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Conserved domains on  [gi|23200464|pdb|1M57|C]
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Chain C, CYTOCHROME C OXIDASE

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10108868)

cytochrome c oxidase subunit 3 is one of main transmembrane subunits of cytochrome c oxidase, the last enzyme in the respiratory electron transport chain of mitochondria or bacteria located in the mitochondrial or bacterial membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-264 9.57e-100

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: 291.34  E-value: 9.57e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       19 FMASVGAFVMLFGAVLWMHG-SGPWMGLIGLVVVLYTMFGWWSDVVTESL-EGDHTPVVRLGLRWGFILFIMSEVMFFSA 96
Cdd:cd01665   1 ILGSFGLLLLALGLVLWMHGyGGPLLLFLGLILLILTMFLWWRDVIRESTfGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       97 WFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVHeNNRRDVAWGLALAIALGA 176
Cdd:cd01665  81 FFWAFFHSSLSP----SVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLL-GNRKKAILGLILTILLGV 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C      177 LFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIWYWHFVDVVWLF 256
Cdd:cd01665 156 YFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLF 235


                ....*...
1M57_C      257 LFASIYIW 264
Cdd:cd01665 236 LFVFVYWW 243
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-264 9.57e-100

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: 291.34  E-value: 9.57e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       19 FMASVGAFVMLFGAVLWMHG-SGPWMGLIGLVVVLYTMFGWWSDVVTESL-EGDHTPVVRLGLRWGFILFIMSEVMFFSA 96
Cdd:cd01665   1 ILGSFGLLLLALGLVLWMHGyGGPLLLFLGLILLILTMFLWWRDVIRESTfGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       97 WFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVHeNNRRDVAWGLALAIALGA 176
Cdd:cd01665  81 FFWAFFHSSLSP----SVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLL-GNRKKAILGLILTILLGV 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C      177 LFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIWYWHFVDVVWLF 256
Cdd:cd01665 156 YFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLF 235


                ....*...
1M57_C      257 LFASIYIW 264
Cdd:cd01665 236 LFVFVYWW 243
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-262 3.74e-88

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 262.42  E-value: 3.74e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         5 KNHDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRLGLRWGF 83
Cdd:MTH00155   2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGtFQGLHTKKVTKGLRWGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        84 ILFIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVhENNRRD 163
Cdd:MTH00155  82 ILFIVSEVFFFISFFWAFFHSSLSP----NIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLM-ENNYKQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       164 VAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAA 243
Cdd:MTH00155 157 ATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAA 236

                        250
                 ....*....|....*....
1M57_C       244 IWYWHFVDVVWLFLFASIY 262
Cdd:MTH00155 237 AWYWHFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-265 1.65e-81

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 245.40  E-value: 1.65e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C          7 HDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGL--IGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRLGLRWGF 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLfiIALFSLLLTMYLWFRDIIREGtFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         84 ILFIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVhENNRRD 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSP----TVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLI-EGNRKQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        164 VAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAA 243
Cdd:pfam00510 156 ALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAA 235

                         250       260
                  ....*....|....*....|..
1M57_C        244 IWYWHFVDVVWLFLFASIYIWG 265
Cdd:pfam00510 236 ILYWHFVDVVWLFLYVSVYWWG 257
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
64-264 1.53e-47

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 156.55  E-value: 1.53e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       64 TESLEGDHTPVVRLGLRWGFILFIMSEVMF-FSAWFWSFFKHALYPMGPEspiidgifppeGIITFDPWhLPLINTLILL 142
Cdd:COG1845   1 AHDVEAPHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAPDWPA-----------GAELLDLP-LPLINTLLLL 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C      143 CSGCAATWAHHALvHENNRRDVAWGLALAIALGALFTVFQAYEYSHAA---FGFAGNIYGANFFMATGFHGFHVIVGTIF 219
Cdd:COG1845  69 LSSFTVALAVRAA-RRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIW 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
1M57_C      220 LLVCLIRVQRGHFTPEKHVGFEAAIWYWHFVDVVWLFLFASIYIW 264
Cdd:COG1845 148 LLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-265 2.34e-09

