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Conserved domains on  [gi|1798176446|gb|QHI43066|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Pterocladiella capillacea]

Protein Classification

cytochrome c oxidase subunit 1( domain architecture ID 10108859)

cytochrome c oxidase subunit 1 is the catalytic subunit of cytochrome c oxidase, which is the component of the respiratory chain that catalyzes the reduction of oxygen to water

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-362 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: 666.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:cd01663    17 SGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:cd01663    95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:cd01663   175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSg 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:cd01663   255 KKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALG 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAV 362
Cdd:cd01663   335 FIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAV 377
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-362 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: 666.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:cd01663    17 SGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:cd01663    95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:cd01663   175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSg 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:cd01663   255 KKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALG 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAV 362
Cdd:cd01663   335 FIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAV 377
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-362 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 628.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00153   24 SGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00153  102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:MTH00153  182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESg 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:MTH00153  262 KKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALG 341

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAV 362
Cdd:MTH00153  342 FVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAV 384
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-364 3.36e-168

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: 478.64  E-value: 3.36e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   2 GILGGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVLiGGFGNWLVPIMIGSPDMAFPRLNNISFWL 81
Cdd:TIGR02891  21 FLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  82 LPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLF 161
Cdd:TIGR02891  98 YLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLF 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 162 VWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRK 241
Cdd:TIGR02891 178 VWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 242 PVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFI 321
Cdd:TIGR02891 258 PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFI 337

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 322 FLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVLP 364
Cdd:TIGR02891 338 FLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFA 380
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-364 3.91e-165

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 472.30  E-value: 3.91e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   3 ILGGCMSILIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPvLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLL 82
Cdd:COG0843    31 LIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  83 PPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFV 162
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 163 WSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKP 242
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 243 VFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIF 322
Cdd:COG0843   268 LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFII 347

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1798176446 323 LFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVLP 364
Cdd:COG0843   348 LFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFA 389
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-363 1.20e-109

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: 327.22  E-value: 1.20e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   2 GILGGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVlIGGFGNWLVPIMIGSPDMAFPRLNNISFWL 81
Cdd:pfam00115  14 FLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  82 LPPSLCLLLTSALvevGVGTGWTVYPPLssiqshsgGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMyRMPLF 161
Cdd:pfam00115  91 VVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 162 VWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRK 241
Cdd:pfam00115 159 VWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 242 PVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHF-KTPMLFTIGF 320
Cdd:pfam00115 233 PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGF 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 321 IFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVL 363
Cdd:pfam00115 313 AFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVF 355
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-362 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: 666.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:cd01663    17 SGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:cd01663    95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:cd01663   175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSg 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:cd01663   255 KKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALG 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAV 362
Cdd:cd01663   335 FIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAV 377
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-362 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 628.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00153   24 SGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00153  102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:MTH00153  182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESg 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:MTH00153  262 KKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALG 341

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAV 362
Cdd:MTH00153  342 FVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAV 384
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-362 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 580.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00167   26 AGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00167  104 LLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:MTH00167  184 FVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSg 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:MTH00167  264 KKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALG 343

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAV 362
Cdd:MTH00167  344 FIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAV 386
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-362 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 580.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGnhLLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00223   23 SGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00223  101 LLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSR 240
Cdd:MTH00223  181 FVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSS 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 241 K-PVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:MTH00223  261 KkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALG 340

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAV 362
Cdd:MTH00223  341 FIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAV 383
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-362 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 571.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00116   26 AGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00116  104 LLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:MTH00116  184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAg 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:MTH00116  264 KKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALG 343

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAV 362
Cdd:MTH00116  344 FIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAV 386
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-362 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 553.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00142   24 AGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00142  102 LLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:MTH00142  182 FVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSg 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:MTH00142  262 KKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALG 341

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAV 362
Cdd:MTH00142  342 FIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAV 384
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-362 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 523.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00182   28 AGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00182  106 LLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPL 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:MTH00182  186 FVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVa 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:MTH00182  266 KKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMG 345

