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Conserved domains on  [gi|1933122329|gb|QPD01007|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Sphingonotus eurasius]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-183 8.66e-118

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 332.56  E-value: 8.66e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   1 LSFFHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKT 80
Cdd:MTH00154   20 LIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  81 IGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRL 160
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179

                         170       180
                  ....*....|....*....|...
gi 1933122329 161 NQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00154  180 NQLNFLINRPGLFFGQCSEICGA 202
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-183 8.66e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 332.56  E-value: 8.66e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   1 LSFFHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKT 80
Cdd:MTH00154   20 LIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  81 IGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRL 160
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179

                         170       180
                  ....*....|....*....|...
gi 1933122329 161 NQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00154  180 NQLNFLINRPGLFFGQCSEICGA 202
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 76-183 1.17e-72

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: 215.13  E-value: 1.17e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  76 ITIKTIGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 155
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|....*...
gi 1933122329 156 TPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEICGA 110
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
76-183 2.90e-67

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 201.10  E-value: 2.90e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  76 ITIKTIGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 155
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*...
gi 1933122329 156 TPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGI 108
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
38-183 5.20e-35

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 122.63  E-value: 5.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  38 HGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKTIGRQWYWSYEYsdfinvefdtymtPEKDLEiddfrll 117
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA------- 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933122329 118 eVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:COG1622   135 -TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGT 199
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 10-183 8.10e-29

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 105.54  E-value: 8.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  10 IVLLLITAIVGYS-LSYMLMMNYTNRNMLHGH-LIETIWTALPA--VTLIFIALPSLRLLYLLDDSSNAMiTIKTIGRQW 85
Cdd:TIGR02866  22 LISLLVAALLAYVvWKFRRKGDEEKPSQIHGNrRLEYVWTVIPLiiVVGLFAATAKGLLYLERPIPKDAL-KVKVTGYQW 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  86 YWSYEYSDFinvefdtymtpekdleiddfrLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 165
Cdd:TIGR02866 101 WWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWF 159

                         170
                  ....*....|....*...
gi 1933122329 166 LVNRPGLFFGQCSDICGA 183
Cdd:TIGR02866 160 NADEPGVYYGFCAELCGA 177
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-183 8.66e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 332.56  E-value: 8.66e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   1 LSFFHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKT 80
Cdd:MTH00154   20 LIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  81 IGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRL 160
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179

                         170       180
                  ....*....|....*....|...
gi 1933122329 161 NQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00154  180 NQLNFLINRPGLFFGQCSEICGA 202
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-183 4.17e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 265.24  E-value: 4.17e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   1 LSFFHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKT 80
Cdd:MTH00117   20 LLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  81 IGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRL 160
Cdd:MTH00117  100 IGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRL 179

                         170       180
                  ....*....|....*....|...
gi 1933122329 161 NQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00117  180 NQTSFITTRPGVFYGQCSEICGA 202
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-183 6.60e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 262.18  E-value: 6.60e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   1 LSFFHDHTMIVLLLITAIVGYSLSyMLMMN-YTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIK 79
Cdd:MTH00140   20 LIFFHDHAMVVLVLIFSFVMYMLV-LLLFNkFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  80 TIGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGR 159
Cdd:MTH00140   99 AIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGR 178

                         170       180
                  ....*....|....*....|....
gi 1933122329 160 LNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00140  179 LNQLSFEPKRPGVFYGQCSEICGA 202
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-183 1.06e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 259.26  E-value: 1.06e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   1 LSFFHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKT 80
Cdd:MTH00139   20 LIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  81 IGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRL 160
Cdd:MTH00139  100 VGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRL 179

                         170       180
                  ....*....|....*....|...
gi 1933122329 161 NQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00139  180 NQVGFFINRPGVFYGQCSEICGA 202
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 4-183 1.75e-85

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 251.31  E-value: 1.75e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   4 FHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKTIGR 83
Cdd:MTH00008   23 FHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  84 QWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQG 163
Cdd:MTH00008  103 QWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQI 182

                         170       180
                  ....*....|....*....|
gi 1933122329 164 TFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00008  183 GFTITRPGVFYGQCSEICGA 202
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-183 7.48e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 249.62  E-value: 7.48e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   1 LSFFHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKT 80
Cdd:MTH00038   20 LIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  81 IGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRL 160
Cdd:MTH00038  100 IGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRL 179

                         170       180
                  ....*....|....*....|...
gi 1933122329 161 NQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00038  180 NQTTFFISRTGLFYGQCSEICGA 202
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 3-183 1.04e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 243.73  E-value: 1.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   3 FFHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKTIG 82
Cdd:MTH00168   22 LFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  83 RQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQ 162
Cdd:MTH00168  102 HQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQ 181

