NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1194587522|gb|ARR97069|]
View 

cytochrome oxidase subunit I, partial (mitochondrion) [Phrynomantis bifasciatus]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-271 0e+00

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: 542.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00153  200 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIG 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00153  280 LLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANS 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00153  360 SIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYS 439

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00153  440 DYPDAYTSWNVISSIGSTISLISILFFIFI 469
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-271 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 542.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00153  200 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIG 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00153  280 LLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANS 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00153  360 SIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYS 439

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00153  440 DYPDAYTSWNVISSIGSTISLISILFFIFI 469
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-271 0e+00

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: 538.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:cd01663   193 LAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIG 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:cd01663   273 ILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANS 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:cd01663   353 SLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYP 432

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:cd01663   433 DYPDAYAGWNMISSIGSLISFVSVLLFLFI 462
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-271 4.55e-125

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 366.37  E-value: 4.55e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIG 81
Cdd:COG0843   204 LAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIA 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:COG0843   283 FLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASV 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:COG0843   363 PLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYA 442

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1194587522 242 DYP--DAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:COG0843   443 TYPpePGWQPLNLISTIGAFILAVGFLLFLIN 474
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-270 3.06e-122

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: 357.69  E-value: 3.06e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIG 81
Cdd:TIGR02891 195 LIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIG 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:TIGR02891 274 FLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASV 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:TIGR02891 354 PLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYY 433

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1194587522 242 DYPDA--YTLWNTASSIGSLISLVAVIL*MF 270
Cdd:TIGR02891 434 TYPPQmgFATLNLISTIGAFILAAGFLVFLW 464
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-260 1.45e-83

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: 256.73  E-value: 1.45e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNttffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIG 81
Cdd:pfam00115 176 LAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIA 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKW-EAPMLWALGFIFLFTVGGLTGIVLAN 160
Cdd:pfam00115 249 FLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLAL 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 161 SSIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRY 240
Cdd:pfam00115 329 PPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRY 408

                         250       260
                  ....*....|....*....|....
gi 1194587522 241 S----DYPDAYTLWNTASSIGSLI 260
Cdd:pfam00115 409 AppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-271 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 542.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00153  200 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIG 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00153  280 LLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANS 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00153  360 SIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYS 439

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00153  440 DYPDAYTSWNVISSIGSTISLISILFFIFI 469
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-271 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 542.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00116  202 LAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIG 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00116  282 FLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANS 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00116  362 SLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYS 441

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00116  442 DYPDAYTLWNTISSIGSLISMTAVIMLMFI 471
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-271 0e+00

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: 538.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:cd01663   193 LAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIG 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:cd01663   273 ILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANS 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:cd01663   353 SLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYP 432

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:cd01663   433 DYPDAYAGWNMISSIGSLISFVSVLLFLFI 462
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-271 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 524.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00167  202 LAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIG 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00167  282 LLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANS 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00167  362 SLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYS 441

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00167  442 DYPDAYTLWNVVSSIGSLISLVAVILFLFI 471
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-271 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 509.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00077  202 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIG 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00077  282 LLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANS 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00077  362 SLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYS 441

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00077  442 DYPDAYTLWNTVSSIGSLISLVAVIMMMFI 471
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-271 3.51e-175

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 492.90  E-value: 3.51e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00183  202 LAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIG 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00183  282 LLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANS 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00183  362 SLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYS 441

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00183  442 DYPDAYTLWNTVSSIGSLISLVAVIMFLFI 471
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-271 5.91e-175

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 492.19  E-value: 5.91e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00223  199 LAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIG 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00223  279 VLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNS 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00223  359 SLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYS 438

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00223  439 DYPDCYTKWNQVSSFGSMISFVSVLFFMFI 468
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-271 1.52e-170

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 481.30  E-value: 1.52e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00103  202 LAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIG 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00103  282 FLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANS 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00103  362 SLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYS 441

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00103  442 DYPDAYTTWNTVSSMGSFISLTAVMLMIFM 471
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-271 3.77e-170

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 479.99  E-value: 3.77e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00142  200 LAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIG 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00142  280 LLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANS 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00142  360 SLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYS 439

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00142  440 DYPDAYTTWNVVSSLGSMISFIAVLMFVFI 469
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-271 1.25e-158

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 451.21  E-value: 1.25e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00037  202 LAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIG 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00037  282 ILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANS 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00037  362 SIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYS 441

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00037  442 DYPDAYTLWNTVSSIGSTISLVATLFFLFL 471
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-271 3.76e-152

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 434.33  E-value: 3.76e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00007  199 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIG 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00007  279 VLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNS 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00007  359 SLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYS 438

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00007  439 DYPDAYTKWNVVSSFGSMLSFVALLLFIFI 468
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-271 2.11e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 402.66  E-value: 2.11e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00182  204 LAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIG 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00182  284 ILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANS 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00182  364 SLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYS 443

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00182  444 DFADAFAGWNLVSSLGSIISIVGVVWFIYI 473
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-271 7.40e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 397.90  E-value: 7.40e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00079  202 LAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIG 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00079  282 LIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNS 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00079  362 SLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYL 441

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00079  442 DYPDVYSVWNVISSYGSMISVFALFLFIYV 471
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-271 7.18e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 395.73  E-value: 7.18e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00184  204 LAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIG 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:MTH00184  284 ILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANS 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:MTH00184  364 SLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYS 443

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00184  444 DFHDSFAGWNQISSLGSVISIVGVVWFIYI 473
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-271 4.88e-129

