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Conserved domains on  [gi|1213499732|gb|ASG92077|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Sphenarium variabile]

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
 1-161 6.80e-102

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 291.73  E-value: 6.80e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00154   32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  81 DFINIEFDAYMLPE-EQQSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGL 159
Cdd:MTH00154  112 DFKNIEFDSYMIPTnELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGL 191


                  ..
gi 1213499732 160 YF 161
Cdd:MTH00154  192 FF 193
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-161 6.80e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 291.73  E-value: 6.80e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00154   32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  81 DFINIEFDAYMLPE-EQQSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGL 159
Cdd:MTH00154  112 DFKNIEFDSYMIPTnELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGL 191


                  ..
gi 1213499732 160 YF 161
Cdd:MTH00154  192 FF 193
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-161 5.80e-60

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: 182.00  E-value: 5.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  64 ITIKSIGRQWYWSYEYSDFINIEFDAYMLPEEQQS-NKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDA 142
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEkGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90
                  ....*....|....*....
gi 1213499732 143 TPGRLNQSTFSINRPGLYF 161
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYY 101
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
64-161 8.73e-56

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 171.05  E-value: 8.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  64 ITIKSIGRQWYWSYEYSDFINIEFDAYMLPEEQ-QSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDA 142
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*....
gi 1213499732 143 TPGRLNQSTFSINRPGLYF 161
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFY 99
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
26-160 3.58e-31

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 111.84  E-value: 3.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  26 HGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYsdfiniefdaymlPEEQQsnkfrllD 105
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGI-------A 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1213499732 106 VDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGLY 160
Cdd:COG1622   135 TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTY 189
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-160 3.82e-25

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: 95.53  E-value: 3.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMiKFKNRN------MLHGH-LIETIWTMIPA-ITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQ 72
Cdd:TIGR02866  21 TLISLLVAALLAYVVW-KFRRKGdeekpsQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  73 WYWSYEYSDFiniefdaymlpeeqqsnkfrLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:TIGR02866 100 WWWDFEYPES--------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWF 159


                  ....*...
gi 1213499732 153 SINRPGLY 160
Cdd:TIGR02866 160 NADEPGVY 167
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-161 6.80e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 291.73  E-value: 6.80e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00154   32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  81 DFINIEFDAYMLPE-EQQSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGL 159
Cdd:MTH00154  112 DFKNIEFDSYMIPTnELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGL 191


                  ..
gi 1213499732 160 YF 161
Cdd:MTH00154  192 FF 193
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-161 2.54e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 232.14  E-value: 2.54e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00140   32 VLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  81 DFINIEFDAYMLPEEQ-QSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGL 159
Cdd:MTH00140  112 DFSVIEFDSYMVPENElELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGV 191


                  ..
gi 1213499732 160 YF 161
Cdd:MTH00140  192 FY 193
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-161 8.11e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 228.26  E-value: 8.11e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00117   32 LLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  81 DFINIEFDAYMLPE-EQQSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGL 159
Cdd:MTH00117  112 DYKDLSFDSYMIPTqDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGV 191


                  ..
gi 1213499732 160 YF 161
Cdd:MTH00117  192 FY 193
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-161 2.16e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 224.60  E-value: 2.16e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00139   32 IMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  81 DFINIEFDAYMLPEEQ-QSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGL 159
Cdd:MTH00139  112 DFKNLSFDSYMIPTEDlSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGV 191


                  ..
gi 1213499732 160 YF 161
Cdd:MTH00139  192 FY 193
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-161 1.99e-73

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 219.73  E-value: 1.99e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00008   32 TLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  81 DFINIEFDAYMLPEEQQS-NKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGL 159
Cdd:MTH00008  112 DFSNLEFDSYMLPTSDLSpGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGV 191


                  ..
gi 1213499732 160 YF 161
Cdd:MTH00008  192 FY 193
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-161 8.88e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 217.93  E-value: 8.88e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00168   32 VLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  81 DFINIEFDAYMLPEEQQSN-KFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGL 159
Cdd:MTH00168  112 DYNDLEFDSYMVPTQDLSPgQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGS 191


                  ..
gi 1213499732 160 YF 161
Cdd:MTH00168  192 FY 193
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-161 2.16e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 214.57  E-value: 2.16e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00038   32 TLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  81 DFINIEFDAYMLPEEQQSNKF-RLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGL 159
Cdd:MTH00038  112 DYNDLEFDSYMVPTSDLSTGLpRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGL 191


