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Conserved domains on  [gi|312922612|gb|ADR10687|]
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cytochrome oxidase subunit III, partial (mitochondrion) [Mytilus edulis]

Protein Classification

cytochrome c oxidase subunit 3 family protein( domain architecture ID 201)

cytochrome c oxidase (CcO) subunit 3 family protein is not required for catalytic activity but may play a role in the assembly of the heme-copper oxidase (such as CcO and cytochrome bo(3) ubiquinol oxidase) multimer complex

CATH:  1.20.120.80
Gene Ontology:  GO:0070069|GO:0009055
PubMed:  8083153|12907296
SCOP:  3000671

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like super family cl00211
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 1-223 4.74e-95

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


The actual alignment was detected with superfamily member MTH00141:

Pssm-ID: 444752  Cd Length: 259  Bit Score: 278.31  E-value: 4.74e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHRTpSFLLMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:MTH00141  32 WFHGG-SFLLLVLGLVLIVLTMFQWWRDIVRESTFqGFHTSKVQRGLRWGFILFIVSEVCFFFAFFWAYFHSSLAPSVEI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMRLKDYDvGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:MTH00141 111 GCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYK-SALQGLGLTIILGVYFTFLQAGEYYEASFSIADG 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALWCL 223
Cdd:MTH00141 190 VYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLS 253
 
Name Accession Description Interval E-value
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-223 4.74e-95

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 278.31  E-value: 4.74e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHRTpSFLLMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:MTH00141  32 WFHGG-SFLLLVLGLVLIVLTMFQWWRDIVRESTFqGFHTSKVQRGLRWGFILFIVSEVCFFFAFFWAYFHSSLAPSVEI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMRLKDYDvGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:MTH00141 111 GCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYK-SALQGLGLTIILGVYFTFLQAGEYYEASFSIADG 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALWCL 223
Cdd:MTH00141 190 VYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLS 253
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-222 2.89e-88

Cytochrome c oxidase subunit III. 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. CcO 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, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. 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 III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 260.14  E-value: 2.89e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHRTPSFLLMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:cd01665   17 WMHGYGGPLLLFLGLILLILTMFLWWRDVIRESTFgGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVEL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMRLKDYDvGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:cd01665   97 GGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRK-KAILGLILTILLGVYFTGLQAYEYYEASFTISDS 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALWC 222
Cdd:cd01665  176 VYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFV 238
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-221 1.93e-62

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 195.32  E-value: 1.93e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612    1 WLHR-TPSFLLMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCE 78
Cdd:pfam00510  29 WFHGySGNMTLFIIALFSLLLTMYLWFRDIIREGTFlGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   79 LGMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMrLKDYDVGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIAD 158
Cdd:pfam00510 109 LGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSL-IEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISD 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312922612  159 SVYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALW 221
Cdd:pfam00510 188 GVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHFVDVVWLFLY 250
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
85-223 3.12e-37

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 128.43  E-value: 3.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  85 PPGIRTPNPSSTsLFETGLLISSGLFVTQAHKSMRLKDYDvGPFIGLVVTIVCGTVFFLVQLREYYW---NSYTIADSVY 161
Cdd:COG1845   49 PAGAELLDLPLP-LINTLLLLLSSFTVALAVRAARRGDRK-GLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAF 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312922612 162 GSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALWCL 223
Cdd:COG1845  127 GSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFAL 188
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 131-223 1.19e-06

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 47.16  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  131 LVVTIVCGTVFFLVQLRE---YYWNSYTIADSVYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACI 207
Cdd:TIGR02897  88 MIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVS 167

                          90
                  ....*....|....*.
gi 312922612  208 WYWHFVDVVWVALWCL 223
Cdd:TIGR02897 168 LYWHFLDVVWVFIFTA 183
 
Name Accession Description Interval E-value
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-223 4.74e-95

