NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1546647470|gb|AZR68400|]
View 

cytochrome oxidase subunit I, partial (mitochondrion) [Baylisascaris columnaris]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-385 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 MTH00079:

Pssm-ID: 469701  Cd Length: 508  Bit Score: 662.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLSTMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVF 80
Cdd:MTH00079  110 LFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVF 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  81 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFG 160
Cdd:MTH00079  190 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFG 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 161 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFT 240
Cdd:MTH00079  270 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFT 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 241 IGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLH 320
Cdd:MTH00079  350 IGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLH 429

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1546647470 321 FAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDYCVNSGPEY 385
Cdd:MTH00079  430 FAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEY 494
 
Name Accession Description Interval E-value
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-385 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 662.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLSTMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVF 80
Cdd:MTH00079  110 LFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVF 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  81 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFG 160
Cdd:MTH00079  190 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFG 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 161 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFT 240
Cdd:MTH00079  270 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFT 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 241 IGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLH 320
Cdd:MTH00079  350 IGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLH 429

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1546647470 321 FAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDYCVNSGPEY 385
Cdd:MTH00079  430 FAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEY 494
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-377 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: 618.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:cd01663   100 LLLLLLSALVEGGAGTGWTVYPPLSSiLAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSV 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:cd01663   180 LITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVF 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:cd01663   260 GYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLF 339

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:cd01663   340 TIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQ 419

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDY 377
Cdd:cd01663   420 HFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNV 477
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 3-367 5.26e-136

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: 397.75  E-value: 5.26e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   3 LILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFV 81
Cdd:TIGR02891 104 LLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILV 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  82 TVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISqSSLYLTGKKEVFGS 161
Cdd:TIGR02891 184 TSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIIS-EILPTFARKPIFGY 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 162 LGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTI 241
Cdd:TIGR02891 263 RAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVI 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 242 GGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHF 321
Cdd:TIGR02891 343 GGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHL 422

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1546647470 322 AGIHGYPRKYLDYPD--IYSVWNIVASYGSMVSVFALFLFIYVLLESF 367
Cdd:TIGR02891 423 LGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSL 470
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
9-368 7.15e-131

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 385.63  E-value: 7.15e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   9 FVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFVTVFLLV 87
Cdd:COG0843   119 FVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILIL 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  88 LSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSsLYLTGKKEVFGSLGMVYA 167
Cdd:COG0843   199 LAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI-IPTFSRKPLFGYKAMVLA 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 168 ILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTIGGLTGV 247
Cdd:COG0843   278 TVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGV 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 248 MLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGY 327
Cdd:COG0843   358 MLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGM 437

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1546647470 328 PRKYLDYP--DIYSVWNIVASYGSMVSVFALFLFIYVLLESFL 368
Cdd:COG0843   438 PRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLR 480
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 12-351 4.38e-87

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: 270.21  E-value: 4.38e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  12 MGCGTSWTVYPPLStmghpgsSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLeHMSLFVWTVFVTVFLLVLSLP 91
Cdd:pfam00115 103 GGATTGWTEYPPLV-------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  92 VLAGAITMLLTDRNLNTSffdpstGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKeVFGSLGMVYAILSI 171
Cdd:pfam00115 175 VLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLI 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 172 GLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVF-QPLLLWVTGFIFLFTIGGLTGVMLS 250
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLA 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 251 NSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGYPRK 330
Cdd:pfam00115 328 LPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRR 407

                         330       340
                  ....*....|....*....|....*
gi 1546647470 331 Y----LDYPDIYSVWNIVASYGSMV 351
Cdd:pfam00115 408 YappfIETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-385 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 662.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLSTMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVF 80
Cdd:MTH00079  110 LFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVF 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  81 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFG 160
Cdd:MTH00079  190 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFG 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 161 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFT 240
Cdd:MTH00079  270 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFT 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 241 IGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLH 320
Cdd:MTH00079  350 IGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLH 429

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1546647470 321 FAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDYCVNSGPEY 385
Cdd:MTH00079  430 FAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEY 494
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-377 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: 618.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:cd01663   100 LLLLLLSALVEGGAGTGWTVYPPLSSiLAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSV 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:cd01663   180 LITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVF 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:cd01663   260 GYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLF 339

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:cd01663   340 TIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQ 419

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDY 377
Cdd:cd01663   420 HFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNV 477
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-385 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 598.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00153  107 LTLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSV 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00153  187 LITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETF 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00153  267 GTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLF 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00153  347 TIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQ 426

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDYCVNSGPEY 385
Cdd:MTH00153  427 HFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEW 492
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-385 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 544.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00223  106 LYLLLSSSAVESGVGTGWTVYPPLSsNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSV 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00223  186 KVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVF 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00223  266 GTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLF 345

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00223  346 TVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQ 425