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: 55.63  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        133 LPLINTLILLCSGCAATWAHHALVHENNRRDVAWGLALAIALGAlFTVFQAYEYSH-AAFGFAGNI--YGANFFMATGFH 209
Cdd:TIGR02897  54 LVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAG-FVGFEIYEFAHyASEGVTPQIgsYWSSFFVLLGTH 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
1M57_C        210 GFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIWYWHFVDVVWLFLFASIYIWG 265
Cdd:TIGR02897 133 GCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 19-264 9.57e-100

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: 291.34  E-value: 9.57e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       19 FMASVGAFVMLFGAVLWMHG-SGPWMGLIGLVVVLYTMFGWWSDVVTESL-EGDHTPVVRLGLRWGFILFIMSEVMFFSA 96
Cdd:cd01665   1 ILGSFGLLLLALGLVLWMHGyGGPLLLFLGLILLILTMFLWWRDVIRESTfGGHHTKKVQKGLRLGMILFILSEVMFFFS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       97 WFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVHeNNRRDVAWGLALAIALGA 176
Cdd:cd01665  81 FFWAFFHSSLSP----SVELGGTWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLL-GNRKKAILGLILTILLGV 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C      177 LFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIWYWHFVDVVWLF 256
Cdd:cd01665 156 YFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLF 235


                ....*...
1M57_C      257 LFASIYIW 264
Cdd:cd01665 236 LFVFVYWW 243
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 5-262 3.74e-88

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 262.42  E-value: 3.74e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         5 KNHDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRLGLRWGF 83
Cdd:MTH00155   2 KNHPFHLVDYSPWPLTGSIGAMTLTSGLIKWFHQFNMNLLILGLIITLLTMFQWWRDVIREGtFQGLHTKKVTKGLRWGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        84 ILFIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVhENNRRD 163
Cdd:MTH00155  82 ILFIVSEVFFFISFFWAFFHSSLSP----NIELGMIWPPKGIIPFNPFQIPLLNTIILLSSGVTVTWAHHSLM-ENNYKQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       164 VAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAA 243
Cdd:MTH00155 157 ATQSLFFTIILGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAA 236

                        250
                 ....*....|....*....
1M57_C       244 IWYWHFVDVVWLFLFASIY 262
Cdd:MTH00155 237 AWYWHFVDVVWLFLYISIY 255
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 5-265 1.19e-84

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 253.66  E-value: 1.19e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         5 KNHDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRLGLRWGF 83
Cdd:MTH00141   2 TRNPFHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSFLLLVLGLVLIVLTMFQWWRDIVREStFQGFHTSKVQRGLRWGF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        84 ILFIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALvHENNRRD 163
Cdd:MTH00141  82 ILFIVSEVCFFFAFFWAYFHSSLAP----SVEIGCCWPPVGIEPLNPFQVPLLNTAVLLASGVTVTWAHHSL-MEGDYKS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       164 VAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAA 243
Cdd:MTH00141 157 ALQGLGLTIILGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAA 236

                        250       260
                 ....*....|....*....|..
1M57_C       244 IWYWHFVDVVWLFLFASIYIWG 265
Cdd:MTH00141 237 AWYWHFVDVVWLFLYLSIYWWG 258
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 5-265 2.09e-83

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 250.28  E-value: 2.09e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         5 KNHDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRLGLRWGF 83
Cdd:MTH00189   3 QAHPFHLVDPSPWPLTGAIAALLLTSGLAMWFHYNSFILLFLGLILLLLTMIQWWRDVVREStFQGFHTPPVQKGLRYGM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        84 ILFIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVhENNRRD 163
Cdd:MTH00189  83 ILFITSEVFFFLGFFWAFFHSSLAP----TVELGMCWPPTGIEPLNPFEVPLLNTAVLLSSGVTVTWAHHSLM-EGNRKE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       164 VAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAA 243
Cdd:MTH00189 158 AIQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAA 237