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 278.31  E-value: 4.74e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHRTpSFLLMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:MTH00141  32 WFHGG-SFLLLVLGLVLIVLTMFQWWRDIVRESTFqGFHTSKVQRGLRWGFILFIVSEVCFFFAFFWAYFHSSLAPSVEI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMRLKDYDvGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:MTH00141 111 GCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSLMEGDYK-SALQGLGLTIILGVYFTFLQAGEYYEASFSIADG 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALWCL 223
Cdd:MTH00141 190 VYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLS 253
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-222 2.89e-88

Cytochrome c oxidase subunit III. 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. CcO 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, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. 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 III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 260.14  E-value: 2.89e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHRTPSFLLMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:cd01665   17 WMHGYGGPLLLFLGLILLILTMFLWWRDVIRESTFgGHHTKKVQKGLRLGMILFILSEVMFFFSFFWAFFHSSLSPSVEL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMRLKDYDvGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:cd01665   97 GGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRK-KAILGLILTILLGVYFTGLQAYEYYEASFTISDS 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALWC 222
Cdd:cd01665  176 VYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFV 238
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-217 1.01e-71

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 218.90  E-value: 1.01e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHrTPSFLLMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:MTH00155  32 WFH-QFNMNLLILGLIITLLTMFQWWRDVIREGTFqGLHTKKVTKGLRWGMILFIVSEVFFFISFFWAFFHSSLSPNIEL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMRLKDYDVGpFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:MTH00155 111 GMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLMENNYKQA-TQSLFFTIILGIYFTMLQAYEYYEAPFTIADS 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVW 217
Cdd:MTH00155 190 VYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDVVW 247
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-222 5.69e-71

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 217.15  E-value: 5.69e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHRTpSFLLMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:MTH00189  33 WFHYN-SFILLFLGLILLLLTMIQWWRDVVRESTFqGFHTPPVQKGLRYGMILFITSEVFFFLGFFWAFFHSSLAPTVEL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMRLKDYdVGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:MTH00189 112 GMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNR-KEAIQALTLTVILGVYFTLLQAMEYYEAPFTIADS 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALWC 222
Cdd:MTH00189 191 VYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVDVVWLFLYV 253
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-221 2.92e-64

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 199.79  E-value: 2.92e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHrTPSFLLMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:MTH00118  34 WFH-YNSTTLLKLGLLSMLLTMLQWWRDIVRESTFqGHHTPTVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPEL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMrLKDYDVGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:MTH00118 113 GGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSI-MEGNRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDS 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALW 221
Cdd:MTH00118 192 VYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVDVVWLFLY 253
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-221 1.93e-62

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 195.32  E-value: 1.93e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612    1 WLHR-TPSFLLMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCE 78
Cdd:pfam00510  29 WFHGySGNMTLFIIALFSLLLTMYLWFRDIIREGTFlGDHTFAVQKGLNLGMILFIISEVFFFLGIFWAFFHSALSPTVE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   79 LGMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMrLKDYDVGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIAD 158
Cdd:pfam00510 109 LGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSL-IEGNRKQALQGLILTILLAVYFTGLQAMEYTEASFTISD 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312922612  159 SVYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALW 221
Cdd:pfam00510 188 GVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAAILYWHFVDVVWLFLY 250
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-221 2.18e-62

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 195.33  E-value: 2.18e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHrTPSFLLMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:MTH00039  33 WFH-GDSILLLLLGLLLLILTSINWWRDVIREATFqGMHTLIVINGLRYGMILFITSEVCFFFAFFWAFFHSSLAPTVEI 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMRLKDYDvGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:MTH00039 112 GVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRT-EAIQALFLTVLLGLYFTALQAWEYYDAPFTIADS 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALW 221
Cdd:MTH00039 191 VYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVDVVWLFLY 252
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-221 4.50e-58

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 184.20  E-value: 4.50e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHrTPSFLLMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:MTH00130  34 WFH-FHSTTLMTLGLILLLLTMYQWWRDIVREGTFqGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYHSSLAPTPEL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMrLKDYDVGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:MTH00130 113 GGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSI-MEGERKQAIQSLTLTILLGFYFTFLQAMEYYEAPFTIADG 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALW 221
Cdd:MTH00130 192 VYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVDVVWLFLY 253
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-221 8.66e-58

