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Conserved domains on  [gi|1938964883|gb|QPK41424|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Capitella teleta]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-216 6.16e-127

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 367.66  E-value: 6.16e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGSFLG-EQVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:MTH00153   25 GMVGTSLSLLIRAELGQPGSLIGdDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:MTH00153  105 PSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVW 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00153  185 SVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-216 6.16e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 367.66  E-value: 6.16e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGSFLG-EQVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:MTH00153   25 GMVGTSLSLLIRAELGQPGSLIGdDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:MTH00153  105 PSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVW 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00153  185 SVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-216 2.61e-124

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. 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 I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 360.26  E-value: 2.61e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   1 GGLVGTTMSVLIRTELAVPGSFLGE-QVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLL 79
Cdd:cd01663    17 SGLVGTSLSLLIRLELSQPGSQLGNdQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  80 PPSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLV 159
Cdd:cd01663    97 PPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1938964883 160 WSLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:cd01663   177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 233
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-216 1.88e-76

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 239.26  E-value: 1.88e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   3 LVGTTMSVLIRTELAVPGS-FLGEQVYNTVVTAHAFLMIFFLVMPvFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLPP 81
Cdd:COG0843    31 LIGGLLALLMRLQLAGPGLgLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  82 SLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVWS 161
Cdd:COG0843   110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1938964883 162 LSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:COG0843   190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-216 2.73e-76

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 237.89  E-value: 2.73e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGS-FLGEQVYNTVVTAHAFLMIFFLVMPVFmGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:TIGR02891  21 FLVGGVLALLMRAQLATPGNtFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:TIGR02891 100 FGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVW 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:TIGR02891 180 GILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPE 235
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-216 9.37e-46

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 156.58  E-value: 9.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGS-FLGEQVYNTVVTAHAFLMIFFLVMPvFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:pfam00115  14 FLVGGLLGLLIRLQLAFPGLnFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSaveGGVATGWTVYPPLssniahggPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMeRVTLLVW 160
Cdd:pfam00115  93 LGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVW 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNtsffdpTGGGDPVLYQHLFWFFGHPE 216
Cdd:pfam00115 161 AILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPE 210
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-216 6.16e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 367.66  E-value: 6.16e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGSFLG-EQVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:MTH00153   25 GMVGTSLSLLIRAELGQPGSLIGdDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:MTH00153  105 PSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVW 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00153  185 SVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-216 2.61e-124

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. 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 I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 360.26  E-value: 2.61e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   1 GGLVGTTMSVLIRTELAVPGSFLGE-QVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLL 79
Cdd:cd01663    17 SGLVGTSLSLLIRLELSQPGSQLGNdQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  80 PPSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLV 159
Cdd:cd01663    97 PPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1938964883 160 WSLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:cd01663   177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 233
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-216 5.37e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 340.12  E-value: 5.37e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGSFLGE-QVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:MTH00167   27 GMVGTALSLLIRAELSQPGSLLGDdQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:MTH00167  107 PSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVW 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00167  187 SILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-216 6.15e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 337.34  E-value: 6.15e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   1 GGLVGTTMSVLIRTELAVPGSFLG-EQVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLL 79
Cdd:MTH00223   23 SGLVGTSLSLLIRAELGQPGALLGdDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  80 PPSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLV 159
Cdd:MTH00223  103 PPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFV 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1938964883 160 WSLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00223  183 WSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 239
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-216 2.26e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 328.20  E-value: 2.26e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGSFLG-EQVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:MTH00116   27 GMVGTALSLLIRAELGQPGTLLGdDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:MTH00116  107 PSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVW 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00116  187 SVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-216 1.56e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 325.91  E-value: 1.56e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGSFLG-EQVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:MTH00142   25 GMVGTGLSLLIRAELGQPGSLLGdDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:MTH00142  105 PALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVW 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00142  185 SVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-216 2.48e-106

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 315.30  E-value: 2.48e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   1 GGLVGTTMSVLIRTELAVPGSFLG-EQVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLL 79
Cdd:MTH00007   23 GGLLGTSMSLLIRIELGQPGAFLGsDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  80 PPSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLV 159
Cdd:MTH00007  103 PPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFV 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1938964883 160 WSLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00007  183 WAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 239
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-216 2.06e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 302.90  E-value: 2.06e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGSFLG-EQVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:MTH00037   27 GMVGTAMSVIIRTELAQPGSLLQdDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:MTH00037  107 PSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVW 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00037  187 SVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPE 242
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-216 2.52e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 299.93  E-value: 2.52e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGSFLG-EQVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:MTH00077   27 GMVGTALSLLIRAELSQPGTLLGdDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:MTH00077  107 PSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVW 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00077  187 SVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 242
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-216 4.86e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 296.83  E-value: 4.86e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGSFLGE-QVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:MTH00183   27 GMVGTALSLLIRAELSQPGALLGDdQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:MTH00183  107 PSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVW 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00183  187 AVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-216 2.21e-97

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 292.56  E-value: 2.21e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGSFLG-EQVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:MTH00103   27 GMVGTALSLLIRAELGQPGTLLGdDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:MTH00103  107 PSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVW 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00103  187 SVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-216 7.70e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 286.33  E-value: 7.70e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGSFLGE-QVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:MTH00182   29 GMIGTAFSMLIRLELSAPGAMLGDdHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:MTH00182  109 PALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVW 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00182  189 SILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-216 8.92e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 285.95  E-value: 8.92e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   1 GGLVGTTMSVLIRTELAVPGSFLGE-QVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLL 79
Cdd:MTH00184   28 AGMIGTAFSMLIRLELSAPGSMLGDdHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  80 PPSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLV 159
Cdd:MTH00184  108 PPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFV 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1938964883 160 WSLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00184  188 WSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-216 1.31e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 280.03  E-value: 1.31e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGSFLGE-QVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:MTH00079   28 GMVGTSLSLIIRLELSKPGLLLGNgQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSnIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:MTH00079  108 TSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVW 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00079  187 TVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPE 242
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-216 5.11e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 263.80  E-value: 5.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGSFLGE-QVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:MTH00026   28 GAIGTAFSMLIRLELSSPGSMLGDdHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:MTH00026  108 PALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVW 187

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00026  188 SVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 243
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-216 6.05e-80

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 246.29  E-value: 6.05e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGS-FLGEQVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPlMLSAPDMAFPRMNNLSFWLLP 80
Cdd:cd00919    16 LLLGGLLALLIRLELATPGSlFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:cd00919    95 PGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVW 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:cd00919   175 SVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPE 230
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-216 1.88e-76

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 239.26  E-value: 1.88e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   3 LVGTTMSVLIRTELAVPGS-FLGEQVYNTVVTAHAFLMIFFLVMPvFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLPP 81
Cdd:COG0843    31 LIGGLLALLMRLQLAGPGLgLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  82 SLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVWS 161
Cdd:COG0843   110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1938964883 162 LSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:COG0843   190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-216 2.73e-76

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 237.89  E-value: 2.73e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGS-FLGEQVYNTVVTAHAFLMIFFLVMPVFmGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:TIGR02891  21 FLVGGVLALLMRAQLATPGNtFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVW 160
Cdd:TIGR02891 100 FGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVW 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:TIGR02891 180 GILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPE 235
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-216 3.44e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 222.25  E-value: 3.44e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   1 GGLVGTTMSVLIRTELAVP-GSFLGEQVYNTVVTAHAFLMIFFLVMPVFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLL 79
Cdd:MTH00048   27 SGFVGLSLSLLIRLNFLDPyYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  80 PPSLILLLASsaVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSmIMERVTLLV 159
Cdd:MTH00048  107 VPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN-VFSRTSIIL 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1938964883 160 WSLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:MTH00048  184 WSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPE 240
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 3-216 8.83e-63

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 202.81  E-value: 8.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   3 LVGTTMSVLIRTELAVP-GSFLGEQVYNTVVTAHAFLMIFFLVMPvFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLPP 81
Cdd:cd01662    23 LRGGVDALLMRTQLALPgNDFLSPEHYNQIFTMHGTIMIFLFAMP-LVFGLMNYLVPLQIGARDVAFPRLNALSFWLFLF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  82 SLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVWS 161
Cdd:cd01662   102 GGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWT 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1938964883 162 LSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:cd01662   182 TLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPE 236
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-216 9.37e-46

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 156.58  E-value: 9.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   2 GLVGTTMSVLIRTELAVPGS-FLGEQVYNTVVTAHAFLMIFFLVMPvFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLP 80
Cdd:pfam00115  14 FLVGGLLGLLIRLQLAFPGLnFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  81 PSLILLLASSaveGGVATGWTVYPPLssniahggPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMeRVTLLVW 160
Cdd:pfam00115  93 LGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVW 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1938964883 161 SLSITAMLLIGSLPVLAAGITMLLTDRNLNtsffdpTGGGDPVLYQHLFWFFGHPE 216
Cdd:pfam00115 161 AILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPE 210
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 9-216 1.77e-40

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I 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: 131928  Cd Length: 643  Bit Score: 145.77  E-value: 1.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   9 SVLIRTELAVPG-SFLGEQVYNTVVTAHAFLMIFFLVMPvFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWLLPPSLILLL 87
Cdd:TIGR02882  72 ALLMRAQLTVPDnKFLDAQHYNEIFTTHGVIMIIFMAMP-FIIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  88 ASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLLVWSLSITAM 167
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1938964883 168 LLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPE 279
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 3-216 1.29e-38

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 140.84  E-value: 1.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883   3 LVGTTMSVLIRTELAVPGS----FLGEQVYNTVVTAHAFLMIFFLVMPvFMGGFGNWLIPLMLSAPDMAFPRMNNLSFWL 78
Cdd:PRK15017   70 LRGFADAIMMRSQQALASAgeagFLPPHHYDQIFTAHGVIMIFFVAMP-FVIGLMNLVVPLQIGARDVAFPFLNNLSFWF 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938964883  79 LPPSLILLLASSAVEGGVATGWTVYPPLSSNIAHGGPAVDMAIFSLHLAGISSIMASMNFLLTVYNMRTSSMIMERVTLL 158
Cdd:PRK15017  149 TVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVF 228

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1938964883 159 VWSLSITAMLLIGSLPVLAAGITMLLTDRNLNTSFFDPTGGGDPVLYQHLFWFFGHPE 216
Cdd:PRK15017  229 TWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPE 286
 
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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