                        250       260
                 ....*....|....*....|..
1M57_C       244 IWYWHFVDVVWLFLFASIYIWG 265
Cdd:MTH00189 238 AWYWHFVDVVWLFLYVSIYWWG 259
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-265 1.31e-82

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 248.33  E-value: 1.31e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         1 MAHaKNHDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRLGL 79
Cdd:MTH00118   1 MTH-QAHPYHMVDPSPWPLTGAMAALLLTSGLAMWFHYNSTTLLKLGLLSMLLTMLQWWRDIVREStFQGHHTPTVQKGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        80 RWGFILFIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVhEN 159
Cdd:MTH00118  80 RYGMILFITSEVFFFLGFFWAFYHSSLAP----TPELGGQWPPTGIKPLNPFEVPLLNTAVLLASGVTVTWAHHSIM-EG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       160 NRRDVAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVG 239
Cdd:MTH00118 155 NRKQAIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFG 234

                        250       260
                 ....*....|....*....|....*.
1M57_C       240 FEAAIWYWHFVDVVWLFLFASIYIWG 265
Cdd:MTH00118 235 FEAAAWYWHFVDVVWLFLYISIYWWG 260
COX3 pfam00510
Cytochrome c oxidase subunit III;
7-265 1.65e-81

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 245.40  E-value: 1.65e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C          7 HDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGL--IGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRLGLRWGF 83
Cdd:pfam00510   1 HPFHMVSPSPWPLFGSFALLLLTSGLVLWFHGYSGNMTLfiIALFSLLLTMYLWFRDIIREGtFLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         84 ILFIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVhENNRRD 163
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSP----TVELGAQWPPVGIHPVNPFEVPLLNTIILLSSGVTVTYAHHSLI-EGNRKQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        164 VAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAA 243
Cdd:pfam00510 156 ALQGLILTILLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLLKYHLTDNHHFGFEAA 235

                         250       260
                  ....*....|....*....|..
1M57_C        244 IWYWHFVDVVWLFLFASIYIWG 265
Cdd:pfam00510 236 ILYWHFVDVVWLFLYVSVYWWG 257
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-265 2.22e-77

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 235.01  E-value: 2.22e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         1 MAHaKNHDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRLGL 79
Cdd:MTH00099   1 MTH-QTHAYHMVNPSPWPLTGALSALLMTSGLIMWFHFNSTTLLTLGLLTNMLTMYQWWRDIIREStFQGHHTPIVQKGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        80 RWGFILFIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVhEN 159
Cdd:MTH00099  80 RYGMILFIISEVFFFAGFFWAFYHSSLAP----TPELGGCWPPTGITPLNPLEVPLLNTSVLLASGVSITWAHHSLM-EG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       160 NRRDVAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVG 239
Cdd:MTH00099 155 NRKHMLQALFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQLKFHFTSNHHFG 234

                        250       260
                 ....*....|....*....|....*.
1M57_C       240 FEAAIWYWHFVDVVWLFLFASIYIWG 265
Cdd:MTH00099 235 FEAAAWYWHFVDVVWLFLYVSIYWWG 260
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-265 3.25e-77

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 234.62  E-value: 3.25e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         1 MAHakNHDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRLGL 79
Cdd:MTH00039   1 MTH--QHPYHLVDQSPWPLTAAIGALIMTSGLVLWFHGDSILLLLLGLLLLILTSINWWRDVIREAtFQGMHTLIVINGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        80 RWGFILFIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVhEN 159
Cdd:MTH00039  79 RYGMILFITSEVCFFFAFFWAFFHSSLAP----TVEIGVSWPPTGINPINPFLVPLLNTAVLLSSGVTITWSHHSIL-EG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       160 NRRDVAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVG 239
Cdd:MTH00039 154 NRTEAIQALFLTVLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHHFG 233

