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Conserved domains on  [gi|1009658528|gb|AMR72730|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Insecta sp. SHSY141205]

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 ...
 1-222 2.31e-117

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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 342.93  E-value: 2.31e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   1 LIMFLVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAA-TGFANWMLPLQIGAPDMALPRLNNWGFW 79
Cdd:cd01663    15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALiGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  80 ILPPSAILLTLPFTLalfgvgDGALATGWTFYPPLSVQG---GIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMT 156
Cdd:cd01663    95 LLPPSLLLLLLSALV------EGGAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMT 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1009658528 157 LMKMPMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:cd01663   169 LEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-222 2.31e-117

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: 342.93  E-value: 2.31e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   1 LIMFLVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAA-TGFANWMLPLQIGAPDMALPRLNNWGFW 79
Cdd:cd01663    15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALiGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  80 ILPPSAILLTLPFTLalfgvgDGALATGWTFYPPLSVQG---GIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMT 156
Cdd:cd01663    95 LLPPSLLLLLLSALV------EGGAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMT 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1009658528 157 LMKMPMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:cd01663   169 LEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-222 7.34e-93

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: 280.65  E-value: 7.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   1 LIMFLVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATGFANWMLPLQIGAPDMALPRLNNWGFWI 80
Cdd:TIGR02891  18 FAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLPLMIGARDMAFPRLNAFSYWL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  81 LPPSAILLTLPFTLalfgvgDGALATGWTFYPPLSV---QGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTL 157
Cdd:TIGR02891  98 YLFGGLLLLASFFT------GGAPDTGWTMYPPLSStsgSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTL 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1009658528 158 MKMPMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:TIGR02891 172 MRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEV 236
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-222 3.97e-88

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 269.69  E-value: 3.97e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   1 LIMFLVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATGFANWMLPLQIGAPDMALPRLNNWGFWI 80
Cdd:COG0843    27 FVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGFGNYLVPLQIGARDMAFPRLNALSFWL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  81 LPPSAILLTLPFtlalfgVGDGALATGWTFYPPLSVQ---GGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTL 157
Cdd:COG0843   107 YLFGGLLLLISL------FVGGAADVGWTFYPPLSGLeasPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTL 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1009658528 158 MKMPMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:COG0843   181 MRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 5-222 8.63e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 267.89  E-value: 8.63e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00153   26 MVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLTLPftlALFGVGDGalaTGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKM 160
Cdd:MTH00153  106 SLTLLLSS---SMVESGAG---TGWTVYPPLSsniAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRM 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00153  180 PLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-222 5.79e-54

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: 178.54  E-value: 5.79e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   1 LIMFLVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATGFANWMLPLQIGAPDMALPRLNNWGFWI 80
Cdd:pfam00115  11 LVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAFPRLNALSFWL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  81 LPPSAILLTLPFtlalfgvgdGALATGWTFYPPLsvqggIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTlMKM 160
Cdd:pfam00115  91 VVLGAVLLLASF---------GGATTGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT-LRM 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGthffdaAGGGDPIMFQHLFWFFGHPEV 222
Cdd:pfam00115 156 PLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEV 211
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-222 2.31e-117

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: 342.93  E-value: 2.31e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   1 LIMFLVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAA-TGFANWMLPLQIGAPDMALPRLNNWGFW 79
Cdd:cd01663    15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALiGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  80 ILPPSAILLTLPFTLalfgvgDGALATGWTFYPPLSVQG---GIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMT 156
Cdd:cd01663    95 LLPPSLLLLLLSALV------EGGAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMT 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1009658528 157 LMKMPMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:cd01663   169 LEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-222 7.34e-93

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: 280.65  E-value: 7.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   1 LIMFLVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATGFANWMLPLQIGAPDMALPRLNNWGFWI 80
Cdd:TIGR02891  18 FAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLPLMIGARDMAFPRLNAFSYWL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  81 LPPSAILLTLPFTLalfgvgDGALATGWTFYPPLSV---QGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTL 157
Cdd:TIGR02891  98 YLFGGLLLLASFFT------GGAPDTGWTMYPPLSStsgSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTL 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1009658528 158 MKMPMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:TIGR02891 172 MRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEV 236
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-222 3.97e-88

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 269.69  E-value: 3.97e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   1 LIMFLVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATGFANWMLPLQIGAPDMALPRLNNWGFWI 80
Cdd:COG0843    27 FVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGFGNYLVPLQIGARDMAFPRLNALSFWL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  81 LPPSAILLTLPFtlalfgVGDGALATGWTFYPPLSVQ---GGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTL 157
Cdd:COG0843   107 YLFGGLLLLISL------FVGGAADVGWTFYPPLSGLeasPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTL 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1009658528 158 MKMPMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:COG0843   181 MRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 5-222 8.63e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 267.89  E-value: 8.63e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00153   26 MVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLTLPftlALFGVGDGalaTGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKM 160
Cdd:MTH00153  106 SLTLLLSS---SMVESGAG---TGWTVYPPLSsniAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRM 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00153  180 PLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 5-222 3.21e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 264.15  E-value: 3.21e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00223   25 LVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLtlpftLALFGVGDGAlATGWTFYPPLSV---QGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKM 160
Cdd:MTH00223  105 SLYLL-----LSSSAVESGV-GTGWTVYPPLSSnlaHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERL 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00223  179 PLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 5-222 6.92e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 247.67  E-value: 6.92e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00167   28 MVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLtlpftLALFGVGDGAlATGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKM 160
Cdd:MTH00167  108 SLLLL-----LASSGVEAGA-GTGWTVYPPLAgnlAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQT 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00167  182 PLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-222 9.71e-78

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: 240.90  E-value: 9.71e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   1 LIMFLVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATGFANWMLPLQIGAPDMALPRLNNWGFWI 80
Cdd:cd00919    13 FVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGARDLAFPRLNNLSFWL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  81 LPPSAILLTLPFtlalfgVGDGALATGWTFYPPLSVQ---GGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTL 157
Cdd:cd00919    93 FPPGLLLLLSSV------LVGGGAGTGWTFYPPLSTLsysSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTL 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1009658528 158 MKMPMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:cd00919   167 DKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEV 231
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 5-222 1.75e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 241.53  E-value: 1.75e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00116   28 MVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLtlpftLALFGVGDGAlATGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKM 160
Cdd:MTH00116  108 SFLLL-----LASSTVEAGA-GTGWTVYPPLAgnlAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQT 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00116  182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 5-222 4.01e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 238.04  E-value: 4.01e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00079   29 MVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGgFGNWMLPLMLGAPDMSFPRLNNLSFWLLPT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLTLPFTLalfgvgDGALATGWTFYPPLSVQGGIG--VDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKMP 161
Cdd:MTH00079  109 SLFLILDSCFV------DMGPGTSWTVYPPLSTLGHPGssVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMS 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1009658528 162 MFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00079  183 LFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEV 243
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 5-222 5.43e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 235.00  E-value: 5.43e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00142   26 MVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLtlpftLALFGVGDGAlATGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKM 160
Cdd:MTH00142  106 ALLLL-----LSSAAVESGA-GTGWTVYPPLSsnlAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERV 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00142  180 PLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-222 6.29e-75

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: 234.40  E-value: 6.29e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   1 LIMFLVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATGFANWMLPLQIGAPDMALPRLNNWGFWI 80
Cdd:cd01662    19 FVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQIGARDVAFPRLNALSFWL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  81 LPPSAILLtlpftLALFGVGDGAlATGWTFYPPLSVQG---GIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTL 157
Cdd:cd01662    99 FLFGGLLL-----NASLLIGGFP-DAGWFAYPPLSGLEyspGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTL 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1009658528 158 MKMPMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:cd01662   173 MRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 5-222 4.81e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 227.79  E-value: 4.81e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00037   28 MVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLIPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLtlpftLALFGVGDGAlATGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKM 160
Cdd:MTH00037  108 SFLLL-----LASAGVESGA-GTGWTIYPPLSsniAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRL 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00037  182 PLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEV 243
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 5-222 2.60e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 225.86  E-value: 2.60e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00182   30 MIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGgFGNWLVPLYIGAPDMAFPRLNNISFWLLPP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLtLPFTLALFGVGdgalaTGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKM 160
Cdd:MTH00182  110 ALILL-LGSAFVEQGAG-----TGWTVYPPLSsiqAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRL 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00182  184 PLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEV 245
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 5-222 4.06e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 225.09  E-value: 4.06e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00184   30 MIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGgFGNWFVPLYIGAPDMAFPRLNNISFWLLPP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLtlpftLALFGVGDGAlATGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKM 160
Cdd:MTH00184  110 ALTLL-----LGSAFVEQGA-GTGWTVYPPLSsiqAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRM 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00184  184 PLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 245
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 5-222 6.14e-70

