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Conserved domains on  [gi|7594838|dbj|BAA94676|]
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cytochrome c oxidase subunit 1, partial (mitochondrion) [Semipallium dianae]

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 ...
 1-301 0e+00

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


The actual alignment was detected with superfamily member MTH00223:

Pssm-ID: 469701  Cd Length: 512  Bit Score: 527.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00223  79 LVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGA 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00223 159 INFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00223 239 EVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 318

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00223 319 SWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLS 379
 
Name Accession Description Interval E-value
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-301 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 527.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00223  79 LVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGA 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00223 159 INFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00223 239 EVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 318

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00223 319 SWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLS 379
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-301 1.68e-175

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: 493.92  E-value: 1.68e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:cd01663  73 LVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGA 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:cd01663 153 INFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 232

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838  161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:cd01663 233 EVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVF 312

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838  241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:cd01663 313 SWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLS 373
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-300 9.58e-124

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: 363.08  E-value: 9.58e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838      1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:TIGR02891  75 LLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGA 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:TIGR02891 155 VNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHP 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    161 EVYVLILPGFGLVSHLLVFYTKKiRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:TIGR02891 235 EVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVF 313

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVL 300
Cdd:TIGR02891 314 NWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVL 373
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-300 8.28e-117

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 346.34  E-value: 8.28e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:COG0843  84 LVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGG 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:COG0843 164 VNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838  161 EVYVLILPGFGLVSHLLVFYTKKiRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:COG0843 244 EVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838  241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVL 300
Cdd:COG0843 323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVL 382
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-300 1.18e-80

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: 250.57  E-value: 1.18e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838      1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPfieQGSGTGWTMYPPLSSTPYqsdictdmVILGLHLAGISSSAAS 80
Cdd:pfam00115  68 LVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVGVDL--------WYIGLLLAGVSSLLGA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     81 INYLATFLNLRGNSYKAgYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNcsffdpSGGGDPVLFQHLFWFFGHP 160
Cdd:pfam00115 137 INFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHP 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    161 EVYVLILPGFGLVSHLLVFYTKKiRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:pfam00115 210 EVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVF 288

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838    241 SWIATIFGSYMSF-EAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVL 300
Cdd:pfam00115 289 NWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVL 349
 
Name Accession Description Interval E-value
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-301 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 527.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00223  79 LVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGA 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00223 159 INFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00223 239 EVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 318

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00223 319 SWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLS 379
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-301 1.68e-175

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: 493.92  E-value: 1.68e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:cd01663  73 LVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGA 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:cd01663 153 INFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 232

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838  161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:cd01663 233 EVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVF 312

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838  241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:cd01663 313 SWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLS 373
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-301 3.31e-164

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 466.27  E-value: 3.31e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00153  80 LVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGA 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00153 160 INFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00153 240 EVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIF 319

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00153 320 SWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLS 380
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-301 3.85e-150

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 430.64  E-value: 3.85e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00167  82 LVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGS 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00167 162 INFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00167 242 EVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 321

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00167 322 SWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-301 4.89e-146

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 420.27  E-value: 4.89e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00116  82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00116 162 INFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00116 242 EVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVF 321

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00116 322 SWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-301 6.84e-145

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 417.20  E-value: 6.84e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00142  80 LVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGA 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00142 160 INFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00142 240 EVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVF 319

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00142 320 SWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLS 380
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-301 2.32e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 402.91  E-value: 2.32e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPyQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00079  83 MLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLG-HPGSSVDLAIFSLHCAGISSILGG 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00079 162 INFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00079 242 EVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVF 321

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00079 322 SWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLS 382
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-301 4.41e-134

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 389.65  E-value: 4.41e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00007  79 LVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGA 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00007 159 INFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00007 239 EVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 318

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00007 319 SWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLS 379
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-301 2.03e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 383.41  E-value: 2.03e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00184  84 FVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGA 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00184 164 MNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00184 244 EVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIF 323

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00184 324 SWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLS 384
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-301 6.11e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 381.87  E-value: 6.11e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00037  82 LIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILAS 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00037 162 INFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHP 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00037 242 EVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 321

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00037 322 SWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLS 382
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-301 1.37e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 381.48  E-value: 1.37e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00182  84 LVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGA 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00182 164 INFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHP 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00182 244 EVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 323

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00182 324 SWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLS 384
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-301 5.07e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 374.64  E-value: 5.07e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00183  82 LIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00183 162 INFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00183 242 EVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00183 322 SWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-301 1.05e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 373.51  E-value: 1.05e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00077  82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00077 162 INFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00077 242 EVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVF 321

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00077 322 SWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-301 4.62e-126

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 369.21  E-value: 4.62e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00103  82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00103 162 INFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00103 242 EVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838   241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00103 322 SWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-301 5.78e-124

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: 362.23  E-value: 5.78e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:cd00919  70 LLPPLIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGA 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:cd00919 150 INFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHP 229

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838  161 EVYVLILPGFGLVSHLLVFYTKKiRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:cd00919 230 EVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVF 308

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838  241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:cd00919 309 NWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLS 369
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-300 9.58e-124

