NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1214785392|gb|ASK05938|]
View 

cytochrome c oxidase subunit I, partial (mitochondrion) [Stenopelmatus sartorianus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-190 1.11e-142

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: 406.56  E-value: 1.11e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00153  247 PGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00153  327 GSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPK 406

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00153  407 WLKIQFFIMFIGVNLTFFPQHFLGLAGMPR 436
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-190 1.11e-142

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 406.56  E-value: 1.11e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00153  247 PGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00153  327 GSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPK 406

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00153  407 WLKIQFFIMFIGVNLTFFPQHFLGLAGMPR 436
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-190 2.69e-120

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: 349.09  E-value: 2.69e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:cd01663   240 PGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMW 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:cd01663   320 GGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNET 399

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:cd01663   400 LGKIHFWLMFIGVNLTFFPQHFLGLAGMPR 429
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-190 1.61e-71

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 225.39  E-value: 1.61e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNeAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:COG0843   251 PAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMW 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:COG0843   330 RGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNER 409

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:COG0843   410 LGKIHFWLWFIGFNLTFFPMHILGLLGMPR 439
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-190 3.22e-70

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: 220.94  E-value: 3.22e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNeAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:TIGR02891 242 PAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPR 430
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-190 1.28e-52

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: 173.53  E-value: 1.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKnEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:pfam00115 217 PAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLW 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLN-YSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNV 159
Cdd:pfam00115 296 GGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSE 375

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1214785392 160 KWLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:pfam00115 376 KLGKLHFWLLFIGFNLTFFPMHILGLLGMPR 406
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-190 1.11e-142

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 406.56  E-value: 1.11e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00153  247 PGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00153  327 GSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPK 406

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00153  407 WLKIQFFIMFIGVNLTFFPQHFLGLAGMPR 436
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-190 2.69e-120

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: 349.09  E-value: 2.69e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:cd01663   240 PGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMW 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:cd01663   320 GGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNET 399

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:cd01663   400 LGKIHFWLMFIGVNLTFFPQHFLGLAGMPR 429
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-190 4.88e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 328.94  E-value: 4.88e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00167  249 PGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLH 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00167  329 GGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNET 408

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00167  409 WTKIHFFVMFIGVNLTFFPQHFLGLAGMPR 438
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-190 1.73e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 327.32  E-value: 1.73e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00223  246 PGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIY 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00223  326 GSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRR 405

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00223  406 WAKAHFFLMFLGVNLTFFPQHFLGLAGMPR 435
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-190 6.99e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 325.89  E-value: 6.99e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00116  249 PGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLH 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00116  329 GGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQT 408

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00116  409 WTKAQFGVMFTGVNLTFFPQHFLGLAGMPR 438
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-190 3.81e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 323.98  E-value: 3.81e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00142  247 PGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLH 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00142  327 GSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPR 406

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00142  407 WLKAHFYTMFIGVNLTFFPQHFLGLAGMPR 436
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-190 1.18e-99

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 297.18  E-value: 1.18e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00103  249 PGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLH 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00103  329 GGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDT 408

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00103  409 WAKIHFTIMFVGVNMTFFPQHFLGLSGMPR 438
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-190 2.13e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 291.44  E-value: 2.13e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00183  249 PGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLH 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00183  329 GGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHST 408

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00183  409 WTKIHFGVMFVGVNLTFFPQHFLGLAGMPR 438
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-190 5.31e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 290.58  E-value: 5.31e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00037  249 PGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQ 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00037  329 GSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPL 408

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00037  409 WSKVHFFLMFIGVNLTFFPQHFLGLAGMPR 438
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-190 1.01e-96

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 289.49  E-value: 1.01e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00007  246 PGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIH 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00007  326 GSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDR 405

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00007  406 WAKAHFFLMFLGVNLTFFPQHFLGLSGMPR 435
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-190 1.05e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 287.22  E-value: 1.05e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00077  249 PGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMH 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00077  329 GGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHST 408

