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Conserved domains on  [gi|619322585|gb|AHY00462|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Chauliognathus sp. UPOL 001299]

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 ...
 1-241 4.00e-169

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: 475.90  E-value: 4.00e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00153 254 HIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYS 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00153 334 PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFF 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSMNTLNLPSSIEWF 240
Cdd:MTH00153 414 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWL 493


                 .
gi 619322585 241 Q 241
Cdd:MTH00153 494 Q 494
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-241 4.00e-169

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 475.90  E-value: 4.00e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00153 254 HIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYS 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00153 334 PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFF 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSMNTLNLPSSIEWF 240
Cdd:MTH00153 414 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWL 493


                 .
gi 619322585 241 Q 241
Cdd:MTH00153 494 Q 494
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-239 8.81e-146

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: 416.11  E-value: 8.81e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:cd01663  247 HIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFE 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:cd01663  327 TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFW 406

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSM-NTLNLPSSIEW 239
Cdd:cd01663  407 LMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIfNVGEGSTSLEW 486
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-221 3.41e-88

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 270.46  E-value: 3.41e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:COG0843  258 EIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFT 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:COG0843  337 TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFW 416

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNF--FLSWNVISSIGSLISTVSILFFIYIMWESF 221
Cdd:COG0843  417 LWFIGFNLTFFPMHILGLLGMPRRYATYPPEpgWQPLNLISTIGAFILAVGFLLFLINLVVSL 479
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 9-221 4.13e-85

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: 261.39  E-value: 4.13e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585    9 KKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYSPQMLWSLG 88
Cdd:TIGR02891 256 RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALG 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   89 FIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFLTMFVGVNM 168
Cdd:TIGR02891 336 FIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNL 415

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 619322585  169 TFFPQHFLGLSGMPRRYSDYP--NFFLSWNVISSIGSLISTVSILFFIYIMWESF 221
Cdd:TIGR02891 416 TFFPMHLLGLLGMPRRYYTYPpqMGFATLNLISTIGAFILAAGFLVFLWNLIWSL 470
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-205 2.16e-60

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: 195.87  E-value: 2.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585    1 HIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKIN-Y 79
Cdd:pfam00115 224 YILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfR 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   80 SPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQF 159
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF 382

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 619322585  160 LTMFVGVNMTFFPQHFLGLSGMPRRYS----DYPNFFLSWNVISSIGSLI 205
Cdd:pfam00115 383 WLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-241 4.00e-169

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 475.90  E-value: 4.00e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00153 254 HIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYS 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00153 334 PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFF 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSMNTLNLPSSIEWF 240
Cdd:MTH00153 414 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWL 493


                 .
gi 619322585 241 Q 241
Cdd:MTH00153 494 Q 494
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-239 8.81e-146

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: 416.11  E-value: 8.81e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:cd01663  247 HIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFE 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:cd01663  327 TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFW 406

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSM-NTLNLPSSIEW 239
Cdd:cd01663  407 LMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIfNVGEGSTSLEW 486
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-241 2.80e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 390.22  E-value: 2.80e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00116 256 HIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWD 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00116 336 PPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFG 415

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSMNTLNLPSSIEWF 240
Cdd:MTH00116 416 VMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWI 495


                 .
gi 619322585 241 Q 241
Cdd:MTH00116 496 H 496
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-239 1.41e-134

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 388.27  E-value: 1.41e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00167 256 HIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWE 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00167 336 TPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFF 415

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSMNTLNLPSSIEW 239
Cdd:MTH00167 416 VMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEW 494
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-239 1.80e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 383.17  E-value: 1.80e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00223 253 HIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYE 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00223 333 APMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFF 412

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSMNTLNLPSSIEW 239
Cdd:MTH00223 413 LMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEW 491
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-239 2.10e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 380.22  E-value: 2.10e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00142 254 HIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYE 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00142 334 PPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFY 413

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSMNTLNLPSSIEW 239
Cdd:MTH00142 414 TMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEW 492
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-239 5.11e-119

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 348.82  E-value: 5.11e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00007 253 HIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYE 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00007 333 TPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFF 412

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSMNTLNLPSSIEW 239
Cdd:MTH00007 413 LMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEW 491
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-240 7.71e-118

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 345.71  E-value: 7.71e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00103 256 HIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWS 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00103 336 PAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFT 415

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSMNTLNLPSSIEWF 240
Cdd:MTH00103 416 IMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWL 495
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-241 2.89e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 341.90  E-value: 2.89e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00183 256 HIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWE 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00183 336 TPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFG 415

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSMNTLNLPSSIEWF 240
Cdd:MTH00183 416 VMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWL 495


                 .
gi 619322585 241 Q 241
Cdd:MTH00183 496 H 496
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-240 9.40e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 337.96  E-value: 9.40e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00037 256 HVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWE 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00037 336 TPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFF 415

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSMNTLNLPSSIEWF 240
Cdd:MTH00037 416 LMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWQ 495
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-239 8.22e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 335.76  E-value: 8.22e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00077 256 HIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWD 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00077 336 AAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFG 415

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSMNTLNLPSSIEW 239
Cdd:MTH00077 416 VMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEW 494
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-222 8.27e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 315.08  E-value: 8.27e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00079 256 QSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQ 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00079 336 PLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFF 415

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFV 222
Cdd:MTH00079 416 LMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFF 477
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-241 3.62e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 298.66  E-value: 3.62e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00182 258 QIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLD 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00182 338 TPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFW 417

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMK----SMNTLNLPSS 236
Cdd:MTH00182 418 LMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKfigwKEGTGESWAS 497


                 ....*
gi 619322585 237 IEWFQ 241
Cdd:MTH00182 498 LEWVH 502
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-241 2.84e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 293.27  E-value: 2.84e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00184 258 QIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLD 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:MTH00184 338 TPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFW 417

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKS---MNTLNLPSSI 237
Cdd:MTH00184 418 LMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFvgwVEDSGHYPSL 497


                 ....
gi 619322585 238 EWFQ 241
Cdd:MTH00184 498 EWAQ 501
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-221 2.95e-96

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: 289.05  E-value: 2.95e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:cd00919  244 EIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFD 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:cd00919  323 PPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFW 402

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESF 221
Cdd:cd00919  403 LWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-221 3.41e-88

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 270.46  E-value: 3.41e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:COG0843  258 EIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFT 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFL 160
Cdd:COG0843  337 TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFW 416

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 619322585 161 TMFVGVNMTFFPQHFLGLSGMPRRYSDYPNF--FLSWNVISSIGSLISTVSILFFIYIMWESF 221
Cdd:COG0843  417 LWFIGFNLTFFPMHILGLLGMPRRYATYPPEpgWQPLNLISTIGAFILAVGFLLFLINLVVSL 479
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 9-221 4.13e-85

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: 261.39  E-value: 4.13e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585    9 KKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYSPQMLWSLG 88
Cdd:TIGR02891 256 RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALG 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   89 FIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFLTMFVGVNM 168
Cdd:TIGR02891 336 FIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNL 415

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 619322585  169 TFFPQHFLGLSGMPRRYSDYP--NFFLSWNVISSIGSLISTVSILFFIYIMWESF 221
Cdd:TIGR02891 416 TFFPMHLLGLLGMPRRYYTYPpqMGFATLNLISTIGAFILAAGFLVFLWNLIWSL 470
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-221 6.11e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 259.56  E-value: 6.11e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKIN-- 78
Cdd:MTH00026 257 QILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNli 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  79 YSPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQ 158
Cdd:MTH00026 337 FTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIH 416

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 619322585 159 FLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESF 221
Cdd:MTH00026 417 FWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAY 479
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 9-221 1.16e-77

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: 242.49  E-value: 1.16e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   9 KKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYSPQMLWSLG 88
Cdd:cd01662  257 RKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIG 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  89 FIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFLTMFVGVNM 168
Cdd:cd01662  337 FLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNL 416

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 619322585 169 TFFPQHFLGLSGMPRRYSDYPNF--FLSWNVISSIGSLISTVSILFFIYIMWESF 221
Cdd:cd01662  417 TFFPMHILGLMGMPRRVYTYLPGpgWDPLNLISTIGAFLIAAGVLLFLINVIVSI 471
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-222 2.67e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 241.89  E-value: 2.67e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   1 HIVSQESGKKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYS 80
Cdd:MTH00048 254 HICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKS 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  81 -PQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQF 159
Cdd:MTH00048 334 dPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHC 413

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 619322585 160 LTMFVGVNMTFFPQHFLGLSGMPRRYSDYPNFFLSWNVISSIGSLISTVSILFFIYIMWESFV 222
Cdd:MTH00048 414 IISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLV 476
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-205 2.16e-60

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: 195.87  E-value: 2.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585    1 HIVSQESGKKeTFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKIN-Y 79
Cdd:pfam00115 224 YILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfR 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   80 SPQMLWSLGFIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQF 159
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF 382

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 619322585  160 LTMFVGVNMTFFPQHFLGLSGMPRRYS----DYPNFFLSWNVISSIGSLI 205
Cdd:pfam00115 383 WLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 9-239 4.70e-54

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


Pssm-ID: 131890  Cd Length: 646  Bit Score: 183.72  E-value: 4.70e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585    9 KKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYSPQMLWSLG 88
Cdd:TIGR02843 306 RKRLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIG 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   89 FIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFLTMFVGVNM 168
Cdd:TIGR02843 386 FMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYL 465

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 619322585  169 TFFPQHFLGLSGMPRRYSDYPN-FFLSWNVISSIGSLISTVSILFFIYIMWESFVLMMKSMNTLNLP---SSIEW 239
Cdd:TIGR02843 466 AFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTGDPwggRTLEW 540
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 9-220 1.54e-44

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 158.18  E-value: 1.54e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585   9 KKETFGYIGMIYAMIAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTKINYSPQMLWSLG 88
Cdd:PRK15017 307 RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIG 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  89 FIFLFTVGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLKMKNKMLKIQFLTMFVGVNM 168
Cdd:PRK15017 387 FIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFV 466

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 619322585 169 TFFPQHFLGLSGMPRRYS-DYPNFFLSWNVISSIGSLISTVSILFFIYIMWES 220
Cdd:PRK15017 467 AFMPLYALGFMGMTRRLSqQIDPQFHTMLMIAASGAALIALGILCQVIQMYVS 519
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 62-217 5.98e-15

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: 73.47  E-value: 5.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585  62 GIKIFSWLATLHGTKINYSPQMLWSLGFIFlftvGGLTGIILSNSSIDIILHDTYYVVAHFHyvLSMGAVFAIMG-GLIH 140
Cdd:cd01660  309 GKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAY 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619322585 141 WF-PLFTGLKMK-NKMLKIQFLTMFVGVNMTFFPQHFLGLSGMPRR--YSDYPNFFL-----SWNVISSIGSLISTVSIL 211
Cdd:cd01660  383 WLvPHLTGRELAaKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPAagewaPYQQLMAIGGTILFVSGA 462


                 ....*.
gi 619322585 212 FFIYIM 217
Cdd:cd01660  463 LFLYIL 468
 
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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