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Conserved domains on  [gi|3913301|sp|O03893|]
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RecName: Full=Cytochrome c oxidase subunit 2; AltName: Full=Cytochrome c oxidase polypeptide II

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 1000633)

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

CATH:  1.10.287.90
EC:  7.1.1.9
Gene Ontology:  GO:0004129|GO:0005507
PubMed:  6307356|8083153
TCDB:  3.D.4.6.2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 super family cl31800
cytochrome c oxidase subunit II; Provisional
 1-187 1.31e-136

cytochrome c oxidase subunit II; Provisional


The actual alignment was detected with superfamily member MTH00117:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 381.18  E-value: 1.31e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301     1 AICSLVLYLLSLMLMEKLS-SNTVDAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTD 79
Cdd:MTH00117  33 LISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    80 FKDLAFDSYMIPTTELPSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIF 159
Cdd:MTH00117 113 YKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVF 192

                        170       180
                 ....*....|....*....|....*...
gi 3913301   160 YGQCSEICGANHSYMPIVVESTPLAHFE 187
Cdd:MTH00117 193 YGQCSEICGANHSFMPIVVESVPLKHFE 220
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-187 1.31e-136

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 381.18  E-value: 1.31e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301     1 AICSLVLYLLSLMLMEKLS-SNTVDAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTD 79
Cdd:MTH00117  33 LISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    80 FKDLAFDSYMIPTTELPSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIF 159
Cdd:MTH00117 113 YKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVF 192

                        170       180
                 ....*....|....*....|....*...
gi 3913301   160 YGQCSEICGANHSYMPIVVESTPLAHFE 187
Cdd:MTH00117 193 YGQCSEICGANHSFMPIVVESVPLKHFE 220
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 60-187 6.04e-93

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: 267.13  E-value: 6.04e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   60 PDLTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTELPSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKT 139
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 3913301  140 DAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTPLAHFE 187
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFL 128
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
62-181 5.07e-86

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 249.25  E-value: 5.07e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301     62 LTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTELPSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDA 141
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 3913301    142 IPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVEST 181
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
28-187 2.52e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 170.01  E-value: 2.52e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   28 VELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLafdsymipttelpsghfrlleVDH 107
Cdd:COG1622  79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301  108 RVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTPLAHFE 187
Cdd:COG1622 138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 28-187 2.40e-41

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: 138.67  E-value: 2.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301     28 VELIWTILPA-IVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYtdfkdlafdsymipttelPSGHFRlleVD 106
Cdd:TIGR02866  56 LEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    107 HRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTPLAHF 186
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194


                  .
gi 3913301    187 E 187
Cdd:TIGR02866 195 D 195
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-187 1.31e-136

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 381.18  E-value: 1.31e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301     1 AICSLVLYLLSLMLMEKLS-SNTVDAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTD 79
Cdd:MTH00117  33 LISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    80 FKDLAFDSYMIPTTELPSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIF 159
Cdd:MTH00117 113 YKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVF 192

                        170       180
                 ....*....|....*....|....*...
gi 3913301   160 YGQCSEICGANHSYMPIVVESTPLAHFE 187
Cdd:MTH00117 193 YGQCSEICGANHSFMPIVVESVPLKHFE 220
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 26-186 6.83e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 323.70  E-value: 6.83e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    26 QEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTELPSGHFRLLEV 105
Cdd:MTH00154  59 QEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDV 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   106 DHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTPLAH 185
Cdd:MTH00154 139 DNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNN 218


                 .
gi 3913301   186 F 186
Cdd:MTH00154 219 F 219
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 20-187 5.27e-112

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 318.97  E-value: 5.27e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    20 SNTVDAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTELPSGH 99
Cdd:MTH00098  53 TSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   100 FRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVE 179
Cdd:MTH00098 133 LRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLE 212


                 ....*...
gi 3913301   180 STPLAHFE 187
Cdd:MTH00098 213 LVPLKYFE 220
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 24-187 8.05e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 315.89  E-value: 8.05e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    24 DAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTELPSGHFRLL 103
Cdd:MTH00129  57 DSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   104 EVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTPL 183
Cdd:MTH00129 137 EADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPL 216


                 ....
gi 3913301   184 AHFE 187
Cdd:MTH00129 217 EHFE 220
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 17-187 1.46e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 315.18  E-value: 1.46e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    17 KLSS-NTVDAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTEL 95
Cdd:MTH00076  49 KLTNtNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    96 PSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMP 175
Cdd:MTH00076 129 TPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMP 208

                        170
                 ....*....|..
gi 3913301   176 IVVESTPLAHFE 187
Cdd:MTH00076 209 IVVEATPLNNFL 220
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 24-187 3.27e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 304.21  E-value: 3.27e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    24 DAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTELPSGHFRLL 103
Cdd:MTH00168  57 DSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   104 EVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTPL 183
Cdd:MTH00168 137 EVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPW 216


                 ....
gi 3913301   184 AHFE 187
Cdd:MTH00168 217 ETFE 220
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 23-187 5.50e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 296.41  E-value: 5.50e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    23 VDAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTELPSGHFRL 102
Cdd:MTH00185  56 LDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRL 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   103 LEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTP 182
Cdd:MTH00185 136 LETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVP 215


                 ....*
gi 3913301   183 LAHFE 187
Cdd:MTH00185 216 LEHFE 220
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 18-187 5.97e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 296.23  E-value: 5.97e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    18 LSSNT----VDAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTT 93
Cdd:MTH00038  47 FSSPTnrffLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTS 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    94 ELPSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSY 173
Cdd:MTH00038 127 DLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSF 206

                        170
                 ....*....|....
gi 3913301   174 MPIVVESTPLAHFE 187
Cdd:MTH00038 207 MPIVIESVPFNTFE 220
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 17-187 1.01e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 293.00  E-value: 1.01e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    17 KLSSNTV-DAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTEL 95
Cdd:MTH00140  49 KFSCRTIlEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENEL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    96 PSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMP 175
Cdd:MTH00140 129 ELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMP 208

                        170
                 ....*....|..
gi 3913301   176 IVVESTPLAHFE 187
Cdd:MTH00140 209 IVVEAVPLEDFV 220
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 18-186 3.49e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 288.92  E-value: 3.49e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    18 LSSNTVDAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTELPS 97
Cdd:MTH00139  51 TSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSS 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    98 GHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIV 177
Cdd:MTH00139 131 GEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIV 210


                 ....*....
gi 3913301   178 VESTPLAHF 186
Cdd:MTH00139 211 VEAISPKFF 219
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 17-179 1.88e-95

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 277.12  E-value: 1.88e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    17 KLSSNTV-DAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTEL 95
Cdd:MTH00008  49 KLSNRYIlEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    96 PSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMP 175
Cdd:MTH00008 129 SPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMP 208


                 ....
gi 3913301   176 IVVE 179
Cdd:MTH00008 209 IVLE 212
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 60-187 6.04e-93

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: 267.13  E-value: 6.04e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   60 PDLTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTELPSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKT 139
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 3913301  140 DAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTPLAHFE 187
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFL 128
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 21-186 1.91e-90

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 264.69  E-value: 1.91e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    21 NTVDAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKD--LAFDSYMIPTTELPSG 98
Cdd:MTH00023  63 FLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSG 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    99 HFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVV 178
Cdd:MTH00023 143 DFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVI 222


                 ....*...
gi 3913301   179 ESTPLAHF 186
Cdd:MTH00023 223 EAVSLDKY 230
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
62-181 5.07e-86

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 249.25  E-value: 5.07e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301     62 LTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTELPSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDA 141
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 3913301    142 IPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVEST 181
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 28-186 9.19e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 250.08  E-value: 9.19e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    28 VELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDF--KDLAFDSYMIPTTELPSGHFRLLEV 105
Cdd:MTH00051  63 IEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEV 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   106 DHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTPLAH 185
Cdd:MTH00051 143 DNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDK 222


