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Conserved domains on  [gi|1184519443|ref|WP_085089574|]
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cytochrome c oxidase subunit II [Azospirillum oryzae]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11446873)

cytochrome c oxidase subunit II, together with subunit I, forms the functional core of the enzyme that catalyzes the reduction of O2 and simultaneously pump protons across the membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 128-256 2.05e-95

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: 276.76  E-value: 2.05e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 128 DMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKD 207
Cdd:cd13912     2 SLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1184519443 208 GVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAW 256
Cdd:cd13912    82 AVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-266 4.20e-84

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


:

Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 251.67  E-value: 4.20e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443   1 MRRQSLYAAGLAAVLSmvggwgattalaneprpWEMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVVRFNA 80
Cdd:COG1622     1 MKRLLLALLLLALLLS-----------------GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRR 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  81 QRNP-VPSKTSHHTVLEVAWTVVPVIILIVIAVPSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITfssymipe 159
Cdd:COG1622    64 RKGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-------- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 160 tdlkpgqrrllevDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHG 239
Cdd:COG1622   136 -------------VNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHA 202

                         250       260
                  ....*....|....*....|....*..
gi 1184519443 240 FMPIAVEAVSREAFDAWVAKAKTAFAP 266
Cdd:COG1622   203 GMRFKVVVVSPEEFDAWLAEQKASAAT 229
 
Name Accession Description Interval E-value
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 128-256 2.05e-95

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: 276.76  E-value: 2.05e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 128 DMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKD 207
Cdd:cd13912     2 SLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1184519443 208 GVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAW 256
Cdd:cd13912    82 AVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 36-259 2.73e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 270.16  E-value: 2.73e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  36 MGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVVRFNAQRNpvpskTSHHTVLEVAWTVVPVIILIVIAVPSF 115
Cdd:MTH00154    7 LSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRF-----LLEGQEIEIIWTILPAIILIFIALPSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 116 KLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGDVIH 195
Cdd:MTH00154   82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184519443 196 SWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWVAK 259
Cdd:MTH00154  162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-266 4.20e-84

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 251.67  E-value: 4.20e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443   1 MRRQSLYAAGLAAVLSmvggwgattalaneprpWEMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVVRFNA 80
Cdd:COG1622     1 MKRLLLALLLLALLLS-----------------GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRR 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  81 QRNP-VPSKTSHHTVLEVAWTVVPVIILIVIAVPSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITfssymipe 159
Cdd:COG1622    64 RKGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-------- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 160 tdlkpgqrrllevDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHG 239
Cdd:COG1622   136 -------------VNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHA 202

                         250       260
                  ....*....|....*....|....*..
gi 1184519443 240 FMPIAVEAVSREAFDAWVAKAKTAFAP 266
Cdd:COG1622   203 GMRFKVVVVSPEEFDAWLAEQKASAAT 229
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
129-248 3.64e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 232.69  E-value: 3.64e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 129 MTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDG 208
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1184519443 209 VPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAV 248
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 55-258 1.79e-58

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: 185.66  E-value: 1.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  55 LLTVIITLIVILVAGLLAYCVVRF-NAQRNPVPSKTSHHTVLEVAWTVVPVIILIVIAVPSF-KLLYAAERIPQADMTIK 132
Cdd:TIGR02866  15 FVLAVSTLISLLVAALLAYVVWKFrRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAkGLLYLERPIPKDALKVK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 133 VTGHQWYWDYEYPDHGnitfssymipetdlkpgqrrlLEVDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDGVPGR 212
Cdd:TIGR02866  95 VTGYQWWWDFEYPESG---------------------FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQ 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1184519443 213 INETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWVA 258
Cdd:TIGR02866 154 TNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 31-100 3.25e-15

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: 69.28  E-value: 3.25e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184519443  31 PRPWEMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVVRFNAQRNPVPSK-TSHHTVLEVAWT 100
Cdd:pfam02790   2 PTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARyTTHGQTIEIIWT 72
 
Name Accession Description Interval E-value
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 128-256 2.05e-95

