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Conserved domains on  [gi|1737619711|ref|YP_009688048|]
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cytochrome c oxidase subunit II (mitochondrion) [Echinococcus granulosus]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475882)

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 MTH00047
cytochrome c oxidase subunit II; Provisional
 1-193 1.56e-120

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 338.85  E-value: 1.56e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711   1 MNLSLLYYDIVCYIVAVCVFIVCFVYVLLCWNVVFGVGTVNFGSENQIIELVWTVIPTVVVLVLCALNVNFITSDLDCFS 80
Cdd:MTH00047    1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSGNGSVNFGSENQVLELLWTVVPTLLVLVLCFLNLNFITSDLDCFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  81 SETIKVVGHQWYWTYEY-FGGGYDSFPIGDYFVVDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFF 159
Cdd:MTH00047   81 SETIKVIGHQWYWSYEYsFGGSYDSFMTDDIFGVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFF 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1737619711 160 CPSQHGSFVGYCAELCGVNHSVMPIVVEVVGGCC 193
Cdd:MTH00047  161 CPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
 
Name Accession Description Interval E-value
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 1-193 1.56e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 338.85  E-value: 1.56e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711   1 MNLSLLYYDIVCYIVAVCVFIVCFVYVLLCWNVVFGVGTVNFGSENQIIELVWTVIPTVVVLVLCALNVNFITSDLDCFS 80
Cdd:MTH00047    1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSGNGSVNFGSENQVLELLWTVVPTLLVLVLCFLNLNFITSDLDCFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  81 SETIKVVGHQWYWTYEY-FGGGYDSFPIGDYFVVDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFF 159
Cdd:MTH00047   81 SETIKVIGHQWYWSYEYsFGGSYDSFMTDDIFGVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFF 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1737619711 160 CPSQHGSFVGYCAELCGVNHSVMPIVVEVVGGCC 193
Cdd:MTH00047  161 CPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
13-189 4.71e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 156.14  E-value: 4.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  13 YIVAVCVFIVCFVYVLLCWNVVF-----GVGTVNFGSENQIIELVWTVIPTVVVLVLCALNVnFITSDLDCFSSE--TIK 85
Cdd:COG1622    38 VSLIIMLVIFVLVFGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTL-RVLHALDDAPEDplTVE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  86 VVGHQWYWTYEYFGGGYdsfpigdyfVVDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQHG 165
Cdd:COG1622   117 VTGYQWKWLFRYPDQGI---------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPG 187

                         170       180
                  ....*....|....*....|....
gi 1737619711 166 SFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:COG1622   188 TYRGQCAELCGTGHAGMRFKVVVV 211
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 83-189 8.31e-43

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: 139.63  E-value: 8.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  83 TIKVVGHQWYWTYEYFGGG---YDSF-------PIGDY--FVVDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAV 150
Cdd:cd13912     4 TIKAIGHQWYWSYEYSDFNdleFDSYmipeddlEKGQLrlLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAV 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1737619711 151 PGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:cd13912    84 PGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAV 122
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
83-189 2.08e-38

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 128.30  E-value: 2.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  83 TIKVVGHQWYWTYEY--FGG-GYDSFPIGDYFVVDKPLRMV---------YGVPYHLVVTSSDVIHSFSVPSLNLKMDAV 150
Cdd:pfam00116   2 TIKAIGHQWYWSYEYtdFGDlEFDSYMIPTEDLEEGQLRLLevdnrvvlpVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1737619711 151 PGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-189 4.79e-37

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: 127.11  E-value: 4.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711   2 NLSLLYYDIVCYIVAVCVFIVC-FVYVLLCWNVVFGVGTVNFGSENQIIELVWTVIPTVVVLVLCALNVN---FITSDLD 77
Cdd:TIGR02866   8 QIAFLFLFVLAVSTLISLLVAAlLAYVVWKFRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKgllYLERPIP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  78 CfSSETIKVVGHQWYWTYEYFGGGydsfpigdyFVVDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHL 157
Cdd:TIGR02866  88 K-DALKVKVTGYQWWWDFEYPESG---------FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNAL 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1737619711 158 FFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:TIGR02866 158 WFNADEPGVYYGFCAELCGAGHSLMLFKVVVV 189
 
