NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1938539053|gb|QPJ78986|]
View 

cytochrome oxidase subunit 1, partial (mitochondrion) [Trachymyrmex cornetzi]

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 ...
 1-360 0e+00

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


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 624.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00153   10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00153   90 MAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00153  170 RSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00153  250 GMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQ 329

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00153  330 INYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTY 369
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-360 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 624.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00153   10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00153   90 MAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00153  170 RSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00153  250 GMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQ 329

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00153  330 INYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTY 369
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-360 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: 596.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:cd01663     3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:cd01663    83 MAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:cd01663   163 RAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:cd01663   243 GIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGS 322

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:cd01663   323 IKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTY 362
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-360 1.04e-133

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: 390.82  E-value: 1.04e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPfMIGGFGNFLIPLMLGSPD 80
Cdd:TIGR02891   6 HKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:TIGR02891  85 MAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNM 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:TIGR02891 165 RAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAF 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:TIGR02891 245 GIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGS 323

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:TIGR02891 324 IRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTY 363
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-360 2.37e-127

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 375.62  E-value: 2.37e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPD 80
Cdd:COG0843    15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:COG0843    94 MAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKM 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:COG0843   174 RAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAF 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:COG0843   254 GIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGR 332

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:COG0843   333 IRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTY 372
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-360 2.71e-88

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: 272.52  E-value: 2.71e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   3 DIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPDMA 82
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  83 YPRMNNMSFWLLPPSLILLIMSnfiSTGTGAGWTLYPPLtsnmfhsgPSVDMTIFSLHIAGMSSILGAINFISTIFNMHQ 162
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLAS---FGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 163 KKISMdKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTsffdpsGGGDPILYQHLFWFFGHPEVYILILPGFGL 242
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 243 ISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMKIN 322
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1938539053 323 -YNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTY 339
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-360 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 624.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00153   10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00153   90 MAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00153  170 RSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00153  250 GMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQ 329

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00153  330 INYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTY 369
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-360 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: 596.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:cd01663     3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:cd01663    83 MAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:cd01663   163 RAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:cd01663   243 GIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGS 322

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:cd01663   323 IKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTY 362
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-360 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 549.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00167   12 HKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00167   92 MAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINM 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00167  172 KPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00167  252 GMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGK 331

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00167  332 IKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTY 371
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-360 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 540.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00223    9 HKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00223   89 MAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINM 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00223  169 RSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00223  249 GMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSK 328

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00223  329 IKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTY 368
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-360 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 539.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00116   12 HKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00116   92 MAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINM 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00116  172 KPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00116  252 GIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGT 331

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00116  332 IKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTY 371
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-360 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 526.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00142   10 HKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00142   90 MAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00142  170 RAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00142  250 GMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSK 329

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00142  330 VKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTY 369
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-360 1.11e-172

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 490.57  E-value: 1.11e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00007    9 HKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00007   89 MAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINM 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00007  169 RWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00007  249 GAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSP 328

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00007  329 IKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTY 368
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-360 4.65e-170

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 484.00  E-value: 4.65e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00103   12 HKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00103   92 MAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINM 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00103  172 KPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00103  252 GMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGN 331

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00103  332 IKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTY 371
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-360 4.78e-169

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 481.35  E-value: 4.78e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00183   12 HKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00183   92 MAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINM 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00183  172 KPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00183  252 GMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGS 331

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00183  332 IKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTY 371
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-360 1.71e-168

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 480.10  E-value: 1.71e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00037   12 HKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00037   92 MAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINM 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00037  172 RTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00037  252 GMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSN 331

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00037  332 LRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTY 371
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-360 2.73e-168

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 479.18  E-value: 2.73e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00079   13 HKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLtSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00079   93 MSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00079  172 RSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00079  252 GIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMK 331

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00079  332 MKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTY 371
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-360 4.46e-166

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 473.66  E-value: 4.46e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00077   12 HKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00077   92 MAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINM 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00077  172 KPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGF 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00077  252 GMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGA 331

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00077  332 IKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTY 371
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-360 5.29e-160

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 458.52  E-value: 5.29e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00184   14 HKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00184   94 MAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNM 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00184  174 RAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00184  254 GIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGS 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00184  334 LRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTY 373
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-360 9.01e-158

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 453.12  E-value: 9.01e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00182   14 HKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00182   94 MAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNM 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00182  174 RAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGF 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00182  254 GMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGT 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00182  334 LRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTY 373
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-360 1.30e-143

