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Conserved domains on  [gi|1214785322|gb|ASK05903|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Stenopelmatoidea gen. sp. Gryll_SA05]

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 ...
 1-190 1.13e-149

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: 424.28  E-value: 1.13e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00153  248 GFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00153  328 SQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKW 407

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00153  408 LKIQFFIMFIGVNLTFFPQHFLGLAGMPRR 437
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-190 1.13e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 424.28  E-value: 1.13e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00153  248 GFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00153  328 SQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKW 407

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00153  408 LKIQFFIMFIGVNLTFFPQHFLGLAGMPRR 437
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-190 1.82e-128

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: 369.50  E-value: 1.82e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:cd01663   241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:cd01663   321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:cd01663   401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRR 430
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-190 2.88e-78

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 242.73  E-value: 2.88e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:COG0843   252 AFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWR 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:COG0843   331 GRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERL 410

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:COG0843   411 GKIHFWLWFIGFNLTFFPMHILGLLGMPRR 440
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-190 2.61e-76

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


Pssm-ID: 213748  Cd Length: 499  Bit Score: 236.74  E-value: 2.61e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:TIGR02891 243 AFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWG 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:TIGR02891 322 GSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERL 401

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:TIGR02891 402 GRWHFWLTFVGFNLTFFPMHLLGLLGMPRR 431
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-190 2.25e-56

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: 183.54  E-value: 2.25e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:pfam00115 218 AFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLN-YSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPK 159
Cdd:pfam00115 297 GWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEK 376

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1214785322 160 WLKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:pfam00115 377 LGKLHFWLLFIGFNLTFFPMHILGLLGMPRR 407
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-190 1.13e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 424.28  E-value: 1.13e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00153  248 GFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00153  328 SQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKW 407

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00153  408 LKIQFFIMFIGVNLTFFPQHFLGLAGMPRR 437
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-190 1.82e-128

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: 369.50  E-value: 1.82e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:cd01663   241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:cd01663   321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:cd01663   401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRR 430
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-190 1.49e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 345.42  E-value: 1.49e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00223  247 GFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYG 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00223  327 SKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRW 406

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00223  407 AKAHFFLMFLGVNLTFFPQHFLGLAGMPRR 436
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-190 1.70e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 342.81  E-value: 1.70e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00167  250 GFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHG 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00167  330 GKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETW 409

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00167  410 TKIHFFVMFIGVNLTFFPQHFLGLAGMPRR 439
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-190 1.03e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 340.92  E-value: 1.03e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00116  250 GFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHG 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00116  330 GTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTW 409

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00116  410 TKAQFGVMFTGVNLTFFPQHFLGLAGMPRR 439
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-190 6.71e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 338.62  E-value: 6.71e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00142  248 GFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHG 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00142  328 SKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRW 407

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00142  408 LKAHFYTMFIGVNLTFFPQHFLGLAGMPRR 437
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-190 5.83e-104

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 308.35  E-value: 5.83e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00103  250 GFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00103  330 GNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTW 409

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00103  410 AKIHFTIMFVGVNMTFFPQHFLGLSGMPRR 439
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-190 1.31e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 304.83  E-value: 1.31e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00037  250 GFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQG 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00037  330 SNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLW 409

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00037  410 SKVHFFLMFIGVNLTFFPQHFLGLAGMPRR 439
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-190 6.11e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 303.00  E-value: 6.11e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00183  250 GFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00183  330 GSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTW 409

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00183  410 TKIHFGVMFVGVNLTFFPQHFLGLAGMPRR 439
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-190 3.81e-100

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 298.35  E-value: 3.81e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00007  247 GFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHG 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00007  327 SPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRW 406

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00007  407 AKAHFFLMFLGVNLTFFPQHFLGLSGMPRR 436
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-190 7.00e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 297.62  E-value: 7.00e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00077  250 GFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHG 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00077  330 GAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTW 409

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00077  410 SKIHFGVMFIGVNLTFFPQHFLGLAGMPRR 439
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-190 1.16e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 284.27  E-value: 1.16e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   2 FGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 81
Cdd:MTH00079  251 FGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGM 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  82 QLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKWL 161
Cdd:MTH00079  331 KMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMM 410

