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Conserved domains on  [gi|170178058|gb|ACB10485|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Lepetodrilus pustulosus]

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 ...
 1-343 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 MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 671.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00153  45 LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGW 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00153 125 TVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAI 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00153 205 TMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFI 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00153 285 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDII 364

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00153 365 LHDTYYVVAHFHYVLSMGAVFAI 387
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-343 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 671.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00153  45 LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGW 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00153 125 TVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAI 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00153 205 TMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFI 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00153 285 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDII 364

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00153 365 LHDTYYVVAHFHYVLSMGAVFAI 387
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-343 0e+00

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: 636.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:cd01663   38 QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGW 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:cd01663  118 TVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAI 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:cd01663  198 TMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFI 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:cd01663  278 VWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIA 357

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:cd01663  358 LHDTYYVVAHFHYVLSMGAVFAI 380
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-343 1.94e-142

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: 412.39  E-value: 1.94e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058    2 LGDDQLYNVIVTAHAFVMIFFLVMPlMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGWT 81
Cdd:TIGR02891  42 FMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   82 VYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAIT 161
Cdd:TIGR02891 121 MYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALI 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  162 MLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYsAKKETFGTLGMIYAMLAIGVLGFIV 241
Cdd:TIGR02891 201 LLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTF-ARKPIFGYRAMVYATVAIGFLSFGV 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  242 WAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIML 321
Cdd:TIGR02891 280 WAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQL 359

                         330       340
                  ....*....|....*....|..
gi 170178058  322 HDTYYVVAHFHYVLSMGAVFAL 343
Cdd:TIGR02891 360 HDTYFVVAHFHYVLVGGSVFAI 381
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
6-343 8.93e-140

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 406.82  E-value: 8.93e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   6 QLYNVIVTAHAFVMIFFLVMPlMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGWTVYPP 85
Cdd:COG0843   55 ETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPP 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  86 LAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAITMLLT 165
Cdd:COG0843  134 LSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLL 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 166 DRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVmHYSAKKETFGTLGMIYAMLAIGVLGFIVWAHH 245
Cdd:COG0843  214 DRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEII-PTFSRKPLFGYKAMVLATVAIAFLSFLVWAHH 292

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 246 MFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIMLHDTY 325
Cdd:COG0843  293 MFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTY 372

                        330
                 ....*....|....*...
gi 170178058 326 YVVAHFHYVLSMGAVFAL 343
Cdd:COG0843  373 FVVAHFHYVLIGGVVFAF 390
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-343 3.71e-93

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: 284.08  E-value: 3.71e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058    1 LLGDDQLYNVIVTAHAFVMIFFLVMPlMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAvesGAGTGW 80
Cdd:pfam00115  34 NFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   81 TVYPPLAGnlahaggsVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFeRLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:pfam00115 110 TEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAAL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  161 TMLLTDRNFNtsffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYsAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:pfam00115 181 LLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKF-AGRPLFGYKLSVLAFWLIAFLGFL 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIK-YDTPMLWAMGFIFLFTMGGLTGIVLANASLDI 319
Cdd:pfam00115 254 VWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNY 333

                         330       340
                  ....*....|....*....|....
gi 170178058  320 MLHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:pfam00115 334 YVHDTYFVVAHFHYVLFGGVVFAL 357
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-343 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 671.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00153  45 LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGW 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00153 125 TVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAI 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00153 205 TMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFI 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00153 285 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDII 364

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00153 365 LHDTYYVVAHFHYVLSMGAVFAI 387
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-343 0e+00

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: 636.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:cd01663   38 QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGW 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:cd01663  118 TVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAI 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:cd01663  198 TMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFI 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:cd01663  278 VWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIA 357

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:cd01663  358 LHDTYYVVAHFHYVLSMGAVFAI 380
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-343 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 615.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00223  44 LLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGW 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00223 124 TVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAI 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00223 204 TMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFI 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00223 284 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIM 363

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00223 364 LHDTYYVVAHFHYVLSMGAVFAL 386
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-343 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 605.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00142  45 LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGW 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00142 125 TVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAI 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00142 205 TMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFI 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00142 285 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVV 364

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00142 365 LHDTYYVVAHFHYVLSMGAVFAL 387
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-343 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 603.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00167  47 LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGW 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00167 127 TVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAI 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00167 207 TMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFI 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00167 287 VWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIV 366

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00167 367 LHDTYYVVAHFHYVLSMGAVFAI 389
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-343 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 596.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00116  47 LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGW 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00116 127 TVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGI 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00116 207 TMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFI 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00116 287 VWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIV 366

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00116 367 LHDTYYVVAHFHYVLSMGAVFAI 389
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-343 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 553.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00007  44 FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGW 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00007 124 TVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAI 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00007 204 TMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFI 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00007 284 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDII 363

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00007 364 LHDTYYVVAHFHYVLSMGAVFAI 386
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-343 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 536.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00037  47 LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGW 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00037 127 TIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAI 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00037 207 TMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFL 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00037 287 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVV 366