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00077  409 WSKIHFGVMFIGVNLTFFPQHFLGLAGMPR 438
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-190 1.29e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 268.86  E-value: 1.29e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00079  249 PAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLF 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00079  329 GMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKL 408

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00079  409 MMSAVFFLMFVGVNLTFFPLHFAGLHGMPR 438
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-190 1.32e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 261.68  E-value: 1.32e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00182  251 PGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIY 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00182  331 GGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEL 410

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00182  411 YGKIHFWLMFIGVNLTFFPQHFLGLAGFPR 440
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-190 3.49e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 250.13  E-value: 3.49e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00184  251 PGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIF 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:MTH00184  331 GGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEV 410

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00184  411 YGKIHFWLMFIGVNLTFFPQHFLGLAGLPR 440
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-190 1.12e-76

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: 236.66  E-value: 1.12e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKnEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:cd00919   237 PAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLW 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:cd00919   316 GGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEK 395

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:cd00919   396 LGKIHFWLWFIGFNLTFFPMHFLGLLGMPR 425
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-190 1.61e-71

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 225.39  E-value: 1.61e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNeAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:COG0843   251 PAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMW 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:COG0843   330 RGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNER 409

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:COG0843   410 LGKIHFWLWFIGFNLTFFPMHILGLLGMPR 439
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-190 5.23e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 224.12  E-value: 5.23e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00026  250 PGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVS 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLN--YSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMN 158
Cdd:MTH00026  330 GSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYK 409

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1214785392 159 VKWLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00026  410 DIYGLIHFWLMFIGVNITFFPQHFLGLAGLPR 441
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-190 3.22e-70

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: 220.94  E-value: 3.22e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNeAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:TIGR02891 242 PAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPR 430
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-190 2.14e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 216.47  E-value: 2.14e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:MTH00048  247 PGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLL 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYS-PSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNV 159
Cdd:MTH00048  327 NSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNK 406

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1214785392 160 KWLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:MTH00048  407 YLLQCHCIISMIGFNLCFFPMHYFGLCGLPR 437
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-190 6.56e-65

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: 207.43  E-value: 6.56e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKnEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:cd01662   243 PAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMW 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:cd01662   322 RGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNER 401

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:cd01662   402 LGKWSFWLWFIGFNLTFFPMHILGLMGMPR 431
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-190 1.28e-52

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: 173.53  E-value: 1.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKnEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:pfam00115 217 PAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLW 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLN-YSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNV 159
Cdd:pfam00115 296 GGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSE 375

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1214785392 160 KWLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:pfam00115 376 KLGKLHFWLLFIGFNLTFFPMHILGLLGMPR 406
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-190 6.52e-44

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 154.24  E-value: 6.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESGKNeAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:TIGR02882 286 PAFGIYSEIISTFAQKR-LFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLY 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:TIGR02882 365 KGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNER 444

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:TIGR02882 445 LGKWCFWFFMIGFNVCFFPMYILGLDGMPR 474
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-190 7.77e-41

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 145.85  E-value: 7.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392   1 PGFGMISHIISQESgKNEAFGT**MIYAMLAIGLLGFVEWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 80
Cdd:PRK15017  293 PVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMY 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  81 GTQLNYSPSLMWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVQWYPLFTGLTMNVK 160
Cdd:PRK15017  372 QGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNET 451

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785392 161 WLKIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:PRK15017  452 WGKRAFWFWIIGFFVAFMPLYALGFMGMTR 481
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 61-190 3.76e-07

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 49.21  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785392  61 TMIIAVPTGIKIFSWLATL-HGTQLNYSPSLMW---------------ALGFVFlFTIGGLTGVVLANSSIDIILHDTYY 124
Cdd:cd01660   282 TFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1214785392 125 VVAHFHyvLSMGAVFAIMAGFVQWY--PLFTGLTMNVKWL-KIQFIVMFTGVNLTFFPQPFLGLAGIPR 190
Cdd:cd01660   361 VPGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPR 427
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH