NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1780015079|gb|QGQ76677|]
View 

cytochrome oxidase subunit I, partial (mitochondrion) [Xylocopa elegans]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-203 1.19e-114

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: 336.07  E-value: 1.19e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00153  305 SATMIIAVPTGIKIFSWLATLHGSQIN-YSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGA 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00153  384 VFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISI 463

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1780015079 161 IIMLFIIMESFMSKRIIMYKFS-QSSLEWLMNYPPLNHSFSETP 203
Cdd:MTH00153  464 LFFIFIIWESMISKRPVLFSLNlSSSIEWLQNLPPAEHSYSELP 507
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-203 1.19e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 336.07  E-value: 1.19e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00153  305 SATMIIAVPTGIKIFSWLATLHGSQIN-YSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGA 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00153  384 VFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISI 463

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1780015079 161 IIMLFIIMESFMSKRIIMYKFS-QSSLEWLMNYPPLNHSFSETP 203
Cdd:MTH00153  464 LFFIFIIWESMISKRPVLFSLNlSSSIEWLQNLPPAEHSYSELP 507
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-190 2.42e-94

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: 283.22  E-value: 2.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:cd01663   298 AATMIIAVPTGIKVFSWLATMWGGSIK-FETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGA 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:cd01663   377 VFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSV 456

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1780015079 161 IIMLFIIMESFMSKRIIMYK--FSQSSLEWLM 190
Cdd:cd01663   457 LLFLFIVWESFVSGRKVIFNvgEGSTSLEWTL 488
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-203 2.73e-59

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 193.81  E-value: 2.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   2 ATMIIAVPTGIKVFSWLATYHGCKMNLyNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGAV 81
Cdd:COG0843   309 ATMLIAVPTGVKVFNWIATMWRGRIRF-TTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVV 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  82 FAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFF--WNSMSSIGSIMSTNS 159
Cdd:COG0843   388 FAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWqpLNLISTIGAFILAVG 467

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1780015079 160 LIIMLFIIMESFMS-KRIIMYKFSQSSLEWLMNYPPLNHSFSETP 203
Cdd:COG0843   468 FLLFLINLVVSLRKgPKAGGNPWGARTLEWATPSPPPLYNFASIP 512
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-199 2.48e-56

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: 185.50  E-value: 2.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   2 ATMIIAVPTGIKVFSWLATYHGCKMNLyNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGAV 81
Cdd:TIGR02891 300 ATMLIAVPTGVKVFNWIATLWGGSIRF-TTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSV 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  82 FAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFF--WNSMSSIGSIMSTNS 159
Cdd:TIGR02891 379 FAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGFatLNLISTIGAFILAAG 458

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1780015079 160 LIIMLFIIMESFMSKRIIMYK-FSQSSLEWLMNYPPLNHSF 199
Cdd:TIGR02891 459 FLVFLWNLIWSLRKGPKAGANpWGATTLEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-137 1.32e-44

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: 153.11  E-value: 1.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   2 ATMIIAVPTGIKVFSWLATYHGCKMNLYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGAV 81
Cdd:pfam00115 275 FSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVV 354

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1780015079  82 FAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSD 137
Cdd:pfam00115 355 FALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-203 1.19e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 336.07  E-value: 1.19e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00153  305 SATMIIAVPTGIKIFSWLATLHGSQIN-YSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGA 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00153  384 VFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISI 463

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1780015079 161 IIMLFIIMESFMSKRIIMYKFS-QSSLEWLMNYPPLNHSFSETP 203
Cdd:MTH00153  464 LFFIFIIWESMISKRPVLFSLNlSSSIEWLQNLPPAEHSYSELP 507
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-190 2.42e-94

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: 283.22  E-value: 2.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:cd01663   298 AATMIIAVPTGIKVFSWLATMWGGSIK-FETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGA 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:cd01663   377 VFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSV 456

