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Conserved domains on  [gi|1337428511|ref|WP_103272013|]
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cytochrome c oxidase subunit 3 [Achromobacter sp. AONIH1]

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 ...
 26-289 1.96e-95

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: 281.33  E-value: 1.96e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  26 TAAALLLMGLGAAAWINSvSWGKWLVLAGFLSLIVILYYWFGDAIRESEAGLN-SKRIDNSYRWGMSWFIFSEVMFFAGF 104
Cdd:cd01665     3 GSFGLLLLALGLVLWMHG-YGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHhTKKVQKGLRLGMILFILSEVMFFFSF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 105 FGALWYVRTITTPWLGdldhklmlwpdfqAVWPNFGPagvvehfQTVGPFWLPTINTALLLSSGVTLTIAHHALRENHRG 184
Cdd:cd01665    82 FWAFFHSSLSPSVELG-------------GTWPPVGI-------EPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRK 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 185 KTIFWLLATVVLGFIFVACQAAEYHHAYTElnlkFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIRLIRGHFTADHHF 264
Cdd:cd01665   142 KAILGLILTILLGVYFTGLQAYEYYEASFT----ISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHL 217

                         250       260
                  ....*....|....*....|....*
gi 1337428511 265 GFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:cd01665   218 GFEAAIWYWHFVDVVWLFLFVFVYW 242
 
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 ...
 26-289 1.96e-95

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: 281.33  E-value: 1.96e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  26 TAAALLLMGLGAAAWINSvSWGKWLVLAGFLSLIVILYYWFGDAIRESEAGLN-SKRIDNSYRWGMSWFIFSEVMFFAGF 104
Cdd:cd01665     3 GSFGLLLLALGLVLWMHG-YGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHhTKKVQKGLRLGMILFILSEVMFFFSF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 105 FGALWYVRTITTPWLGdldhklmlwpdfqAVWPNFGPagvvehfQTVGPFWLPTINTALLLSSGVTLTIAHHALRENHRG 184
Cdd:cd01665    82 FWAFFHSSLSPSVELG-------------GTWPPVGI-------EPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRK 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 185 KTIFWLLATVVLGFIFVACQAAEYHHAYTElnlkFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIRLIRGHFTADHHF 264
Cdd:cd01665   142 KAILGLILTILLGVYFTGLQAYEYYEASFT----ISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHL 217

                         250       260
                  ....*....|....*....|....*
gi 1337428511 265 GFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:cd01665   218 GFEAAIWYWHFVDVVWLFLFVFVYW 242
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 8-289 6.34e-69

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 214.43  E-value: 6.34e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511   8 HKEAPYYYVPAdSGHPVRTAAALLLMGLGAAAWINSVSwgKWLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSY 86
Cdd:MTH00118    3 HQAHPYHMVDP-SPWPLTGAMAALLLTSGLAMWFHYNS--TTLLKLGLLSMLLTMLQWWRDIVRESTfQGHHTPTVQKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  87 RWGMSWFIFSEVMFFAGFFGALWYVRTITTPWLGdldhklmlwpdfqAVWPnfgPAGVvehfQTVGPFWLPTINTALLLS 166
Cdd:MTH00118   80 RYGMILFITSEVFFFLGFFWAFYHSSLAPTPELG-------------GQWP---PTGI----KPLNPFEVPLLNTAVLLA 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 167 SGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHhaytELNLKFNSGAYGSLFYMLTGFHGFHVLLGATML 246
Cdd:MTH00118  140 SGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYY----EAPFTISDSVYGSTFFVATGFHGLHVIIGSTFL 215

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1337428511 247 TVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:MTH00118  216 IVCLLRLIKFHFTTNHHFGFEAAAWYWHFVDVVWLFLYISIYW 258
COX3 pfam00510
Cytochrome c oxidase subunit III;
12-289 3.78e-65