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 183.39  E-value: 8.66e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHRTPSFLLMgMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:MTH00099  34 WFHFNSTTLLT-LGLLTNMLTMYQWWRDIIRESTFqGHHTPIVQKGLRYGMILFIISEVFFFAGFFWAFYHSSLAPTPEL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMrLKDYDVGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:MTH00099 113 GGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSL-MEGNRKHMLQALFITILLGLYFTLLQASEYYEAPFTISDG 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALW 221
Cdd:MTH00099 192 IYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLY 253
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 10-221 1.43e-57

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 183.03  E-value: 1.43e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  10 LMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCELGMRWPPPGI 88
Cdd:MTH00024  42 ILYLGLLVIVGVMFVWWQDVIRESTFqGHHSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELGVVWPPQGI 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  89 RTPNPSSTSLFETGLLISSGLFVTQAHKSMrLKDYDVGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADSVYGSVFYLL 168
Cdd:MTH00024 122 NPLNPFSVPLLNTAVLLSSGATVTWAHHAI-ISGKRKEAILGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVA 200

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 312922612 169 TGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALW 221
Cdd:MTH00024 201 TGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVDVVWLFLY 253
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-221 2.36e-56

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 179.94  E-value: 2.36e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHRTpSFLLMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:MTH00075  34 WFHFG-SMIIMLLGLIIMLLTMFQWWRDIVREGTFqGHHTPPVQKGLRYGMILFITSEVFFFLGFFWAFYNSSLAPTPEL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMRLKDYDvGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:MTH00075 113 GECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRK-EAIQSLALTIILGLYFTLLQAMEYYEAPFTIADG 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALW 221
Cdd:MTH00075 192 VYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDVVWLFLY 253
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-221 8.38e-56

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 178.44  E-value: 8.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHRTPSFLLMgMSLVCMLLSTFSWWRDLIREGD-IGFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:MTH00219  35 WFHHYNLDLLI-LGLLIIVLTMIQWWRDVIRESTfMGLHTSKVSTGLRIGMILFIVSEILFFFAFFWAFFHSSLAPTIEL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMRLKDYDvGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:MTH00219 114 GSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHK-EAQQGLLFTILLGLYFTMLQGMEYLEASFSISDS 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALW 221
Cdd:MTH00219 193 VYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFVDVVWLFLY 254
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-221 1.13e-54

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 175.41  E-value: 1.13e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHRTpSFLLMGMSLVCMLLSTFSWWRDLIREGD-IGFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:MTH00009  32 WFHGY-GTLCLILGLIIIILTMIQWWRDVIREGTyMGHHTSYVTKGLRWGMILFIASEVMFFFAFFWAFFHSSLAPTPEL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMrLKDYDVGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:MTH00009 111 GCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSL-IEGDRPEATQALILTVLLGAYFTFLQAGEYIEAPFTIADS 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALW 221
Cdd:MTH00009 190 VYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFVDVVWIFLY 251
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-221 5.88e-54

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 173.83  E-value: 5.88e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612   1 WLHRTPSFLLMgMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCEL 79
Cdd:MTH00052  35 YFHYSQSWVLI-LGLITIIFTMVVWWRDVIRESTYqGHHTLIVKQGLKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEI 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  80 GMRWPPPGIRTPNPSSTSLFETGLLISSGLFVTQAHKSMrLKDYDVGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADS 159
Cdd:MTH00052 114 GAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGI-ISGKRKEAIIGLALTVALGLLFTGLQAMEYYEAPFTISDS 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALW 221
Cdd:MTH00052 193 VYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFVDVVWLFLF 254
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 15-221 1.06e-51

