|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
3.92e-153 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 434.30 E-value: 3.92e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00153 73 IGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00153 153 ISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00153 233 FWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIV 285
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-213 |
1.33e-135 |
|
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: 388.76 E-value: 1.33e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:cd01663 66 IGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:cd01663 146 ISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:cd01663 226 FWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIV 278
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-213 |
1.10e-84 |
|
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: 259.08 E-value: 1.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:TIGR02891 68 LAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:TIGR02891 148 ISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIV 213
Cdd:TIGR02891 228 FWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGV 279
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-213 |
2.88e-82 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 253.90 E-value: 2.88e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:COG0843 77 LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:COG0843 157 VGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHL 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIV 213
Cdd:COG0843 237 FWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLV 288
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-213 |
2.08e-52 |
|
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: 173.91 E-value: 2.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*dsGAGTGWTVYPPLAGaiahgggsVDLAIFSLHLAG 80
Cdd:pfam00115 61 LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHL 160
Cdd:pfam00115 130 VSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHL 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIV 213
Cdd:pfam00115 203 FWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLV 254
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
3.92e-153 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 434.30 E-value: 3.92e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00153 73 IGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00153 153 ISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00153 233 FWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIV 285
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-213 |
1.33e-135 |
|
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: 388.76 E-value: 1.33e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:cd01663 66 IGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:cd01663 146 ISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:cd01663 226 FWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIV 278
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
4.22e-128 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 370.85 E-value: 4.22e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00223 72 IGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00223 152 VSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00223 232 FWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIV 284
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
1.97e-127 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 369.01 E-value: 1.97e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00167 75 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00167 155 VSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00167 235 FWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIV 287
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
1.98e-127 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 369.04 E-value: 1.98e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00116 75 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00116 155 VSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00116 235 FWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIV 287
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
1.49e-125 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 364.04 E-value: 1.49e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00142 73 IGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00142 153 VSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHL 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00142 233 FWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIV 285
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-213 |
7.21e-114 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 334.56 E-value: 7.21e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00007 72 IGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00007 152 VSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00007 232 FWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIV 284
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
1.49e-113 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 333.83 E-value: 1.49e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00077 75 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00077 155 VSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHL 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00077 235 FWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIV 287
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-213 |
9.73e-113 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 331.46 E-value: 9.73e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00103 75 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00103 155 VSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00103 235 FWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIV 287
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
4.45e-111 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 327.56 E-value: 4.45e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00037 75 IGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00037 155 ASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHL 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00037 235 FWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLV 287
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
1.41e-110 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 326.11 E-value: 1.41e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00183 75 IGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00183 155 VSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00183 235 FWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIV 287
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
3.22e-104 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 310.21 E-value: 3.22e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00182 77 IGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00182 157 VSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHL 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00182 237 FWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIV 289
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
7.68e-104 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 309.06 E-value: 7.68e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00184 77 IGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00184 157 ISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHL 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00184 237 FWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIV 289
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
6.60e-103 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 306.22 E-value: 6.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAgAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00079 76 IGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00079 155 ISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHL 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00079 235 FWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVV 287
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
1.56e-95 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 288.45 E-value: 1.56e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00026 76 IGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00026 156 LSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHL 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00026 236 FWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIV 288
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-213 |
1.57e-85 |
|
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: 260.16 E-value: 1.57e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPlMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:cd00919 64 FGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:cd00919 143 VSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHL 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIV 213
Cdd:cd00919 223 FWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLV 274
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-213 |
1.10e-84 |
|
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: 259.08 E-value: 1.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:TIGR02891 68 LAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:TIGR02891 148 ISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIV 213
Cdd:TIGR02891 228 FWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGV 279
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-213 |
2.88e-82 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 253.90 E-value: 2.88e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:COG0843 77 LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:COG0843 157 VGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHL 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIV 213
Cdd:COG0843 237 FWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLV 288
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-213 |
1.58e-73 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 230.72 E-value: 1.58e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*dsGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:MTH00048 76 IGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:MTH00048 154 VSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHM 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIV 213
Cdd:MTH00048 233 FWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVV 285
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
3-213 |
3.80e-67 |
|
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: 213.98 E-value: 3.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 3 GFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAGIS 82
Cdd:cd01662 71 GLMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 83 SILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFW 162
Cdd:cd01662 151 TLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFW 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2091691979 163 FFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIV 213
Cdd:cd01662 231 IFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGV 280
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-213 |
2.08e-52 |
|
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: 173.91 E-value: 2.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*dsGAGTGWTVYPPLAGaiahgggsVDLAIFSLHLAG 80
Cdd:pfam00115 61 LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHL 160
Cdd:pfam00115 130 VSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHL 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIV 213
Cdd:pfam00115 203 FWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLV 254
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-213 |
7.72e-41 |
|
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: 146.54 E-value: 7.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 1 IGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAG 80
Cdd:TIGR02882 112 IIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 81 ISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHL 160
Cdd:TIGR02882 192 IGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANL 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2091691979 161 FWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIV 213
Cdd:TIGR02882 272 FWIWGHPEVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLV 323
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
3-213 |
7.99e-41 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 146.62 E-value: 7.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 3 GFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSM*DSGAGTGWTVYPPLAGAIAHGGGSVDLAIFSLHLAGIS 82
Cdd:PRK15017 121 GLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2091691979 83 SILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFW 162
Cdd:PRK15017 201 TTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2091691979 163 FFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIV 213
Cdd:PRK15017 281 AWGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIV 330
|
|
|