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: 276.76  E-value: 2.05e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 128 DMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKD 207
Cdd:cd13912     2 SLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1184519443 208 GVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAW 256
Cdd:cd13912    82 AVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 36-259 2.73e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 270.16  E-value: 2.73e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  36 MGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVVRFNAQRNpvpskTSHHTVLEVAWTVVPVIILIVIAVPSF 115
Cdd:MTH00154    7 LSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRF-----LLEGQEIEIIWTILPAIILIFIALPSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 116 KLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGDVIH 195
Cdd:MTH00154   82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184519443 196 SWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWVAK 259
Cdd:MTH00154  162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 36-257 2.31e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 254.86  E-value: 2.31e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  36 MGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVvrFNaqrnpvpsKTSHHTV-----LEVAWTVVPVIILIVI 110
Cdd:MTH00140    7 LGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLL--FN--------KFSCRTIleaqkLETIWTIVPALILVFL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 111 AVPSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTA 190
Cdd:MTH00140   77 ALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTS 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184519443 191 GDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWV 257
Cdd:MTH00140  157 ADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWL 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 31-259 3.04e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 252.14  E-value: 3.04e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  31 PRPWEMGMQPSASPVKHLMTSFND---LLTVIITLIVILVAGLLaycvvrfnaqrnpVPSKTSH-HTV----LEVAWTVV 102
Cdd:MTH00117    2 ANPSQLGFQDASSPIMEELLFFHDhalMVALLISSLVLYLLTLM-------------LTTKLTHtNTVdaqeVELIWTIL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 103 PVIILIVIAVPSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNT 182
Cdd:MTH00117   69 PAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMES 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184519443 183 TVRVLVTAGDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWVAK 259
Cdd:MTH00117  149 PIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-266 4.20e-84

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 251.67  E-value: 4.20e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443   1 MRRQSLYAAGLAAVLSmvggwgattalaneprpWEMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVVRFNA 80
Cdd:COG1622     1 MKRLLLALLLLALLLS-----------------GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRR 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  81 QRNP-VPSKTSHHTVLEVAWTVVPVIILIVIAVPSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITfssymipe 159
Cdd:COG1622    64 RKGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-------- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 160 tdlkpgqrrllevDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHG 239
Cdd:COG1622   136 -------------VNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHA 202

                         250       260
                  ....*....|....*....|....*..
gi 1184519443 240 FMPIAVEAVSREAFDAWVAKAKTAFAP 266
Cdd:COG1622   203 GMRFKVVVVSPEEFDAWLAEQKASAAT 229
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 36-259 1.03e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 250.67  E-value: 1.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  36 MGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYC-----VVRFNAQRNpvpsktshhtVLEVAWTVVPVIILIVI 110
Cdd:MTH00168    7 LGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLvtskyTNRFLLDSQ----------MIEFVWTIIPAFILISL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 111 AVPSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTA 190
Cdd:MTH00168   77 ALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTS 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184519443 191 GDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWVAK 259
Cdd:MTH00168  157 ADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 34-257 3.17e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 249.63  E-value: 3.17e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  34 W-EMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVVRFNAQRNPVPSKtshhtVLEVAWTVVPVIILIVIAV 112
Cdd:MTH00139    4 WgQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQ-----EVETIWTVLPAFILLFLAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 113 PSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGD 192
Cdd:MTH00139   79 PSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAAD 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184519443 193 VIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWV 257
Cdd:MTH00139  159 VLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 33-258 5.00e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 246.54  E-value: 5.00e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  33 PWEMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVVRFNAQRNPVPSKTshhtvLEVAWTVVPVIILIVIAV 112
Cdd:MTH00038    4 WLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQE-----LETIWTIVPAFILIFIAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 113 PSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGD 192
Cdd:MTH00038   79 PSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSAD 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184519443 193 VIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWVA 258
Cdd:MTH00038  159 VLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 29-258 3.09e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 239.68  E-value: 3.09e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  29 NEPRPWEMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLlaycVVRFNAQRNPVPSKTSHhTVLEVAWTVVPVIILI 108
Cdd:MTH00051    2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWL----IIRALTTKYYHKYLFEG-TLIEIIWTLIPAAILI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 109 VIAVPSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGN--ITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRV 186
Cdd:MTH00051   77 FIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTdtIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184519443 187 LVTAGDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWVA 258
Cdd:MTH00051  157 LVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVA 228
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 31-257 7.22e-79