                        250       260
                 ....*....|....*....|....*.
1M57_C       240 FEAAIWYWHFVDVVWLFLFASIYIWG 265
Cdd:MTH00039 234 FEAAAWYWHFVDVVWLFLYVCIYWWG 259
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-265 7.41e-77

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 233.89  E-value: 7.41e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         1 MAHaKNHDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTE-SLEGDHTPVVRLGL 79
Cdd:MTH00130   1 MAH-QAHAYHMVDPSPWPLTGAVAALLMTSGLAIWFHFHSTTLMTLGLILLLLTMYQWWRDIVREgTFQGHHTPPVQKGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        80 RWGFILFIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVhEN 159
Cdd:MTH00130  80 RYGMILFITSEVFFFLGFFWAFYHSSLAP----TPELGGCWPPTGITTLDPFEVPLLNTAVLLASGVTVTWAHHSIM-EG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       160 NRRDVAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVG 239
Cdd:MTH00130 155 ERKQAIQSLTLTILLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFG 234

                        250       260
                 ....*....|....*....|....*.
1M57_C       240 FEAAIWYWHFVDVVWLFLFASIYIWG 265
Cdd:MTH00130 235 FEAAAWYWHFVDVVWLFLYISIYWWG 260
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 7-265 2.15e-75

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 230.02  E-value: 2.15e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         7 HDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRLGLRWGFIL 85
Cdd:MTH00024   6 HPYHLVEPSPWPFLGAGGAFFITVGSVVYFHYGFSFILYLGLLVIVGVMFVWWQDVIREStFQGHHSLIVKQGLKYGMLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        86 FIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVhENNRRDVA 165
Cdd:MTH00024  86 FILSEVLFFFSFFWAFFHSSLAP----AVELGVVWPPQGINPLNPFSVPLLNTAVLLSSGATVTWAHHAII-SGKRKEAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       166 WGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIW 245
Cdd:MTH00024 161 LGLFLTVFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASW 240

                        250       260
                 ....*....|....*....|
1M57_C       246 YWHFVDVVWLFLFASIYIWG 265
Cdd:MTH00024 241 YWHFVDVVWLFLYLCIYWWG 260
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-265 5.64e-75

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 228.86  E-value: 5.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         1 MAHaKNHDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRLGL 79
Cdd:MTH00075   1 MAH-QAHAFHMVDPSPWPLTGAIAALLLTSGLAMWFHFGSMIIMLLGLIIMLLTMFQWWRDIVREGtFQGHHTPPVQKGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        80 RWGFILFIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVHeN 159
Cdd:MTH00075  80 RYGMILFITSEVFFFLGFFWAFYNSSLAP----TPELGECWPPTGITPLDPFEVPLLNTAVLLASGVTVTWAHHSIMQ-G 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       160 NRRDVAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVG 239
Cdd:MTH00075 155 NRKEAIQSLALTIILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFG 234

                        250       260
                 ....*....|....*....|....*.
1M57_C       240 FEAAIWYWHFVDVVWLFLFASIYIWG 265
Cdd:MTH00075 235 FEAAAWYWHFVDVVWLFLYVSIYWWG 260
PLN02194 PLN02194
cytochrome-c oxidase
 1-265 4.59e-71

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 219.15  E-value: 4.59e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         1 MAHAKNHDYHILPPSIWPFMASVGAFVMLFGAVLWMH--GSGPWMGLIGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRL 77
Cdd:PLN02194   1 MIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHpfQGGARLLSLGLIFILYTMFVWWRDVLREStLEGHHTKVVQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        78 GLRWGFILFIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVH 157
Cdd:PLN02194  81 GPRYGSILFIVSEVMFFFAFFWASSHSSLAP----AVEIGGIWPPKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       158 ENNRRDVaWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKH 237
Cdd:PLN02194 157 GKEKRAV-YALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHH 235

