NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1337388450|gb|AUW40184|]
View 

cytochrome oxidase subunit I, partial (mitochondrion) [Ciona edwardsi]

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 ...
 1-245 5.94e-171

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 MTH00167:

Pssm-ID: 469701  Cd Length: 512  Bit Score: 481.10  E-value: 5.94e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:MTH00167  135 NLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRN 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:MTH00167  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFT 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00167  295 VGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00167  375 AHFHY 379
 
Name Accession Description Interval E-value
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-245 5.94e-171

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 481.10  E-value: 5.94e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:MTH00167  135 NLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRN 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:MTH00167  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFT 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00167  295 VGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00167  375 AHFHY 379
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-245 1.36e-162

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: 458.87  E-value: 1.36e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:cd01663   126 ILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRN 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:cd01663   206 FNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFT 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:cd01663   286 VGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVV 365


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:cd01663   366 AHFHY 370
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-245 1.70e-110

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 327.85  E-value: 1.70e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   3 GHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRNFN 82
Cdd:COG0843   139 ASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLG 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  83 TTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKdNIFGYYGMVWAMGGIGFLGFLVWAHHMFSVG 162
Cdd:COG0843   219 THFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPG 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 163 MDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVVAH 242
Cdd:COG0843   298 ISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAH 377


                  ...
gi 1337388450 243 FHY 245
Cdd:COG0843   378 FHY 380
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 3-245 1.04e-108

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: 322.25  E-value: 1.04e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   3 GHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRNFN 82
Cdd:TIGR02891 130 GSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFG 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  83 TTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKdNIFGYYGMVWAMGGIGFLGFLVWAHHMFSVG 162
Cdd:TIGR02891 210 THFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTG 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 163 MDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVVAH 242
Cdd:TIGR02891 289 MPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAH 368


                  ...
gi 1337388450 243 FHY 245
Cdd:TIGR02891 369 FHY 371
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 7-245 2.08e-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: 2.08e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   7 TGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMsNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRNFNTtff 86
Cdd:pfam00115 116 VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA--- 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  87 dpnGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKdNIFGYYGMVWAMGGIGFLGFLVWAHHMFSVGMDVD 166
Cdd:pfam00115 192 ---GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPW 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 167 SRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWG-LPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVVAHFHY 245
Cdd:pfam00115 268 LQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHY 347
 
Name Accession Description Interval E-value
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-245 5.94e-171

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 481.10  E-value: 5.94e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:MTH00167  135 NLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRN 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:MTH00167  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFT 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00167  295 VGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00167  375 AHFHY 379
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-245 1.36e-162

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: 458.87  E-value: 1.36e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:cd01663   126 ILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRN 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:cd01663   206 FNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFT 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:cd01663   286 VGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVV 365


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:cd01663   366 AHFHY 370
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-245 2.82e-157

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 446.24  E-value: 2.82e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:MTH00153  133 NIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRN 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:MTH00153  213 LNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFT 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00153  293 VGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVV 372


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00153  373 AHFHY 377
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-245 2.32e-146

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 418.73  E-value: 2.32e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:MTH00116  135 NLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRN 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:MTH00116  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFT 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00116  295 VGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVV 374


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00116  375 AHFHY 379
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-245 2.99e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 405.52  E-value: 2.99e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:MTH00223  132 NLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRN 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:MTH00223  212 FNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFT 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00223  292 VGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVV 371


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00223  372 AHFHY 376
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-245 1.52e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 386.00  E-value: 1.52e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:MTH00142  133 NLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRN 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:MTH00142  213 FNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFT 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00142  293 VGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVV 372


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00142  373 AHFHY 377
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-245 1.80e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 370.79  E-value: 1.80e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:MTH00183  135 NLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRN 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:MTH00183  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFT 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00183  295 VGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00183  375 AHFHY 379
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-245 3.33e-126

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 367.29  E-value: 3.33e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:MTH00103  135 NLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRN 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:MTH00103  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFT 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00103  295 VGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00103  375 AHFHY 379
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-245 7.22e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 361.45  E-value: 7.22e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:MTH00037  135 NIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRN 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:MTH00037  215 INTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFT 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00037  295 VGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVV 374


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00037  375 AHFHY 379
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-245 2.65e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 357.33  E-value: 2.65e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:MTH00077  135 NLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRN 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:MTH00077  215 LNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFT 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00077  295 VDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00077  375 AHFHY 379
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-245 5.79e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 356.30  E-value: 5.79e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:MTH00079  135 TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRN 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:MTH00079  215 LNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYT 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00079  295 VGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVV 374


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00079  375 SHFHY 379
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 3-245 3.58e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 352.21  E-value: 3.58e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   3 GHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRNFN 82
Cdd:MTH00184  139 AHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFN 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  83 TTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFSVG 162
Cdd:MTH00184  219 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVG 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 163 MDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVVAH 242
Cdd:MTH00184  299 MDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAH 378


                  ...
gi 1337388450 243 FHY 245
Cdd:MTH00184  379 FHY 381
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 4-245 1.17e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 351.05  E-value: 1.17e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   4 HSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRNFNT 83
Cdd:MTH00182  140 HSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNT 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  84 TFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFSVGM 163
Cdd:MTH00182  220 TFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGM 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 164 DVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVVAHF 243
Cdd:MTH00182  300 DVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHF 379


                  ..
gi 1337388450 244 HY 245
Cdd:MTH00182  380 HY 381
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-245 7.83e-119

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 348.43  E-value: 7.83e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:MTH00007  132 NLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRN 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:MTH00007  212 LNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFT 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00007  292 VGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVV 371


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00007  372 AHFHY 376
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-245 1.72e-111

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: 327.95  E-value: 1.72e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   1 NIGHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRN 80
Cdd:cd00919   123 LSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRN 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  81 FNTTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKdNIFGYYGMVWAMGGIGFLGFLVWAHHMFS 160
Cdd:cd00919   203 FGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFT 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 161 VGMDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:cd00919   282 VGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVV 361


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:cd00919   362 AHFHY 366
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-245 1.70e-110

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 327.85  E-value: 1.70e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   3 GHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRNFN 82
Cdd:COG0843   139 ASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLG 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  83 TTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKdNIFGYYGMVWAMGGIGFLGFLVWAHHMFSVG 162
Cdd:COG0843   219 THFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPG 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 163 MDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVVAH 242
Cdd:COG0843   298 ISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAH 377


                  ...
gi 1337388450 243 FHY 245
Cdd:COG0843   378 FHY 380
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 3-245 1.04e-108

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: 322.25  E-value: 1.04e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   3 GHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRNFN 82
Cdd:TIGR02891 130 GSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFG 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  83 TTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKdNIFGYYGMVWAMGGIGFLGFLVWAHHMFSVG 162
Cdd:TIGR02891 210 THFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTG 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 163 MDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVVAH 242
Cdd:TIGR02891 289 MPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAH 368


                  ...
gi 1337388450 243 FHY 245
Cdd:TIGR02891 369 FHY 371
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 5-245 5.10e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 310.46  E-value: 5.10e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   5 SNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSmSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRNFNTT 84
Cdd:MTH00048  138 SSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSA 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  85 FFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFSVGMD 164
Cdd:MTH00048  217 FFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLD 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 165 VDSRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLL-WAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVVAHF 243
Cdd:MTH00048  297 VKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHF 376


                  ..
gi 1337388450 244 HY 245
Cdd:MTH00048  377 HY 378
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 3-245 1.88e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 310.02  E-value: 1.88e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   3 GHSNTGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRNFN 82
Cdd:MTH00026  138 AHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFN 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  83 TTFFDPNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFSVG 162
Cdd:MTH00026  218 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVG 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 163 MDVDSRAYFTSATMIIAVPTGIKVFSWVSTLLGA--KIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVV 240
Cdd:MTH00026  298 MDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVV 377


                  ....*
gi 1337388450 241 AHFHY 245
Cdd:MTH00026  378 AHFHF 382
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 8-245 3.44e-95

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: 287.55  E-value: 3.44e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   8 GVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRNFNTTFFD 87
Cdd:cd01662   136 GVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFT 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  88 PNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKdNIFGYYGMVWAMGGIGFLGFLVWAHHMFSVGMDVDS 167
Cdd:cd01662   216 NALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALV 294

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1337388450 168 RAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVVAHFHY 245
Cdd:cd01662   295 NAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHY 372
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 7-245 2.08e-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: 2.08e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   7 TGVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMsNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRNFNTtff 86
Cdd:pfam00115 116 VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA--- 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  87 dpnGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSGKdNIFGYYGMVWAMGGIGFLGFLVWAHHMFSVGMDVD 166
Cdd:pfam00115 192 ---GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPW 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 167 SRAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWG-LPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVVAHFHY 245
Cdd:pfam00115 268 LQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHY 347
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 8-244 1.20e-60

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 201.70  E-value: 1.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450   8 GVDMAIFSLHLAGVSSILGSVNFLVTLFNMKNKGKSMSNLSLFCWSLIVTTILLVLSLPVLAAAITMLLFDRNFNTTFFD 87
Cdd:PRK15017  186 GVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFT 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  88 PNGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVIIFYSgKDNIFGYYGMVWAMGGIGFLGFLVWAHHMFSVGMDVDS 167
Cdd:PRK15017  266 NDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANV 344

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1337388450 168 RAYFTSATMIIAVPTGIKVFSWVSTLLGAKIHWGLPLLWAYGFLFLFTIGGLTGIVLANCSLDLVLHDTYYVVAHFH 244
Cdd:PRK15017  345 NAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFH 421
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 93-244 7.79e-08

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: 52.29  E-value: 7.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450  93 DPILYQHLFWFFGHPEVYILILPGfgmishVIIFYSGKDNIFGYYGMVWAMGGIGFLGFLVWA-----HHMFS-VGMDVD 166
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPA------YIAWYTILPKIAGGKLFSDPLARLAFILFLLFStpvgfHHQFAdPGIGPG 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337388450 167 SRAYFTSATMIIAVPTGIKVFSWVSTLLGA--------------KIHWGLPLLWAYGF-LFLFTIGGLTGIVLANCSLDL 231
Cdd:cd01660   274 WKFIHMVLTFMVALPSLLTAFTVFASLEIAgrlrggkglfgwirALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNY 353

                         170
                  ....*....|...
gi 1337388450 232 VLHDTYYVVAHFH 244
Cdd:cd01660   354 VVHNTAWVPGHFH 366
 
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