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: 373.79  E-value: 4.88e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIG 81
Cdd:cd00919   190 LAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIG 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:cd00919   269 FLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANV 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:cd00919   349 PLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYA 428

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:cd00919   429 DYPDGFAPWNFISSVGAFILGLGLLLFLGN 458
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-271 4.55e-125

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 366.37  E-value: 4.55e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIG 81
Cdd:COG0843   204 LAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIA 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:COG0843   283 FLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASV 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:COG0843   363 PLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYA 442

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1194587522 242 DYP--DAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:COG0843   443 TYPpePGWQPLNLISTIGAFILAVGFLLFLIN 474
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-270 3.06e-122

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: 357.69  E-value: 3.06e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIG 81
Cdd:TIGR02891 195 LIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIG 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:TIGR02891 274 FLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASV 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:TIGR02891 354 PLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYY 433

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1194587522 242 DYPDA--YTLWNTASSIGSLISLVAVIL*MF 270
Cdd:TIGR02891 434 TYPPQmgFATLNLISTIGAFILAAGFLVFLW 464
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-271 2.49e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 343.92  E-value: 2.49e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00026  203 LAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIG 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGG--VIKWEAPMLWALGFIFLFTVGGLTGIVLA 159
Cdd:MTH00026  283 VLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLS 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 160 NSSIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRR 239
Cdd:MTH00026  363 NSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRR 442

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1194587522 240 YSDYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00026  443 YADYPDNFEDFNQISSFGSIISIIAVIWFIVV 474
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-267 1.52e-113

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: 335.70  E-value: 1.52e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIG 81
Cdd:cd01662   196 LTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIG 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:cd01662   275 FLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASP 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:cd01662   355 PADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVY 434

                         250       260
                  ....*....|....*....|....*...
gi 1194587522 242 DYP--DAYTLWNTASSIGSLISLVAVIL 267
Cdd:cd01662   435 TYLpgPGWDPLNLISTIGAFLIAAGVLL 462
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-271 2.34e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 327.79  E-value: 2.34e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIG 81
Cdd:MTH00048  200 LAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIV 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHG-GVIKWEAPMLWALGFIFLFTVGGLTGIVLAN 160
Cdd:MTH00048  280 CLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNsRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSA 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 161 SSIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRY 240
Cdd:MTH00048  360 SVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRV 439

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1194587522 241 SDYPDAYTLWNTASSIGSLISLVAVIL*MFI 271
Cdd:MTH00048  440 CVYEPSYYWINVVCTVGSFISAFSGCFFVFI 470
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-260 1.45e-83

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: 256.73  E-value: 1.45e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNttffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKePFGYMGMVWAMLSIG 81
Cdd:pfam00115 176 LAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIA 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKW-EAPMLWALGFIFLFTVGGLTGIVLAN 160
Cdd:pfam00115 249 FLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLAL 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 161 SSIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRY 240
Cdd:pfam00115 329 PPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRY 408

                         250       260
                  ....*....|....*....|....
gi 1194587522 241 S----DYPDAYTLWNTASSIGSLI 260
Cdd:pfam00115 409 AppfiETVPAFQPLNWIRTIGGVL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 2-270 1.70e-78

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


Pssm-ID: 131890  Cd Length: 646  Bit Score: 249.59  E-value: 1.70e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEpFGYMGMVWAMLSIG 81
Cdd:TIGR02843 245 LTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRL-FGYTSMVWATIAIT 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:TIGR02843 324 VLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVP 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:TIGR02843 404 PADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLN 483

                         250       260       270
                  ....*....|....*....|....*....|
gi 1194587522 242 DYPD-AYTLWNTASSIGSLISLVAVIL*MF 270
Cdd:TIGR02843 484 HYDNpEWHPMLIIAAFGAFLIACGILCQII 513
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-270 6.10e-66

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 217.11  E-value: 6.10e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522   2 LAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSgKKEPFGYMGMVWAMLSIG 81
Cdd:PRK15017  246 LTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCIT 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  82 LLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGVIKWEAPMLWALGFIFLFTVGGLTGIVLANS 161
Cdd:PRK15017  325 VLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVP 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 162 SIDIVLHDTYYVVAHFHYVLSMGAVFAILAGFVHWFPLFTGYSLHETWTKIHFGIMFVGVNLTFFPQHFLGLAGMPRRYS 241
Cdd:PRK15017  405 GADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLS 484

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1194587522 242 DY--PDAYTLWNTASSIGSLISL-VAVIL*MF 270
Cdd:PRK15017  485 QQidPQFHTMLMIAASGAALIALgILCQVIQM 516
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 27-271 3.94e-16

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: 77.71  E-value: 3.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522  27 DPVLYQHLFWFFGHPEVYILILPGFGIISHVVAYYSGKKEPFGYMGMVWAMLSIgLLGFIVWAHHMFTtDLNVDTRAYF- 105
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFA-DPGIGPGWKFi 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 106 -TSATMIIAIPTGVKVFSWLATM-HGGVIK-------------WEAPMLWALGF-IFLFTVGGLTGIVLANSSIDIVLHD 169
Cdd:cd01660   278 hMVLTFMVALPSLLTAFTVFASLeIAGRLRggkglfgwiralpWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHN 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587522 170 TYYVVAHFHyvLSMGAVFAILA-GFVHWF-PLFTGYSLHETW-TKIHFGIMFVGVNLTFFPQHFLGLAGMPRR--YSDYP 244
Cdd:cd01660   358 TAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1194587522 245 DAY-----TLWNTASSIGSLISLVAVIL*MFI 271
Cdd:cd01660   436 GLPaagewAPYQQLMAIGGTILFVSGALFLYI 467
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH