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Conserved domains on  [gi|1006714735|gb|AMQ62956|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Digenea fam. A sp. SB.CM.1]

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 ...
 1-223 7.95e-128

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 MTH00048:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 370.55  E-value: 7.95e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00048  285 VWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDN 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00048  365 VLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEP 444

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGAWGSNALVLNVAVVPVPHHGEYLS 223
Cdd:MTH00048  445 SYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLGLWGSSSCVVNVLMSPVPYHNDYFY 507
 
Name Accession Description Interval E-value
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-223 7.95e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 370.55  E-value: 7.95e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00048  285 VWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDN 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00048  365 VLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEP 444

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGAWGSNALVLNVAVVPVPHHGEYLS 223
Cdd:MTH00048  445 SYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLGLWGSSSCVVNVLMSPVPYHNDYFY 507
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-212 1.88e-95

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: 287.07  E-value: 1.88e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRlYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:cd01663   278 VWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIK-FETPMLWALGFIFLFTIGGLTGVVLANSSLDI 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:cd01663   357 ALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPD 436

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGAWGSNALVLNVAV 212
Cdd:cd01663   437 AYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEGSTSLEWTL 488
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-219 5.24e-58

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: 190.90  E-value: 5.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWwIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:TIGR02891 279 VWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLF-ALGFIFLFVIGGLTGVMLASVPLDW 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:TIGR02891 358 QLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPP 437

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1006714735 161 S--FVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVG-AWGSNALVLNVAVVPvPHHG 219
Cdd:TIGR02891 438 QmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGAnPWGATTLEWTTSSPP-PAHN 498
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-206 3.50e-57

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 189.57  E-value: 3.50e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWwIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:COG0843   288 VWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLF-ALGFIILFVIGGLTGVMLASVPLDY 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:COG0843   367 QVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPP 446

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1006714735 161 --SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVG-AWGSNAL 206
Cdd:COG0843   447 epGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAGGnPWGARTL 495
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-175 2.16e-39

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: 140.40  E-value: 2.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:pfam00115 254 VWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNY 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRV----C 156
Cdd:pfam00115 334 YVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYappfI 413

                         170
                  ....*....|....*....
gi 1006714735 157 VYDPSFVWLNSVASFGAVL 175
Cdd:pfam00115 414 ETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-223 7.95e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 370.55  E-value: 7.95e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00048  285 VWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDN 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00048  365 VLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEP 444

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGAWGSNALVLNVAVVPVPHHGEYLS 223
Cdd:MTH00048  445 SYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLGLWGSSSCVVNVLMSPVPYHNDYFY 507
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-212 1.88e-95

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: 287.07  E-value: 1.88e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRlYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:cd01663   278 VWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIK-FETPMLWALGFIFLFTIGGLTGVVLANSSLDI 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:cd01663   357 ALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPD 436

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGAWGSNALVLNVAV 212
Cdd:cd01663   437 AYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEGSTSLEWTL 488
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-192 2.32e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 228.60  E-value: 2.32e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRlYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00153  285 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQIN-YSPSLLWALGFVFLFTIGGLTGVVLANSSIDI 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00153  364 ILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD 443

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLV 192
Cdd:MTH00153  444 AYTSWNVISSIGSTISLISILFFIFIIWESMI 475
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-198 2.03e-70

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 223.70  E-value: 2.03e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRlYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00223  284 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIK-YEAPMLWALGFIFLFTVGGLTGIILSNSSLDI 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00223  363 MLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPD 442

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVV 198
Cdd:MTH00223  443 CYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVV 480
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-218 1.05e-67

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 216.50  E-value: 1.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWwIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00116  287 VWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLW-ALGFIFLFTIGGLTGIVLANSSLDI 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00116  366 VLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPD 445

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGAWGSNALVLNVAVVPVPHH 218
Cdd:MTH00116  446 AYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPPPYH 503
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-218 5.02e-67

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 214.93  E-value: 5.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWwIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00167  287 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLW-ALGFIFLFTVGGLTGIVLANSSLDI 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00167  366 VLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPD 445

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGAWGSNALVLNVAVVPVPHH 218
Cdd:MTH00167  446 AYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPPPHH 503
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-191 3.99e-64

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: 205.84  E-value: 3.99e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRlYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:cd00919   274 VWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIR-FDPPMLFALGFLFLFTIGGLTGVVLANVPLDI 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:cd00919   353 VLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPD 432

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESL 191
Cdd:cd00919   433 GFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-193 1.25e-63

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 205.73  E-value: 1.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRlYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00142  285 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVK-YEPPMLWALGFIFLFTVGGLTGIVLANSSLDV 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00142  364 VLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPD 443

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVV 193
Cdd:MTH00142  444 AYTTWNVVSSLGSMISFIAVLMFVFIVWESFVS 476
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-192 2.38e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 197.21  E-value: 2.38e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSrLYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00079  287 VWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKM-KFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDI 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00079  366 ILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPD 445

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLV 192
Cdd:MTH00079  446 VYSVWNVISSYGSMISVFALFLFIYVLLESFF 477
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-218 2.73e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 192.06  E-value: 2.73e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWwIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00183  287 VWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLW-ALGFIFLFTVGGLTGIVLANSSLDI 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00183  366 VLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPD 445

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGAWGSNALVLNVAVVPVPHH 218
Cdd:MTH00183  446 AYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPPPYH 503
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-218 3.79e-58

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 191.58  E-value: 3.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRlYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00037  287 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLR-WETPLLWALGFVFLFTIGGLTGIVLANSSIDV 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00037  366 VLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPD 445

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGA-WGSNALVLNVAVVPVPHH 218
Cdd:MTH00037  446 AYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPeFSSSSLEWQYSSFPPSHH 504
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-219 5.24e-58

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: 190.90  E-value: 5.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWwIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:TIGR02891 279 VWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLF-ALGFIFLFVIGGLTGVMLASVPLDW 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:TIGR02891 358 QLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPP 437

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1006714735 161 S--FVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVG-AWGSNALVLNVAVVPvPHHG 219
Cdd:TIGR02891 438 QmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGAnPWGATTLEWTTSSPP-PAHN 498
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-200 5.43e-58

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 191.27  E-value: 5.43e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRlYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00007  284 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIK-YETPMLWALGFIFLFTTGGLTGIVLSNSSLDI 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00007  363 ILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPD 442

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGA 200
Cdd:MTH00007  443 AYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIAS 482
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-218 6.10e-58

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 191.25  E-value: 6.10e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRlYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00103  287 VWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIK-WSPAMLWALGFIFLFTVGGLTGIVLANSSLDI 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00103  366 VLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPD 445

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGAWGSNALVLNVAVVPVPHH 218
Cdd:MTH00103  446 AYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPPPYH 503
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-206 3.50e-57

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 189.57  E-value: 3.50e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWwIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:COG0843   288 VWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLF-ALGFIILFVIGGLTGVMLASVPLDY 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:COG0843   367 QVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPP 446

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1006714735 161 --SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVG-AWGSNAL 206
Cdd:COG0843   447 epGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAGGnPWGARTL 495
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-218 4.95e-57

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 188.61  E-value: 4.95e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWwIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00077  287 VWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLW-ALGFIFLFTVGGLTGIVLANSSLDI 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00077  366 VLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPD 445

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGAWGSNALVLNVAVVPVPHH 218
Cdd:MTH00077  446 AYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPPPYH 503
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-199 1.37e-53

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 179.64  E-value: 1.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWwIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00184  289 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLW-AIGFVFLFTMGGLTGIVLANSSLDV 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00184  368 VLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHD 447

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVG 199
Cdd:MTH00184  448 SFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVG 486
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-204 1.62e-52

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 176.94  E-value: 1.62e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWwIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:MTH00182  289 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLW-AMGFVFLFTLGGLTGVVLANSSLDI 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:MTH00182  368 VLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFAD 447

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1006714735 161 SFVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGaWGSN 204
Cdd:MTH00182  448 AFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIG-WKEG 490
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-219 7.55e-52

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: 174.69  E-value: 7.55e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWwIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:cd01662   280 VWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLW-AIGFLVTFVIGGLTGVMLASPPADF 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:cd01662   359 QVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLP 438

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1006714735 161 S--FVWLNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGA--WGSNALVLNVAvVPVPHHG 219
Cdd:cd01662   439 GpgWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATGdpWGARTLEWATS-SPPPAYN 500
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-190 1.81e-46

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 161.33  E-value: 1.81e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGC-RSRLYEPILWWIIGFIFLFTVGGVTGIVLSASILD 79
Cdd:MTH00026  288 VWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgRNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLD 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  80 VRLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYD 159
Cdd:MTH00026  368 ILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYP 447

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1006714735 160 PSFVWLNSVASFGAVLSVVSAFAVMFILWES 190
Cdd:MTH00026  448 DNFEDFNQISSFGSIISIIAVIWFIVVIFDA 478
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-175 2.16e-39

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: 140.40  E-value: 2.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWWIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:pfam00115 254 VWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNY 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRV----C 156
Cdd:pfam00115 334 YVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYappfI 413

                         170
                  ....*....|....*....
gi 1006714735 157 VYDPSFVWLNSVASFGAVL 175
Cdd:pfam00115 414 ETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-218 2.77e-39

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: 143.07  E-value: 2.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWwIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:TIGR02882 323 VWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLF-SLAFIPNFLIGGVTGVMLAMASADY 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNKWLLQGHWLISMVGFNLCFFPMHYLGMQGLPRRVCVYDP 160
Cdd:TIGR02882 402 QYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYSP 481

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1006714735 161 SFVW--LNSVASFGAVLSVVSAFAVMFILWESLVVGNRVVGAWGSNALVLNVAVV-PVPHH 218
Cdd:TIGR02882 482 SDGWfpLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPWNGRTLEWATAsPPPKY 542
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-175 9.92e-30

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 116.19  E-value: 9.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735   1 VWAHHMFLVGLDLKTAIFFSSVTMVIGIPTGIKVFSWLYMLAGCRSRLYEPILWwIIGFIFLFTVGGVTGIVLSASILDV 80
Cdd:PRK15017  330 VWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLW-TIGFIVTFSVGGMTGVLLAVPGADF 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  81 RLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSLNK-WLLQGHWLIsMVGFNLCFFPMHYLGMQGLPRRVCV-Y 158
Cdd:PRK15017  409 VLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNEtWGKRAFWFW-IIGFFVAFMPLYALGFMGMTRRLSQqI 487

                         170
                  ....*....|....*..
gi 1006714735 159 DPSFVWLNSVASFGAVL 175
Cdd:PRK15017  488 DPQFHTMLMIAASGAAL 504
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 60-154 1.38e-05

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: 45.35  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1006714735  60 IFLFTVGGVTGIVLSASILDVRLHDTWFVVAHFHYVLSLGSYSTVIISFIWWWPVITGYSL-NKWLLQGHWLISMVGFNL 138
Cdd:cd01660   333 MLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELaAKRLALAQPWLWFVGMTI 412

                          90
                  ....*....|....*.
gi 1006714735 139 CFFPMHYLGMQGLPRR 154
Cdd:cd01660   413 MSTAMHVAGLLGAPRR 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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