                         170       180
                  ....*....|....*....|....*....
gi 1214785322 162 KIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00079  411 SAVFFLMFVGVNLTFFPLHFAGLHGMPRK 439
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-190 5.28e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 275.16  E-value: 5.28e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00182  252 GFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYG 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00182  332 GTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELY 411

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00182  412 GKIHFWLMFIGVNLTFFPQHFLGLAGFPRR 441
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-190 8.35e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 264.38  E-value: 8.35e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00184  252 GFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFG 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:MTH00184  332 GSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVY 411

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00184  412 GKIHFWLMFIGVNLTFFPQHFLGLAGLPRR 441
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-190 1.30e-81

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: 249.37  E-value: 1.30e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:cd00919   238 AFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWG 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:cd00919   317 GRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKL 396

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:cd00919   397 GKIHFWLWFIGFNLTFFPMHFLGLLGMPRR 426
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-190 2.88e-78

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 242.73  E-value: 2.88e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:COG0843   252 AFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWR 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:COG0843   331 GRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERL 410

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:COG0843   411 GKIHFWLWFIGFNLTFFPMHILGLLGMPRR 440
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-190 2.61e-76

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


Pssm-ID: 213748  Cd Length: 499  Bit Score: 236.74  E-value: 2.61e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:TIGR02891 243 AFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWG 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKW 160
Cdd:TIGR02891 322 GSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERL 401

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214785322 161 LKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:TIGR02891 402 GRWHFWLTFVGFNLTFFPMHLLGLLGMPRR 431
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-190 3.53e-75

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 234.91  E-value: 3.53e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00026  251 GFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSG 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLN--YSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNP 158
Cdd:MTH00026  331 SGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKD 410

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1214785322 159 KWLKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00026  411 IYGLIHFWLMFIGVNITFFPQHFLGLAGLPRR 442
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-190 7.05e-72

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: 225.15  E-value: 7.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   2 FGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 81
Cdd:cd01662   245 FGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRG 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  82 QLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKWL 161
Cdd:cd01662   324 RIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLG 403

                         170       180
                  ....*....|....*....|....*....
gi 1214785322 162 KIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:cd01662   404 KWSFWLWFIGFNLTFFPMHILGLMGMPRR 432
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-190 4.83e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 223.40  E-value: 4.83e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00048  248 GFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLN 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLNYS-PSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPK 159
Cdd:MTH00048  328 SRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKY 407

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1214785322 160 WLKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:MTH00048  408 LLQCHCIISMIGFNLCFFPMHYFGLCGLPRR 438
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-190 2.25e-56

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: 183.54  E-value: 2.25e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   1 GFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:pfam00115 218 AFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  81 TQLN-YSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPK 159
Cdd:pfam00115 297 GWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEK 376

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1214785322 160 WLKIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:pfam00115 377 LGKLHFWLLFIGFNLTFFPMHILGLLGMPRR 407
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-190 2.26e-47

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: 163.49  E-value: 2.26e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   2 FGMISHIISQESgKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 81
Cdd:TIGR02882 288 FGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKG 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  82 QLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKWL 161
Cdd:TIGR02882 367 KIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLG 446

                         170       180
                  ....*....|....*....|....*....
gi 1214785322 162 KIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:TIGR02882 447 KWCFWFFMIGFNVCFFPMYILGLDGMPRR 475
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-190 3.17e-44

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 155.09  E-value: 3.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322   2 FGMISHIISQESgKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 81
Cdd:PRK15017  295 FGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQG 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  82 QLNYSPSLLWALGFVFLFTIGGLTGVILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLMMNPKWL 161
Cdd:PRK15017  374 RIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWG 453

                         170       180
                  ....*....|....*....|....*....
gi 1214785322 162 KIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:PRK15017  454 KRAFWFWIIGFFVAFMPLYALGFMGMTRR 482
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 60-190 8.34e-10

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: 56.91  E-value: 8.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322  60 TMIIAVPTGIKIFSWLATL-HGTQLNYSPSLLW---------------ALGFVFlFTIGGLTGVILANSSLDIILHDTYY 123
Cdd:cd01660   282 TFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214785322 124 VVAHFHyvLSMGAVFAIMAGFIQWY--PLFTGLMMNPKWL-KIQFMIMFIGVNLTFFPQHFLGLAGMPRR 190
Cdd:cd01660   361 VPGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRR 428
 
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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