                         170       180
                  ....*....|....*....|.
gi 1933122329 163 GTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00168  182 LAFLSSRPGSFYGQCSEICGA 202
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-183 1.77e-79

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 235.77  E-value: 1.77e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   1 LSFFHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKT 80
Cdd:MTH00098   20 LLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  81 IGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRL 160
Cdd:MTH00098  100 MGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRL 179

                         170       180
                  ....*....|....*....|...
gi 1933122329 161 NQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00098  180 NQTTLMSTRPGLYYGQCSEICGS 202
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 4-183 6.36e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 229.28  E-value: 6.36e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   4 FHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKTIGR 83
Cdd:MTH00076   23 FHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  84 QWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQG 163
Cdd:MTH00076  103 QWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQT 182

                         170       180
                  ....*....|....*....|
gi 1933122329 164 TFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00076  183 SFIASRPGVYYGQCSEICGA 202
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 4-183 1.45e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 226.13  E-value: 1.45e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   4 FHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKTIGR 83
Cdd:MTH00129   23 FHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  84 QWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQG 163
Cdd:MTH00129  103 QWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQT 182

                         170       180
                  ....*....|....*....|
gi 1933122329 164 TFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00129  183 AFIASRPGVFYGQCSEICGA 202
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-183 3.44e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 225.15  E-value: 3.44e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   1 LSFFHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKT 80
Cdd:MTH00185   20 LIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  81 IGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRL 160
Cdd:MTH00185  100 MGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRL 179

                         170       180
                  ....*....|....*....|...
gi 1933122329 161 NQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00185  180 NQATFIISRPGLYYGQCSEICGA 202
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 3-183 4.98e-75

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 225.01  E-value: 4.98e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   3 FFHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKTIG 82
Cdd:MTH00023   31 FFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  83 RQWYWSYEYSDFI--NVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRL 160
Cdd:MTH00023  111 HQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRL 190

                         170       180
                  ....*....|....*....|...
gi 1933122329 161 NQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00023  191 NQTGFFIKRPGVFYGQCSEICGA 213
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 76-183 1.17e-72

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: 215.13  E-value: 1.17e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  76 ITIKTIGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 155
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|....*...
gi 1933122329 156 TPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEICGA 110
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 3-183 1.18e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 218.88  E-value: 1.18e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   3 FFHDHTMIVLLLITAIVGYSLSYMLMMNYTNRNMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKTIG 82
Cdd:MTH00051   24 FFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  83 RQWYWSYEYSDF--INVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRL 160
Cdd:MTH00051  104 HQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRL 183

                         170       180
                  ....*....|....*....|...
gi 1933122329 161 NQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00051  184 NQTSFFIKRPGVFYGQCSEICGA 206
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
76-183 2.90e-67

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 201.10  E-value: 2.90e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  76 ITIKTIGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 155
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*...
gi 1933122329 156 TPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGI 108
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-183 1.16e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 181.76  E-value: 1.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   4 FHDHTMIVLLLITAIVGYSLSYMLM-MNYTNR--NMLHGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSS-NAMITIK 79
Cdd:MTH00027   51 LHDQILFILTIIVGVVLWLIIRILLgNNYYSYywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSANITIK 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  80 TIGRQWYWSYEYSDF--INVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATP 157
Cdd:MTH00027  131 VTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVP 210

                         170       180
                  ....*....|....*....|....*.
gi 1933122329 158 GRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00027  211 GRINETGFLIKRPGIFYGQCSEICGA 236
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-183 1.22e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 165.18  E-value: 1.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329   1 LSFFHDHTMIVLLLITAIVGYSLSYMLMMNYT---NRNMLHGHLIETIWTALPAVTLIFIAL---PSLRLLYLLDDSSNa 74
Cdd:MTH00080   19 MDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNfyfKSKKIEYQFGELLCSVFPVLILLMQMVpslSLLYYYGLMNLDSN- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  75 mITIKTIGRQWYWSYEYSDFINVEFDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKID 154
Cdd:MTH00080   98 -LTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMD 176

                         170       180
                  ....*....|....*....|....*....
gi 1933122329 155 ATPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00080  177 AMSGILSTLCYSFPMPGVFYGQCSEICGA 205
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
38-183 5.20e-35

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 122.63  E-value: 5.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  38 HGHLIETIWTALPAVTLIFIALPSLRLLYLLDDSSNAMITIKTIGRQWYWSYEYsdfinvefdtymtPEKDLEiddfrll 117
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA------- 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933122329 118 eVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:COG1622   135 -TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGT 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 41-183 2.54e-29

