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Conserved domains on  [gi|1213499534|gb|ASG91978|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Sphenarium histrio]

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 ...
 1-355 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: 722.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00153  128 PPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITML 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00153  208 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWA 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00153  288 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHD 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00153  368 TYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTS 447

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTIMF 355
Cdd:MTH00153  448 WNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-355 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 722.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00153  128 PPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITML 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00153  208 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWA 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00153  288 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHD 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00153  368 TYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTS 447

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTIMF 355
Cdd:MTH00153  448 WNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-355 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: 641.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:cd01663   121 PPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITML 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:cd01663   201 LTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWA 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:cd01663   281 HHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHD 360

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:cd01663   361 TYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAG 440

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTIMF 355
Cdd:cd01663   441 WNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIF 475
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-351 4.70e-147

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 425.70  E-value: 4.70e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:COG0843   132 PPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLL 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:COG0843   212 LLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWA 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:COG0843   291 HHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHD 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAY 318
Cdd:COG0843   371 TYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGW 450

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1213499534 319 LSWNMISSMGSTISIVGILMFIFIVWESMISKR 351
Cdd:COG0843   451 QPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-351 2.13e-145

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: 420.48  E-value: 2.13e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:TIGR02891 123 PPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:TIGR02891 203 LLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWA 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:TIGR02891 282 HHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHD 361

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDA--Y 318
Cdd:TIGR02891 362 TYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgF 441

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1213499534 319 LSWNMISSMGSTISIVGILMFIFIVWESMISKR 351
Cdd:TIGR02891 442 ATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP 474
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 14-331 3.71e-95

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: 289.86  E-value: 3.71e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  14 VDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLdQTPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNtsffdp 93
Cdd:pfam00115 118 VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------ 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  94 AGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTR 173
Cdd:pfam00115 191 AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQ 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 174 AYFTSATMIIAVPTGIKVFSWLATLYGTKFKFN-PPLLWAIGFIFLFTIGGLTGLILANSSLDIILHDTYYVVAHFHYVL 252
Cdd:pfam00115 270 ALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVL 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 253 SMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYS----DYPDAYLSWNMISSMG 328
Cdd:pfam00115 350 FGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIG 429


                  ...
gi 1213499534 329 STI 331
Cdd:pfam00115 430 GVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-355 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 722.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00153  128 PPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITML 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00153  208 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWA 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00153  288 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHD 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00153  368 TYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTS 447

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTIMF 355
Cdd:MTH00153  448 WNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-355 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: 641.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:cd01663   121 PPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITML 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:cd01663   201 LTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWA 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:cd01663   281 HHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHD 360

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:cd01663   361 TYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAG 440

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTIMF 355
Cdd:cd01663   441 WNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIF 475
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-354 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 605.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00116  130 PPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITML 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00116  210 LTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWA 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00116  290 HHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHD 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00116  370 TYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL 449

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTIM 354
Cdd:MTH00116  450 WNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVL 483
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-355 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 605.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00223  127 PPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITML 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00223  207 LTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWA 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00223  287 HHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHD 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00223  367 TYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTK 446

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTIMF 355
Cdd:MTH00223  447 WNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-351 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 599.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00167  130 PPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITML 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00167  210 LTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWA 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00167  290 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHD 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00167  370 TYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL 449

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKR 351
Cdd:MTH00167  450 WNVVSSIGSLISLVAVILFLFIIWEAFSSKR 480
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-355 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 595.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00142  128 PPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITML 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00142  208 LTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWA 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00142  288 HHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHD 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00142  368 TYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTT 447

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTIMF 355
Cdd:MTH00142  448 WNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMW 482
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-354 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 536.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00007  127 PPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITML 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00007  207 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWA 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00007  287 HHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHD 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00007  367 TYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTK 446

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTIM 354
Cdd:MTH00007  447 WNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVI 480
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-355 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 535.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00103  130 PPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITML 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00103  210 LTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWA 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00103  290 HHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHD 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00103  370 TYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTT 449

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTIMF 355
Cdd:MTH00103  450 WNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLT 484
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-355 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 531.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00183  130 PPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITML 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00183  210 LTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWA 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00183  290 HHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHD 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00183  370 TYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL 449

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTIMF 355
Cdd:MTH00183  450 WNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-355 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 528.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00037  130 PPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITML 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00037  210 LTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWA 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00037  290 HHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHD 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00037  370 TYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL 449

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTIMF 355
Cdd:MTH00037  450 WNTVSSIGSTISLVATLFFLFLIWEAFASQREVIS 484
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-353 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 526.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00077  130 PPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITML 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00077  210 LTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWA 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00077  290 HHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHD 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00077  370 TYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL 449

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTI 353
Cdd:MTH00077  450 WNTVSSIGSLISLVAVIMMMFIIWEAFSSKREV 482
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-354 1.88e-176

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 499.59  E-value: 1.88e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSgAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00079  131 PPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITML 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00079  210 LTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWA 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00079  290 HHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHD 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00079  370 TYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSV 449

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKRTIM 354
Cdd:MTH00079  450 WNVISSYGSMISVFALFLFIYVLLESFFSYRLVL 483
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-351 1.74e-172

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 490.10  E-value: 1.74e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00182  132 PPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITML 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00182  212 LTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWA 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00182  292 HHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHD 371

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00182  372 TYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAG 451

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESMISKR 351
Cdd:MTH00182  452 WNLVSSLGSIISIVGVVWFIYIIYDAYVREE 482
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-346 2.20e-168

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 479.71  E-value: 2.20e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00184  132 PPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITML 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00184  212 LTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWA 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00184  292 HHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHD 371

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:MTH00184  372 TYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAG 451

                         330       340
                  ....*....|....*....|....*.
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWES 346
Cdd:MTH00184  452 WNQISSLGSVISIVGVVWFIYIVYDA 477
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-347 4.47e-157

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: 448.52  E-value: 4.47e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:cd00919   118 PPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVML 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:cd00919   198 LLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWA 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:cd00919   277 HHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHD 356

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLS 320
Cdd:cd00919   357 TYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAP 436

                         330       340
                  ....*....|....*....|....*..
gi 1213499534 321 WNMISSMGSTISIVGILMFIFIVWESM 347
Cdd:cd00919   437 WNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-351 4.70e-147

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 425.70  E-value: 4.70e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:COG0843   132 PPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLL 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:COG0843   212 LLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWA 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:COG0843   291 HHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHD 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAY 318
Cdd:COG0843   371 TYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGW 450

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1213499534 319 LSWNMISSMGSTISIVGILMFIFIVWESMISKR 351
Cdd:COG0843   451 QPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-351 2.13e-145

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: 420.48  E-value: 2.13e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:TIGR02891 123 PPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:TIGR02891 203 LLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWA 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:TIGR02891 282 HHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHD 361

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDA--Y 318
Cdd:TIGR02891 362 TYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgF 441

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1213499534 319 LSWNMISSMGSTISIVGILMFIFIVWESMISKR 351
Cdd:TIGR02891 442 ATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP 474
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-346 5.91e-145

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 420.57  E-value: 5.91e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00026  131 PPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITML 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00026  211 LTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWA 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGT--KFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIIL 238
Cdd:MTH00026  291 HHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILL 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 239 HDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAY 318
Cdd:MTH00026  371 HDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNF 450

                         330       340
                  ....*....|....*....|....*...
gi 1213499534 319 LSWNMISSMGSTISIVGILMFIFIVWES 346
Cdd:MTH00026  451 EDFNQISSFGSIISIIAVIWFIVVIFDA 478
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-354 6.81e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 386.34  E-value: 6.81e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLdQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:MTH00048  129 PPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITML 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00048  208 LFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWA 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLL-WAIGFIFLFTIGGLTGLILANSSLDIILH 239
Cdd:MTH00048  288 HHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLH 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 240 DTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYL 319
Cdd:MTH00048  368 DTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYY 447

