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Conserved domains on  [gi|116090130|gb|ABJ55767|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Parafontaria longa]

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 ...
 1-179 9.78e-122

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


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 353.02  E-value: 9.78e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00153 238 HPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00153 318 IFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPL 397

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00153 398 FTGLTMNPKWLKIQFFIMF 416
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-179 9.78e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 353.02  E-value: 9.78e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00153 238 HPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00153 318 IFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPL 397

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00153 398 FTGLTMNPKWLKIQFFIMF 416
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-179 1.03e-108

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: 319.04  E-value: 1.03e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:cd01663  231 HPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIK 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:cd01663  311 VFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPK 390

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:cd01663  391 ITGLSYNETLGKIHFWLMF 409
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-179 2.55e-68

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 216.53  E-value: 2.55e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKsEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:COG0843  242 HPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVK 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:COG0843  321 VFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPK 400

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:COG0843  401 MTGRMLNERLGKIHFWLWF 419
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-179 5.13e-66

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: 209.77  E-value: 5.13e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130    1 HPEVYILILPGFGMVSHMISYQSGKsEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:TIGR02891 233 HPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVK 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:TIGR02891 312 VFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPK 391

                         170
                  ....*....|....*....
gi 116090130  161 FFGVTFNSSLLKLHFVLMF 179
Cdd:TIGR02891 392 VTGRMYNERLGRWHFWLTF 410
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-179 1.01e-49

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: 165.82  E-value: 1.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130    1 HPEVYILILPGFGMVSHMISYQSGKsEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:pfam00115 208 HPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVK 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   81 IFSWLATLYGSR-FIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFP 159
Cdd:pfam00115 287 VFNWLATLWGGWiRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLP 366

                         170       180
                  ....*....|....*....|
gi 116090130  160 LFFGVTFNSSLLKLHFVLMF 179
Cdd:pfam00115 367 KLTGRMYSEKLGKLHFWLLF 386
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-179 9.78e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 353.02  E-value: 9.78e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00153 238 HPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00153 318 IFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPL 397

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00153 398 FTGLTMNPKWLKIQFFIMF 416
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-179 1.03e-108

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: 319.04  E-value: 1.03e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:cd01663  231 HPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIK 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:cd01663  311 VFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPK 390

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:cd01663  391 ITGLSYNETLGKIHFWLMF 409
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-179 2.26e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 300.83  E-value: 2.26e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00167 240 HPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00167 320 VFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00167 400 FTGLTLNETWTKIHFFVMF 418
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-179 7.23e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 294.58  E-value: 7.23e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00223 237 HPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00223 317 VFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPL 396

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00223 397 FTGVTLHRRWAKAHFFLMF 415
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-179 1.08e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 294.31  E-value: 1.08e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00116 240 HPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIK 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00116 320 VFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00116 400 FTGYTLHQTWTKAQFGVMF 418
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-179 3.54e-96

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 287.78  E-value: 3.54e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00142 238 HPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIK 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00142 318 VFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPL 397

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00142 398 FTGLTLNPRWLKAHFYTMF 416
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-179 3.38e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 267.47  E-value: 3.38e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00037 240 HPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00037 320 VFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPL 399

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00037 400 FSGVSLHPLWSKVHFFLMF 418
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-179 2.20e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 265.25  E-value: 2.20e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00183 240 HPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVK 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00183 320 VFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPL 399

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00183 400 FSGYTLHSTWTKIHFGVMF 418
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-179 7.24e-87

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 263.69  E-value: 7.24e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00007 237 HPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00007 317 VFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPL 396

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00007 397 FTGLTLHDRWAKAHFFLMF 415
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-179 4.07e-86

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 262.13  E-value: 4.07e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00103 240 HPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVK 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00103 320 VFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPL 399

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00103 400 FSGYTLNDTWAKIHFTIMF 418
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-179 1.59e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 255.25  E-value: 1.59e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00077 240 HPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVK 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00077 320 VFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPL 399

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00077 400 FSGYTLHSTWSKIHFGVMF 418
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-179 1.01e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 248.06  E-value: 1.01e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00079 240 HPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVK 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00079 320 VFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPF 399