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 204.57  E-value: 3.78e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  12 PYYYVPAdSGHPVRTAAALLLMGLGAAAWINSVSWGKWLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSYRWGM 90
Cdd:pfam00510   2 PFHMVSP-SPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTfLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  91 SWFIFSEVMFFAGFFGALWYVRTITTPWLGdldhklmlwpdfqAVWPNFGpagvvehFQTVGPFWLPTINTALLLSSGVT 170
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELG-------------AQWPPVG-------IHPVNPFEVPLLNTIILLSSGVT 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 171 LTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHHAytelNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVIL 250
Cdd:pfam00510 141 VTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEA----SFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCF 216

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1337428511 251 IRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:pfam00510 217 LRLLKYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYW 255
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
83-290 8.24e-63

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 196.22  E-value: 8.24e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  83 DNSYRWGMSWFIFSEVMFFAGFFGALWYVRTITTPWlgdldhklmlwpdfqavwpnfgPAGvvehfQTVGPFWLPTINTA 162
Cdd:COG1845    13 RSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPDW----------------------PAG-----AELLDLPLPLINTL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 163 LLLSSGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHHAYTElNLKFNSGAYGSLFYMLTGFHGFHVLLG 242
Cdd:COG1845    66 LLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAE-GLTPTSNAFGSFFFLLTGFHGLHVIIG 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1337428511 243 ATMLTVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYWM 290
Cdd:COG1845   145 LIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 154-288 1.57e-13

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: 67.57  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 154 FWLPTINTALLLSSGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHHAYTElNLKFNSGAYGSLFYMLTG 233
Cdd:TIGR02897  52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEFAHYASE-GVTPQIGSYWSSFFVLLG 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1337428511 234 FHGFHVLLGATMLTVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVY 288
Cdd:TIGR02897 131 THGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVY 185
 
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 ...
 26-289 1.96e-95

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: 281.33  E-value: 1.96e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  26 TAAALLLMGLGAAAWINSvSWGKWLVLAGFLSLIVILYYWFGDAIRESEAGLN-SKRIDNSYRWGMSWFIFSEVMFFAGF 104
Cdd:cd01665     3 GSFGLLLLALGLVLWMHG-YGGPLLLFLGLILLILTMFLWWRDVIRESTFGGHhTKKVQKGLRLGMILFILSEVMFFFSF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 105 FGALWYVRTITTPWLGdldhklmlwpdfqAVWPNFGPagvvehfQTVGPFWLPTINTALLLSSGVTLTIAHHALRENHRG 184
Cdd:cd01665    82 FWAFFHSSLSPSVELG-------------GTWPPVGI-------EPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRK 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 185 KTIFWLLATVVLGFIFVACQAAEYHHAYTElnlkFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIRLIRGHFTADHHF 264
Cdd:cd01665   142 KAILGLILTILLGVYFTGLQAYEYYEASFT----ISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHL 217

                         250       260
                  ....*....|....*....|....*
gi 1337428511 265 GFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:cd01665   218 GFEAAIWYWHFVDVVWLFLFVFVYW 242
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 8-289 6.34e-69

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 214.43  E-value: 6.34e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511   8 HKEAPYYYVPAdSGHPVRTAAALLLMGLGAAAWINSVSwgKWLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSY 86
Cdd:MTH00118    3 HQAHPYHMVDP-SPWPLTGAMAALLLTSGLAMWFHYNS--TTLLKLGLLSMLLTMLQWWRDIVRESTfQGHHTPTVQKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  87 RWGMSWFIFSEVMFFAGFFGALWYVRTITTPWLGdldhklmlwpdfqAVWPnfgPAGVvehfQTVGPFWLPTINTALLLS 166
Cdd:MTH00118   80 RYGMILFITSEVFFFLGFFWAFYHSSLAPTPELG-------------GQWP---PTGI----KPLNPFEVPLLNTAVLLA 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 167 SGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHhaytELNLKFNSGAYGSLFYMLTGFHGFHVLLGATML 246
Cdd:MTH00118  140 SGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTALQAMEYY----EAPFTISDSVYGSTFFVATGFHGLHVIIGSTFL 215

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1337428511 247 TVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:MTH00118  216 IVCLLRLIKFHFTTNHHFGFEAAAWYWHFVDVVWLFLYISIYW 258
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 14-289 3.52e-68