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAV 362
Cdd:MTH00182  346 FVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAV 388
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-363 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 519.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00184   28 AGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFW 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00184  106 LLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPL 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:MTH00184  186 FVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAa 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:MTH00184  266 KKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIG 345

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVL 363
Cdd:MTH00184  346 FVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVF 389
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-362 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 511.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00037   26 AGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00037  104 LIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSR 240
Cdd:MTH00037  184 FVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSG 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 241 K-PVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:MTH00037  264 KqEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALG 343

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAV 362
Cdd:MTH00037  344 FVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAV 386
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-363 1.91e-178

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 505.19  E-value: 1.91e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00103   26 AGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00103  104 LLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:MTH00103  184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSg 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:MTH00103  264 KKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALG 343

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVL 363
Cdd:MTH00103  344 FIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVF 387
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-363 2.58e-177

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 502.55  E-value: 2.58e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00077   26 AGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00077  104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:MTH00077  184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSa 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:MTH00077  264 KKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALG 343

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVL 363
Cdd:MTH00077  344 FIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVF 387
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-363 3.26e-177

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 502.12  E-value: 3.26e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   2 GILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWL 81
Cdd:MTH00007   24 GLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  82 LPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLF 161
Cdd:MTH00007  102 LPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 162 VWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRK 241
Cdd:MTH00007  182 VWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGK 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 242 P-VFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGF 320
Cdd:MTH00007  262 LePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGF 341

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 321 IFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVL 363
Cdd:MTH00007  342 IFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVF 384
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-363 3.41e-177

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 502.15  E-value: 3.41e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00183   26 AGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFW 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00183  104 LLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:MTH00183  184 FVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSg 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:MTH00183  264 KKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALG 343

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVL 363
Cdd:MTH00183  344 FIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVF 387
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-362 7.63e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 490.73  E-value: 7.63e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGnhLLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00079   27 SGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSiQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00079  105 LLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:MTH00079  184 FVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTg 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIG 319
Cdd:MTH00079  264 KKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLG 343

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 320 FIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAV 362
Cdd:MTH00079  344 FIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAV 386
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-364 3.36e-168

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: 478.64  E-value: 3.36e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   2 GILGGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVLiGGFGNWLVPIMIGSPDMAFPRLNNISFWL 81
Cdd:TIGR02891  21 FLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  82 LPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLF 161
Cdd:TIGR02891  98 YLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLF 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 162 VWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRK 241
Cdd:TIGR02891 178 VWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 242 PVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFI 321
Cdd:TIGR02891 258 PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFI 337

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 322 FLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVLP 364
Cdd:TIGR02891 338 FLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFA 380
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-364 3.91e-165

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 472.30  E-value: 3.91e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   3 ILGGCMSILIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPvLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLL 82
Cdd:COG0843    31 LIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  83 PPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFV 162
Cdd:COG0843   108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 163 WSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKP 242
Cdd:COG0843   188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 243 VFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIF 322
Cdd:COG0843   268 LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFII 347

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1798176446 323 LFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVLP 364
Cdd:COG0843   348 LFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFA 389
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-364 2.43e-164

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: 467.39  E-value: 2.43e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPiMIGSPDMAFPRLNNISFW 80
Cdd:cd00919    15 ALLLGGLLALLIRLELATPGS--LFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFW 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:cd00919    92 LFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSR 240
Cdd:cd00919   172 FVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSG 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 241 KPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGF 320
Cdd:cd00919   252 KPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGF 331

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1798176446 321 IFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVLP 364
Cdd:cd00919   332 LFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFA 375
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-363 1.77e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 462.95  E-value: 1.77e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00026   27 SGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPL 160
Cdd:MTH00026  105 LLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS- 239
Cdd:MTH00026  185 FVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSy 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 240 RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEG--SIHFKTPMLFT 317
Cdd:MTH00026  265 KKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWA 344

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1798176446 318 IGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVL 363
Cdd:MTH00026  345 LGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVF 390
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 3-364 1.89e-148

