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Conserved domains on  [gi|1931117355|gb|QPB40232|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Uvarovistia satunini]

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 ...
 1-328 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: 669.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00153  154 SSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00153  234 WFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00153  314 TGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIH 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:MTH00153  394 WFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWES 473


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:MTH00153  474 MISKRPVL 481
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-328 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 669.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00153  154 SSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00153  234 WFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00153  314 TGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIH 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:MTH00153  394 WFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWES 473


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:MTH00153  474 MISKRPVL 481
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-328 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: 592.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:cd01663   147 SSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:cd01663   227 WFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVP 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:cd01663   307 TGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYY 386

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:cd01663   387 WFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWES 466


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:cd01663   467 FVSGRKVI 474
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-304 1.17e-136

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 398.35  E-value: 1.17e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:COG0843   158 GSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:COG0843   238 WFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVP 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:COG0843   317 TGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYY 396

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTSWNVVSSLGST 304
Cdd:COG0843   397 WFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAF 462
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-303 1.19e-134

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: 391.97  E-value: 1.19e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:TIGR02891 149 SSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLF 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:TIGR02891 229 WFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVP 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:TIGR02891 308 TGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYY 387

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDS--YTSWNVVSSLGS 303
Cdd:TIGR02891 388 WFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGA 452
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-304 3.89e-94

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: 286.01  E-value: 3.89e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLdQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLF 80
Cdd:pfam00115 131 SSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:pfam00115 204 WWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVP 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLT-YSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFI 239
Cdd:pfam00115 283 SGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIY 362

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1931117355 240 QWYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYS----DYPDSYTSWNVVSSLGST 304
Cdd:pfam00115 363 YWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGV 431
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-328 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 669.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00153  154 SSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00153  234 WFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00153  314 TGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIH 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:MTH00153  394 WFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWES 473


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:MTH00153  474 MISKRPVL 481
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-328 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: 592.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:cd01663   147 SSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:cd01663   227 WFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVP 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:cd01663   307 TGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYY 386

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:cd01663   387 WFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWES 466


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:cd01663   467 FVSGRKVI 474
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-328 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 557.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00167  156 SSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00167  236 WFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVP 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00167  316 TGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTH 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:MTH00167  396 WFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEA 475


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:MTH00167  476 FSSKRKLL 483
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-328 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 550.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00223  153 SSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00223  233 WFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVP 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00223  313 TGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNH 392

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:MTH00223  393 WFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEA 472


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:MTH00223  473 FVSQRSVV 480
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-328 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 545.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00142  154 SSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00142  234 WFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVP 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00142  314 TGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIH 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:MTH00142  394 WFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWES 473


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:MTH00142  474 FVSQRLVM 481
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-328 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 545.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00116  156 SSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00116  236 WFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIP 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00116  316 TGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTH 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:MTH00116  396 WFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEA 475


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:MTH00116  476 FSSKRKVL 483
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-328 1.43e-175

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 496.33  E-value: 1.43e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00103  156 SSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00103  236 WFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIP 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00103  316 TGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVH 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:MTH00103  396 WFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEA 475


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:MTH00103  476 FASKREVL 483
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-328 4.79e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 490.20  E-value: 4.79e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00183  156 SSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00183  236 WFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIP 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00183  316 TGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVH 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:MTH00183  396 WFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEA 475


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:MTH00183  476 FAAKREVL 483
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-328 9.13e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 489.34  E-value: 9.13e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00037  156 SSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00037  236 WFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVP 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00037  316 TGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTH 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:MTH00037  396 WFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEA 475


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:MTH00037  476 FASQREVI 483
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-328 1.90e-171

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 485.95  E-value: 1.90e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00007  153 SSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00007  233 WFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVP 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00007  313 TGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNH 392

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:MTH00007  393 WFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEA 472


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:MTH00007  473 FSAQRGVI 480
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-328 1.58e-168

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 478.67  E-value: 1.58e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00077  156 SSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00077  236 WFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIP 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00077  316 TGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVH 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:MTH00077  396 WFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEA 475


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:MTH00077  476 FSSKREVL 483
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-328 5.36e-163

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 464.15  E-value: 5.36e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00079  156 SSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00079  236 WFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVP 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00079  316 TGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISL 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:MTH00079  396 WWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLES 475


                  ....*...
gi 1931117355 321 MISNRTVL 328
Cdd:MTH00079  476 FFSYRLVL 483
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-304 7.99e-156

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 446.58  E-value: 7.99e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00182  158 SSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00182  238 WFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVP 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00182  318 TGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYY 397

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGST 304
Cdd:MTH00182  398 WFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSI 461
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-303 2.39e-151