                  ..
gi 1213499732 160 YF 161
Cdd:MTH00038  192 FY 193
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 2-161 3.64e-66

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 201.10  E-value: 3.64e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   2 MITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYSD 81
Cdd:MTH00098   33 LISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  82 FINIEFDAYMLP-EEQQSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGLY 160
Cdd:MTH00098  113 YEDLSFDSYMIPtSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLY 192


                  .
gi 1213499732 161 F 161
Cdd:MTH00098  193 Y 193
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-161 6.22e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 200.50  E-value: 6.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   2 MITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYSD 81
Cdd:MTH00185   33 LISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  82 FINIEFDAYMLP-EEQQSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGLY 160
Cdd:MTH00185  113 YEQLEFDSYMTPtQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLY 192


                  .
gi 1213499732 161 F 161
Cdd:MTH00185  193 Y 193
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-161 9.63e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 200.01  E-value: 9.63e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00076   32 FLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  81 DFINIEFDAYMLP-EEQQSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGL 159
Cdd:MTH00076  112 DYEDLSFDSYMIPtQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGV 191


                  ..
gi 1213499732 160 YF 161
Cdd:MTH00076  192 YY 193
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-161 2.74e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 199.17  E-value: 2.74e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   2 MITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYSD 81
Cdd:MTH00129   33 LISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  82 FINIEFDAYMLPEEQQS-NKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGLY 160
Cdd:MTH00129  113 YEDLGFDSYMIPTQDLTpGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVF 192


                  .
gi 1213499732 161 F 161
Cdd:MTH00129  193 Y 193
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-161 1.83e-63

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 194.58  E-value: 1.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00023   41 IIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYS 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  81 DFI--NIEFDAYMLP-EEQQSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRP 157
Cdd:MTH00023  121 DYEgeTLEFDSYMVPtSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRP 200


                  ....
gi 1213499732 158 GLYF 161
Cdd:MTH00023  201 GVFY 204
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-161 2.70e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 188.84  E-value: 2.70e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00051   34 TIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYS 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  81 DF--INIEFDAYMLP-EEQQSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRP 157
Cdd:MTH00051  114 DYgtDTIEFDSYMIPtSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRP 193


                  ....
gi 1213499732 158 GLYF 161
Cdd:MTH00051  194 GVFY 197
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-161 5.80e-60

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: 182.00  E-value: 5.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  64 ITIKSIGRQWYWSYEYSDFINIEFDAYMLPEEQQS-NKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDA 142
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEkGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90
                  ....*....|....*....
gi 1213499732 143 TPGRLNQSTFSINRPGLYF 161
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYY 101
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
64-161 8.73e-56

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 171.05  E-value: 8.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  64 ITIKSIGRQWYWSYEYSDFINIEFDAYMLPEEQ-QSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDA 142
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*....
gi 1213499732 143 TPGRLNQSTFSINRPGLYF 161
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFY 99
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-161 2.35e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 159.42  E-value: 2.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   2 MITIIVGYSLNYIMMIKFKNR------NMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSN-NTLITIKSIGRQWY 74
Cdd:MTH00027   58 ILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSANITIKVTGHQWY 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  75 WSYEYSDF--INIEFDAYMLPE-EQQSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQST 151
Cdd:MTH00027  138 WSYSYEDYgeKNIEFDSYMIPTaDLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETG 217

                         170
                  ....*....|
gi 1213499732 152 FSINRPGLYF 161
Cdd:MTH00027  218 FLIKRPGIFY 227
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 13-161 1.67e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 145.92  E-value: 1.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  13 YIMMIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLD----DSNntlITIKSIGRQWYWSYEYSDFINIEFD 88
Cdd:MTH00080   46 LISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlmnlDSN---LTVKVTGHQWYWSYEFSDIPGLEFD 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1213499732  89 AYMLPEEQQS-NKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGLYF 161
Cdd:MTH00080  123 SYMKSLDQLRlGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFY 196
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
26-160 3.58e-31

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 111.84  E-value: 3.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  26 HGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYsdfiniefdaymlPEEQQsnkfrllD 105
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGI-------A 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1213499732 106 VDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGLY 160
Cdd:COG1622   135 TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTY 189
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 29-160 2.91e-27