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 169.09  E-value: 1.06e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  15 LVCMLLSTFSWWRDLIREGD-IGFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCELGMRWPPPGIRTPNP 93
Cdd:MTH00028  47 LFLIIITASAWWRDVIREGThQGHHTQIVVRGLKLGMLLFILSEVCLFFAFFWAFFHSSLAPSVELGSVWPPKGIEALDP 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  94 SSTSLFETGLLISSGLFVTQAHKSM-----------------------------------RLKDYDVGPFIGLVVTIVCG 138
Cdd:MTH00028 127 FAVPLLNTTILLSSGATVTWAHHAIigtgnpaslekgtqgiegpnpsngappdpqkgptfLLSDFRTNAVIGLLMTILLG 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612 139 TVFFLVQLREYYWNSYTIADSVYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWV 218
Cdd:MTH00028 207 IIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWL 286


                 ...
gi 312922612 219 ALW 221
Cdd:MTH00028 287 FLY 289
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 13-223 3.74e-49

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 161.28  E-value: 3.74e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  13 MSLVCMLLSTFSWWRDLIREGDIGFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCELGMRWPPPGIRTPN 92
Cdd:MTH00083  42 FSLLYLLFISFLWGKDISMEGLSGYHNFFVMDGFKFGMILFIFSEFMFFFSIFWTFFDAALVPVHELGGVWSPIGIHLVN 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  93 PSSTSLFETGLLISSGLFVTQAHKSMRLKDYDVGPFigLVVTIVCGTVFFLVQLREYYWNSYTIADSVYGSVFYLLTGFH 172
Cdd:MTH00083 122 YLGVPLLNTIILLSSGVSVTWSHHSLCLSNKSCTNS--LLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFH 199

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 312922612 173 GMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALWCL 223
Cdd:MTH00083 200 GIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDVVWLFLFVF 250
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 38-223 1.88e-48

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


Pssm-ID: 238227  Cd Length: 183  Bit Score: 156.98  E-value: 1.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  38 HTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCELGMrwpppgirTPNPSSTSLFETGLLISSGLFVTQAHKS 117
Cdd:cd00386    1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFGA--------GLDPLDLPLLNTNTLLLSGSSVTWAHAS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612 118 MRLKDYDVGPFI-GLVVTIVCGTVFFLVQLREYYWNSYTIADSVYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFS 196
Cdd:cd00386   73 LAARRGNRKKARlWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFT 152

                        170       180
                 ....*....|....*....|....*..
gi 312922612 197 SQRHFGFEACIWYWHFVDVVWVALWCL 223
Cdd:cd00386  153 PRHHLGLEAAALYWHFVDVVWLFLFPL 179
PLN02194 PLN02194
cytochrome-c oxidase
 10-221 4.40e-45

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 150.97  E-value: 4.40e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  10 LMGMSLVCMLLSTFSWWRDLIREGDI-GFHTRFVIKSFRDGVALFILSEVMFFFTFFWTFFHNALSPSCELGMRWPPPGI 88
Cdd:PLN02194  45 LLSLGLIFILYTMFVWWRDVLRESTLeGHHTKVVQLGPRYGSILFIVSEVMFFFAFFWASSHSSLAPAVEIGGIWPPKGI 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  89 RTPNPSSTSLFETGLLISSGLFVTQAHKSMrLKDYDVGPFIGLVVTIVCGTVFFLVQLREYYWNSYTIADSVYGSVFYLL 168
Cdd:PLN02194 125 EVLDPWEIPFLNTPILPSSGAAVTWAHHAI-LAGKEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLA 203

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 312922612 169 TGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALW 221
Cdd:PLN02194 204 TGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLF 256
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
85-223 3.12e-37

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 128.43  E-value: 3.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  85 PPGIRTPNPSSTsLFETGLLISSGLFVTQAHKSMRLKDYDvGPFIGLVVTIVCGTVFFLVQLREYYW---NSYTIADSVY 161
Cdd:COG1845   49 PAGAELLDLPLP-LINTLLLLLSSFTVALAVRAARRGDRK-GLRLWLLLTLLLGLAFLGLQAYEYSHliaEGLTPTSNAF 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312922612 162 GSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVALWCL 223
Cdd:COG1845  127 GSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFAL 188
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 98-220 3.26e-20

NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.