Name Accession Description Interval E-value
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 1-193 1.56e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 338.85  E-value: 1.56e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711   1 MNLSLLYYDIVCYIVAVCVFIVCFVYVLLCWNVVFGVGTVNFGSENQIIELVWTVIPTVVVLVLCALNVNFITSDLDCFS 80
Cdd:MTH00047    1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSGNGSVNFGSENQVLELLWTVVPTLLVLVLCFLNLNFITSDLDCFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  81 SETIKVVGHQWYWTYEY-FGGGYDSFPIGDYFVVDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFF 159
Cdd:MTH00047   81 SETIKVIGHQWYWSYEYsFGGSYDSFMTDDIFGVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFF 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1737619711 160 CPSQHGSFVGYCAELCGVNHSVMPIVVEVVGGCC 193
Cdd:MTH00047  161 CPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
13-189 4.71e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 156.14  E-value: 4.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  13 YIVAVCVFIVCFVYVLLCWNVVF-----GVGTVNFGSENQIIELVWTVIPTVVVLVLCALNVnFITSDLDCFSSE--TIK 85
Cdd:COG1622    38 VSLIIMLVIFVLVFGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTL-RVLHALDDAPEDplTVE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  86 VVGHQWYWTYEYFGGGYdsfpigdyfVVDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQHG 165
Cdd:COG1622   117 VTGYQWKWLFRYPDQGI---------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPG 187

                         170       180
                  ....*....|....*....|....
gi 1737619711 166 SFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:COG1622   188 TYRGQCAELCGTGHAGMRFKVVVV 211
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 13-190 2.19e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 154.37  E-value: 2.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  13 YIVAVCVFIVCFVYVLLcWNVVFGVGTVNFGSENQIIELVWTVIPTVVVLVLcALNVNFITSDLDCFSSE--TIKVVGHQ 90
Cdd:MTH00168   26 HALLILVLILTLVLYSL-LVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISL-ALPSLRLLYLMDEIDKPdlTIKAVGHQ 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  91 WYWTYEY--FGG-GYDSF-------PIGDYFVVDKPLRMV--YGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLF 158
Cdd:MTH00168  104 WYWSYEYtdYNDlEFDSYmvptqdlSPGQFRLLEVDNRLVlpMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLA 183

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1737619711 159 FCPSQHGSFVGYCAELCGVNHSVMPIVVEVVG 190
Cdd:MTH00168  184 FLSSRPGSFYGQCSEICGANHSFMPIVVEFVP 215
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 5-190 3.04e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 151.63  E-value: 3.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711   5 LLYYDIVCYIVAVCVFIVCFVYVLLCWNVVfgvgTVNFGSENQIIELVWTVIPTVVVLVLC-----ALNVNFITSDldcf 79
Cdd:MTH00140   21 IFFHDHAMVVLVLIFSFVMYMLVLLLFNKF----SCRTILEAQKLETIWTIVPALILVFLAlpslrLLYLLDETNN---- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  80 SSETIKVVGHQWYWTYEYFGGG---YDSF-------PIGDY--FVVDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKM 147
Cdd:MTH00140   93 PLLTVKAIGHQWYWSYEYSDFSvieFDSYmvpenelELGDFrlLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKV 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1737619711 148 DAVPGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVVG 190
Cdd:MTH00140  173 DAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVP 215
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 41-189 1.22e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 149.98  E-value: 1.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  41 NFGSENQIIELVWTVIPTVVVLVLC--ALNVNFITSDLDcFSSETIKVVGHQWYWTYEY--FGG-GYDSFPIGDYFV--- 112
Cdd:MTH00154   53 RFLLEGQEIEIIWTILPAIILIFIAlpSLRLLYLLDEVN-NPSITLKTIGHQWYWSYEYsdFKNiEFDSYMIPTNELenn 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711 113 ------VDKplRMV--YGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPI 184
Cdd:MTH00154  132 gfrlldVDN--RLVlpMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPI 209