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 238.88  E-value: 7.22e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  31 PRPWEMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVVRFNAQRNPVPSktshhTVLEVAWTVVPVIILIVI 110
Cdd:MTH00023   11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDG-----TFLEIVWTIIPAVILVFI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 111 AVPSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHG--NITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLV 188
Cdd:MTH00023   86 ALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILV 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184519443 189 TAGDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWV 257
Cdd:MTH00023  166 TGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
129-248 3.64e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 232.69  E-value: 3.64e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 129 MTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDG 208
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1184519443 209 VPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAV 248
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 35-259 6.83e-78

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 235.91  E-value: 6.83e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  35 EMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAglLAYCVVRFNAQRNPVPSKTSHhtvLEVAWTVVPVIILIVIAVPS 114
Cdd:MTH00008    6 QLMFQDAASPVMLQLISFHDHALLILTLVLTVVG--YAMTSLMFNKLSNRYILEAQQ---IETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 115 FKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGDVI 194
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184519443 195 HSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWVAK 259
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 31-256 1.06e-77

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 235.38  E-value: 1.06e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  31 PRPWEMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVVrfnaqrnpvpSKTSHHTVL-----EVAWTVVPVI 105
Cdd:MTH00098    2 AYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLT----------TKLTHTSTMdaqevETIWTILPAI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 106 ILIVIAVPSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVR 185
Cdd:MTH00098   72 ILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIR 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184519443 186 VLVTAGDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAW 256
Cdd:MTH00098  152 MLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 32-256 3.94e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 234.22  E-value: 3.94e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  32 RPWEMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAgllaYCVVRFnaqrnpVPSKTSHHTVL-----EVAWTVVPVII 106
Cdd:MTH00129    3 HPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVL----YIIVAM------VSTKLTNKYILdsqeiEIIWTVLPAVI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 107 LIVIAVPSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRV 186
Cdd:MTH00129   73 LILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRV 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 187 LVTAGDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAW 256
Cdd:MTH00129  153 LVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 33-262 1.37e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 225.04  E-value: 1.37e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  33 PWEMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVVRFNAQRNPVPSKTshhtvLEVAWTVVPVIILIVIAV 112
Cdd:MTH00076    4 PSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQE-----IEMVWTIMPAIILIVIAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 113 PSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGD 192
Cdd:MTH00076   79 PSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAED 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 193 VIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWVAKAKT 262
Cdd:MTH00076  159 VLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 33-259 1.94e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 224.76  E-value: 1.94e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  33 PWEMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVVRFNAQRNPVPSKTshhtvLEVAWTVVPVIILIVIAV 112
Cdd:MTH00185    4 PSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQE-----IEIVWTILPAIILIMIAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 113 PSFKLLYAAERIPQADMTIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGD 192
Cdd:MTH00185   79 PSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAED 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184519443 193 VIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWVAK 259
Cdd:MTH00185  159 VLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSL 225
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 28-259 5.27e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 212.19  E-value: 5.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  28 ANEPrpWEMGMQPSASPVKHLMTSFNDLLTVIITLIVilvaGLLAYCVVRFNAQRNPVPSKTSH--HTVLEVAWTVVPVI 105
Cdd:MTH00027   29 ANEP--WQLGFQDAGSPVMEEIIMLHDQILFILTIIV----GVVLWLIIRILLGNNYYSYYWNKldGSLIEVIWTLIPAF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 106 ILIVIAVPSFKLLYAA-ERIPQADMTIKVTGHQWYWDYEYPDHG--NITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNT 182
Cdd:MTH00027  103 ILILIAFPSLRLLYIMdECGFSANITIKVTGHQWYWSYSYEDYGekNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDT 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184519443 183 TVRVLVTAGDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWVAK 259
Cdd:MTH00027  183 NVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 51-256 7.73e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 210.64  E-value: 7.73e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  51 SFNDLLTVIITLIVILVAGLLAYCVVRFNAQrnpvpSKTSHHTVLEVAWTVVPVIILIVIAVPSFKLLYAAERIP-QADM 129
Cdd:MTH00080   24 NFNCSLLFGEFVLAFVVFLFLYLISNNFYFK-----SKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 130 TIKVTGHQWYWDYEYPDHGNITFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDGV 209
Cdd:MTH00080   99 TVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1184519443 210 PGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAW 256
Cdd:MTH00080  179 SGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEW 225
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 55-258 1.79e-58