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00037 367 LHDTYYVVAHFHYVLSMGAVFAI 389
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-343 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 530.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00183  47 LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGW 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00183 127 TVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGI 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00183 207 TMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFI 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00183 287 VWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIV 366

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00183 367 LHDTYYVVAHFHYVLSMGAVFAI 389
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-343 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 524.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00103  47 LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGW 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00103 127 TVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGI 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00103 207 TMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFI 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00103 287 VWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIV 366

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00103 367 LHDTYYVVAHFHYVLSMGAVFAI 389
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-343 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 524.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00077  47 LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGW 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00077 127 TVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGI 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00077 207 TMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFI 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00077 287 VWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIV 366

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00077 367 LHDTYYVVAHFHYVLSMGAVFAI 389
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-343 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 522.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00182  49 MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGW 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00182 129 TVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAI 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00182 209 TMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFI 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00182 289 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIV 368

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00182 369 LHDTYYVVAHFHYVLSMGAVFAI 391
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-343 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 514.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00184  49 MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGW 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00184 129 TVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAI 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00184 209 TMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFI 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00184 289 VWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVV 368

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00184 369 LHDTYYVVAHFHYVLSMGAVFAI 391
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-341 3.67e-177

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 500.75  E-value: 3.67e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00079  48 LLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSW 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAgNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00079 128 TVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAI 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00079 207 TMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCV 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:MTH00079 287 VWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDII 366

                        330       340
                 ....*....|....*....|.
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVF 341
Cdd:MTH00079 367 LHDTYYVVSHFHYVLSLGAVF 387
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-343 1.03e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 462.56  E-value: 1.03e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:MTH00026  48 MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGW 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:MTH00026 128 TVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAI 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:MTH00026 208 TMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFI 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGS--VIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLD 318
Cdd:MTH00026 288 VWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLD 367

                        330       340
                 ....*....|....*....|....*
gi 170178058 319 IMLHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:MTH00026 368 ILLHDTYYVVAHFHFVLSMGAVFAI 392
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-343 1.23e-149

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: 429.26  E-value: 1.23e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPlMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGW 80
Cdd:cd00919   36 LFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGW 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  81 TVYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:cd00919  115 TFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAAL 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 161 TMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKeTFGTLGMIYAMLAIGVLGFI 240
Cdd:cd00919  195 VMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFL 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIM 320
Cdd:cd00919  274 VWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIV 353

                        330       340
                 ....*....|....*....|...
gi 170178058 321 LHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:cd00919  354 LHDTYYVVAHFHYVLSGGVVFAI 376
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-343 1.94e-142

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: 412.39  E-value: 1.94e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058    2 LGDDQLYNVIVTAHAFVMIFFLVMPlMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGWT 81
Cdd:TIGR02891  42 FMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   82 VYPPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAIT 161
Cdd:TIGR02891 121 MYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALI 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  162 MLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYsAKKETFGTLGMIYAMLAIGVLGFIV 241
Cdd:TIGR02891 201 LLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTF-ARKPIFGYRAMVYATVAIGFLSFGV 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  242 WAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIML 321
Cdd:TIGR02891 280 WAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQL 359

                         330       340
                  ....*....|....*....|..
gi 170178058  322 HDTYYVVAHFHYVLSMGAVFAL 343
Cdd:TIGR02891 360 HDTYFVVAHFHYVLVGGSVFAI 381
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
6-343 8.93e-140

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 406.82  E-value: 8.93e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   6 QLYNVIVTAHAFVMIFFLVMPlMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGWTVYPP 85
Cdd:COG0843   55 ETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPP 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  86 LAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAITMLLT 165
Cdd:COG0843  134 LSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLL 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 166 DRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVmHYSAKKETFGTLGMIYAMLAIGVLGFIVWAHH 245
Cdd:COG0843  214 DRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEII-PTFSRKPLFGYKAMVLATVAIAFLSFLVWAHH 292

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 246 MFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIMLHDTY 325
Cdd:COG0843  293 MFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTY 372

                        330
                 ....*....|....*...
gi 170178058 326 YVVAHFHYVLSMGAVFAL 343
Cdd:COG0843  373 FVVAHFHYVLIGGVVFAF 390
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 8-339 4.28e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 384.03  E-value: 4.28e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   8 YNVIVTAHAFVMIFFLVMPLMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVesGAGTGWTVYPPLA 87
Cdd:MTH00048  55 YNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLS 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  88 GNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTaINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAITMLLTDR 167
Cdd:MTH00048 133 SSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICT-IYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDR 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 168 NFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGFIVWAHHMF 247
Cdd:MTH00048 212 NFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMF 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 248 TVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPML-WAMGFIFLFTMGGLTGIVLANASLDIMLHDTYY 326
Cdd:MTH00048 292 TVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWF 371

                        330
                 ....*....|...
gi 170178058 327 VVAHFHYVLSMGA 339
Cdd:MTH00048 372 VVAHFHYVLSLGS 384
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 6-343 5.62e-125

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: 367.68  E-value: 5.62e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   6 QLYNVIVTAHAFVMIFFLVMPLMIGgFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGWTVYPP 85
Cdd:cd01662   47 EHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPP 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  86 LAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAITMLLT 165
Cdd:cd01662  126 LSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLEL 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 166 DRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSaKKETFGTLGMIYAMLAIGVLGFIVWAHH 245
Cdd:cd01662  206 DRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFS-RKPLFGYRSMVYATVAIGFLSFGVWVHH 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 246 MFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIMLHDTY 325
Cdd:cd01662  285 MFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTY 364

                        330
                 ....*....|....*...
gi 170178058 326 YVVAHFHYVLSMGAVFAL 343
Cdd:cd01662  365 FVVAHFHYVLIGGVVFPL 382
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-343 3.71e-93

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: 284.08  E-value: 3.71e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058    1 LLGDDQLYNVIVTAHAFVMIFFLVMPlMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAvesGAGTGW 80
Cdd:pfam00115  34 NFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   81 TVYPPLAGnlahaggsVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFeRLPLFVWSIKITAVLLLLSLPVLAGAI 160
Cdd:pfam00115 110 TEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAAL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  161 TMLLTDRNFNtsffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYsAKKETFGTLGMIYAMLAIGVLGFI 240
Cdd:pfam00115 181 LLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKF-AGRPLFGYKLSVLAFWLIAFLGFL 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  241 VWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIK-YDTPMLWAMGFIFLFTMGGLTGIVLANASLDI 319
Cdd:pfam00115 254 VWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNY 333

                         330       340
                  ....*....|....*....|....
gi 170178058  320 MLHDTYYVVAHFHYVLSMGAVFAL 343
Cdd:pfam00115 334 YVHDTYFVVAHFHYVLFGGVVFAL 357
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 4-342 1.61e-86

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: 273.27  E-value: 1.61e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058    4 DDQLYNVIVTAHAFVMIFFLVMPLMIGgFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGWTVY 83
Cdd:TIGR02882  88 DAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   84 PPLAGNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAITML 163
Cdd:TIGR02882 167 APLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALM 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  164 LTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYsAKKETFGTLGMIYAMLAIGVLGFIVWA 243
Cdd:TIGR02882 247 TTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTF-AQKRLFGYKSMVWSTVGIAFLSFLVWV 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  244 HHMFTVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIMLHD 323
Cdd:TIGR02882 326 HHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHN 405

                         330
                  ....*....|....*....
gi 170178058  324 TYYVVAHFHYVLSMGAVFA 342
Cdd:TIGR02882 406 TYFLVAHFHYVLITGVVFA 424
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 8-341 1.11e-83

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 266.42  E-value: 1.11e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   8 YNVIVTAHAFVMIFFLVMPLMIGgFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLSLLLTSAAVESGAGTGWTVYPPLA 87
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  88 GNLAHAGGSVDLTIFSLHLAGISSILSSVNFITTAINMRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGAITMLLTDR 167
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 168 NFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHVVMHYSaKKETFGTLGMIYAMLAIGVLGFIVWAHHMF 247
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFF 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 248 TVGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSVIKYDTPMLWAMGFIFLFTMGGLTGIVLANASLDIMLHDTYYV 327
Cdd:PRK15017 337 TMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFL 416

                        330
                 ....*....|....
gi 170178058 328 VAHFHYVLSMGAVF 341
Cdd:PRK15017 417 IAHFHNVIIGGVVF 430
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-343 1.81e-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: 55.76  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058   1 LLGDDQLYNVIVTAHAFVMIFFLVMpLMIGGFGNWLVPLMLGAPDMAfPRLNNMSFWLLPPSLSLllTSAAVESG-AGTG 79
Cdd:cd01660   37 LPSSGILYYQGLTLHGVLLAIVFTT-FFIMGFFYAIVARALLRSLFN-RRLAWAGFWLMVIGTVM--AAVPILLGqASVL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058  80 WTVYPPLAGNLAHAGGSVDLTIFSLhlagissILSSVNFITTAInmRWQGMEFERLPLFVWSIKITAVLLLLSLPVLAGA 159
Cdd:cd01660  113 YTFYPPLQAHPLFYIGAALVVVGSW-------ISGFAMFVTLWR--WKKANPGKKVPLATFMVVTTMILWLVASLGVALE 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 160 ITMLLTDRNFNTsffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFgMISHVVMHYSAKKETFGTLGMIYAMLAIGVLGF 239
Cdd:cd01660  184 VLFQLLPWSLGL-----VDTVDVLLSRTLFWWFGHPLVYFWLLPAY-IAWYTILPKIAGGKLFSDPLARLAFILFLLFST 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170178058 240 IVWAHHMFT-VGMDVDTRAYFTAATMVIAVPTGIKIFSWLATIHGSV--------------IKYDTPMLWAMGF-IFLFT 303
Cdd:cd01660  258 PVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLEIAGrlrggkglfgwiraLPWGDPMFLALFLaMLMFI 337

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 170178058 304 MGGLTGIVLANASLDIMLHDTYYVVAHFHyvLSMGAVFAL 343
Cdd:cd01660  338 PGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVAL 375
 
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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