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 435.02  E-value: 2.39e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00184  158 SSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00184  238 WFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVP 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:MTH00184  318 TGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYY 397

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGS 303
Cdd:MTH00184  398 WFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGS 460
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-321 1.11e-143

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: 413.46  E-value: 1.11e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:cd00919   144 SSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:cd00919   224 WFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVP 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:cd00919   303 TGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYY 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWES 320
Cdd:cd00919   383 WFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLS 462


                  .
gi 1931117355 321 M 321
Cdd:cd00919   463 L 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-304 1.17e-136

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 398.35  E-value: 1.17e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:COG0843   158 GSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:COG0843   238 WFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVP 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:COG0843   317 TGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYY 396

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTSWNVVSSLGST 304
Cdd:COG0843   397 WFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAF 462
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-303 1.19e-134

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: 391.97  E-value: 1.19e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:TIGR02891 149 SSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLF 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:TIGR02891 229 WFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVP 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:TIGR02891 308 TGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYY 387

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDS--YTSWNVVSSLGS 303
Cdd:TIGR02891 388 WFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGA 452
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-303 2.08e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 387.45  E-value: 2.08e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00026  157 SSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00026  237 WFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVP 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGT--QLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGF 238
Cdd:MTH00026  317 TGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGF 396

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1931117355 239 IQWYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGS 303
Cdd:MTH00026  397 YLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGS 461
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-303 2.04e-123

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: 363.44  E-value: 2.04e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:cd01662   150 GTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:cd01662   230 WIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVP 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQ 240
Cdd:cd01662   309 TGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYY 388

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1931117355 241 WYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTSWNVVSSLGS 303
Cdd:cd01662   389 WFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGA 453
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-328 1.01e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 356.68  E-value: 1.01e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLdQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 80
Cdd:MTH00048  155 SSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:MTH00048  234 WFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVP 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLTYS-PALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFI 239
Cdd:MTH00048  314 TGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFI 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 240 QWYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWE 319
Cdd:MTH00048  394 WWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWE 473


                  ....*....
gi 1931117355 320 SMISNRTVL 328
Cdd:MTH00048  474 SLVVKNEVL 482
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-304 3.89e-94

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: 286.01  E-value: 3.89e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   1 SSILGAVNFITTTINMRAPGMSLdQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLF 80
Cdd:pfam00115 131 SSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLF 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  81 WFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVP 160
Cdd:pfam00115 204 WWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVP 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 161 TGIKIFSWLATLHGTQLT-YSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFI 239
Cdd:pfam00115 283 SGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIY 362

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1931117355 240 QWYPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYS----DYPDSYTSWNVVSSLGST 304
Cdd:pfam00115 363 YWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGV 431
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-303 6.01e-77

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: 247.84  E-value: 6.01e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   2 SILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFW 81
Cdd:TIGR02882 194 TLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFW 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  82 FFGHPEVYILILPGFGMVSHIISQESgKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPT 161
Cdd:TIGR02882 274 IWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPT 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 162 GIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQW 241
Cdd:TIGR02882 353 GVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYW 432

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1931117355 242 YPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDY--PDSYTSWNVVSSLGS 303
Cdd:TIGR02882 433 YPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGA 496
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-290 4.53e-70

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 230.21  E-value: 4.53e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355   2 SILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFW 81
Cdd:PRK15017  201 TTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  82 FFGHPEVYILILPGFGMVSHIISQESgKKEAFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPT 161
Cdd:PRK15017  281 AWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPT 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 162 GIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQW 241
Cdd:PRK15017  360 GVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYW 439

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1931117355 242 YPLFTGLTLNPKWLKIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDYPD 290
Cdd:PRK15017  440 WPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 72-304 9.97e-18

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: 83.49  E-value: 9.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355  72 DPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIyAMMAIGLLGFVVWAHHMFT-VGMDVDTRAYF 150
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 151 TSATMIIAVPTGIKIFSWLATL-HGTQLTYSPALLW---------------VLGFVFlFTIGGLTGVVLANSSLDIILHD 214
Cdd:cd01660   279 MVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHN 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931117355 215 TYYVVAHFHyvLSMGAVFAIMAGFIQWY--PLFTGLTLNPKWL-KIQFTIMFVGVNLTFFPQHFLGLAGMPRR--YSDYP 289
Cdd:cd01660   358 TAWVPGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435

                         250       260
                  ....*....|....*....|
gi 1931117355 290 DSY-----TSWNVVSSLGST 304
Cdd:cd01660   436 GLPaagewAPYQQLMAIGGT 455
 
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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