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1213499534 320 SWNMISSMGSTISIVGILMFIFIVWESMISKRTIM 354
Cdd:MTH00048  448 WINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-347 6.30e-127

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: 373.45  E-value: 6.30e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:cd01662   124 PPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALL 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:cd01662   204 ELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWV 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:cd01662   283 HHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHD 362

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAY 318
Cdd:cd01662   363 TYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGW 442

                         330       340
                  ....*....|....*....|....*....
gi 1213499534 319 LSWNMISSMGSTISIVGILMFIFIVWESM 347
Cdd:cd01662   443 DPLNLISTIGAFLIAAGVLLFLINVIVSI 471
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 14-331 3.71e-95

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: 289.86  E-value: 3.71e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  14 VDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLdQTPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNtsffdp 93
Cdd:pfam00115 118 VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------ 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  94 AGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTR 173
Cdd:pfam00115 191 AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQ 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 174 AYFTSATMIIAVPTGIKVFSWLATLYGTKFKFN-PPLLWAIGFIFLFTIGGLTGLILANSSLDIILHDTYYVVAHFHYVL 252
Cdd:pfam00115 270 ALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVL 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 253 SMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYS----DYPDAYLSWNMISSMG 328
Cdd:pfam00115 350 FGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIG 429


                  ...
gi 1213499534 329 STI 331
Cdd:pfam00115 430 GVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-346 9.34e-78

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: 250.93  E-value: 9.34e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   2 PLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITMLL 81
Cdd:TIGR02882 168 PLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMT 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  82 TDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAH 161
Cdd:TIGR02882 248 TDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVH 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 162 HMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHDT 241
Cdd:TIGR02882 327 HFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNT 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 242 YYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDY--PDAYL 319
Cdd:TIGR02882 407 YFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWF 486

                         330       340
                  ....*....|....*....|....*..
gi 1213499534 320 SWNMISSMGSTISIVGILMFIFIVWES 346
Cdd:TIGR02882 487 PLNLISTIGALLMAIGFIFLVYNIYYS 513
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-347 2.48e-75

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 244.85  E-value: 2.48e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534   1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSNKMTLDQTPLFVWSVVITALLLLLSLPVLAGAITML 80
Cdd:PRK15017  174 PPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALL 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:PRK15017  254 TLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWL 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:PRK15017  333 HHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHN 412

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLFMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPD-AYL 319
Cdd:PRK15017  413 SLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFH 492

                         330       340
                  ....*....|....*....|....*...
gi 1213499534 320 SWNMISSMGSTISIVGILMFIFIVWESM 347
Cdd:PRK15017  493 TMLMIAASGAALIALGILCQVIQMYVSI 520
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 98-347 2.75e-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: 85.80  E-value: 2.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534  98 DPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIgLMGFIVWAHHMFT-VGMDVDTRAYF 176
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFAdPGIGPGWKFIH 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 177 TSATMIIAVPTGIKVFSWLAT------------LYGTKFKF---NPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHDT 241
Cdd:cd01660   279 MVLTFMVALPSLLTAFTVFASleiagrlrggkgLFGWIRALpwgDPMFLALFLAMLMFIPGGAGGIINASYQLNYVVHNT 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499534 242 YYVVAHFHyvLSMGAVFAIMG-GIIQWY-PLFTGLFMNNKWL-KIQFMIMFIGVNMTFFPQHFLGLAGMPRR--YSDYPD 316
Cdd:cd01660   359 AWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGG 436

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1213499534 317 AYL-----SWNMISSMGSTISIVGILMFIFIVWESM 347
Cdd:cd01660   437 LPAagewaPYQQLMAIGGTILFVSGALFLYILFRTL 472
 
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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