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 222.08  E-value: 6.14e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00007   25 LLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGgFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLtlpftLALFGVGDGAlATGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKM 160
Cdd:MTH00007  105 ALILL-----VSSAAVEKGV-GTGWTVYPPLAsnlAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERI 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00007  179 PLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 5-222 1.10e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 221.34  E-value: 1.10e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00183   28 MVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLLPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLtlpftLALFGVGDGAlATGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKM 160
Cdd:MTH00183  108 SFLLL-----LASSGVEAGA-GTGWTVYPPLAgnlAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQT 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00183  182 PLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 5-222 2.57e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 220.58  E-value: 2.57e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00077   28 MVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLtlpftLALFGVGDGAlATGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKM 160
Cdd:MTH00077  108 SFLLL-----LASSGVEAGA-GTGWTVYPPLAgnlAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQT 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00077  182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEV 243
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 5-222 3.46e-68

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 217.44  E-value: 3.46e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   5 LVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPP 83
Cdd:MTH00103   28 MVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  84 SAILLtlpftLALFGVGDGAlATGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKM 160
Cdd:MTH00103  108 SFLLL-----LASSMVEAGA-GTGWTVYPPLAgnlAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQT 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00103  182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 6-222 7.37e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 204.09  E-value: 7.37e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   6 VGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPPs 84
Cdd:MTH00026   30 IGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGgFGNWFVPLMIGAPDMAFPRLNNISFWLLPP- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  85 AILLTLPFTLALFGVGdgalaTGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKMP 161
Cdd:MTH00026  109 ALFLLLGSSLVEQGAG-----TGWTVYPPLAsiqAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIP 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1009658528 162 MFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00026  184 LFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 244
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 6-222 4.37e-61

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 198.75  E-value: 4.37e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   6 VGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATG-FANWMLPLQIGAPDMALPRLNNWGFWILPPS 84
Cdd:MTH00048   30 VGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGgFGNYLLPLLLGLSDLNLPRLNALSAWLLVPS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  85 AILLTLPFtlaLFGVGdgalaTGWTFYPPLSVQ---GGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLmKMP 161
Cdd:MTH00048  110 IVFLLLSM---CLGAG-----VGWTFYPPLSSSlfsSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTS 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1009658528 162 MFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:MTH00048  181 IILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEV 241
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-222 5.79e-54

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: 178.54  E-value: 5.79e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528   1 LIMFLVGGSMILGIRAELFKPGLQLMNPEFFNQLIGVHALIMIFAALMPAATGFANWMLPLQIGAPDMALPRLNNWGFWI 80
Cdd:pfam00115  11 LVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAFPRLNALSFWL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  81 LPPSAILLTLPFtlalfgvgdGALATGWTFYPPLsvqggIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTlMKM 160
Cdd:pfam00115  91 VVLGAVLLLASF---------GGATTGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT-LRM 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009658528 161 PMFAWGWLITAFLLIATIPVLAGAVTMLLTDRHFGthffdaAGGGDPIMFQHLFWFFGHPEV 222
Cdd:pfam00115 156 PLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEV 211
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 25-222 3.74e-45

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 158.95  E-value: 3.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528  25 LMNPEFFNQLIGVHALIMIFAALMPAATGFANWMLPLQIGAPDMALPRLNNWGFWILPPSAILLTLPFtlalfGVGDGAl 104
Cdd:PRK15017   93 FLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSL-----GVGEFA- 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009658528 105 ATGWTFYPPLS---VQGGIGVDFAIFAVHLLGISSVLGSINIIVTIYNMRAPGMTLMKMPMFAWGWLITAFLLIATIPVL 181
Cdd:PRK15017  167 QTGWLAYPPLSgieYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPIL 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1009658528 182 AGAVTMLLTDRHFGTHFFDAAGGGDPIMFQHLFWFFGHPEV 222
Cdd:PRK15017  247 TVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEV 287
 
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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