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 212.44  E-value: 3.52e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  14 YYVPADSGHPVRTAAALLLMGLGAAAWINSVSWgkWLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSYRWGMSW 92
Cdd:MTH00141    6 FHLVEFSPWPLTGSIGALFLTVGLVSWFHGGSF--LLLVLGLVLIVLTMFQWWRDIVRESTfQGFHTSKVQRGLRWGFIL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  93 FIFSEVMFFAGFFGALWYVRTITTPWLGdldhklmlwpdfqAVWPnfgPAGVVehfqTVGPFWLPTINTALLLSSGVTLT 172
Cdd:MTH00141   84 FIVSEVCFFFAFFWAYFHSSLAPSVEIG-------------CCWP---PVGIE----PLNPFQVPLLNTAVLLASGVTVT 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 173 IAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHhaytELNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIR 252
Cdd:MTH00141  144 WAHHSLMEGDYKSALQGLGLTIILGVYFTFLQAGEYY----EASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVR 219

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1337428511 253 LIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:MTH00141  220 LLLGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLSIYW 256
COX3 pfam00510
Cytochrome c oxidase subunit III;
12-289 3.78e-65

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 204.57  E-value: 3.78e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  12 PYYYVPAdSGHPVRTAAALLLMGLGAAAWINSVSWGKWLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSYRWGM 90
Cdd:pfam00510   2 PFHMVSP-SPWPLFGSFALLLLTSGLVLWFHGYSGNMTLFIIALFSLLLTMYLWFRDIIREGTfLGDHTFAVQKGLNLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  91 SWFIFSEVMFFAGFFGALWYVRTITTPWLGdldhklmlwpdfqAVWPNFGpagvvehFQTVGPFWLPTINTALLLSSGVT 170
Cdd:pfam00510  81 ILFIISEVFFFLGIFWAFFHSALSPTVELG-------------AQWPPVG-------IHPVNPFEVPLLNTIILLSSGVT 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 171 LTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHHAytelNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVIL 250
Cdd:pfam00510 141 VTYAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTEA----SFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCF 216

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1337428511 251 IRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:pfam00510 217 LRLLKYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYW 255
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 23-289 3.90e-65

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 204.82  E-value: 3.90e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  23 PVRTAAALLLMGLGAAAWINSVSWGkwLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSYRWGMSWFIFSEVMFF 101
Cdd:MTH00189   16 PLTGAIAALLLTSGLAMWFHYNSFI--LLFLGLILLLLTMIQWWRDVVRESTfQGFHTPPVQKGLRYGMILFITSEVFFF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 102 AGFFGALWYVRTITTPWLGdldhklMLWPdfqavwpnfgPAGVvehfQTVGPFWLPTINTALLLSSGVTLTIAHHALREN 181
Cdd:MTH00189   94 LGFFWAFFHSSLAPTVELG------MCWP----------PTGI----EPLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 182 HRGKTIFWLLATVVLGFIFVACQAAEYHHAytelNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIRLIRGHFTAD 261
Cdd:MTH00189  154 NRKEAIQALTLTVILGVYFTLLQAMEYYEA----PFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSS 229

                         250       260
                  ....*....|....*....|....*...
gi 1337428511 262 HHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:MTH00189  230 HHFGFEAAAWYWHFVDVVWLFLYVSIYW 257
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 23-288 3.99e-65

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 204.64  E-value: 3.99e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  23 PVRTAAALLLMGLGAAAWINSVSWGkwLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSYRWGMSWFIFSEVMFF 101
Cdd:MTH00155   15 PLTGSIGAMTLTSGLIKWFHQFNMN--LLILGLIITLLTMFQWWRDVIREGTfQGLHTKKVTKGLRWGMILFIVSEVFFF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 102 AGFFGALWYVRTITTPWLGdldhklMLWPdfqavwpnfgPAGVvehfQTVGPFWLPTINTALLLSSGVTLTIAHHALREN 181
Cdd:MTH00155   93 ISFFWAFFHSSLSPNIELG------MIWP----------PKGI----IPFNPFQIPLLNTIILLSSGVTVTWAHHSLMEN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 182 HRGKTIFWLLATVVLGFIFVACQAAEYHhaytELNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIRLIRGHFTAD 261
Cdd:MTH00155  153 NYKQATQSLFFTIILGIYFTMLQAYEYY----EAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRHLNNHFSSN 228

                         250       260
                  ....*....|....*....|....*..
gi 1337428511 262 HHFGFEGAAWYWHFVDVVWLGLYLFVY 288
Cdd:MTH00155  229 HHFGFEAAAWYWHFVDVVWLFLYISIY 255
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
83-290 8.24e-63

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 196.22  E-value: 8.24e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  83 DNSYRWGMSWFIFSEVMFFAGFFGALWYVRTITTPWlgdldhklmlwpdfqavwpnfgPAGvvehfQTVGPFWLPTINTA 162
Cdd:COG1845    13 RSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPDW----------------------PAG-----AELLDLPLPLINTL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 163 LLLSSGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHHAYTElNLKFNSGAYGSLFYMLTGFHGFHVLLG 242
Cdd:COG1845    66 LLLLSSFTVALAVRAARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAE-GLTPTSNAFGSFFFLLTGFHGLHVIIG 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1337428511 243 ATMLTVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYWM 290
Cdd:COG1845   145 LIWLLVVLVRALRGGFTPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 8-289 4.57e-60

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 191.90  E-value: 4.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511   8 HKEAPYYYVPAdSGHPVRTAAALLLMGLGAAAWINSVSwgKWLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSY 86
Cdd:MTH00130    3 HQAHAYHMVDP-SPWPLTGAVAALLMTSGLAIWFHFHS--TTLMTLGLILLLLTMYQWWRDIVREGTfQGHHTPPVQKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  87 RWGMSWFIFSEVMFFAGFFGALWYVRTITTPWLGdldhklmlwpdfqAVWPnfgPAGVVehfqTVGPFWLPTINTALLLS 166
Cdd:MTH00130   80 RYGMILFITSEVFFFLGFFWAFYHSSLAPTPELG-------------GCWP---PTGIT----TLDPFEVPLLNTAVLLA 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 167 SGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHHAytelNLKFNSGAYGSLFYMLTGFHGFHVLLGATML 246
Cdd:MTH00130  140 SGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTFLQAMEYYEA----PFTIADGVYGSTFFVATGFHGLHVIIGSTFL 215

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1337428511 247 TVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:MTH00130  216 AVCLLRQIQYHFTSEHHFGFEAAAWYWHFVDVVWLFLYISIYW 258
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 8-289 4.95e-59

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 189.17  E-value: 4.95e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511   8 HKEAPYYYVPAdSGHPVRTAAALLLMGLGAAAWINSVSwgKWLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSY 86
Cdd:MTH00099    3 HQTHAYHMVNP-SPWPLTGALSALLMTSGLIMWFHFNS--TTLLTLGLLTNMLTMYQWWRDIIRESTfQGHHTPIVQKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  87 RWGMSWFIFSEVMFFAGFFGALWYVRTITTPWLGdldhklmlwpdfqAVWPnfgPAGVvehfQTVGPFWLPTINTALLLS 166
Cdd:MTH00099   80 RYGMILFIISEVFFFAGFFWAFYHSSLAPTPELG-------------GCWP---PTGI----TPLNPLEVPLLNTSVLLA 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 167 SGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHhaytELNLKFNSGAYGSLFYMLTGFHGFHVLLGATML 246
Cdd:MTH00099  140 SGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTLLQASEYY----EAPFTISDGIYGSTFFMATGFHGLHVIIGSTFL 215

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1337428511 247 TVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:MTH00099  216 IVCFLRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYW 258
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 12-289 1.65e-58

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 187.63  E-value: 1.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  12 PYYYVPaDSGHPVRTAAALLLMGLGAAAWINSVSWgkWLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSYRWGM 90
Cdd:MTH00039    6 PYHLVD-QSPWPLTAAIGALIMTSGLVLWFHGDSI--LLLLLGLLLLILTSINWWRDVIREATfQGMHTLIVINGLRYGM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  91 SWFIFSEVMFFAGFFGALWYVRTITTPWLGdldhklMLWPdfqavwpnfgPAGVvehfQTVGPFWLPTINTALLLSSGVT 170
Cdd:MTH00039   83 ILFITSEVCFFFAFFWAFFHSSLAPTVEIG------VSWP----------PTGI----NPINPFLVPLLNTAVLLSSGVT 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 171 LTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHHAytelNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVIL 250
Cdd:MTH00039  143 ITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEYYDA----PFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCL 218

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1337428511 251 IRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:MTH00039  219 FRLINHHFSNNHHFGFEAAAWYWHFVDVVWLFLYVCIYW 257
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 79-290 2.76e-57

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: 182.02  E-value: 2.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  79 SKRIDNSYRWGMSWFIFSEVMFFAGFFGALWYVRTITTPWLGdldhklmlwpdfqavwpnfgpagvvehfQTVGPFWLPT 158
Cdd:cd00386     2 TASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFG----------------------------AGLDPLDLPL 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 159 INTALLLSSGVTLTIAHH--ALRENHRGKTIFWLLATVVLGFIFVACQAAEYHHAYTELNlkfnSGAYGSLFYMLTGFHG 236
Cdd:cd00386    54 LNTNTLLLSGSSVTWAHAslAARRGNRKKARLWLLLTILLGLAFLGLQAYEYSHLIFTIS----DSVFGSTFFLLTGFHG 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1337428511 237 FHVLLGATMLTVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYWM 290
Cdd:cd00386   130 LHVIIGLIFLLVVLIRLRRGHFTPRHHLGLEAAALYWHFVDVVWLFLFPLVYLW 183
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 23-289 1.65e-56

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 182.64  E-value: 1.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  23 PVRTAAALLLMGLGAAAWINSVSwgKWLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSYRWGMSWFIFSEVMFF 101
Cdd:MTH00075   17 PLTGAIAALLLTSGLAMWFHFGS--MIIMLLGLIIMLLTMFQWWRDIVREGTfQGHHTPPVQKGLRYGMILFITSEVFFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 102 AGFFGALWYVRTITTPWLGDldhklmlwpdfqaVWPnfgPAGVVehfqTVGPFWLPTINTALLLSSGVTLTIAHHALREN 181
Cdd:MTH00075   95 LGFFWAFYNSSLAPTPELGE-------------CWP---PTGIT----PLDPFEVPLLNTAVLLASGVTVTWAHHSIMQG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 182 HRGKTIFWLLATVVLGFIFVACQAAEYHHAytelNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIRLIRGHFTAD 261
Cdd:MTH00075  155 NRKEAIQSLALTIILGLYFTLLQAMEYYEA----PFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQ 230

                         250       260
                  ....*....|....*....|....*...
gi 1337428511 262 HHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:MTH00075  231 HHFGFEAAAWYWHFVDVVWLFLYVSIYW 258
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 49-289 4.72e-56

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 181.49  E-value: 4.72e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  49 WLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSYRWGMSWFIFSEVMFFAGFFGALWYVRTITTPWLGdldhklm 127
Cdd:MTH00024   41 FILYLGLLVIVGVMFVWWQDVIRESTfQGHHSLIVKQGLKYGMLLFILSEVLFFFSFFWAFFHSSLAPAVELG------- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 128 lwpdfqAVWPnfgPAGVVehfqTVGPFWLPTINTALLLSSGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAE 207
Cdd:MTH00024  114 ------VVWP---PQGIN----PLNPFSVPLLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 208 YHHAytelNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFV 287
Cdd:MTH00024  181 YYEA----PFAISDSVYGSTFFVATGFHGLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVDVVWLFLYLCI 256


                  ..
gi 1337428511 288 YW 289
Cdd:MTH00024  257 YW 258
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 49-289 9.03e-52

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 170.36  E-value: 9.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  49 WLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSYRWGMSWFIFSEVMFFAGFFGALWYVRTITTPWLGdldhklm 127
Cdd:MTH00052   42 WVLILGLITIIFTMVVWWRDVIRESTyQGHHTLIVKQGLKYGMILFIVSEVCLFFSFFWAFFHSSLAPTIEIG------- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 128 lwpdfqAVWPnfgPAGVvehfQTVGPFWLPTINTALLLSSGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAE 207
Cdd:MTH00052  115 ------AVWP---PRGV----DPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTGLQAME 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 208 YHHAytelNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFV 287
Cdd:MTH00052  182 YYEA----PFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFVDVVWLFLFIFM 257


                  ..
gi 1337428511 288 YW 289
Cdd:MTH00052  258 YW 259
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 23-289 1.80e-50

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 167.27  E-value: 1.80e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  23 PVRTAAALLLMGLGAAAWINSVSWGkwLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSYRWGMSWFIFSEVMFF 101
Cdd:MTH00219   18 PLTGSLGALMLTSGLVAWFHHYNLD--LLILGLLIIVLTMIQWWRDVIRESTfMGLHTSKVSTGLRIGMILFIVSEILFF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 102 AGFFGALWYVRTITTPWLGdldhklmlwpdfqAVWPnfgPAGVvehfQTVGPFWLPTINTALLLSSGVTLTIAHHALREN 181
Cdd:MTH00219   96 FAFFWAFFHSSLAPTIELG-------------SCWP---PTGI----NPLNPFQVPLLNTAVLLASGVTVTWAHHSLMES 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 182 HRGKTIFWLLATVVLGFIFVACQAAEYhhayTELNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIRLIRGHFTAD 261
Cdd:MTH00219  156 NHKEAQQGLLFTILLGLYFTMLQGMEY----LEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGLMLHFSKN 231

                         250       260
                  ....*....|....*....|....*...
gi 1337428511 262 HHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:MTH00219  232 HHFGFEAAAWYWHFVDVVWLFLYVSIYW 259
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 23-289 3.46e-47

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 158.46  E-value: 3.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  23 PVRTAAALLLMGLGAAAWINSvsWGKWLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSYRWGMSWFIFSEVMFF 101
Cdd:MTH00009   15 PLTGSIGAFTLTVGLASWFHG--YGTLCLILGLIIIILTMIQWWRDVIREGTyMGHHTSYVTKGLRWGMILFIASEVMFF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 102 AGFFGALWYVRTITTPWLGdldhklmlwpdfqAVWPnfgPAGVvehfQTVGPFWLPTINTALLLSSGVTLTIAHHALREN 181
Cdd:MTH00009   93 FAFFWAFFHSSLAPTPELG-------------CSWP---PTGI----EPLNPFSVPLLNTAVLLASGVTVTWAHHSLIEG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 182 HRGKTIFWLLATVVLGFIFVACQAAEYhhayTELNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIRLIRGHFTAD 261
Cdd:MTH00009  153 DRPEATQALILTVLLGAYFTFLQAGEY----IEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRTWSHHFSTG 228

                         250       260
                  ....*....|....*....|....*...
gi 1337428511 262 HHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:MTH00009  229 HHFGFEAAAWYWHFVDVVWIFLYLCIYW 256
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 55-289 1.25e-45

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 154.34  E-value: 1.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  55 FLSLIVILYYWFGDAIRESEAGLNSKRIDNSYRWGMSWFIFSEVMFFAGFFgalWYVrtittpwlgdLDHKLMLWPDFQA 134
Cdd:MTH00083   44 LLYLLFISFLWGKDISMEGLSGYHNFFVMDGFKFGMILFIFSEFMFFFSIF---WTF----------FDAALVPVHELGG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 135 VWPNFGpagvvehFQTVGPFWLPTINTALLLSSGVTLTIAHHALRENHRgKTIFWLLATVVLGFIFVACQAAEYhhayTE 214
Cdd:MTH00083  111 VWSPIG-------IHLVNYLGVPLLNTIILLSSGVSVTWSHHSLCLSNK-SCTNSLLLTCFLGLYFTSFQLMEY----KE 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1337428511 215 LNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:MTH00083  179 ASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDVVWLFLFVFVYW 253
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 50-289 1.53e-42