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: 185.66  E-value: 1.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443  55 LLTVIITLIVILVAGLLAYCVVRF-NAQRNPVPSKTSHHTVLEVAWTVVPVIILIVIAVPSF-KLLYAAERIPQADMTIK 132
Cdd:TIGR02866  15 FVLAVSTLISLLVAALLAYVVWKFrRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAkGLLYLERPIPKDALKVK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 133 VTGHQWYWDYEYPDHGnitfssymipetdlkpgqrrlLEVDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDGVPGR 212
Cdd:TIGR02866  95 VTGYQWWWDFEYPESG---------------------FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQ 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1184519443 213 INETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWVA 258
Cdd:TIGR02866 154 TNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 151-259 3.86e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 149.97  E-value: 3.86e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 151 TFSSYMIPETDLKPGQRRLLEVDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQC 230
Cdd:PTZ00047   50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                          90       100
                  ....*....|....*....|....*....
gi 1184519443 231 SEICGTNHGFMPIAVEAVSREAFDAWVAK 259
Cdd:PTZ00047  130 SEMCGTLHGFMPIVVEAVSPEAYAAHAKK 158
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 130-248 8.99e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 137.39  E-value: 8.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 130 TIKVTGHQWYWDYEYPDhgNITFSSYMIPETDLkpgqrrlleVDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDGV 209
Cdd:MTH00047   83 TIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAI 151

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1184519443 210 PGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAV 248
Cdd:MTH00047  152 PGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 128-248 1.91e-31

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


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 112.71  E-value: 1.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 128 DMTIKVTGHQWYWDYEYPDhgnitfssymipetdlkpGQRRLLEVDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKD 207
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPD------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1184519443 208 GVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAV 248
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 129-246 3.38e-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: 111.62  E-value: 3.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 129 MTIKVTGHQWYWDYEYPDHGnitfssymipetdlkpgqrrlleVDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDG 208
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVR-----------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1184519443 209 VPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVE 246
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 128-241 4.82e-31

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 111.96  E-value: 4.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 128 DMTIKVTGHQWYWDYEYPDhGNITFSSYMIPETdlkpgqrrllevdNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKD 207
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPG-GDGKLGTDDDVTS-------------PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1184519443 208 GVPGRINETWFKAEREGVYYGQCSEICGTNHGFM 241
Cdd:cd13919    67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 128-241 9.07e-31

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 110.80  E-value: 9.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 128 DMTIKVTGHQWYWDYEYPDhgnitfssymipetdlkpGQRRllevDNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKD 207
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPN------------------GKRE----INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1184519443 208 GVPGRINETWFKAEREGVYYGQCSEICGTNHGFM 241
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 115-257 1.65e-28

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: 106.39  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 115 FKLLYAAERIPQAD---MTIKVTGHQWYWDYEYPDHGnitfssymipetdlkpGQRrllevdNRVVVPVNTTVRVLVTAG 191
Cdd:cd13918    16 GMLLYVEDPPDEADedaLEVEVEGFQFGWQFEYPNGV----------------TTG------NTLRVPADTPIALRVTST 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184519443 192 DVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWV 257
Cdd:cd13918    74 DVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 130-257 7.97e-25

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: 95.55  E-value: 7.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 130 TIKVTGHQWYWDYEYPDHGNITFssymipetdlkpgqrrllevdNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDGV 209
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1184519443 210 PGRINETWFKAEREGVYYGQCSEICGTNHGFMPIAVEAVSREAFDAWV 257
Cdd:cd13914    61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 31-100 3.25e-15