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 106.96  E-value: 2.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  41 LIETIWTALPA-VTLIFIALPSLRLLYLLDDSSNAmiTIKTIGRQWYWSYEYSDfiNVEFDTYMTpekdleidDFRLLeV 119
Cdd:MTH00047   48 VLELLWTVVPTlLVLVLCFLNLNFITSDLDCFSSE--TIKVIGHQWYWSYEYSF--GGSYDSFMT--------DDIFG-V 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933122329 120 DNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:MTH00047  115 DKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGV 178
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 99-183 4.49e-29

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 105.29  E-value: 4.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  99 FDTYMTPEKDLEIDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFLVNRPGLFFGQCS 178
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130


                  ....*
gi 1933122329 179 DICGA 183
Cdd:PTZ00047  131 EMCGT 135
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 10-183 8.10e-29

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 105.54  E-value: 8.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  10 IVLLLITAIVGYS-LSYMLMMNYTNRNMLHGH-LIETIWTALPA--VTLIFIALPSLRLLYLLDDSSNAMiTIKTIGRQW 85
Cdd:TIGR02866  22 LISLLVAALLAYVvWKFRRKGDEEKPSQIHGNrRLEYVWTVIPLiiVVGLFAATAKGLLYLERPIPKDAL-KVKVTGYQW 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  86 YWSYEYSDFinvefdtymtpekdleiddfrLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 165
Cdd:TIGR02866 101 WWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWF 159

                         170
                  ....*....|....*...
gi 1933122329 166 LVNRPGLFFGQCSDICGA 183
Cdd:TIGR02866 160 NADEPGVYYGFCAELCGA 177
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 76-183 3.34e-20

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: 80.42  E-value: 3.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  76 ITIKTIGRQWYWSYEYSDfinvefdtymtpekdleiddfrlLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 155
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100
                  ....*....|....*....|....*...
gi 1933122329 156 TPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGL 85
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 76-183 6.03e-20

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: 79.97  E-value: 6.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  76 ITIKTIGRQWYWSYEYSDfinvefdtymtpekdleiDDFRLLEVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 155
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPD------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100
                  ....*....|....*....|....*...
gi 1933122329 156 TPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFCGA 91
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 76-183 4.30e-17

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: 72.67  E-value: 4.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  76 ITIKTIGRQWYWSYEYSDFinvefDTYMTPEKDLEIDDFRLlevdnrtilPMNTEVRVLTSASDVLHSWAVPALGIKIDA 155
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100
                  ....*....|....*....|....*...
gi 1933122329 156 TPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGL 95
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 76-182 6.44e-17

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: 71.89  E-value: 6.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  76 ITIKTIGRQWYWSYEYsdfinvefdtymtPEKDLEIddfrllevdNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 155
Cdd:cd13915     2 LEIQVTGRQWMWEFTY-------------PNGKREI---------NELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100
                  ....*....|....*....|....*..
gi 1933122329 156 TPGRLNQGTFLVNRPGLFFGQCSDICG 182
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCG 86
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-58 7.30e-13

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: 61.19  E-value: 7.30e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933122329   1 LSFFHDHTMIVLLLITAIVGYSLSYMLMmNY-------TNRNMLHGHLIETIWTALPAVTLIFIA 58
Cdd:pfam02790  20 LLELHDYIMFILTLILILVLYILVTCLI-RFnrrknpiTARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 76-183 8.27e-13

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: 61.66  E-value: 8.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  76 ITIKTIGRQWYWSYEYSDfinvefdtymtpekdLEIDDFrllevdNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 155
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPE---------------ANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100
                  ....*....|....*....|....*...
gi 1933122329 156 TPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYCGA 87
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 76-183 4.43e-09

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: 52.46  E-value: 4.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122329  76 ITIKTIGRQWYWSYEYSDfiNVEFDTYMtpekdleiddfrllevdnrtILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 155
Cdd:cd13918    33 LEVEVEGFQFGWQFEYPN--GVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPELRVKADA 90

                          90       100
                  ....*....|....*....|....*...
gi 1933122329 156 TPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:cd13918    91 IPGEYTSTWFEADEPGTYEAKCYELCGS 118
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 125-183 2.63e-03

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: 35.62  E-value: 2.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1933122329 125 LPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGA 87
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 121-183 3.78e-03

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: 35.22  E-value: 3.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933122329 121 NRTILPMNTEVR-VLTSASdVLHSWAVPALGIKIDATPGRLNQGTFLVNRPGLFFGQCSDICGA 183
Cdd:cd04212    25 NELVIPVGRPVNfRLTSDS-VMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGE 87
 
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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