                  ....*
gi 1737619711 185 VVEVV 189
Cdd:MTH00154  210 VIESV 214
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 13-189 1.44e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 144.84  E-value: 1.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  13 YIVAVCVFIVCFVYVLLCwNVVFGVGTVNFGSENQIIELVWTVIPTVVVLVLCALNVN---FITSDLDCFSseTIKVVGH 89
Cdd:MTH00038   26 YALIILTLITILVFYGLA-SLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQllyLMDEVNNPFL--TIKAIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  90 QWYWTYEYFGggYDSFPIGDYFV--------------VDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLN 155
Cdd:MTH00038  103 QWYWSYEYTD--YNDLEFDSYMVptsdlstglprlleVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLN 180

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1737619711 156 HLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:MTH00038  181 QTTFFISRTGLFYGQCSEICGANHSFMPIVIESV 214
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 83-189 8.31e-43

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: 139.63  E-value: 8.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  83 TIKVVGHQWYWTYEYFGGG---YDSF-------PIGDY--FVVDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAV 150
Cdd:cd13912     4 TIKAIGHQWYWSYEYSDFNdleFDSYmipeddlEKGQLrlLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAV 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1737619711 151 PGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:cd13912    84 PGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAV 122
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-189 1.48e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 142.16  E-value: 1.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711   1 MNLSLLYYDIVCYIVAVCVFIVCFVYVLLCWNvvfgvgtvNFGS----ENQIIELVWTVIPTVVVLVLCALNVNFITSdL 76
Cdd:MTH00139   17 MEQLIFFHDHAMVILIMILSFVGYISLSLMSN--------KFTSrsllESQEVETIWTVLPAFILLFLALPSLRLLYL-M 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  77 DCFS--SETIKVVGHQWYWTYEYF---GGGYDSFPI-------GDYFVVDKPLRMVygVPYH----LVVTSSDVIHSFSV 140
Cdd:MTH00139   88 DEVSdpYLTFKAVGHQWYWSYEYSdfkNLSFDSYMIptedlssGEFRLLEVDNRLV--LPYKsnirALITAADVLHSWTV 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1737619711 141 PSLNLKMDAVPGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:MTH00139  166 PSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAI 214
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 47-189 3.07e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 141.20  E-value: 3.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  47 QIIELVWTVIPtVVVLVLCAL----------NVNfiTSDLdcfsseTIKVVGHQWYWTYEYFGG---GYDSF-------P 106
Cdd:MTH00117   59 QEVELIWTILP-AIVLILLALpslrilylmdEIN--NPHL------TIKAIGHQWYWSYEYTDYkdlSFDSYmiptqdlP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711 107 IGDYFVVDKPLRMVY--GVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPI 184
Cdd:MTH00117  130 NGHFRLLEVDHRMVIpmESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPI 209


                  ....*
gi 1737619711 185 VVEVV 189
Cdd:MTH00117  210 VVESV 214
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 45-189 3.25e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 136.38  E-value: 3.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  45 ENQIIELVWTVIPTVVvLVLCALNVNFITSDLDCFSSE--TIKVVGHQWYWTYEYFGG---GYDSFPI-------GDYFV 112
Cdd:MTH00129   57 DSQEIEIIWTVLPAVI-LILIALPSLRILYLMDEINDPhlTIKAMGHQWYWSYEYTDYedlGFDSYMIptqdltpGQFRL 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737619711 113 VDKPLRMVYGV--PYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:MTH00129  136 LEADHRMVVPVesPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAV 214
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 45-189 1.60e-39

