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Conserved domains on  [gi|2178351184|gb|UIX25993|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Dinophysis tripos]

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 ...
 1-244 2.69e-90

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: 275.52  E-value: 2.69e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:cd01663     3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:cd01663    80 APDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSI-LAHSGPSVDLAIFSLHLAGISSILGAINFITT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:cd01663   159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238


                  ....
gi 2178351184 241 VPAF 244
Cdd:cd01663   239 LPGF 242
 
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 ...
 1-244 2.69e-90

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: 275.52  E-value: 2.69e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:cd01663     3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:cd01663    80 APDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSI-LAHSGPSVDLAIFSLHLAGISSILGAINFITT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:cd01663   159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238


                  ....
gi 2178351184 241 VPAF 244
Cdd:cd01663   239 LPGF 242
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-244 1.12e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 248.74  E-value: 1.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00223    9 HKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQ---LYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00223   86 APDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLS-SNLAHAGPSVDLAIFSLHLAGVSSILGAINFITT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00223  165 IINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 244


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00223  245 LPGF 248
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-244 1.48e-71

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: 227.49  E-value: 1.48e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQG 80
Cdd:TIGR02891   6 HKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAE---TYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWT 159
Cdd:TIGR02891  82 ARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSS--TSGSPGVGVDLwLLGLHLLGISSILGAVNFIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 160 TIINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYIL 239
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239


                  ....*
gi 2178351184 240 IVPAF 244
Cdd:TIGR02891 240 FLPAF 244
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-244 1.78e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 223.08  E-value: 1.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQG 80
Cdd:COG0843    15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPE---TYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWT 159
Cdd:COG0843    91 ARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSG--LEASPGVGVDLwLLGLALFGVGSILGGVNFIV 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 160 TIINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYIL 239
Cdd:COG0843   169 TILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYIL 248


                  ....*
gi 2178351184 240 IVPAF 244
Cdd:COG0843   249 ILPAF 253
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-244 1.03e-45

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: 158.51  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   3 RLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGgFGNYFVPIFQGSP 82
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPL---TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  83 EVVYPRINNFSILILSLSylfVILSLISEFGGGTGWTLYPPLSTSFLslspsstgnLIFGLLISGISSCLTSLNFWTTII 162
Cdd:pfam00115  77 DMAFPRLNALSFWLVVLG---AVLLLASFGGATTGWTEYPPLVGVDL---------WYIGLLLAGVSSLLGAINFIVTIL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 163 NLRSYYLTLKtMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFfdpifeGDPIFYQHLFWFFGHPEVYILIVP 242
Cdd:pfam00115 145 KRRAPGMTLR-MPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGG------GDPLLDQHLFWWFGHPEVYILILP 217


                  ..
gi 2178351184 243 AF 244
Cdd:pfam00115 218 AF 219
 
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 ...
 1-244 2.69e-90

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: 275.52  E-value: 2.69e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:cd01663     3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:cd01663    80 APDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSI-LAHSGPSVDLAIFSLHLAGISSILGAINFITT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:cd01663   159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238


                  ....
gi 2178351184 241 VPAF 244
Cdd:cd01663   239 LPGF 242
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-244 1.12e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 248.74  E-value: 1.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00223    9 HKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQ---LYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00223   86 APDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLS-SNLAHAGPSVDLAIFSLHLAGVSSILGAINFITT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00223  165 IINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 244


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00223  245 LPGF 248
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-244 7.72e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 246.70  E-value: 7.72e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00153   10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLI---GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00153   87 APDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLS-SNIAHSGASVDLAIFSLHLAGISSILGAINFITT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00153  166 IINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 245


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00153  246 LPGF 249
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-244 3.51e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 232.26  E-value: 3.51e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00167   12 HKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00167   89 APDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLA-GNLAHAGASVDLAIFSLHLAGVSSILGSINFITT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00167  168 IINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILI 247


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00167  248 LPGF 251
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-244 6.79e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 231.52  E-value: 6.79e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00116   12 HKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00116   89 APDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGN-LAHAGASVDLAIFSLHLAGVSSILGAINFITT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00116  168 CINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILI 247


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00116  248 LPGF 251
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-265 1.06e-72

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: 229.34  E-value: 1.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFqG 80
Cdd:cd00919     1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQ---LYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLI-G 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSFLSLSPSStGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:cd00919    77 ARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGV-DLAILGLHLAGVSSILGAINFITT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:cd00919   156 ILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILI 235

                         250       260
                  ....*....|....*....|....*
gi 2178351184 241 VPAFGIISIIISGILQKIIFGNQSM 265
Cdd:cd00919   236 LPAFGAISEIIPTFSGKPLFGYKLM 260
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-244 4.72e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 229.18  E-value: 4.72e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGnriISPENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00079   13 HKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPG---LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00079   90 APDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST--LGHPGSSVDLAIFSLHCAGISSILGGINFMVT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00079  168 TKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILI 247


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00079  248 LPAF 251
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-244 1.48e-71

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: 227.49  E-value: 1.48e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQG 80
Cdd:TIGR02891   6 HKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAE---TYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWT 159
Cdd:TIGR02891  82 ARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSS--TSGSPGVGVDLwLLGLHLLGISSILGAVNFIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 160 TIINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYIL 239
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239


                  ....*
gi 2178351184 240 IVPAF 244
Cdd:TIGR02891 240 FLPAF 244
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-244 2.75e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 227.30  E-value: 2.75e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00142   10 HKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLL---GDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00142   87 APDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLS-SNLAHSGGSVDLAIFSLHLAGVSSILGAINFITT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00142  166 VINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 245


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00142  246 LPGF 249
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-244 1.78e-69

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 223.08  E-value: 1.78e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQG 80
Cdd:COG0843    15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPE---TYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWT 159
Cdd:COG0843    91 ARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSG--LEASPGVGVDLwLLGLALFGVGSILGGVNFIV 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 160 TIINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYIL 239
Cdd:COG0843   169 TILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYIL 248


                  ....*
gi 2178351184 240 IVPAF 244
Cdd:COG0843   249 ILPAF 253
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-244 1.19e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 220.47  E-value: 1.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00184   14 HKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSML---GDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00184   91 APDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLS-SIQAHSGGSVDMAIFSLHLAGISSILGAMNFITT 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00184  170 IFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILI 249


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00184  250 LPGF 253
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-244 2.63e-68

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 219.37  E-value: 2.63e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00103   12 HKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00103   89 APDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGN-LAHAGASVDLTIFSLHLAGVSSILGAINFITT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00103  168 IINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILI 247


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00103  248 LPGF 251
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-244 4.60e-67

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 216.31  E-value: 4.60e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00007    9 HKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQ---LYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSFLSLSPSsTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00007   86 APDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPS-VDLAIFSLHLAGVSSILGAINFITT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00007  165 VINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 244


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00007  245 LPGF 248
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-244 7.73e-67

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 215.96  E-value: 7.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00077   12 HKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSFLSLSPSsTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00077   89 APDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGAS-VDLTIFSLHLAGVSSILGAINFITT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00077  168 SINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILI 247


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00077  248 LPGF 251
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-244 3.33e-66

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 214.02  E-value: 3.33e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00183   12 HKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTSfLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00183   89 APDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGN-LAHAGASVDLTIFSLHLAGVSSILGAINFITT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00183  168 IINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILI 247


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00183  248 LPGF 251
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-244 1.53e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 212.76  E-value: 1.53e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00182   14 HKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAML---GDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00182   91 APDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLS-SIQAHSGGAVDMAIFSLHLAGVSSILGAINFITT 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00182  170 IFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILI 249


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00182  250 LPGF 253
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-244 6.02e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 210.84  E-value: 6.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00037   12 HKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLL---QDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00037   89 APDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLS-SNIAHAGGSVDLAIFSLHLAGASSILASINFITT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00037  168 IINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILI 247


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00037  248 LPGF 251
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-265 3.57e-62

