGEknIEF 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   122 DSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNGLLTKVTCSFSCSGLFFGQCSE 201
Cdd:MTH00027 153 DSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSE 232

                        170       180
                 ....*....|....*....|....
gi 2735944   202 ICGANHSFMPIVLELTSLECWKGW 225
Cdd:MTH00027 233 ICGANHSFMPIVVESVSLSKYIDW 256
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
29-225 1.19e-30

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 113.00  E-value: 1.19e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   29 IIFFGFFVMFLVsggIYFFgnsFKFNLKRSD--------SRMIELILQVLIVNFLIMMAGPGFWLIQYQGRMfRQSELTL 100
Cdd:COG1622  43 MLVIFVLVFGLL---LYFA---IRYRRRKGDadpaqfhhNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDA-PEDPLTV 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944  101 KVIGHQWYWSYEYGDSGKLcfdsfmkslddlslgdfrlfdVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNG 180
Cdd:COG1622 116 EVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPG 174

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 2735944  181 LLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGW 225
Cdd:COG1622 175 RVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 22-225 1.40e-29

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: 109.39  E-value: 1.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944     22 IHNYYSHIIFFGFFVMFLVSGG-IYFFgnsFKFNLKRSD--------SRMIELILQVLIVNFLIMMAGPGFWLIQYQGRM 92
Cdd:TIGR02866   9 IAFLFLFVLAVSTLISLLVAALlAYVV---WKFRRKGDEekpsqihgNRRLEYVWTVIPLIIVVGLFAATAKGLLYLERP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944     93 FRQSELTLKVIGHQWYWSYEYGDSGklcfdsfmkslddlslgdfrlFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCF 172
Cdd:TIGR02866  86 IPKDALKVKVTGYQWWWDFEYPESG---------------------FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELG 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2735944    173 IKMDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLELTSLECWKGW 225
Cdd:TIGR02866 145 GKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 96-215 2.51e-29

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 108.50  E-value: 2.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944    96 SELTLKVIGHQWYWSYEYGDSGklCFDSFMKSLddlslgdfrLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKM 175
Cdd:MTH00047  80 SSETIKVIGHQWYWSYEYSFGG--SYDSFMTDD---------IFGVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKM 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 2735944   176 DALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLE 215
Cdd:MTH00047 149 DAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 121-220 2.43e-25

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 97.20  E-value: 2.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   121 FDSFMKSLDDLSLGDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNGLLTKVTCSFSCSGLFFGQCS 200
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|
gi 2735944   201 EICGANHSFMPIVLELTSLE 220
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVSPE 150
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 97-210 8.76e-22

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: 86.13  E-value: 8.76e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   97 ELTLKVIGHQWYWSYEYGDSgklcfdsfmkslddlslgDFRLFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMD 176
Cdd:cd04213   1 ALTIEVTGHQWWWEFRYPDE------------------PGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                        90       100       110
                ....*....|....*....|....*....|....
gi 2735944  177 ALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFM 210
Cdd:cd04213  63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 98-215 6.35e-18

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: 75.80  E-value: 6.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   98 LTLKVIGHQWYWSYEYGDSGklcfdsfmkslddlslgdfrlfdVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDA 177
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 2735944  178 LNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMPIVLE 215
Cdd:cd13842  58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 97-210 7.42e-18

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: 76.14  E-value: 7.42e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   97 ELTLKVIGHQWYWSYEYGDS-GKLCFDSFMKSlDDLslgdfrlfdvdnrcVLPVGVNVGVYCTSSDVIHSFAIPKCFIKM 175
Cdd:cd13919   1 ALVVEVTAQQWAWTFRYPGGdGKLGTDDDVTS-PEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQ 65

                        90       100       110
                ....*....|....*....|....*....|....*
gi 2735944  176 DALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFM 210
Cdd:cd13919  66 DAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-210 9.78e-16

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: 69.97  E-value: 9.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   98 LTLKVIGHQWYWSYEYGDSGKlcfdsfmkslddlslgdfrlfdVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDA 177
Cdd:cd13915   2 LEIQVTGRQWMWEFTYPNGKR----------------------EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                        90       100       110
                ....*....|....*....|....*....|...
gi 2735944  178 LNGLLTKVTCSFSCSGLFFGQCSEICGANHSFM 210
Cdd:cd13915  60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 99-210 5.29e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 68.59  E-value: 5.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   99 TLKVIGHQWYWSYEYGDSGklcfdsfmkslddlslgdfrlFDVDNRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDAL 178
Cdd:cd13914   2 EIEVEAYQWGWEFSYPEAN---------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 2735944  179 ----NGLLTKVTcsfsCSGLFFGQCSEICGANHSFM 210
Cdd:cd13914  61 pgqyNTIKTEAT----EEGEYQLYCAEYCGAGHSQM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-222 1.65e-11

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: 59.78  E-value: 1.65e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   98 LTLKVIGHQWYWSYEYGDSGKlcfdsfmkSLDDLslgdfrlfdvdnrcVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDA 177
Cdd:cd13918  33 LEVEVEGFQFGWQFEYPNGVT--------TGNTL--------------RVPADTPIALRVTSTDVFHTFGIPELRVKADA 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 2735944  178 LNGLLTKVTCSFSCSGLFFGQCSEICGANHSFMP---IVLELTSLECW 222
Cdd:cd13918  91 IPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTgdvIVMDEEEFEAW 138
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 143-210 2.67e-09

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: 52.96  E-value: 2.67e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2735944  143 NRCVLPVGVNVGVYCTSSDVIHSFAIPKCFIKMDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFM 210
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 99-210 1.20e-03

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: 36.98  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2735944   99 TLKVIGHQWYWSyeygdsgklcfdsfmkslddLSlgdfrlfdvdnRCVLPVGVNVGVYCTSSDVIHSFAI--PKCFI--K 174
Cdd:cd13916   2 VVAVTGHQWYWE--------------------LS-----------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQ 50

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 2735944  175 MDALNGLLTKVTCSFSCSGLFFGQCSEICGANHSFM 210
Cdd:cd13916  51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
 
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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