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1780015079 161 IIMLFIIMESFMSKRIIMYK--FSQSSLEWLM 190
Cdd:cd01663   457 LLFLFIVWESFVSGRKVIFNvgEGSTSLEWTL 488
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-203 1.34e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 274.66  E-value: 1.34e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00116  307 SATMIIAIPTGIKVFSWLATLHGGTIK-WDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGA 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00116  386 VFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAV 465

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1780015079 161 IIMLFIIMESFMSKR-IIMYKFSQSSLEWLMNYPPLNHSFSETP 203
Cdd:MTH00116  466 IMLMFIIWEAFSSKRkVLQPELTTTNIEWIHGCPPPYHTFEEPA 509
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-203 5.03e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 270.31  E-value: 5.03e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00223  304 AATMIIAVPTGIKVFSWLATIYGSKIK-YEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGA 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00223  383 VFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSV 462

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1780015079 161 IIMLFIIMESFMSKR-IIMYKFSQSSLEWLMNYPPLNHSFSETP 203
Cdd:MTH00223  463 LFFMFIVWEAFVSQRsVVWSGHLSTSLEWDNLLPADFHNNSETG 506
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-203 8.41e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 270.01  E-value: 8.41e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMnLYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00167  307 SATMIIAVPTGIKVFSWLATLHGGKI-KWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGA 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00167  386 VFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAV 465

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1780015079 161 IIMLFIIMESFMSKR-IIMYKFSQSSLEWLMNYPPLNHSFSETP 203
Cdd:MTH00167  466 ILFLFIIWEAFSSKRkLLPVELTSTNVEWLHGCPPPHHTWEEPP 509
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-203 1.00e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 261.97  E-value: 1.00e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00142  305 AATMVIAVPTGIKVFSWLATLHGSKVK-YEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGA 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00142  384 VFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAV 463

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1780015079 161 IIMLFIIMESFMSKRIIMY-KFSQSSLEWLMNYPPLNHSFSETP 203
Cdd:MTH00142  464 LMFVFIVWESFVSQRLVMWsSHLSTSLEWSHRLPPDFHTYDELP 507
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-203 2.52e-81

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 250.57  E-value: 2.52e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00103  307 SATMIIAIPTGVKVFSWLATLHGGNIK-WSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGA 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00103  386 VFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAV 465

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1780015079 161 IIMLFIIMESFMSKR-IIMYKFSQSSLEWLMNYPPLNHSFSETP 203
Cdd:MTH00103  466 MLMIFMIWEAFASKReVLTVELTTTNLEWLHGCPPPYHTFEEPT 509
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-202 1.77e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 248.70  E-value: 1.77e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00077  307 SATMIIAIPTGVKVFSWLATMHGGAIK-WDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGA 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00077  386 VFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAV 465

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1780015079 161 IIMLFIIMESFMSKRIIM-YKFSQSSLEWLMNYPPLNHSFSET 202
Cdd:MTH00077  466 IMMMFIIWEAFSSKREVLtTELTSTNIEWLHGCPPPYHTFEEP 508
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-203 1.12e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 244.06  E-value: 1.12e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00183  307 SATMIIAIPTGVKVFSWLATLHGGSIK-WETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGA 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00183  386 VFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAV 465

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1780015079 161 IIMLFIIMESFMSKR-IIMYKFSQSSLEWLMNYPPLNHSFSETP 203
Cdd:MTH00183  466 IMFLFILWEAFAAKReVLSVELTSTNVEWLHGCPPPYHTFEEPA 509
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-203 1.14e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 243.97  E-value: 1.14e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00037  307 AATMIIAVPTGIKVFSWMATLQGSNLR-WETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGA 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00037  386 VFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVAT 465

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1780015079 161 IIMLFIIMESFMSKRIIMY-KFSQSSLEWLMN-YPPLNHSFSETP 203
Cdd:MTH00037  466 LFFLFLIWEAFASQREVISpEFSSSSLEWQYSsFPPSHHTFDETP 510
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-202 1.55e-75

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 235.57  E-value: 1.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00007  304 AATMIIAVPTGIKVFSWLATIHGSPIK-YETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGA 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00007  383 VFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVAL 462

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1780015079 161 IIMLFIIMESFMSKR-IIMYKFSQSSLEWLMNYPPLNHSFSET 202
Cdd:MTH00007  463 LLFIFILWEAFSAQRgVIASPHMSSSLEWQDTLPLDFHNLPET 505
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-201 5.00e-72

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 226.49  E-value: 5.00e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNLyNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00079  307 AATMVIAVPTGVKVFSWLATLFGMKMKF-QPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGA 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00079  386 VFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFAL 465

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1780015079 161 IIMLFIIMESFMSKRIIM-YKFSQSSLEWLMNYPPLNHSFSE 201
Cdd:MTH00079  466 FLFIYVLLESFFSYRLVLhDNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-203 9.98e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 205.44  E-value: 9.98e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNLyNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00182  309 AATMIIAVPTGIKVFSWLATIYGGTLRL-DTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGA 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00182  388 VFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGV 467

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1780015079 161 IIMLFIIMESFMSKRIIM-----YKFSQSSLEWLMNYPPLNHSFSETP 203
Cdd:MTH00182  468 VWFIYIIYDAYVREEKFIgwkegTGESWASLEWVHSSPPLFHTYNELP 515
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-171 6.32e-63

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: 201.61  E-value: 6.32e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:cd00919   294 AATMIIAVPTGIKVFNWLATLWGGRIR-FDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGV 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:cd00919   373 VFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGL 452

                         170
                  ....*....|.
gi 1780015079 161 IIMLFIIMESF 171
Cdd:cd00919   453 LLFLGNLFLSL 463
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-203 7.24e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 195.05  E-value: 7.24e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNLyNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00184  309 AATMIIAVPTGIKIFSWIATIFGGSLRL-DTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGA 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00184  388 VFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGV 467

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1780015079 161 IIMLFIIMESFMSKRIIM----YKFSQSSLEWLMNYPPLNHSFSETP 203
Cdd:MTH00184  468 VWFIYIVYDAYVREIKFVgwveDSGHYPSLEWAQTSPPAHHTYNELP 514
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-203 2.73e-59

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 193.81  E-value: 2.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   2 ATMIIAVPTGIKVFSWLATYHGCKMNLyNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGAV 81
Cdd:COG0843   309 ATMLIAVPTGVKVFNWIATMWRGRIRF-TTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVV 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  82 FAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFF--WNSMSSIGSIMSTNS 159
Cdd:COG0843   388 FAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWqpLNLISTIGAFILAVG 467

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1780015079 160 LIIMLFIIMESFMS-KRIIMYKFSQSSLEWLMNYPPLNHSFSETP 203
Cdd:COG0843   468 FLLFLINLVVSLRKgPKAGGNPWGARTLEWATPSPPPLYNFASIP 512
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-199 2.48e-56

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: 185.50  E-value: 2.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   2 ATMIIAVPTGIKVFSWLATYHGCKMNLyNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGAV 81
Cdd:TIGR02891 300 ATMLIAVPTGVKVFNWIATLWGGSIRF-TTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSV 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  82 FAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFF--WNSMSSIGSIMSTNS 159
Cdd:TIGR02891 379 FAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGFatLNLISTIGAFILAAG 458

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1780015079 160 LIIMLFIIMESFMSKRIIMYK-FSQSSLEWLMNYPPLNHSF 199
Cdd:TIGR02891 459 FLVFLWNLIWSLRKGPKAGANpWGATTLEWTTSSPPPAHNF 499
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-203 5.25e-51

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 172.12  E-value: 5.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNL-YNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMG 79
Cdd:MTH00026  308 AATMIIAVPTGIKIFSWLATVSGSGRNLiFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMG 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  80 AVFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNS 159
Cdd:MTH00026  388 AVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIA 467