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 134.60  E-value: 1.60e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  45 ENQIIELVWTVIPTVVVLVLC--ALNVNFITSDLDCfSSETIKVVGHQWYWTYEY---FGGGYDSFPI-------GDYFV 112
Cdd:MTH00008   57 EAQQIETIWTILPALILLFLAfpSLRLLYLMDEVSN-PSITLKTIGHQWYWSYEYsdfSNLEFDSYMLptsdlspGQFRL 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711 113 VDKPLRMVygVPYHL----VVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEV 188
Cdd:MTH00008  136 LEVDNRAV--LPMQTeirvLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEA 213


                  .
gi 1737619711 189 V 189
Cdd:MTH00008  214 V 214
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 21-189 2.55e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 134.24  E-value: 2.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  21 IVCFVYVLLCWNVVFGVGTV---NFGSENQIIELVWTVIPTVVvLVLCALNVNFITSDLDCFSSE--TIKVVGHQWYWTY 95
Cdd:MTH00185   30 IVFLISTLVLYIIVAMVTTKltnKYILDSQEIEIVWTILPAII-LIMIALPSLRILYLMDEINDPhlTIKAMGHQWYWSY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  96 EYFGG---GYDSFPI-------GDYFVVDKPLRMVYGV--PYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQ 163
Cdd:MTH00185  109 EYTDYeqlEFDSYMTptqdltpGQFRLLETDHRMVVPMesPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISR 188

                         170       180
                  ....*....|....*....|....*.
gi 1737619711 164 HGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:MTH00185  189 PGLYYGQCSEICGANHSFMPIVVEAV 214
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 19-190 1.61e-38

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 132.18  E-value: 1.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  19 VFIVCFVYVLLCWNVVFGVGTVNFGS---ENQIIELVWTVIPTVVvLVLCALNVNFITSDLD--CFSSETIKVVGHQWYW 93
Cdd:MTH00023   37 MFLLIIIITVVLWLIVEALNGKFYDRflvDGTFLEIVWTIIPAVI-LVFIALPSLKLLYLMDevVSPALTIKAIGHQWYW 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  94 TYEY--FGG---GYDSFPI-------GDYFVVDKPLRMVYGVPYH--LVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFF 159
Cdd:MTH00023  116 SYEYsdYEGetlEFDSYMVptsdlnsGDFRLLEVDNRLVVPINTHvrILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGF 195

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1737619711 160 CPSQHGSFVGYCAELCGVNHSVMPIVVEVVG 190
Cdd:MTH00023  196 FIKRPGVFYGQCSEICGANHSFMPIVIEAVS 226
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
83-189 2.08e-38

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 128.30  E-value: 2.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  83 TIKVVGHQWYWTYEY--FGG-GYDSFPIGDYFVVDKPLRMV---------YGVPYHLVVTSSDVIHSFSVPSLNLKMDAV 150
Cdd:pfam00116   2 TIKAIGHQWYWSYEYtdFGDlEFDSYMIPTEDLEEGQLRLLevdnrvvlpVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1737619711 151 PGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 47-189 3.82e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 131.05  E-value: 3.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  47 QIIELVWTVIPTVVVLVLcALNVNFITSDLDCFSSE--TIKVVGHQWYWTYEY--FGG-GYDSFPI-------GDYFVVD 114
Cdd:MTH00076   59 QEIEMVWTIMPAIILIVI-ALPSLRILYLMDEINDPhlTVKAIGHQWYWSYEYtdYEDlSFDSYMIptqdltpGQFRLLE 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737619711 115 KPLRMV--YGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:MTH00076  138 VDNRMVvpMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEAT 214
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-188 3.95e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 130.90  E-value: 3.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711   6 LYYDIVCYivavCVFIVCFVYVLLCWNVVFGVGTVNFGSENQIIELVWTVIPTVVVLVLCALNVNFI-TSDLDCFSSE-T 83
Cdd:MTH00080   24 NFNCSLLF----GEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLyYYGLMNLDSNlT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  84 IKVVGHQWYWTYEY---FGGGYDSFP-------IGDYFVVDKPLRMV--YGVPYHLVVTSSDVIHSFSVPSLNLKMDAVP 151
Cdd:MTH00080  100 VKVTGHQWYWSYEFsdiPGLEFDSYMksldqlrLGEPRLLEVDNRCVlpCDTNIRFCITSSDVIHSWALPSLSIKMDAMS 179