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDYCVNSGPEY 385
Cdd:MTH00223  426 HFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEW 491
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-385 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 542.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00167  109 LLLLLASSGVEAGAGTGWTVYPPLAgNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSI 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00167  189 LVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPF 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00167  269 GYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLF 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00167  349 TVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQ 428

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDYCVNSGPEY 385
Cdd:MTH00167  429 HFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEW 494
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-374 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 520.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00116  109 FLLLLASSTVEAGAGTGWTVYPPLAgNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSV 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00116  189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPF 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00116  269 GYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLF 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00116  349 TIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQ 428

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFL 374
Cdd:MTH00116  429 HFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVL 483
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-385 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 514.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00142  107 LLLLLSSAAVESGAGTGWTVYPPLSSnLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSV 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00142  187 KITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVF 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00142  267 GTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLF 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00142  347 TVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQ 426

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDYCVNSGPEY 385
Cdd:MTH00142  427 HFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEW 492
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-371 2.46e-166

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 475.16  E-value: 2.46e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPL-STMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00007  106 LILLVSSAAVEKGVGTGWTVYPPLaSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAV 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00007  186 VITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPF 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00007  266 GTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLF 345

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00007  346 TTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQ 425

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHR 371
Cdd:MTH00007  426 HFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQR 477
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 3-371 6.22e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 461.99  E-value: 6.22e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   3 LILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFV 81
Cdd:MTH00037  111 LLLASAGVESGAGTGWTIYPPLSSnIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFI 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  82 TVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFGS 161
Cdd:MTH00037  191 TAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGY 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 162 LGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTI 241
Cdd:MTH00037  271 LGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTI 350

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 242 GGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHF 321
Cdd:MTH00037  351 GGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHF 430

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1546647470 322 AGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHR 371
Cdd:MTH00037  431 LGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQR 480
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-371 2.34e-160

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 460.12  E-value: 2.34e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   2 FLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVF 80
Cdd:MTH00103  110 LLLLASSMVEAGAGTGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVL 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  81 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFG 160
Cdd:MTH00103  190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFG 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 161 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFT 240
Cdd:MTH00103  270 YMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFT 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 241 IGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLH 320
Cdd:MTH00103  350 VGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQH 429

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1546647470 321 FAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHR 371
Cdd:MTH00103  430 FLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKR 480
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-371 7.20e-159

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 456.69  E-value: 7.20e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00183  109 FLLLLASSGVEAGAGTGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAV 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00183  189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPF 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00183  269 GYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLF 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00183  349 TVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQ 428

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHR 371
Cdd:MTH00183  429 HFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKR 480
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-374 1.31e-158

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 456.21  E-value: 1.31e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00182  111 LILLLGSAFVEQGAGTGWTVYPPLSSIqAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSI 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00182  191 LITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIF 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00182  271 GYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLF 350

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00182  351 TLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQ 430

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFL 374
Cdd:MTH00182  431 HFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFI 485
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-374 2.46e-158

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 455.17  E-value: 2.46e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00077  109 FLLLLASSGVEAGAGTGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSV 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00077  189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPF 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00077  269 GYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLF 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00077  349 TVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQ 428

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFL 374
Cdd:MTH00077  429 HFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVL 483
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 3-373 1.49e-156

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 450.82  E-value: 1.49e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   3 LILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFV 81
Cdd:MTH00184  113 LLLGSAFVEQGAGTGWTVYPPLSSiQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILV 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  82 TVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFGS 161
Cdd:MTH00184  193 TTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGY 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 162 LGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTI 241
Cdd:MTH00184  273 LGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTM 352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 242 GGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHF 321
Cdd:MTH00184  353 GGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHF 432

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1546647470 322 AGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLF 373
Cdd:MTH00184  433 LGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKF 484
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-367 8.38e-146

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: 421.17  E-value: 8.38e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLSTMG-HPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:cd00919    97 LLLLLSSVLVGGGAGTGWTFYPPLSTLSySSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSV 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKeVF 159
Cdd:cd00919   177 LVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LF 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:cd00919   256 GYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLF 335

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:cd00919   336 TIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPM 415

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESF 367
Cdd:cd00919   416 HFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-367 2.82e-140

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 409.79  E-value: 2.82e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   1 MFLILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00026  110 LFLLLGSSLVEQGAGTGWTVYPPLASIqAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSV 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00026  190 FITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIF 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATL--FGMKMVFQPLLLWVTGFIF 237
Cdd:MTH00026  270 GYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVsgSGRNLIFTTPMAWALGFIF 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 238 LFTIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFF 317
Cdd:MTH00026  350 LFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFF 429

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1546647470 318 PLHFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESF 367
Cdd:MTH00026  430 PQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAY 479
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 3-367 5.26e-136

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: 397.75  E-value: 5.26e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   3 LILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFV 81
Cdd:TIGR02891 104 LLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILV 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  82 TVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISqSSLYLTGKKEVFGS 161
Cdd:TIGR02891 184 TSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIIS-EILPTFARKPIFGY 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 162 LGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTI 241
Cdd:TIGR02891 263 RAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVI 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 242 GGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHF 321
Cdd:TIGR02891 343 GGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHL 422

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1546647470 322 AGIHGYPRKYLDYPD--IYSVWNIVASYGSMVSVFALFLFIYVLLESF 367
Cdd:TIGR02891 423 LGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSL 470
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
9-368 7.15e-131

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 385.63  E-value: 7.15e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   9 FVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFVTVFLLV 87
Cdd:COG0843   119 FVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILIL 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  88 LSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSsLYLTGKKEVFGSLGMVYA 167
Cdd:COG0843   199 LAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI-IPTFSRKPLFGYKAMVLA 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 168 ILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTIGGLTGV 247
Cdd:COG0843   278 TVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGV 357

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 248 MLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGY 327
Cdd:COG0843   358 MLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGM 437

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1546647470 328 PRKYLDYP--DIYSVWNIVASYGSMVSVFALFLFIYVLLESFL 368
Cdd:COG0843   438 PRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLR 480
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-367 3.41e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 367.85  E-value: 3.41e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   2 FLILDACFvdmGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHmSLFVWTVF 80
Cdd:MTH00048  112 FLLLSMCL---GAGVGWTFYPPLSSsLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRT-SIILWSYL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  81 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFG 160
Cdd:MTH00048  188 FTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFG 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 161 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKM-VFQPLLLWVTGFIFLF 239
Cdd:MTH00048  268 YYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVrKSDPVVWWVVSFIVLF 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00048  348 TIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPM 427

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESF 367
Cdd:MTH00048  428 HYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESL 475
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 9-367 5.21e-119

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: 354.19  E-value: 5.21e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470   9 FVDMGCGTSWTVYPPLSTMGH-PGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFVTVFLLV 87
Cdd:cd01662   111 LIGGFPDAGWFAYPPLSGLEYsPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILIL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  88 LSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISqSSLYLTGKKEVFGSLGMVYA 167
Cdd:cd01662   191 FAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFS-EIVPTFSRKPLFGYRSMVYA 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 168 ILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTIGGLTGV 247
Cdd:cd01662   270 TVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGV 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 248 MLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGY 327
Cdd:cd01662   350 MLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGM 429

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1546647470 328 PRKYLDYP--DIYSVWNIVASYGSMVSVFALFLFIYVLLESF 367
Cdd:cd01662   430 PRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSI 471
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 12-351 4.38e-87

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: 270.21  E-value: 4.38e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  12 MGCGTSWTVYPPLStmghpgsSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLeHMSLFVWTVFVTVFLLVLSLP 91
Cdd:pfam00115 103 GGATTGWTEYPPLV-------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  92 VLAGAITMLLTDRNLNTSffdpstGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKeVFGSLGMVYAILSI 171
Cdd:pfam00115 175 VLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLI 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 172 GLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVF-QPLLLWVTGFIFLFTIGGLTGVMLS 250
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLA 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 251 NSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGYPRK 330
Cdd:pfam00115 328 LPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRR 407

                         330       340
                  ....*....|....*....|....*
gi 1546647470 331 Y----LDYPDIYSVWNIVASYGSMV 351
Cdd:pfam00115 408 YappfIETVPAFQPLNWIRTIGGVL 432
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 16-330 6.99e-73

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 239.45  E-value: 6.99e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  16 TSWTVYPPLSTMGH-PGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLA 94
Cdd:PRK15017  168 TGWLAYPPLSGIEYsPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILT 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470  95 GAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTgKKEVFGSLGMVYAILSIGLI 174
Cdd:PRK15017  248 VTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVL 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 175 GCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTIGGLTGVMLSNSSL 254
Cdd:PRK15017  327 SFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGA 406

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1546647470 255 DIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGYPRK 330
Cdd:PRK15017  407 DFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRR 482
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 118-368 2.89e-13

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: 70.78  E-value: 2.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 118 NPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFGSLGMVYAILSIgLIGCVVWAHHMYT-VGMDLDSRAYF 196
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFAdPGIGPGWKFIH 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 197 TAATMVIAVPT-------------------GVKVFSWLATLFGMKMVFQPLLLwvtGFIFlFTIGGLTGVMLSNSSLDII 257
Cdd:cd01660   279 MVLTFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALFL---AMLM-FIPGGAGGIINASYQLNYV 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 258 LHDTYYVVSHFHYVLSlGAVFGIFTGVTLW-WSFITG-FVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGYPRK--YLD 333
Cdd:cd01660   355 VHNTAWVPGHFHLTVG-GAVALTFMAVAYWlVPHLTGrELAAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQ 433

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1546647470 334 YPDIY-----SVWNIVASYGSMVSVFALFLFIYVLLESFL 368
Cdd:cd01660   434 YGGLPaagewAPYQQLMAIGGTILFVSGALFLYILFRTLL 473
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH