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Conserved domains on  [gi|313504476|gb|ADR63919|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Tetrapterocarpon sp. Bruneau & Ranaivojaona 1395]

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 ...
 1-232 8.27e-152

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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 431.52  E-value: 8.27e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSG-KPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:cd01663  240 PGFGIISHIISTFSGkKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMW 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:cd01663  320 GGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNET 399

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVVTITSSSGNN 232
Cdd:cd01663  400 LGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRK 472
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-232 8.27e-152

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: 431.52  E-value: 8.27e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSG-KPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:cd01663  240 PGFGIISHIISTFSGkKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMW 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:cd01663  320 GGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNET 399

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVVTITSSSGNN 232
Cdd:cd01663  400 LGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRK 472
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-223 7.03e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 363.80  E-value: 7.03e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00153 247 PGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00153 327 GSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPK 406

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVV 223
Cdd:MTH00153 407 WLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFII 470
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-231 9.35e-106

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: 314.55  E-value: 9.35e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476    1 PGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWG 80
Cdd:TIGR02891 242 PAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWG 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   81 GSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPETL 160
Cdd:TIGR02891 322 GSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERL 401

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313504476  161 GQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDA--YAGWNALSSFGSYISVVGIRRFFVVVTITSSSGN 231
Cdd:TIGR02891 402 GRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP 474
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-241 2.32e-102

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 307.05  E-value: 2.32e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWG 80
Cdd:COG0843  251 PAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWR 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  81 GSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPETL 160
Cdd:COG0843  331 GRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERL 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476 161 GQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYP--DAYAGWNALSSFGSYISVVGIRRFFVVVTITSSSGNnktKRAN 238
Cdd:COG0843  411 GKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP---KAGG 487


                 ...
gi 313504476 239 IPW 241
Cdd:COG0843  488 NPW 490
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-211 2.42e-74

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: 232.08  E-value: 2.42e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476    1 PGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWG 80
Cdd:pfam00115 217 PAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   81 GSIQ-YKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:pfam00115 297 GWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEK 376

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 313504476  160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIP----DYPDAYAGWNALSSFGSYI 211
Cdd:pfam00115 377 LGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-232 8.27e-152

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: 431.52  E-value: 8.27e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSG-KPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:cd01663  240 PGFGIISHIISTFSGkKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMW 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:cd01663  320 GGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNET 399

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVVTITSSSGNN 232
Cdd:cd01663  400 LGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRK 472
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-223 7.03e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 363.80  E-value: 7.03e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00153 247 PGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00153 327 GSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPK 406

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVV 223
Cdd:MTH00153 407 WLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFII 470
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-223 7.97e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 350.90  E-value: 7.97e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00167 249 PGFGMISHIVVYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLH 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00167 329 GGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNET 408

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVV 223
Cdd:MTH00167 409 WTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFII 472
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-223 3.75e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 349.28  E-value: 3.75e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGK-PVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00223 246 PGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIY 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00223 326 GSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRR 405

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVV 223
Cdd:MTH00223 406 WAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIV 469
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-216 5.19e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 336.29  E-value: 5.19e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00116 249 PGFGIISHIVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLH 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00116 329 GGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQT 408

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGI 216
Cdd:MTH00116 409 WTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAV 465
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-223 7.88e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 328.22  E-value: 7.88e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00142 247 PGFGMISHIINHYSGKKeVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLH 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00142 327 GSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPR 406

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVV 223
Cdd:MTH00142 407 WLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIV 470
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-223 8.59e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 320.62  E-value: 8.59e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00184 251 PGFGIISQIIPTFAAKKqIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIF 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00184 331 GGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEV 410

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVV 223
Cdd:MTH00184 411 YGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIV 474
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-223 1.34e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 320.23  E-value: 1.34e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGK-PVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00182 251 PGFGMISQIIPTFVAKkQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIY 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00182 331 GGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEL 410

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVV 223
Cdd:MTH00182 411 YGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYII 474
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-223 2.46e-106

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: 314.85  E-value: 2.46e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWG 80
Cdd:cd00919  237 PAFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWG 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  81 GSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPETL 160
Cdd:cd00919  317 GRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKL 396

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313504476 161 GQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVV 223
Cdd:cd00919  397 GKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNL 459
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-231 9.35e-106

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: 314.55  E-value: 9.35e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476    1 PGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWG 80
Cdd:TIGR02891 242 PAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWG 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   81 GSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPETL 160
Cdd:TIGR02891 322 GSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERL 401

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313504476  161 GQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDA--YAGWNALSSFGSYISVVGIRRFFVVVTITSSSGN 231
Cdd:TIGR02891 402 GRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP 474
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-241 2.32e-102

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 307.05  E-value: 2.32e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWG 80
Cdd:COG0843  251 PAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWR 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  81 GSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPETL 160
Cdd:COG0843  331 GRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERL 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476 161 GQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYP--DAYAGWNALSSFGSYISVVGIRRFFVVVTITSSSGNnktKRAN 238
Cdd:COG0843  411 GKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP---KAGG 487


                 ...
gi 313504476 239 IPW 241
Cdd:COG0843  488 NPW 490
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-234 2.03e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 301.75  E-value: 2.03e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00037 249 PGFGMISHVIAHYSGKQePFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQ 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00037 329 GSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPL 408

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVVTITSSSGNNKT 234
Cdd:MTH00037 409 WSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVI 483
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-223 2.53e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 298.76  E-value: 2.53e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00183 249 PGFGMISHIVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLH 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00183 329 GGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHST 408

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVV 223
Cdd:MTH00183 409 WTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFIL 472
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-223 9.23e-99

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 297.20  E-value: 9.23e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00007 246 PGFGAISHIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIH 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00007 326 GSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDR 405

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVV 223
Cdd:MTH00007 406 WAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFIL 469
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-216 2.23e-98

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 296.41  E-value: 2.23e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00103 249 PGFGMISHIVTYYSGKKePFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLH 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00103 329 GGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDT 408

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGI 216
Cdd:MTH00103 409 WAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAV 465
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-216 2.35e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 293.77  E-value: 2.35e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00077 249 PGFGMISHIVTYYSAKKePFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMH 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00077 329 GGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHST 408

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGI 216
Cdd:MTH00077 409 WSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAV 465
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-223 3.83e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 293.13  E-value: 3.83e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00079 249 PAFGIISQSTLYLTGKKeVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLF 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:MTH00079 329 GMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKL 408

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313504476 160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVV 223
Cdd:MTH00079 409 MMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVL 472
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-241 2.70e-94

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: 285.24  E-value: 2.70e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWG 80
Cdd:cd01662  243 PAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWR 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  81 GSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPETL 160
Cdd:cd01662  323 GRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERL 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476 161 GQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYP--DAYAGWNALSSFGSYISVVGIrrFFVVVTITSSSGNNKTKRAN 238
Cdd:cd01662  403 GKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGV--LLFLINVIVSIRKGKRDATG 480


                 ...
gi 313504476 239 IPW 241
Cdd:cd01662  481 DPW 483
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-223 9.36e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 269.58  E-value: 9.36e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFS-GKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00026 250 PGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVS 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GG--SIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYP 157
Cdd:MTH00026 330 GSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYK 409

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313504476 158 ETLGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVV 223
Cdd:MTH00026 410 DIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVI 475
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-211 2.42e-74

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: 232.08  E-value: 2.42e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476    1 PGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWG 80
Cdd:pfam00115 217 PAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   81 GSIQ-YKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPET 159
Cdd:pfam00115 297 GWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEK 376

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 313504476  160 LGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIP----DYPDAYAGWNALSSFGSYI 211
Cdd:pfam00115 377 LGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-231 1.40e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 209.15  E-value: 1.40e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMW 79
Cdd:MTH00048 247 PGFGIISHICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLL 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  80 GGSIQYKTPML-FAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPE 158
Cdd:MTH00048 327 NSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNK 406

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313504476 159 TLGQIHFWITFFGVNPTLFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIRRFFVVVTITSSSGN 231
Cdd:MTH00048 407 YLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKN 479
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-191 3.10e-51

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 176.66  E-value: 3.10e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476   1 PGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWG 80
Cdd:PRK15017 293 PVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQ 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  81 GSIQYKTPMLFAVGFIFLFTIGGLTGIVPANSGLDIALHDTYYAVAHFHYVLSMGAVFALFAGFHYWVGKIFGRTYPETL 160
Cdd:PRK15017 373 GRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETW 452

                        170       180       190
                 ....*....|....*....|....*....|.
gi 313504476 161 GQIHFWITFFGVNPTLFPMHFLGLSGMPRRI 191
Cdd:PRK15017 453 GKRAFWFWIIGFFVAFMPLYALGFMGMTRRL 483
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 60-226 2.07e-14

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: 71.93  E-value: 2.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476  60 TMIIAVPTGIKIFSWIATM--------------WGGSIQYKTPMLFAVGF-IFLFTIGGLTGIVPANSGLDIALHDTYYA 124
Cdd:cd01660  282 TFMVALPSLLTAFTVFASLeiagrlrggkglfgWIRALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTAWV 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313504476 125 VAHFHyvLSMGAVFAL-FAGFHYW-VGKIFGRTYP-ETLGQIHFWITFFGVNPTLFPMHFLGLSGMPRR--IPDYPDAY- 198
Cdd:cd01660  362 PGHFH--LTVGGAVALtFMAVAYWlVPHLTGRELAaKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPa 439

                        170       180       190
                 ....*....|....*....|....*....|..
gi 313504476 199 ----AGWNALSSFGSYISVVGIRRFFVVVTIT 226
Cdd:cd01660  440 agewAPYQQLMAIGGTILFVSGALFLYILFRT 471
 
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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