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 100.80  E-value: 2.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  29 LIETIWTMIPaiTLIFIALPSLRLLYMLDDSN-NTLITIKSIGRQWYWSYEYSDfiNIEFDAYMlpeeqqsNKFRLLdVD 107
Cdd:MTH00047   48 VLELLWTVVP--TLLVLVLCFLNLNFITSDLDcFSSETIKVIGHQWYWSYEYSF--GGSYDSFM-------TDDIFG-VD 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1213499732 108 NRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGLY 160
Cdd:MTH00047  116 KPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVF 168
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-160 3.82e-25

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: 95.53  E-value: 3.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732   1 IMITIIVGYSLNYIMMiKFKNRN------MLHGH-LIETIWTMIPA-ITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQ 72
Cdd:TIGR02866  21 TLISLLVAALLAYVVW-KFRRKGdeekpsQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  73 WYWSYEYSDFiniefdaymlpeeqqsnkfrLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:TIGR02866 100 WWWDFEYPES--------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWF 159


                  ....*...
gi 1213499732 153 SINRPGLY 160
Cdd:TIGR02866 160 NADEPGVY 167
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 94-161 2.55e-19

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 79.48  E-value: 2.55e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1213499732  94 EEQQSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGLYF 161
Cdd:PTZ00047   59 EDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFY 126
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 64-160 6.19e-16

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: 68.86  E-value: 6.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  64 ITIKSIGRQWYWSYEYSDfiniefdaymlpeeqqsnkfrlLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDAT 143
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAV 58

                          90
                  ....*....|....*..
gi 1213499732 144 PGRLNQSTFSINRPGLY 160
Cdd:cd13842    59 PGYTSELWFVADKPGTY 75
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-160 6.10e-15

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 66.11  E-value: 6.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  64 ITIKSIGRQWYWSYEYsdfiniefdaymlPEEQQSnkfrlldvDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDAT 143
Cdd:cd13915     2 LEIQVTGRQWMWEFTY-------------PNGKRE--------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVV 60

                          90
                  ....*....|....*..
gi 1213499732 144 PGRLNQSTFSINRPGLY 160
Cdd:cd13915    61 PGRYTYLWFEATKPGEY 77
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-160 1.55e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 63.04  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  64 ITIKSIGRQWYWSYEYsdfiniefdaymlPEEQQSNKFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDAT 143
Cdd:cd13919     2 LVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAV 68

                          90
                  ....*....|....*..
gi 1213499732 144 PGRLNQSTFSINRPGLY 160
Cdd:cd13919    69 PGRTTRLWFTPTREGEY 85
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 64-161 3.33e-11

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: 56.47  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  64 ITIKSIGRQWYWSYEYSDFINIEFdaymlpeeQQSNKFRLldvdnrtlvPMNSEIRMLTSASDVLHSWTIPSMGIKVDAT 143
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGI--------VTANELHI---------PVGRPVRLRLTSADVIHSFWVPSLAGKMDMI 64

                          90
                  ....*....|....*...
gi 1213499732 144 PGRLNQSTFSINRPGLYF 161
Cdd:cd04213    65 PGRTNRLWLQADEPGVYR 82
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-52 2.38e-10

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: 54.26  E-value: 2.38e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1213499732   1 IMITIIVGYSLNYIMM------IKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRL 52
Cdd:pfam02790  32 TLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIALPSFKL 89
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-160 1.85e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 52.41  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  64 ITIKSIGRQWYWSYEYsdfiniefdaymlPEEQQSNkfrlldvDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDAT 143
Cdd:cd13914     1 VEIEVEAYQWGWEFSY-------------PEANVTT-------SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90
                  ....*....|....*..
gi 1213499732 144 PGRLNQSTFSINRPGLY 160
Cdd:cd13914    61 PGQYNTIKTEATEEGEY 77
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 52-160 1.13e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 48.22  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499732  52 LLYMLD---DSNNTLITIKSIGRQWYWSYEYSDfiniefdaymlpEEQQSNKFRlldvdnrtlVPMNSEIRMLTSASDVL 128
Cdd:cd13918    18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYPN------------GVTTGNTLR---------VPADTPIALRVTSTDVF 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1213499732 129 HSWTIPSMGIKVDATPGRLNQSTFSINRPGLY 160
Cdd:cd13918    77 HTFGIPELRVKADAIPGEYTSTWFEADEPGTY 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 112-160 5.00e-04

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: 37.55  E-value: 5.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1213499732 112 VPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSINRPGLY 160
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEY 77
 
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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