Pssm-ID: 239213  Cd Length: 186  Bit Score: 84.21  E-value: 3.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  98 LFETGLLISSGLFVTQAHKSMRLKDYDVGpFIGLVVTIVCGTVFFLVQLREYYWN---SYTIADSVYGSVFYLLTGFHGM 174
Cdd:cd02862   55 ALNTLVLLTSSFTVALAVRAARAGRRRRA-RRWLAAAVLLGLVFLVIKYFEYAHKiaaGIDPDAGLFFTLYFLLTGFHLL 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 312922612 175 HVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVAL 220
Cdd:cd02862  134 HVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVL 179
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 83-220 1.72e-16

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239216  Cd Length: 184  Bit Score: 74.33  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  83 WPPPGIRTPNPSSTSlfeTGLLISSGLFVTQAHKSMRLKDyDVGPFIGLVVTIVCGTVFFLVQLREY---YWNSYTIADS 159
Cdd:cd02865   41 QPGAPLPLPNLLSLN---TAVLAASSVAMQWARRAARRNR-RVLARLGLALAGALALAFLAGQLLAWhalNDAGYGPTSN 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312922612 160 VYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWVAL 220
Cdd:cd02865  117 PAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVL 177
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 91-218 3.77e-13

Ubiquinol oxidase subunit III subfamily. 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. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.


Pssm-ID: 239214  Cd Length: 186  Bit Score: 65.34  E-value: 3.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  91 PNPSSTSLFETG--------LLISS---GLFVTQAHKSMRLKDYdvgpfIGLVVTIVCGTVFFLVQLRE---YYWNSYTI 156
Cdd:cd02863   40 GGPPGHELFELPlvfietflLLLSSftcGLAMIAMNKNNKKKVI-----LWLIITFLLGLGFVGMEIYEfhhLIAEGAGP 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312922612 157 ADSVYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWV 218
Cdd:cd02863  115 DRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWI 176
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 161-218 1.46e-09

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239215  Cd Length: 202  Bit Score: 55.59  E-value: 1.46e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312922612 161 YGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFssQRHFGF---EACIWYWHFVDVVWV 218
Cdd:cd02864  135 FGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKY--QRIGRYeivEIAGLYWHFVDLVWV 193
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 98-217 4.70e-09

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 54.54  E-value: 4.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  98 LFETGLLISSGLFVTQAHKSMRLKDYDvgpfIGLVVTIVCGTVFFLVQLREYYWNSYTIADSVYGSVFYLLTGFHGMHVV 177
Cdd:MTH00049  94 FVGCFLLLGSSITVTAYHHLLGWKYCD----LFLYLTILLGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVV 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 312922612 178 VGTIWLMVSLVRlwrGEFSSQRHFGfEACIWYWHFVDVVW 217
Cdd:MTH00049 170 LGVVGLSTLLLV---GSSSFGVYRS-TVLTWYWHFVDYIW 205
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 98-218 2.19e-07

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 49.39  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  98 LFETGLLISSGLFVTQAHKSMRlKDYDVGPFIGLVVTIVCGTVFFLVQLREYYW---NSYTIADSVYGSVFYLLTGFHGM 174
Cdd:PRK10663  70 LVETFLLLFSSITYGMAAIAMY-KNNKSQVISWLALTFLFGAGFIGMEIYEFHHlivEGMGPDRSGFLSAFFALVGTHGL 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 312922612 175 HVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACIWYWHFVDVVWV 218
Cdd:PRK10663 149 HVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWI 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 131-223 1.19e-06

cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131943  Cd Length: 190  Bit Score: 47.16  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922612  131 LVVTIVCGTVFFLVQLRE---YYWNSYTIADSVYGSVFYLLTGFHGMHVVVGTIWLMVSLVRLWRGEFSSQRHFGFEACI 207
Cdd:TIGR02897  88 MIITLLLGAGFVGFEIYEfahYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVS 167

                          90
                  ....*....|....*.
gi 312922612  208 WYWHFVDVVWVALWCL 223
Cdd:TIGR02897 168 LYWHFLDVVWVFIFTA 183
 
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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