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1737619711 152 GRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEV 188
Cdd:MTH00080  180 GILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEV 216
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 47-189 2.37e-37

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 129.07  E-value: 2.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  47 QIIELVWTVIPTVVvLVLCALNVNFITSDLDCFS--SETIKVVGHQWYWTYEY--FGG-GYDSFPI-------GDYFVVD 114
Cdd:MTH00098   59 QEVETIWTILPAII-LILIALPSLRILYMMDEINnpSLTVKTMGHQWYWSYEYtdYEDlSFDSYMIptsdlkpGELRLLE 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737619711 115 KPLRMVYGV--PYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:MTH00098  138 VDNRVVLPMemPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELV 214
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-189 4.79e-37

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: 127.11  E-value: 4.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711   2 NLSLLYYDIVCYIVAVCVFIVC-FVYVLLCWNVVFGVGTVNFGSENQIIELVWTVIPTVVVLVLCALNVN---FITSDLD 77
Cdd:TIGR02866   8 QIAFLFLFVLAVSTLISLLVAAlLAYVVWKFRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKgllYLERPIP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  78 CfSSETIKVVGHQWYWTYEYFGGGydsfpigdyFVVDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHL 157
Cdd:TIGR02866  88 K-DALKVKVTGYQWWWDFEYPESG---------FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNAL 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1737619711 158 FFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:TIGR02866 158 WFNADEPGVYYGFCAELCGAGHSLMLFKVVVV 189
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 45-189 5.19e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 128.36  E-value: 5.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  45 ENQIIELVWTVIPTVVVLVLCALNVNFITS-DLDCFSSETIKVVGHQWYWTYEYFGGGYDSFPIGDYFV----------- 112
Cdd:MTH00051   59 EGTLIEIIWTLIPAAILIFIAFPSLKLLYLmDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIptsdlnsgdlr 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711 113 ---VDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:MTH00051  139 lleVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGV 218
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 82-189 1.01e-30

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: 108.11  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  82 ETIKVVGHQWYWTYEYFGggYDSFPIGDYFVVDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCP 161
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPG--GDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTP 79

                          90       100
                  ....*....|....*....|....*...
gi 1737619711 162 SQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:cd13919    80 TREGEYEVRCAELCGLGHYRMRATVKVV 107
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 19-189 1.33e-30

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 112.43  E-value: 1.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  19 VFIVCFVYVLLCWNVVFGVGTVNFGS------ENQIIELVWTVIPTVVVLVLC--ALNVNFITSDLDCFSSETIKVVGHQ 90
Cdd:MTH00027   56 LFILTIIVGVVLWLIIRILLGNNYYSyywnklDGSLIEVIWTLIPAFILILIAfpSLRLLYIMDECGFSANITIKVTGHQ 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  91 WYWTYEYFGGGYDSFPIGDYFV--------------VDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNH 156
Cdd:MTH00027  136 WYWSYSYEDYGEKNIEFDSYMIptadlefgdlrlleVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINE 215

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1737619711 157 LFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:MTH00027  216 TGFLIKRPGIFYGQCSEICGANHSFMPIVVESV 248
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 81-189 1.07e-28

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


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 102.70  E-value: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  81 SETIKVVGHQWYWTYEYFGGGydsfpiGDYFVVDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFC 160
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEP------GRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQ 74

                          90       100
                  ....*....|....*....|....*....
gi 1737619711 161 PSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:cd04213    75 ADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-188 1.29e-28

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 102.32  E-value: 1.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  83 TIKVVGHQWYWTYEYFGGGYDSFPIgdYFVVDKPLRmvygvpyhLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPS 162
Cdd:cd13915     3 EIQVTGRQWMWEFTYPNGKREINEL--HVPVGKPVR--------LILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEAT 72