                        250       260
                 ....*....|....*....|....*...
1M57_C       238 VGFEAAIWYWHFVDVVWLFLFASIYIWG 265
Cdd:PLN02194 236 VGFEAAAWYWHFVDVVWLFLFVSIYWWG 263
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-265 2.49e-70

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 217.35  E-value: 2.49e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         1 MAHAKNHDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRLGL 79
Cdd:MTH00052   1 MMQQYYHPYHLVDPSPWPYIGGCGALFTTVGGVMYFHYSQSWVLILGLITIIFTMVVWWRDVIREStYQGHHTLIVKQGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        80 RWGFILFIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVhEN 159
Cdd:MTH00052  81 KYGMILFIVSEVCLFFSFFWAFFHSSLAP----TIEIGAVWPPRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGII-SG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       160 NRRDVAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVG 239
Cdd:MTH00052 156 KRKEAIIGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFG 235

                        250       260
                 ....*....|....*....|....*.
1M57_C       240 FEAAIWYWHFVDVVWLFLFASIYIWG 265
Cdd:MTH00052 236 FEAAAWYWHFVDVVWLFLFIFMYWWG 261
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 7-265 2.40e-69

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 214.65  E-value: 2.40e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         7 HDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTES-LEGDHTPVVRLGLRWGFIL 85
Cdd:MTH00219   7 NPYHLVDYSPWPLTGSLGALMLTSGLVAWFHHYNLDLLILGLLIIVLTMIQWWRDVIREStFMGLHTSKVSTGLRIGMIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        86 FIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVhENNRRDVA 165
Cdd:MTH00219  87 FIVSEILFFFAFFWAFFHSSLAP----TIELGSCWPPTGINPLNPFQVPLLNTAVLLASGVTVTWAHHSLM-ESNHKEAQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       166 WGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIW 245
Cdd:MTH00219 162 QGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAW 241

                        250       260
                 ....*....|....*....|
1M57_C       246 YWHFVDVVWLFLFASIYIWG 265
Cdd:MTH00219 242 YWHFVDVVWLFLYVSIYWWG 261
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 7-265 1.60e-66

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 207.38  E-value: 1.60e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         7 HDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTESL-EGDHTPVVRLGLRWGFIL 85
Cdd:MTH00009   4 QPFHLVEYSPWPLTGSIGAFTLTVGLASWFHGYGTLCLILGLIIIILTMIQWWRDVIREGTyMGHHTSYVTKGLRWGMIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        86 FIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVhENNRRDVA 165
Cdd:MTH00009  84 FIASEVMFFFAFFWAFFHSSLAP----TPELGCSWPPTGIEPLNPFSVPLLNTAVLLASGVTVTWAHHSLI-EGDRPEAT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       166 WGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIW 245
Cdd:MTH00009 159 QALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAW 238

                        250       260
                 ....*....|....*....|
1M57_C       246 YWHFVDVVWLFLFASIYIWG 265
Cdd:MTH00009 239 YWHFVDVVWIFLYLCIYWWG 258
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 7-265 7.91e-65

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 204.53  E-value: 7.91e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         7 HDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTE-SLEGDHTPVVRLGLRWGFIL 85
Cdd:MTH00028   6 HPYHLVDPSPWPFVGASGAFLFTSGAVILFHYSDYRLALTGLFLIIITASAWWRDVIREgTHQGHHTQIVVRGLKLGMLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        86 FIMSEVMFFSAWFWSFFKHALYPmgpeSPIIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVHENN----- 160
Cdd:MTH00028  86 FILSEVCLFFAFFWAFFHSSLAP----SVELGSVWPPKGIEALDPFAVPLLNTTILLSSGATVTWAHHAIIGTGNpasle 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       161 ------------------------------RRDVAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHG 210
Cdd:MTH00028 162 kgtqgiegpnpsngappdpqkgptfllsdfRTNAVIGLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHG 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
1M57_C       211 FHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIWYWHFVDVVWLFLFASIYIWG 265
Cdd:MTH00028 242 LHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYWWG 296
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 71-264 1.07e-53

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: 172.00  E-value: 1.07e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       71 HTPVVRLGLRWGFILFIMSEVMFFSAWFWSFFKHALYPmgpespiidgifPPEGIITFDPWHLPLINTLILLCSGCAATW 150
Cdd:cd00386   1 HTASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSP------------PVEFGAGLDPLDLPLLNTNTLLLSGSSVTW 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C      151 AHHAL-VHENNRRDVAWGLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQR 229
Cdd:cd00386  69 AHASLaARRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRR 148

                       170       180       190
                ....*....|....*....|....*....|....*
1M57_C      230 GHFTPEKHVGFEAAIWYWHFVDVVWLFLFASIYIW 264
Cdd:cd00386 149 GHFTPRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 7-265 7.50e-52

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 169.75  E-value: 7.50e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C         7 HDYHILPPSIWPFMASVGAFVMLFGAVLWMHGSGPWMGLIGLVVVLYTMFGWWSDVVTESLEGDHTPVVRLGLRWGFILF 86
Cdd:MTH00083   3 HNFHILSLSSYPYMMFFSSLGLTSSLVVFFKYGLFYSFFFSLLYLLFISFLWGKDISMEGLSGYHNFFVMDGFKFGMILF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        87 IMSEVMFFSAWFWSFFKHALYPMGPespiIDGIFPPEGIITFDPWHLPLINTLILLCSGCAATWAHHALVHENNrrDVAW 166
Cdd:MTH00083  83 IFSEFMFFFSIFWTFFDAALVPVHE----LGGVWSPIGIHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNK--SCTN 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       167 GLALAIALGALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIWY 246
Cdd:MTH00083 157 SLLLTCFLGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILY 236

                        250
                 ....*....|....*....
1M57_C       247 WHFVDVVWLFLFASIYIWG 265
Cdd:MTH00083 237 WHFVDVVWLFLFVFVYWWS 255
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
64-264 1.53e-47

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 156.55  E-value: 1.53e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       64 TESLEGDHTPVVRLGLRWGFILFIMSEVMF-FSAWFWSFFKHALYPMGPEspiidgifppeGIITFDPWhLPLINTLILL 142
Cdd:COG1845   1 AHDVEAPHAPERRSPGKLGMWLFLASEVMLfAALFAAYFVLRASAPDWPA-----------GAELLDLP-LPLINTLLLL 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C      143 CSGCAATWAHHALvHENNRRDVAWGLALAIALGALFTVFQAYEYSHAA---FGFAGNIYGANFFMATGFHGFHVIVGTIF 219
Cdd:COG1845  69 LSSFTVALAVRAA-RRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIW 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
1M57_C      220 LLVCLIRVQRGHFTPEKHVGFEAAIWYWHFVDVVWLFLFASIYIW 264
Cdd:COG1845 148 LLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 131-263 7.34e-22

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: 89.60  E-value: 7.34e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C      131 WHLPLINTLILLCSGCAATWAHHAlVHENNRRDVAWGLALAIALGALFTVFQAYEYSHAaFGFAGNIYGANFFMA----T 206
Cdd:cd02862  51 LLLGALNTLVLLTSSFTVALAVRA-ARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHK-IAAGIDPDAGLFFTLyfllT 128

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
1M57_C      207 GFHGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIWYWHFVDVVWLFLFASIYI 263
Cdd:cd02862 129 GFHLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLYL 185
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 136-264 8.93e-17

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: 76.39  E-value: 8.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C      136 INTLILLCSGCAATWAHHALvHENNRRDVAWGLALAIALGALFTVFQAYEY----SHAAFGFAGN-----IYGANFFMAT 206
Cdd:cd02864  65 IMTFILITSSGTMAMAVNFG-YRGNRKAAARLMLATALLGATFVGMQAFEWtkliVEEGVRPWGNpwgaaQFGASFFMIT 143

