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Conserved domains on  [gi|1883393032|gb|QMS43849|]
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cytochrome c oxidase III, partial (mitochondrion) [Hepatozoon clamatae]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like super family cl00211
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 39-213 3.76e-13

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


The actual alignment was detected with superfamily member cd00386:

Pssm-ID: 444752  Cd Length: 183  Bit Score: 64.92  E-value: 3.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032  39 ILTEALLFAGYFWGAFQLSWSSMTE--AAIPASSRSLILTITLLLSSASIVCSYLLTIRDKSIYGGASFVVLTIVAIGIT 116
Cdd:cd00386    17 ILSEVMLFGSFFWAYFHSRLSPPVEfgAGLDPLDLPLLNTNTLLLSGSSVTWAHASLAARRGNRKKARLWLLLTILLGLA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 117 FSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLArigTFTLIYQDNNSNTLPFGQAYSIptqhdnyslV 196
Cdd:cd00386    97 FLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLV---VLIRLRRGHFTPRHHLGLEAAA---------L 164

                         170
                  ....*....|....*..
gi 1883393032 197 YWHFVELVWLVLQFVFY 213
Cdd:cd00386   165 YWHFVDVVWLFLFPLVY 181
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 39-213 3.76e-13

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: 64.92  E-value: 3.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032  39 ILTEALLFAGYFWGAFQLSWSSMTE--AAIPASSRSLILTITLLLSSASIVCSYLLTIRDKSIYGGASFVVLTIVAIGIT 116
Cdd:cd00386    17 ILSEVMLFGSFFWAYFHSRLSPPVEfgAGLDPLDLPLLNTNTLLLSGSSVTWAHASLAARRGNRKKARLWLLLTILLGLA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 117 FSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLArigTFTLIYQDNNSNTLPFGQAYSIptqhdnyslV 196
Cdd:cd00386    97 FLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLV---VLIRLRRGHFTPRHHLGLEAAA---------L 164

                         170
                  ....*....|....*..
gi 1883393032 197 YWHFVELVWLVLQFVFY 213
Cdd:cd00386   165 YWHFVDVVWLFLFPLVY 181
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 107-213 7.60e-10

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 57.11  E-value: 7.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 107 VLTIVaIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLArigTFTLIYQDNNSNTLPFGQAYSI 186
Cdd:MTH00155  162 FFTII-LGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLV---CLIRHLNNHFSSNHHFGFEAAA 237

                          90       100
                  ....*....|....*....|....*..
gi 1883393032 187 ptqhdnyslVYWHFVELVWLVLQFVFY 213
Cdd:MTH00155  238 ---------WYWHFVDVVWLFLYISIY 255
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
39-213 5.19e-07

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 48.31  E-value: 5.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032  39 ILTEALLFAGYFWGAFqlsWSSMTEAAIPASSRSLILTITLLLSSASIVCSYLLT-----IRDKSIYGGASFVVLTIVaI 113
Cdd:COG1845    24 LASEVMLFAALFAAYF---VLRASAPDWPAGAELLDLPLPLINTLLLLLSSFTVAlavraARRGDRKGLRLWLLLTLL-L 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 114 GITFSSLQTTEFMMI---HYSINDSLQCCLFFTLTGLHFSHVFVGVVLLL-----ARIGTFTliyqdnnsntlpfgqays 185
Cdd:COG1845   100 GLAFLGLQAYEYSHLiaeGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLvvlvrALRGGFT------------------ 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 1883393032 186 iPTQHDNYSLV--YWHFVELVWLVLQFVFY 213
Cdd:COG1845   162 -PENHTGVEAAalYWHFVDVVWIFLFALVY 190
COX3 pfam00510
Cytochrome c oxidase subunit III;
5-213 9.65e-07

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 48.18  E-value: 9.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032   5 LLSCNFIFFLLFLYSLRESYFS---TFSAISSCCLGIIL---TEALLFAGYFWGAFQLSWSSMTE--AAIPASSRSLILT 76
Cdd:pfam00510  44 LFSLLLTMYLWFRDIIREGTFLgdhTFAVQKGLNLGMILfiiSEVFFFLGIFWAFFHSALSPTVElgAQWPPVGIHPVNP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032  77 ITLLLSSASIVCSYLLTI-----------RDKSIYGgasfVVLTIVaIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLT 145
Cdd:pfam00510 124 FEVPLLNTIILLSSGVTVtyahhsliegnRKQALQG----LILTIL-LAVYFTGLQAMEYTEASFTISDGVYGSTFYFAT 198

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1883393032 146 GLHFSHVFVGVVLLLArigTFTLIYQDNNSNTLPFGQAYSIptqhdnyslVYWHFVELVWLVLQFVFY 213
Cdd:pfam00510 199 GFHGLHVIIGTAFLAV---CFLRLLKYHLTDNHHFGFEAAI---------LYWHFVDVVWLFLYVSVY 254
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 39-213 3.76e-13

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: 64.92  E-value: 3.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032  39 ILTEALLFAGYFWGAFQLSWSSMTE--AAIPASSRSLILTITLLLSSASIVCSYLLTIRDKSIYGGASFVVLTIVAIGIT 116
Cdd:cd00386    17 ILSEVMLFGSFFWAYFHSRLSPPVEfgAGLDPLDLPLLNTNTLLLSGSSVTWAHASLAARRGNRKKARLWLLLTILLGLA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 117 FSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLArigTFTLIYQDNNSNTLPFGQAYSIptqhdnyslV 196
Cdd:cd00386    97 FLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLV---VLIRLRRGHFTPRHHLGLEAAA---------L 164

                         170
                  ....*....|....*..
gi 1883393032 197 YWHFVELVWLVLQFVFY 213
Cdd:cd00386   165 YWHFVDVVWLFLFPLVY 181
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 107-213 7.60e-10

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 57.11  E-value: 7.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 107 VLTIVaIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLArigTFTLIYQDNNSNTLPFGQAYSI 186
Cdd:MTH00155  162 FFTII-LGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLV---CLIRHLNNHFSSNHHFGFEAAA 237

                          90       100
                  ....*....|....*....|....*..
gi 1883393032 187 ptqhdnyslVYWHFVELVWLVLQFVFY 213
Cdd:MTH00155  238 ---------WYWHFVDVVWLFLYISIY 255
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 107-213 1.17e-08

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 53.92  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 107 VLTIVAIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLArigTFTLIYQDNNSNTLPFGQAYSI 186
Cdd:MTH00028  199 LLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIV---CFIRLLSNQFTNSHHLGLEAAI 275

                          90       100
                  ....*....|....*....|....*..
gi 1883393032 187 ptqhdnyslVYWHFVELVWLVLQFVFY 213
Cdd:MTH00028  276 ---------WYWHFVDVVWLFLYVFVY 293
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 111-213 5.67e-08

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: 51.36  E-value: 5.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 111 VAIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLArigTFTLIYQDNNSNTLPFGQAYSIptqh 190
Cdd:cd01665   151 ILLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTV---CLIRLLKGHFSSNHHLGFEAAI---- 223

                          90       100
                  ....*....|....*....|...
gi 1883393032 191 dnyslVYWHFVELVWLVLQFVFY 213
Cdd:cd01665   224 -----WYWHFVDVVWLFLFVFVY 241
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 111-212 2.05e-07

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 50.18  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 111 VAIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLarIGTFTLIYQDNnsntlpfgqaysipTQH 190
Cdd:MTH00052  168 VALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLL--VCLFRLINHQF--------------TRH 231

                          90       100
                  ....*....|....*....|....*.
gi 1883393032 191 DNY----SLVYWHFVELVWLVLqFVF 212
Cdd:MTH00052  232 HHFgfeaAAWYWHFVDVVWLFL-FIF 256
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
39-213 5.19e-07

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


Pssm-ID: 441450  Cd Length: 192  Bit Score: 48.31  E-value: 5.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032  39 ILTEALLFAGYFWGAFqlsWSSMTEAAIPASSRSLILTITLLLSSASIVCSYLLT-----IRDKSIYGGASFVVLTIVaI 113
Cdd:COG1845    24 LASEVMLFAALFAAYF---VLRASAPDWPAGAELLDLPLPLINTLLLLLSSFTVAlavraARRGDRKGLRLWLLLTLL-L 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 114 GITFSSLQTTEFMMI---HYSINDSLQCCLFFTLTGLHFSHVFVGVVLLL-----ARIGTFTliyqdnnsntlpfgqays 185
Cdd:COG1845   100 GLAFLGLQAYEYSHLiaeGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLvvlvrALRGGFT------------------ 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 1883393032 186 iPTQHDNYSLV--YWHFVELVWLVLQFVFY 213
Cdd:COG1845   162 -PENHTGVEAAalYWHFVDVVWIFLFALVY 190
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 103-208 7.24e-07

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 48.41  E-value: 7.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 103 ASFVVLTIVAIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLArigtfTLIYQDNNSNTlpfgq 182
Cdd:MTH00118  159 AIQALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIV-----CLLRLIKFHFT----- 228

                          90       100
                  ....*....|....*....|....*...
gi 1883393032 183 aysiPTQHDNYSLV--YWHFVELVWLVL 208
Cdd:MTH00118  229 ----TNHHFGFEAAawYWHFVDVVWLFL 252
COX3 pfam00510
Cytochrome c oxidase subunit III;
5-213 9.65e-07

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 48.18  E-value: 9.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032   5 LLSCNFIFFLLFLYSLRESYFS---TFSAISSCCLGIIL---TEALLFAGYFWGAFQLSWSSMTE--AAIPASSRSLILT 76
Cdd:pfam00510  44 LFSLLLTMYLWFRDIIREGTFLgdhTFAVQKGLNLGMILfiiSEVFFFLGIFWAFFHSALSPTVElgAQWPPVGIHPVNP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032  77 ITLLLSSASIVCSYLLTI-----------RDKSIYGgasfVVLTIVaIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLT 145
Cdd:pfam00510 124 FEVPLLNTIILLSSGVTVtyahhsliegnRKQALQG----LILTIL-LAVYFTGLQAMEYTEASFTISDGVYGSTFYFAT 198

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1883393032 146 GLHFSHVFVGVVLLLArigTFTLIYQDNNSNTLPFGQAYSIptqhdnyslVYWHFVELVWLVLQFVFY 213
Cdd:pfam00510 199 GFHGLHVIIGTAFLAV---CFLRLLKYHLTDNHHFGFEAAI---------LYWHFVDVVWLFLYVSVY 254
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 94-213 1.36e-06

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 47.58  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032  94 IRDKSIYGGASFVVLTIVaIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLarIGTFTLIYQDN 173
Cdd:MTH00141  149 LMEGDYKSALQGLGLTII-LGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLL--VCLVRLLLGHF 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1883393032 174 NSNtlpfgqaysiptQHDNYSLV--YWHFVELVWLVLQFVFY 213
Cdd:MTH00141  226 STN------------HHFGFEAAawYWHFVDVVWLFLYLSIY 255
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 104-213 7.45e-06

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 45.33  E-value: 7.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 104 SFVVLTIVaIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLarigtFTLIYQDNNSNTLPFGQA 183
Cdd:MTH00083  156 NSLLLTCF-LGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLL-----FNLLRLLKSHFNYNHHLG 229

                          90       100       110
                  ....*....|....*....|....*....|
gi 1883393032 184 YsiptqhdNYSLVYWHFVELVWLVLQFVFY 213
Cdd:MTH00083  230 L-------EFAILYWHFVDVVWLFLFVFVY 252
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 111-213 9.08e-06

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 45.10  E-value: 9.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 111 VAIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLARIGTFTLIYQDNNSNtlpFGQAYSIptqh 190
Cdd:MTH00039  166 VLLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSNNHH---FGFEAAA---- 238

                          90       100
                  ....*....|....*....|...
gi 1883393032 191 dnyslVYWHFVELVWLVLQFVFY 213
Cdd:MTH00039  239 -----WYWHFVDVVWLFLYVCIY 256
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 100-208 1.67e-05

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 44.19  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 100 YGGASFVVLTIVAIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLARIGTfTLIYQDNNSNTLP 179
Cdd:MTH00189  155 RKEAIQALTLTVILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLR-QIQGHFTSSHHFG 233

                          90       100
                  ....*....|....*....|....*....
gi 1883393032 180 FGQAysiptqhdnysLVYWHFVELVWLVL 208
Cdd:MTH00189  234 FEAA-----------AWYWHFVDVVWLFL 251
COX3 MTH00024
cytochrome c oxidase subunit III; Validated
 111-213 6.67e-05

cytochrome c oxidase subunit III; Validated


Pssm-ID: 214403  Cd Length: 261  Bit Score: 42.43  E-value: 6.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 111 VAIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLL---LARIgtftLIYQDNNSNTLPFGQAYSip 187
Cdd:MTH00024  167 VFLGVLFTGLQAIEYYEAPFAISDSVYGSTFFVATGFHGLHVIIGTTFLfvcLLRL----LSNQFTRRQHVGFEAASW-- 240

                          90       100
                  ....*....|....*....|....*.
gi 1883393032 188 tqhdnyslvYWHFVELVWLVLQFVFY 213
Cdd:MTH00024  241 ---------YWHFVDVVWLFLYLCIY 257
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 98-213 1.24e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 41.70  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032  98 SIYGGASFVVLTIVAIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLArigTFTLIYQDNNSNT 177
Cdd:MTH00219  155 SNHKEAQQGLLFTILLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFV---CFMRGLMLHFSKN 231

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1883393032 178 LPFGQaysiptqhdNYSLVYWHFVELVWLVLQFVFY 213
Cdd:MTH00219  232 HHFGF---------EAAAWYWHFVDVVWLFLYVSIY 258
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 140-213 1.27e-04

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: 41.07  E-value: 1.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1883393032 140 LFFTLTGLHFSHVFVGVVLLL-----ARIGTFTLIYQDNNSNtlpfgqaysiptqhdnySLVYWHFVELVWLVLQFVFY 213
Cdd:cd02862   123 LYFLLTGFHLLHVLIGLGILLwvawrARRGRYSARDYEGVEA-----------------AALYWHMVDLVWIVLFPLLY 184
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 108-213 1.27e-04

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 41.65  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 108 LTIVaIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLArigtfTLIYQDNnsntlpfgqaYSIP 187
Cdd:MTH00075  165 LTII-LGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLV-----CLLRQIN----------FHFT 228

                          90       100
                  ....*....|....*....|....*....
gi 1883393032 188 TQHD---NYSLVYWHFVELVWLVLQFVFY 213
Cdd:MTH00075  229 SQHHfgfEAAAWYWHFVDVVWLFLYVSIY 257
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 107-213 1.57e-04

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 41.64  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 107 VLTIVAIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLlarigTFTLIYQDNNSNTlpfgqaysi 186
Cdd:MTH00099  163 LFITILLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFL-----IVCFLRQLKFHFT--------- 228

                          90       100
                  ....*....|....*....|....*....
gi 1883393032 187 PTQHDNYSLV--YWHFVELVWLVLQFVFY 213
Cdd:MTH00099  229 SNHHFGFEAAawYWHFVDVVWLFLYVSIY 257
PLN02194 PLN02194
cytochrome-c oxidase
 103-213 5.69e-04

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 40.03  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 103 ASFVVLTIVAIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLArIGTFTLIYQDNNSNTLPFGQ 182
Cdd:PLN02194  162 AVYALVATVLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLII-CGIRQYLGHLTKEHHVGFEA 240

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1883393032 183 AysiptqhdnysLVYWHFVELVWLVLQFVFY 213
Cdd:PLN02194  241 A-----------AWYWHFVDVVWLFLFVSIY 260
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 107-213 2.74e-03

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: 37.48  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 107 VLTIVAIGITFSSLQTTEFMMIHYSIND---------SLQCCLFFTLTGLHFSHVFVGVVLLLarigtftliyqdnnsnT 177
Cdd:cd02864    96 MLATALLGATFVGMQAFEWTKLIVEEGVrpwgnpwgaAQFGASFFMITGFHGTHVTIGVIYLI----------------I 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1883393032 178 LPFGQAYSIPTQHDNYSLV-----YWHFVELVWLVLQFVFY 213
Cdd:cd02864   160 IARKVWRGKYQRIGRYEIVeiaglYWHFVDLVWVFIFAFFY 200
COX3 MTH00049
cytochrome c oxidase subunit III; Validated
 105-213 3.14e-03

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177124  Cd Length: 215  Bit Score: 37.20  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883393032 105 FVVLTIVaIGITFSSLQTTEFMMIHYSINDSLQCCLFFTLTGLHFSHVFVGVVLLLarigtfTLIYQDNNSntlpFGQAY 184
Cdd:MTH00049  122 FLYLTIL-LGLLFVVLQVFEFEESGVNSLDSSYYASCFCTVGLHFSHVVLGVVGLS------TLLLVGSSS----FGVYR 190

                          90       100
                  ....*....|....*....|....*....
gi 1883393032 185 SiptqhdNYSLVYWHFVELVWLVLQFVFY 213
Cdd:MTH00049  191 S------TVLTWYWHFVDYIWLLVYLIVY 213
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 140-213 6.31e-03

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: 36.19  E-value: 6.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1883393032 140 LFFTLTGLHFSHVFVGVVLLLarIGTFTLIyqdnnsnTLPFGQAYSIPTQhdnYSLVYWHFVELVWLVLQFVFY 213
Cdd:cd02865   121 FFYLLTGLHGLHVIGGLVALA--IVLAGLI-------RGHYGPRRRLPVE---LCALYWHFLLLVWLVLLALLY 182
 
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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