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00079 400 MTGIVYDKLMMSAVFFLMF 418
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-179 1.48e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 242.80  E-value: 1.48e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00182 242 HPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00182 322 VFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00182 402 ITGYCYNELYGKIHFWLMF 420
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-179 1.32e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 235.11  E-value: 1.32e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00184 242 HPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:MTH00184 322 IFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00184 402 ITGYCYNEVYGKIHFWLMF 420
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-179 3.74e-70

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: 219.32  E-value: 3.74e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKsEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:cd00919  228 HPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIK 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:cd00919  307 VFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPK 386

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:cd00919  387 MTGRMLSEKLGKIHFWLWF 405
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-179 2.55e-68

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 216.53  E-value: 2.55e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKsEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:COG0843  242 HPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVK 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:COG0843  321 VFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPK 400

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:COG0843  401 MTGRMLNERLGKIHFWLWF 419
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-179 5.13e-66

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: 209.77  E-value: 5.13e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130    1 HPEVYILILPGFGMVSHMISYQSGKsEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:TIGR02891 233 HPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVK 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:TIGR02891 312 VFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPK 391

                         170
                  ....*....|....*....
gi 116090130  161 FFGVTFNSSLLKLHFVLMF 179
Cdd:TIGR02891 392 VTGRMYNERLGRWHFWLTF 410
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-179 1.84e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 206.40  E-value: 1.84e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00026 241 HPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIK 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGS--RFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWF 158
Cdd:MTH00026 321 IFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWF 400

                        170       180
                 ....*....|....*....|.
gi 116090130 159 PLFFGVTFNSSLLKLHFVLMF 179
Cdd:MTH00026 401 GKITGYAYKDIYGLIHFWLMF 421
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-179 1.38e-63

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


Pssm-ID: 238832  Cd Length: 501  Bit Score: 203.20  E-value: 1.38e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKsEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:cd01662  234 HPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVK 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:cd01662  313 IFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPK 392

                        170
                 ....*....|....*....
gi 116090130 161 FFGVTFNSSLLKLHFVLMF 179
Cdd:cd01662  393 MFGRMLNERLGKWSFWLWF 411
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-177 7.15e-62

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 199.13  E-value: 7.15e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSGKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:MTH00048 238 HPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIK 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRF-IYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFP 159
Cdd:MTH00048 318 VFSWLYMLLNSRVrKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWP 397

                        170
                 ....*....|....*...
gi 116090130 160 LFFGVTFNSSLLKLHFVL 177
Cdd:MTH00048 398 LITGLSLNKYLLQCHCII 415
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-175 2.23e-50

cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]


Pssm-ID: 131890  Cd Length: 646  Bit Score: 171.39  E-value: 2.23e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130    1 HPEVYILILPGFGMVSHMISYQSGKsEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:TIGR02843 283 HPEVYILILPAFGIFSEVVATFSRK-RLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVK 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:TIGR02843 362 IFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPK 441

                         170
                  ....*....|....*
gi 116090130  161 FFGVTFNSSLLKLHF 175
Cdd:TIGR02843 442 AFGFKLNEKLGKRSF 456
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-179 1.01e-49

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: 165.82  E-value: 1.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130    1 HPEVYILILPGFGMVSHMISYQSGKsEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:pfam00115 208 HPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVK 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   81 IFSWLATLYGSR-FIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFP 159
Cdd:pfam00115 287 VFNWLATLWGGWiRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLP 366

                         170       180
                  ....*....|....*....|
gi 116090130  160 LFFGVTFNSSLLKLHFVLMF 179
Cdd:pfam00115 367 KLTGRMYSEKLGKLHFWLLF 386
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-175 2.43e-43

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 152.40  E-value: 2.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130   1 HPEVYILILPGFGMVSHMISYQSgKSEPFGSLGMIYAMGAIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 80
Cdd:PRK15017 284 HPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVK 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116090130  81 IFSWLATLYGSRFIYDVTLMWSLGFVFLFTVGGLTGVVLANSSIDIMMHDTYYVVAHFHYVLSMGAVFAILGAITFWFPL 160
Cdd:PRK15017 363 IFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPK 442

                        170
                 ....*....|....*
gi 116090130 161 FFGVTFNSSLLKLHF 175
Cdd:PRK15017 443 AFGFKLNETWGKRAF 457
 
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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