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: 414.62  E-value: 1.30e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPlMLGSPD 80
Cdd:cd00919     1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:cd00919    80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:cd00919   160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:cd00919   240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:cd00919   319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTY 358
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-360 9.94e-140

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 407.48  E-value: 9.94e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00026   13 HKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00026   93 MAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNM 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00026  173 RTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00026  253 GIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSG 332

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1938539053 321 IN--YNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00026  333 RNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTY 374
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-360 1.04e-133

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: 390.82  E-value: 1.04e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPfMIGGFGNFLIPLMLGSPD 80
Cdd:TIGR02891   6 HKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:TIGR02891  85 MAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNM 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:TIGR02891 165 RAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAF 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:TIGR02891 245 GIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGS 323

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:TIGR02891 324 IRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTY 363
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-360 6.54e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 381.33  E-value: 6.54e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGS-CNNLINNDqIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSP 79
Cdd:MTH00048   13 HKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDpYYNVISLD-VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  80 DMAYPRMNNMSFWLLPPSLILLIMSNFIstGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFN 159
Cdd:MTH00048   92 DLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYS 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 160 MHQKKISMdKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPG 239
Cdd:MTH00048  170 AFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPG 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 240 FGLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGM 319
Cdd:MTH00048  249 FGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNS 328

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1938539053 320 KIN-YNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:MTH00048  329 RVRkSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTW 370
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-360 2.37e-127

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 375.62  E-value: 2.37e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPD 80
Cdd:COG0843    15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:COG0843    94 MAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKM 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:COG0843   174 RAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAF 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:COG0843   254 GIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGR 332

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:COG0843   333 IRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTY 372
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-360 1.01e-112

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: 337.25  E-value: 1.01e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGgFGNFLIPLMLGSPD 80
Cdd:cd01662     7 HKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:cd01662    86 VAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKM 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:cd01662   166 RAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAF 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:cd01662   246 GIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGR 324

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:cd01662   325 IRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTY 364
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-360 2.71e-88

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: 272.52  E-value: 2.71e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   3 DIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPDMA 82
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  83 YPRMNNMSFWLLPPSLILLIMSnfiSTGTGAGWTLYPPLtsnmfhsgPSVDMTIFSLHIAGMSSILGAINFISTIFNMHQ 162
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLAS---FGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 163 KKISMdKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTsffdpsGGGDPILYQHLFWFFGHPEVYILILPGFGL 242
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 243 ISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMKIN 322
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1938539053 323 -YNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTY 339
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-360 1.89e-76

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


Pssm-ID: 131928  Cd Length: 643  Bit Score: 247.46  E-value: 1.89e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGgFGNFLIPLMLGSPD 80
Cdd:TIGR02882  50 HKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARD 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:TIGR02882 129 VAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKM 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:TIGR02882 209 RAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAF 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 241 GLISHIIMNESgKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:TIGR02882 289 GIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGK 367

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1938539053 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTY 360
Cdd:TIGR02882 368 IRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTY 407
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-359 5.43e-74

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 241.76  E-value: 5.43e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053   1 HKDIGILYFLLAIWSGMIGSAMSMIIRLE--LGSCNNL-INNDQIYNSLITSHAFIMIFFMVMPFMIGgFGNFLIPLMLG 77
Cdd:PRK15017   54 HKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAgFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053  78 SPDMAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTI 157
Cdd:PRK15017  133 ARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTI 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 158 FNMHQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILIL 237
Cdd:PRK15017  213 LKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILIL 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 238 PGFGLISHIIMNESgKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLH 317
Cdd:PRK15017  293 PVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMY 371

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1938539053 318 GMKINYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDT 359
Cdd:PRK15017  372 QGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNS 413
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 216-359 3.41e-03

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: 39.19  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 216 DPILYQHLFWFFGHPEVYILILPGFGLISHIIMNESGKKETFGSLGMIyAMITIGFLGFIVWAHHMFT-IGLDVDTRAYF 294
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938539053 295 TSATMIIAIPTGIKIFSWISTL-------HGMK-INYNPTLWWS----MGFIF---LFSMGGFTGIMLSNSSIDIILHDT 359
Cdd:cd01660   279 MVLTFMVALPSLLTAFTVFASLeiagrlrGGKGlFGWIRALPWGdpmfLALFLamlMFIPGGAGGIINASYQLNYVVHNT 358
 
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