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: 363.08  E-value: 9.58e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838      1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:TIGR02891  75 LLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGA 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:TIGR02891 155 VNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHP 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    161 EVYVLILPGFGLVSHLLVFYTKKiRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:TIGR02891 235 EVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVF 313

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVL 300
Cdd:TIGR02891 314 NWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVL 373
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-300 8.28e-117

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 346.34  E-value: 8.28e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:COG0843  84 LVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGG 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:COG0843 164 VNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838  161 EVYVLILPGFGLVSHLLVFYTKKiRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:COG0843 244 EVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838  241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVL 300
Cdd:COG0843 323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVL 382
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-301 9.28e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 341.22  E-value: 9.28e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00026  83 FVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGA 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00026 163 MNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00026 243 EVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIF 322

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7594838   241 SWIATIFGS--YMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00026 323 SWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLS 385
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-301 1.00e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 327.40  E-value: 1.00e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIeqGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:MTH00048  83 LLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGS 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    81 INYLATFLNLRGNSYkAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:MTH00048 161 INFICTIYSAFMTNV-FSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHP 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   161 EVYVLILPGFGLVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:MTH00048 240 EVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVF 319

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7594838   241 SWIATIFGSYMSFEAPML-WVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVLS 301
Cdd:MTH00048 320 SWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLS 381
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-300 7.67e-109

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: 324.92  E-value: 7.67e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:cd01662  76 LVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGA 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:cd01662 156 INFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHP 235

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838  161 EVYVLILPGFGLVSHLLVFYTKKiRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:cd01662 236 EVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIF 314

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838  241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVL 300
Cdd:cd01662 315 NWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVL 374
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-300 1.18e-80

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: 250.57  E-value: 1.18e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838      1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPfieQGSGTGWTMYPPLSSTPYqsdictdmVILGLHLAGISSSAAS 80
Cdd:pfam00115  68 LVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVGVDL--------WYIGLLLAGVSSLLGA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     81 INYLATFLNLRGNSYKAgYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNcsffdpSGGGDPVLFQHLFWFFGHP 160
Cdd:pfam00115 137 INFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHP 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    161 EVYVLILPGFGLVSHLLVFYTKKiRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:pfam00115 210 EVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVF 288

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7594838    241 SWIATIFGSYMSF-EAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVL 300
Cdd:pfam00115 289 NWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVL 349
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-300 6.79e-72

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 234.06  E-value: 6.79e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     2 LPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAASI 81
Cdd:PRK15017 127 VPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    82 NYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHPE 161
Cdd:PRK15017 207 NFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPE 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   162 VYVLILPGFGLVSHLLVFYTKKiRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVFS 241
Cdd:PRK15017 287 VYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFN 365

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 7594838   242 WIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVL 300
Cdd:PRK15017 366 WLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVI 424
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-300 6.50e-68

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 222.81  E-value: 6.50e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838      1 LLPLLLGGIDMSFPRVNTLSFWVVPVALYMVVVSPFIEQGSGTGWTMYPPLSSTPYQSDICTDMVILGLHLAGISSSAAS 80
Cdd:TIGR02882 119 VVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838     81 INYLATFLNLRGNSYKAGYCPPFVWALSVTSFLLLVSLPVLAGGLTMLILDRHFNCSFFDPSGGGDPVLFQHLFWFFGHP 160
Cdd:TIGR02882 199 INFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHP 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    161 EVYVLILPGFGLVSHLLVFYTKKiRVFGSVAMMYAMISIGVLGFIVWGHHMFTVGLDVDTRFYFTAVTMLIAVPTGVKVF 240
Cdd:TIGR02882 279 EVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIF 357

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838    241 SWIATIFGSYMSFEAPMLWVIGFIFKFTVGGVTGIILSNASLDVALHDTYYVVAHFHYVL 300
Cdd:TIGR02882 358 NWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVL 417
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 14-297 3.26e-09

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: 57.30  E-value: 3.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   14 PRVNTLSFWVVPVALYMVVVSPFIEQGSgTGWTMYPPLSSTPyqsdictdMVILGLHLAGISSSAASINYLATFLNLRgn 93
Cdd:cd01660  83 RRLAWAGFWLMVIGTVMAAVPILLGQAS-VLYTFYPPLQAHP--------LFYIGAALVVVGSWISGFAMFVTLWRWK-- 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838   94 SYKAGYCPPFVWALSVTSFLL--LVSLPVLAGGLTMLIldrhfNCSFFDpSGGGDPVLFQHLFWFFGHPEVYVLILPGFg 171
Cdd:cd01660 152 KANPGKKVPLATFMVVTTMILwlVASLGVALEVLFQLL-----PWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAY- 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7594838  172 LVSHLLVFYTKKIRVFGSVAMMYAMISIGVLGFIVWGHHMFT-VGLDVDTRFYFTAVTMLIAVPT--------------- 235
Cdd:cd01660 225 IAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSlltaftvfasleiag 304

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7594838  236 ----GVKVFSWIATIFGSYMSFEAPMLWVIGFIFkftvGGVTGIILSNASLDVALHDTYYVVAHFH 297
Cdd:cd01660 305 rlrgGKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGHFH 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.
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