                 .
gi 3913301   186 F 186
Cdd:MTH00051 223 Y 223
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 17-186 3.65e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 217.96  E-value: 3.65e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    17 KLSSNTVDAQEVELIWTILPAIVLILLALPSLQILYMMDEID-EPDLTLKAIGHQWYWSYEYTDFKDLAFDSYMIPTTEL 95
Cdd:MTH00080  52 YFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    96 PSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMP 175
Cdd:MTH00080 132 RLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMP 211

                        170
                 ....*....|.
gi 3913301   176 IVVESTPLAHF 186
Cdd:MTH00080 212 IAVEVTLLDNF 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 21-186 4.41e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 219.13  E-value: 4.41e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    21 NTVDAQEVELIWTILPAIVLILLALPSLQILYMMDE-IDEPDLTLKAIGHQWYWSYEYTDF--KDLAFDSYMIPTTELPS 97
Cdd:MTH00027  85 NKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEF 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    98 GHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIV 177
Cdd:MTH00027 165 GDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIV 244


                 ....*....
gi 3913301   178 VESTPLAHF 186
Cdd:MTH00027 245 VESVSLSKY 253
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
28-187 2.52e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 170.01  E-value: 2.52e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   28 VELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYTDFKDLafdsymipttelpsghfrlleVDH 107
Cdd:COG1622  79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301  108 RVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTPLAHFE 187
Cdd:COG1622 138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 24-179 1.43e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 151.65  E-value: 1.43e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    24 DAQEVELIWTILPA-IVLILLALPSLQILYMMDeiDEPDLTLKAIGHQWYWSYEYTDfkDLAFDSYMiptTELPSGhfrl 102
Cdd:MTH00047  45 ENQVLELLWTVVPTlLVLVLCFLNLNFITSDLD--CFSSETIKVIGHQWYWSYEYSF--GGSYDSFM---TDDIFG---- 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3913301   103 leVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVE 179
Cdd:MTH00047 114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 28-187 2.40e-41

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: 138.67  E-value: 2.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301     28 VELIWTILPA-IVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWSYEYtdfkdlafdsymipttelPSGHFRlleVD 106
Cdd:TIGR02866  56 LEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    107 HRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTPLAHF 186
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194


                  .
gi 3913301    187 E 187
Cdd:TIGR02866 195 D 195
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 84-180 6.94e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 126.09  E-value: 6.94e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    84 AFDSYMIPTTELPSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQC 163
Cdd:PTZ00047  50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                         90
                 ....*....|....*..
gi 3913301   164 SEICGANHSYMPIVVES 180
Cdd:PTZ00047 130 SEMCGTLHGFMPIVVEA 146
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 62-179 1.14e-31

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 110.46  E-value: 1.14e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   62 LTLKAIGHQWYWSYEYTDfkdlafdsymipttelpsghfrlLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDA 141
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 3913301  142 IPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVE 179
Cdd:cd13842  58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 61-174 1.29e-28

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: 102.70  E-value: 1.29e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   61 DLTLKAIGHQWYWSYEYtdfkdlafdsymipttelPSGHFRLLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTD 140
Cdd:cd04213   1 ALTIEVTGHQWWWEFRY------------------PDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                        90       100       110
                ....*....|....*....|....*....|....
gi 3913301  141 AIPGRLNQTSFITTRPGIFYGQCSEICGANHSYM 174
Cdd:cd04213  63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 61-179 8.82e-24

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: 90.39  E-value: 8.82e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   61 DLTLKAIGHQWYWSYEY--TDFKDLAFDSYMIPTTELPSGHfrllevdhrvvvpmesPIRVIVTAGDVLHSWAVPTLGVK 138
Cdd:cd13919   1 ALVVEVTAQQWAWTFRYpgGDGKLGTDDDVTSPELHLPVGR----------------PVLFNLRSKDVIHSFWVPEFRVK 64