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
1M57_C      207 GFHGFHVIVGTIFLLVCLIRVQRGHFTPE-KHVGFEAAIWYWHFVDVVWLFLFASIYIW 264
Cdd:cd02864 144 GFHGTHVTIGVIYLIIIARKVWRGKYQRIgRYEIVEIAGLYWHFVDLVWVFIFAFFYLW 202
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 133-264 1.30e-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: 75.48  E-value: 1.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C      133 LPLINTLILLCSgCAATWAHHALVHENNRRDVAWGLALAIALGALFTVFQAYEY---SHAAFGFAGNIYGANFFMATGFH 209
Cdd:cd02865  51 LLSLNTAVLAAS-SVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWhalNDAGYGPTSNPAGSFFYLLTGLH 129

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
1M57_C      210 GFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIWYWHFVDVVWLFLFASIYIW 264
Cdd:cd02865 130 GLHVIGGLVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYGT 184
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 132-265 1.16e-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: 67.65  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C      132 HLPLINTLILLCSGCAATWAHHALvHENNRRDVAWGLALAIALGALFTVFQAYEYSH---AAFGFAGNIYGANFFMATGF 208
Cdd:cd02863  51 PLVFIETFLLLLSSFTCGLAMIAM-NKNNKKKVILWLIITFLLGLGFVGMEIYEFHHliaEGAGPDRSAFLSAFFTLVGT 129

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
1M57_C      209 HGFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIWYWHFVDVVWLFLFASIYIWG 265
Cdd:cd02863 130 HGLHVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVYLLG 186
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 15-263 9.63e-10

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 56.85  E-value: 9.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        15 SIWPFMASVGAFVMLFGAVLWMhgsgPWMGLIGLVVVLYTMFGWWSDVVTESLEGDHTpvvrlglrwGFILFIMSEVMFF 94
Cdd:MTH00049   2 SWFPLFNASFVGFGLVGLFLWK----PFILLVFLILWVLLIVIFVSDGLVQVKHHYES---------AFWLFILSEVIIF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        95 SAWFWSFFKHALYPMGPESpiidgifppegiitfDPWHLPLINTLILLCSGCAATWAHHALVHENNRrdvaWGLALAIAL 174
Cdd:MTH00049  69 GSLLVCCLWFDDWSYISLS---------------SSLEIPFVGCFLLLGSSITVTAYHHLLGWKYCD----LFLYLTILL 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       175 GALFTVFQAYEYSHAAFGFAGNIYGANFFMATGFHGFHVIVGTIFLLVCLIrvqrghFTPEKHVGF--EAAIWYWHFVDV 252
Cdd:MTH00049 130 GLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLSTLLL------VGSSSFGVYrsTVLTWYWHFVDY 203

                        250
                 ....*....|.
1M57_C       253 VWLFLFASIYI 263
Cdd:MTH00049 204 IWLLVYLIVYV 214
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 133-265 2.34e-09

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: 55.63  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C        133 LPLINTLILLCSGCAATWAHHALVHENNRRDVAWGLALAIALGAlFTVFQAYEYSH-AAFGFAGNI--YGANFFMATGFH 209
Cdd:TIGR02897  54 LVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAG-FVGFEIYEFAHyASEGVTPQIgsYWSSFFVLLGTH 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
1M57_C        210 GFHVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIWYWHFVDVVWLFLFASIYIWG 265
Cdd:TIGR02897 133 GCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVYLIG 188
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 135-265 3.23e-07

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 49.78  E-value: 3.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1M57_C       135 LINTLILLCSGCAATWAHHALVHENNRRDVAWGLALAIALGAlFTVFQAYEYSH---AAFGFAGNIYGANFFMATGFHGF 211
Cdd:PRK10663  70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAG-FIGMEIYEFHHlivEGMGPDRSGFLSAFFALVGTHGL 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
1M57_C       212 HVIVGTIFLLVCLIRVQRGHFTPEKHVGFEAAIWYWHFVDVVWLFLFASIYIWG 265
Cdd:PRK10663 149 HVTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
 
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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