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1780015079 160 LIIMLFIIMESF----------MSKRIIMYKFSQ----SSLEWLMNYPPLNHSFSETP 203
Cdd:MTH00026  468 VIWFIVVIFDAYyreepfdiniMAKGPLIPFSCQpahfDTLEWSLTSPPEHHTYNELP 525
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-199 1.02e-50

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: 170.84  E-value: 1.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   2 ATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGAV 81
Cdd:cd01662   301 ATMIIAVPTGVKIFNWLFTMWRGRIR-FETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVV 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  82 FAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFF--WNSMSSIGSIMSTNS 159
Cdd:cd01662   380 FPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWdpLNLISTIGAFLIAAG 459

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1780015079 160 LIIMLFIIMESFMSKRIIMYK--FSQSSLEWLMNYPPLNHSF 199
Cdd:cd01662   460 VLLFLINVIVSIRKGKRDATGdpWGARTLEWATSSPPPAYNF 501
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-186 7.86e-49

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 166.01  E-value: 7.86e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   1 SATMIIAVPTGIKVFSWLATYHGCKMNLYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGA 80
Cdd:MTH00048  305 SVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGS 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  81 VFAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYFFWNSMSSIGSIMSTNSL 160
Cdd:MTH00048  385 YSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSG 464

                         170       180
                  ....*....|....*....|....*.
gi 1780015079 161 IIMLFIIMESFMSKRIIMYKFSQSSL 186
Cdd:MTH00048  465 CFFVFILWESLVVKNEVLGLWGSSSC 490
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-137 1.32e-44

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: 153.11  E-value: 1.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   2 ATMIIAVPTGIKVFSWLATYHGCKMNLYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGAV 81
Cdd:pfam00115 275 FSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVV 354

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1780015079  82 FAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSD 137
Cdd:pfam00115 355 FALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-203 1.27e-35

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: 131.90  E-value: 1.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   2 ATMIIAVPTGIKVFSWLATYHGCKMNlYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGAV 81
Cdd:TIGR02882 344 TTMAIAIPTGVKIFNWLLTLYKGKIR-FTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVV 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079  82 FAIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDY--PDAYFFWNSMSSIGSIMSTNS 159
Cdd:TIGR02882 423 FACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIG 502

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1780015079 160 LIIMLFIIMESFM--SKRIIMYKFSQSSLEWLMNYPPLNHSFSETP 203
Cdd:TIGR02882 503 FIFLVYNIYYSHRksPREATGDPWNGRTLEWATASPPPKYNFAVTP 548
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 3-143 1.93e-30

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 117.34  E-value: 1.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   3 TMIIAVPTGIKVFSWLATYHGCKMnLYNNSIMWSLGFVILFTIGGLTGIMLSNSSIDIILHDTYYVVGHFHYVLSMGAVF 82
Cdd:PRK15017  352 TMIIAIPTGVKIFNWLFTMYQGRI-VFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVF 430

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1780015079  83 AIISSFIHWYPLIYGTMLNQKWLKIQFIIMFIGVNMTFFPQHFLGLMGMPRRYSDYPDAYF 143
Cdd:PRK15017  431 GCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQF 491
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 3-140 1.37e-11

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: 62.69  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1780015079   3 TMIIAVPTGIKVFSWLAT------------YHGCKMNLYNNSIMWSLGFV--ILFTIGGLTGIMLSNSSIDIILHDTYYV 68
Cdd:cd01660   282 TFMVALPSLLTAFTVFASleiagrlrggkgLFGWIRALPWGDPMFLALFLamLMFIPGGAGGIINASYQLNYVVHNTAWV 361

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1780015079  69 VGHFHyvLSMGAVFAIISSFIHWY--PLIYGTMLNQKWL-KIQFIIMFIGVNMTFFPQHFLGLMGMPRR--YSDYPD 140
Cdd:cd01660   362 PGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGG 436
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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