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: 69.28  E-value: 3.25e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184519443  31 PRPWEMGMQPSASPVKHLMTSFNDLLTVIITLIVILVAGLLAYCVVRFNAQRNPVPSK-TSHHTVLEVAWT 100
Cdd:pfam02790   2 PTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARyTTHGQTIEIIWT 72
CyoA TIGR01433
cytochrome o ubiquinol oxidase subunit II; This enzyme catalyzes the oxidation of ubiquinol ...
 129-261 6.27e-12

cytochrome o ubiquinol oxidase subunit II; This enzyme catalyzes the oxidation of ubiquinol with the concomitant reduction of molecular oxygen to water. This acts as the terminal electron acceptor in the respiratory chain. Subunit II is responsible for binding and oxidation of the ubiquinone substrate. This sequence is closely related to QoxA, which oxidizes quinol in gram positive bacteria but which is in complex with subunits which utilize cytochromes a in the reduction of molecular oxygen. Slightly more distantly related is subunit II of cytochrome c oxidase which uses cyt. c as the oxidant. [Energy metabolism, Electron transport]


Pssm-ID: 213620 [Multi-domain]  Cd Length: 226  Bit Score: 63.69  E-value: 6.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 129 MTIKVTGHQWYWDYEYPDHGNITFssymipetdlkpgqrrllevdNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDG 208
Cdd:TIGR01433 115 ITIEVVALDWKWLFIYPEQGIATV---------------------NEIAFPVNTPINFKITSNSVMNSFFIPQLGSQIYA 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1184519443 209 VPGRINETWFKAEREGVYYGQCSEICGtnHGF--MPIAVEAVSREAFDAWVAKAK 261
Cdd:TIGR01433 174 MAGMQTKLHLIANEPGVYDGISANYSG--PGFsgMKFKAIATDRAAFDQWVAKAK 226
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 174-241 1.73e-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: 54.11  E-value: 1.73e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184519443 174 NRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFM 241
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 131-243 6.58e-08

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: 49.92  E-value: 6.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 131 IKVTGHQWYWDYEYPDhgnitfssymipetdlkpgqrRLLEVDNRVVVPVNTTVRV-LVTAGDVIHSWAIPAFGLKKDG- 208
Cdd:cd00920     1 ITVTASDWGWSFTYNG---------------------VLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAm 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1184519443 209 --------------VPGRINETWFKAEREGVYYGQCSEICGTNHGfMPI 243
Cdd:cd00920    60 agganpglvntlviGPGESAEVTFTTDQAGVYWFYCTIPGHNHAG-MVG 107
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 129-248 6.58e-08

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: 49.47  E-value: 6.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 129 MTIKVTGHQWYWDYEYPDHGNITFssymipetdlkpgqrrllevdNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDG 208
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQGIATV---------------------NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYA 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1184519443 209 VPGRINETWFKAEREGVYYGQCSEICGtnHGF--MPIAVEAV 248
Cdd:cd04212    60 MAGMQTQLHLIADKPGTYQGLSANYSG--EGFsdMKFKVLAV 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 130-241 4.66e-07

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: 46.99  E-value: 4.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 130 TIKVTGHQWYWdyeypdhgnitfssymipetdlkpgqrrllEVDnRVVVPVNTTVRVLVTAGDVIHSWAI--PAFGL--K 205
Cdd:cd13916     2 VVAVTGHQWYW------------------------------ELS-RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQ 50

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1184519443 206 KDGVPGRINETWFKAEREGVYYGQCSEICGTNHGFM 241
Cdd:cd13916    51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 129-261 2.38e-06

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 48.26  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184519443 129 MTIKVTGHQWYWDYEYPDHGNITFssymipetdlkpgqrrllevdNRVVVPVNTTVRVLVTAGDVIHSWAIPAFGLKKDG 208
Cdd:PRK10525  127 ITIEVVSMDWKWFFIYPEQGIATV---------------------NEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYA 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1184519443 209 VPGRINETWFKAEREGVYYGQCSEICGtnHGFMPIAVEAVS---REAFDAWVAKAK 261
Cdd:PRK10525  186 MAGMQTRLHLIANEPGTYDGISASYSG--PGFSGMKFKAIAtpdRAEFDQWVAKAK 239
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 174-238 3.93e-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: 38.76  E-value: 3.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184519443 174 NRVVVPVNTTVRVLVT----AGDVIHSWAIPAFGLKKDGVPGRINETWFKAEREGVYYGQCSEICGTNH 238
Cdd:cd04223    16 DIIEVKEGDEVTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALH 84
 
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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