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 147.91  E-value: 1.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  50 LVLAGFLSLIVILYYWFGDAIRE-SEAGLNSKRIDNSYRWGMSWFIFSEVMFFAGFFGALWYVRTITTPWLGdldhklml 128
Cdd:MTH00028   42 LALTGLFLIIITASAWWRDVIREgTHQGHHTQIVVRGLKLGMLLFILSEVCLFFAFFWAFFHSSLAPSVELG-------- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 129 wpdfqAVWPnfgPAGVvehfQTVGPFWLPTINTALLLSSGVTLTIAHHA------------------------------- 177
Cdd:MTH00028  114 -----SVWP---PKGI----EALDPFAVPLLNTTILLSSGATVTWAHHAiigtgnpaslekgtqgiegpnpsngappdpq 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 178 -----LRENHRGKTIFWLLATVVLGFIFVACQAAEYhhayTELNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIR 252
Cdd:MTH00028  182 kgptfLLSDFRTNAVIGLLMTILLGIIFTGLQAFEY----KEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIR 257

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1337428511 253 LIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:MTH00028  258 LLSNQFTNSHHLGLEAAIWYWHFVDVVWLFLYVFVYW 294
PLN02194 PLN02194
cytochrome-c oxidase
 14-289 2.83e-38

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 135.56  E-value: 2.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  14 YYVPADSGHPVRTAAALLLMGLGAAAWINSVSWGKWLVLAGFLSLIVILYYWFGDAIRESE-AGLNSKRIDNSYRWGMSW 92
Cdd:PLN02194    9 YHLVDPSPWPISGSLGALATTVGGVMYMHPFQGGARLLSLGLIFILYTMFVWWRDVLRESTlEGHHTKVVQLGPRYGSIL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  93 FIFSEVMFFAGFFGALWYVRTITTPWLGdldhklmlwpdfqAVWPnfgPAGVvehfQTVGPFWLPTINTALLLSSGVTLT 172
Cdd:PLN02194   89 FIVSEVMFFFAFFWASSHSSLAPAVEIG-------------GIWP---PKGI----EVLDPWEIPFLNTPILPSSGAAVT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 173 IAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHHAytelNLKFNSGAYGSLFYMLTGFHGFHVLLGATMLTVILIR 252
Cdd:PLN02194  149 WAHHAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQA----PFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIR 224

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1337428511 253 LIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:PLN02194  225 QYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYW 261
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 89-290 2.29e-26

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: 101.93  E-value: 2.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  89 GMSWFIFSEVMFFAGFFGALWYVRTITtpwlgdldhklmlwpdfqavwpnfgPAGVVEHFQTVGPfWLPTINTALLLSSG 168
Cdd:cd02862    12 GMWVFILSELLAFGALFIAYAVYRALY-------------------------PELFAAGSAHLDL-LLGALNTLVLLTSS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 169 VTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHHAYTELNLKfNSGAYGSLFYMLTGFHGFHVLLGATMLTV 248
Cdd:cd02862    66 FTVALAVRAARAGRRRRARRWLAAAVLLGLVFLVIKYFEYAHKIAAGIDP-DAGLFFTLYFLLTGFHLLHVLIGLGILLW 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1337428511 249 ILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYWM 290
Cdd:cd02862   145 VAWRARRGRYSARDYEGVEAAALYWHMVDLVWIVLFPLLYLV 186
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 158-290 2.59e-26

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: 101.93  E-value: 2.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 158 TINTALLLSSGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHHAYTElNLKFNSGAYGSLFYMLTGFHGF 237
Cdd:cd02863    54 FIETFLLLLSSFTCGLAMIAMNKNNKKKVILWLIITFLLGLGFVGMEIYEFHHLIAE-GAGPDRSAFLSAFFTLVGTHGL 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1337428511 238 HVLLGATMLTVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYWM 290
Cdd:cd02863   133 HVTFGLIWILVMIIQLKKRGLTPDTARRLFCLSLFWHFLDIVWIFVFTVVYLL 185
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 84-290 5.14e-22