                          90       100
                  ....*....|....*....|....*.
gi 1737619711 163 QHGSFVGYCAELCGVNHSVMPIVVEV 188
Cdd:cd13915    73 KPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 82-189 1.22e-26

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: 97.86  E-value: 1.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  82 ETIKVVGHQWYWTYEYFGGGYDSFPigdyfvvdkPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCP 161
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEANVTTSE---------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEA 71

                          90       100
                  ....*....|....*....|....*...
gi 1737619711 162 SQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:cd13914    72 TEEGEYQLYCAEYCGAGHSQMLSTVTVV 99
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 82-187 2.27e-24

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: 91.59  E-value: 2.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  82 ETIKVVGHQWYWTYEYFGGGydsfpigdyfvVDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCP 161
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVR-----------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVA 69

                          90       100
                  ....*....|....*....|....*.
gi 1737619711 162 SQHGSFVGYCAELCGVNHSVMPIVVE 187
Cdd:cd13842    70 DKPGTYTIICAEYCGLGHSYMLGKVE 95
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 113-189 9.90e-21

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 84.10  E-value: 9.90e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737619711 113 VDKPLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:PTZ00047   71 VDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAV 147
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-189 2.31e-19

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: 79.81  E-value: 2.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  83 TIKVVGHQWYWTYEYFGGGYDsfpiGDYFVV--DKPLRmvygvpyhLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFC 160
Cdd:cd13918    34 EVEVEGFQFGWQFEYPNGVTT----GNTLRVpaDTPIA--------LRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFE 101

                          90       100
                  ....*....|....*....|....*....
gi 1737619711 161 PSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:cd13918   102 ADEPGTYEAKCYELCGSGHSLMTGDVIVM 130
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-189 1.34e-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: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 52.77  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  83 TIKVVGHQWYWTYeyfggGYDSFPIGDyfvvdkplrmvygvPYHLVVTSSDVIHSFSVPSLNLKM----DAVPGRLNHLF 158
Cdd:cd13916     2 VVAVTGHQWYWEL-----SRTEIPAGK--------------PVEFRVTSADVNHGFGIYDPDMRLlaqtQAMPGYTNVLR 62

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1737619711 159 FCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:cd13916    63 YTFDKPGTYTILCLEYCGLAHHVMMAEFTVV 93
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 116-189 1.47e-09

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 52.96  E-value: 1.47e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737619711 116 PLRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:cd13913    26 EIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 117-187 4.73e-06

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


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 43.13  E-value: 4.73e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737619711 117 LRMVYGVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQHGSFVGYCAELCGVNHSVM--PIVVE 187
Cdd:cd13917    16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMhgRIIVE 88
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 39-182 8.45e-05

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 42.09  E-value: 8.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  39 TVNFGSENQIIELVWTViPTVVVLVLCALNVNfITSDLDCF----SSE---TIKVVGHQWYWTYEYFGGGYDS-----FP 106
Cdd:PRK10525   79 SPNWSHSNKVEAVVWTV-PILIIIFLAVLTWK-TTHALEPSkplaHDEkpiTIEVVSMDWKWFFIYPEQGIATvneiaFP 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737619711 107 IGdyfvvdkplrmvygVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHLFFCPSQHGSFVGYCAELCGVNHSVM 182
Cdd:PRK10525  157 AN--------------VPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGM 218
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 83-189 1.20e-04

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 39.45  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737619711  83 TIKVVGHQWYWTYEYFGGGYDS-----FPIGdyfvvdkplrmvygVPYHLVVTSSDVIHSFSVPSLNLKMDAVPGRLNHL 157
Cdd:cd04212     2 EIQVVSLDWKWLFIYPEQGIATvnelvIPVG--------------RPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQL 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1737619711 158 FFCPSQHGSFVGYCAELCGVNHSVMPIVVEVV 189
Cdd:cd04212    68 HLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
 
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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