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 3913301  139 TDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYM--PIVVE 179
Cdd:cd13919  65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 38-187 1.68e-22

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: 88.28  E-value: 1.68e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   38 IVLILLALPSLQILYMMD---EIDEPDLTLKAIGHQWYWSYEYTDFKDLAfdSYMipttelpsghfrllevdhrvVVPME 114
Cdd:cd13918   6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTG--NTL--------------------RVPAD 63

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3913301  115 SPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTPLAHFE 187
Cdd:cd13918  64 TPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFE 136
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 61-178 7.59e-22

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: 85.37  E-value: 7.59e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   61 DLTLKAIGHQWYWSYEYtdfkdlafdsymipttelPSGhfrlLEVDHRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTD 140
Cdd:cd13915   1 ALEIQVTGRQWMWEFTY------------------PNG----KREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 3913301  141 AIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVV 178
Cdd:cd13915  59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 63-174 2.39e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 71.29  E-value: 2.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   63 TLKAIGHQWYWSYEYTDFKdlafdsymIPTTElpsghfrllevdhRVVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAI 142
Cdd:cd13914   2 EIEVEAYQWGWEFSYPEAN--------VTTSE-------------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                        90       100       110
                ....*....|....*....|....*....|..
gi 3913301  143 PGRLNQTSFITTRPGIFYGQCSEICGANHSYM 174
Cdd:cd13914  61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 109-179 4.45e-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: 51.80  E-value: 4.45e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3913301  109 VVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYM--PIVVE 179
Cdd:cd13913  27 IEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 20-50 4.84e-08

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 48.87  E-value: 4.84e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 3913301     20 SNTVDAQEVELIWTILPAIVLILLALPSLQI 50
Cdd:pfam02790  59 RYTTHGQTIEIIWTIIPAVILILIALPSFKL 89
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 63-174 2.51e-06

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: 44.29  E-value: 2.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301   63 TLKAIGHQWYWSyeytdfkdlafdsymIPTTELPSGhfrllevdhrvvvpmeSPIRVIVTAGDVLHSWAV----PTLGVK 138
Cdd:cd13916   2 VVAVTGHQWYWE---------------LSRTEIPAG----------------KPVEFRVTSADVNHGFGIydpdMRLLAQ 50

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 3913301  139 TDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYM 174
Cdd:cd13916  51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 100-179 4.97e-04

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 38.37  E-value: 4.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301  100 FRLLEVDHRVVVPMESPIRVIVT-AGDVLHSWAVPTLGVKTDAI---------------PGRLNQTSFITTRPGIFYGQC 163
Cdd:cd00920  16 GVLLFGPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYWFYC 95

                        90
                ....*....|....*.
gi 3913301  164 SEICGaNHSYMPIVVE 179
Cdd:cd00920  96 TIPGH-NHAGMVGTIN 110
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 117-174 5.91e-04

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


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 37.60  E-value: 5.91e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3913301  117 IRVIVT----AGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYM 174
Cdd:cd04223  26 VTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 109-181 8.58e-04

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: 37.14  E-value: 8.58e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3913301  109 VVVPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVEST 181
Cdd:cd04212  27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 17-182 2.09e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 37.86  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    17 KLSSNTVDAQEVELI-WTIlPAIVLILLALPSLQILYMMDEI-----DEPDLTLKAIGHQWYWSYEYTD-----FKDLAF 85
Cdd:PRK10525  77 KYSPNWSHSNKVEAVvWTV-PILIIIFLAVLTWKTTHALEPSkplahDEKPITIEVVSMDWKWFFIYPEqgiatVNEIAF 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913301    86 dsymipttelpsghfrllevdhrvvvPMESPIRVIVTAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSE 165
Cdd:PRK10525 156 --------------------------PANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISAS 209

                        170
                 ....*....|....*..
gi 3913301   166 ICGANHSYMPIVVESTP 182
Cdd:PRK10525 210 YSGPGFSGMKFKAIATP 226
 
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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