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: 91.02  E-value: 5.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  84 NSYRWGMSWFIFSEVMFFAGFFGALWYVRTITTPWlgdldhklmlwpdfqavWPNFGPAGVVEHFQTVGPFWLPTINTAL 163
Cdd:cd02864     7 SWGKAMMWFFLLSDAFIFSSFLIAYMTARISTTEP-----------------WPLPSDVFALRIGHFNIPLVLIAIMTFI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 164 LLSSGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEY-----HHAYTELNLKFNSGAYGSLFYMLTGFHGFH 238
Cdd:cd02864    70 LITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWtklivEEGVRPWGNPWGAAQFGASFFMITGFHGTH 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1337428511 239 VLLGATMLTVILIRLIRGHFTADHHF-GFEGAAWYWHFVDVVWLGLYLFVYWM 290
Cdd:cd02864   150 VTIGVIYLIIIARKVWRGKYQRIGRYeIVEIAGLYWHFVDLVWVFIFAFFYLW 202
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 83-289 2.05e-19

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: 83.57  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511  83 DNSYRWGMSWFIFSEVMFFAGFFGALWYVRTITTpwlgdldhklmlwpdfqaVWPNFGPAGVvehfqtvgpfWLPTINTA 162
Cdd:cd02865     6 RSPGWWGLWVFMAVEGTLFALLISAYFMRMTSGD------------------WQPGAPLPLP----------NLLSLNTA 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 163 LLLSSGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHhAYTELNLKFNSGAYGSLFYMLTGFHGFHVLLG 242
Cdd:cd02865    58 VLAASSVAMQWARRAARRNRRVLARLGLALAGALALAFLAGQLLAWH-ALNDAGYGPTSNPAGSFFYLLTGLHGLHVIGG 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1337428511 243 ATMLTVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYW 289
Cdd:cd02865   137 LVALAIVLAGLIRGHYGPRRRLPVELCALYWHFLLLVWLVLLALLYG 183
QoxC TIGR02897
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ...
 154-288 1.57e-13

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: 67.57  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 154 FWLPTINTALLLSSGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHHAYTElNLKFNSGAYGSLFYMLTG 233
Cdd:TIGR02897  52 LPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMIITLLLGAGFVGFEIYEFAHYASE-GVTPQIGSYWSSFFVLLG 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1337428511 234 FHGFHVLLGATMLTVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVY 288
Cdd:TIGR02897 131 THGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYWHFLDVVWVFIFTAVY 185
PRK10663 PRK10663
cytochrome o ubiquinol oxidase subunit III; Provisional
 159-290 8.71e-13

cytochrome o ubiquinol oxidase subunit III; Provisional


Pssm-ID: 182628  Cd Length: 204  Bit Score: 65.96  E-value: 8.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 159 INTALLLSSGVTLTIAHHALRENHRGKTIFWLLATVVLGFIFVACQAAEYHHAYTElNLKFNSGAYGSLFYMLTGFHGFH 238
Cdd:PRK10663   71 VETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHHLIVE-GMGPDRSGFLSAFFALVGTHGLH 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1337428511 239 VLLGATMLTVILIRLIRGHFTADHHFGFEGAAWYWHFVDVVWLGLYLFVYWM 290
Cdd:PRK10663  150 VTSGLIWMAVLMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLM 201
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 153-288 4.41e-10

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 58.39  E-value: 4.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 153 PFWLPTINTALLLSSGVTLTIAHHALRENHRGktiFWLLATVVLGFIFVACQAAEYHHayTELNLKFNSgaYGSLFYMLT 232
Cdd:MTH00049   89 SLEIPFVGCFLLLGSSITVTAYHHLLGWKYCD---LFLYLTILLGLLFVVLQVFEFEE--SGVNSLDSS--YYASCFCTV 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428511 233 GFHGFHVLLGATMLTVILI----RLIRGHFTAdhhfgfegAAWYWHFVDVVWLGLYLFVY 288
Cdd:MTH00049  162 GLHFSHVVLGVVGLSTLLLvgssSFGVYRSTV--------LTWYWHFVDYIWLLVYLIVY 213
 
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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