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: 428.54  E-value: 1.89e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   3 ILGGCMSILIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPVLIGgFGNWLVPIMIGSPDMAFPRLNNISFWLL 82
Cdd:cd01662    23 LRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  83 PPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFV 162
Cdd:cd01662   100 LFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 163 WSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKP 242
Cdd:cd01662   180 WTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 243 VFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIF 322
Cdd:cd01662   260 LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLV 339

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1798176446 323 LFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVLP 364
Cdd:cd01662   340 TFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFP 381
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-361 4.03e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 374.40  E-value: 4.03e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   1 SGILGGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFW 80
Cdd:MTH00048   27 SGFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSLCLLLTSALVevGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPgQTMYRMPL 160
Cdd:MTH00048  105 LLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMT-NVFSRTSI 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 161 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSR 240
Cdd:MTH00048  182 ILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSN 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 241 KP-VFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPML-FTI 318
Cdd:MTH00048  262 NDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVV 341

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 319 GFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGA 361
Cdd:MTH00048  342 SFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGS 384
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-363 1.20e-109

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: 327.22  E-value: 1.20e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   2 GILGGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVlIGGFGNWLVPIMIGSPDMAFPRLNNISFWL 81
Cdd:pfam00115  14 FLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  82 LPPSLCLLLTSALvevGVGTGWTVYPPLssiqshsgGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMyRMPLF 161
Cdd:pfam00115  91 VVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 162 VWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRK 241
Cdd:pfam00115 159 VWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 242 PVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHF-KTPMLFTIGF 320
Cdd:pfam00115 233 PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGF 312

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1798176446 321 IFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVL 363
Cdd:pfam00115 313 AFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVF 355
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 9-363 2.64e-93

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 292.22  E-value: 2.64e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   9 SILIRME--LAQPGNHLLLGNHQvYNVLITAHAFLMIFFMVMPVLIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSL 86
Cdd:PRK15017   76 AIMMRSQqaLASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGV 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  87 CLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIF 166
Cdd:PRK15017  154 ILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASL 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 167 VTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGY 246
Cdd:PRK15017  234 CANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGY 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 247 IGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFLFTI 326
Cdd:PRK15017  314 TSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSV 393

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1798176446 327 GGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVL 363
Cdd:PRK15017  394 GGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVF 430
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 2-354 9.04e-10

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: 59.99  E-value: 9.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446   2 GILGGCMSILIRMelaqpGNHLLLGNHQVYNVLITAHAFLMIFfmVMPVL-IGGFGNWLVPIMIGSPDMAfPRLNNISFW 80
Cdd:cd01660    20 GGLFGLLQVLVRT-----GVFPLPSSGILYYQGLTLHGVLLAI--VFTTFfIMGFFYAIVARALLRSLFN-RRLAWAGFW 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446  81 LLPPSlcllltSALVEVGVGTG-----WTVYPPLssiQSHSGGAVDLAIFSLhisgASSILGAVNFI-STILNMRNPGQt 154
Cdd:cd01660    92 LMVIG------TVMAAVPILLGqasvlYTFYPPL---QAHPLFYIGAALVVV----GSWISGFAMFVtLWRWKKANPGK- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 155 myRMPLFVWSIFVTAFLLLLAVPVLagAITMLLtdrnfntsFFDPAGGG-----DPVLYQHLFWFFGHPEVYILILPGFG 229
Cdd:cd01660   158 --KVPLATFMVVTTMILWLVASLGV--ALEVLF--------QLLPWSLGlvdtvDVLLSRTLFWWFGHPLVYFWLLPAYI 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1798176446 230 MVSHIVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYT-VGLDVDTRAYFTAATMIIAVPTGIKIFSWIATM----- 303
Cdd:cd01660   226 AWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeiagr 305

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1798176446 304 ---------WEGSIHFKTPMLFTIGF-IFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFH 354
Cdd:cd01660   306 lrggkglfgWIRALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFH 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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