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: 203.20  E-value: 3.57e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPENqnfYNISITLHGFLMIFFLVMPgLFGGFGNYFVPIFQG 80
Cdd:cd01662     7 HKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH---YNQIFTMHGTIMIFLFAMP-LVFGLMNYLVPLQIG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLSTsfLSLSPSSTGNL-IFGLLISGISSCLTSLNFWT 159
Cdd:cd01662    83 ARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSG--LEYSPGVGVDYwILGLQFSGIGTLLGAINFIV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 160 TIINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYIL 239
Cdd:cd01662   161 TILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYIL 240

                         250       260
                  ....*....|....*....|....*.
gi 2178351184 240 IVPAFGIISIIISGILQKIIFGNQSM 265
Cdd:cd01662   241 ILPAFGIFSEIVPTFSRKPLFGYRSM 266
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-244 7.87e-62

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 203.32  E-value: 7.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIispENQNFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00026   13 HKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSML---GDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLISEFGGGTGWTLYPPLStSFLSLSPSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00026   90 APDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLA-SIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITT 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00026  169 VMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILI 248


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00026  249 LPGF 252
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-244 6.38e-57

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 189.89  E-value: 6.38e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGGFGNYFVPIFQG 80
Cdd:MTH00048   13 HKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLD---VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  81 SPEVVYPRINNFSILILSLSYLFVILSLIseFGGGTGWTLYPPLSTSFLSLSpSSTGNLIFGLLISGISSCLTSLNFWTT 160
Cdd:MTH00048   90 LSDLNLPRLNALSAWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSS-WGVDFLMFSLHLAGVSSLFGSINFICT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 161 IINLRSYYLTLKTmPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEVYILI 240
Cdd:MTH00048  167 IYSAFMTNVFSRT-SIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLI 245


                  ....
gi 2178351184 241 VPAF 244
Cdd:MTH00048  246 LPGF 249
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-244 1.03e-45

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: 158.51  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   3 RLGIYYLLSAFIFGISGTLISILIRIELYSSGNRIISPEnqnFYNISITLHGFLMIFFLVMPGLFGgFGNYFVPIFQGSP 82
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPL---TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  83 EVVYPRINNFSILILSLSylfVILSLISEFGGGTGWTLYPPLSTSFLslspsstgnLIFGLLISGISSCLTSLNFWTTII 162
Cdd:pfam00115  77 DMAFPRLNALSFWLVVLG---AVLLLASFGGATTGWTEYPPLVGVDL---------WYIGLLLAGVSSLLGAINFIVTIL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 163 NLRSYYLTLKtMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFfdpifeGDPIFYQHLFWFFGHPEVYILIVP 242
Cdd:pfam00115 145 KRRAPGMTLR-MPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGG------GDPLLDQHLFWWFGHPEVYILILP 217


                  ..
gi 2178351184 243 AF 244
Cdd:pfam00115 218 AF 219
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-265 3.49e-39

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 144.31  E-value: 3.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184   1 HKRLGIYYLLSAFIFGISGTLISILIRIE--LYSSGNRIISPENQnfYNISITLHGFLMIFFLVMPGLFGgFGNYFVPIF 78
Cdd:PRK15017   54 HKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAGFLPPHH--YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQ 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184  79 QGSPEVVYPRINNFSILILSLSYLFVILSL-ISEFGGgTGWTLYPPLSTsfLSLSPS-STGNLIFGLLISGISSCLTSLN 156
Cdd:PRK15017  131 IGARDVAFPFLNNLSFWFTVVGVILVNVSLgVGEFAQ-TGWLAYPPLSG--IEYSPGvGVDYWIWSLQLSGIGTTLTGIN 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2178351184 157 FWTTIINLRSYYLTLKTMPLFLWSLLITGGMLLLTLPILSGALLMVTADLHSNTLFFDPIFEGDPIFYQHLFWFFGHPEV 236
Cdd:PRK15017  208 FFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEV 287

                         250       260
                  ....*....|....*....|....*....
gi 2178351184 237 YILIVPAFGIISIIISGILQKIIFGNQSM 265
Cdd:PRK15017  288 YILILPVFGVFSEIAATFSRKRLFGYTSL 316
 
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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