|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
1.01e-143 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 410.41 E-value: 1.01e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00153 72 MIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00153 152 GISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQH 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00153 232 LFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWA 287
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-216 |
8.76e-140 |
|
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: 399.55 E-value: 8.76e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:cd01663 65 LIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:cd01663 145 GISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:cd01663 225 LFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWA 280
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-216 |
5.51e-89 |
|
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: 270.25 E-value: 5.51e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:TIGR02891 67 ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:TIGR02891 147 GISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQH 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:TIGR02891 227 LFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWA 281
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-216 |
6.57e-88 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 268.53 E-value: 6.57e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:COG0843 76 FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:COG0843 156 GVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQH 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:COG0843 236 LFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWA 290
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-216 |
1.20e-53 |
|
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: 177.38 E-value: 1.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGvesGAGTGWTIYPPLssglahagGSVDLAIFSLHLA 80
Cdd:pfam00115 60 FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFdRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNttffdpAGGGDPILFQH 160
Cdd:pfam00115 129 GVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQH 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:pfam00115 202 LFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWA 256
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
1.01e-143 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 410.41 E-value: 1.01e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00153 72 MIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00153 152 GISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQH 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00153 232 LFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWA 287
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-216 |
8.76e-140 |
|
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: 399.55 E-value: 8.76e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:cd01663 65 LIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:cd01663 145 GISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:cd01663 225 LFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWA 280
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
2.84e-133 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 384.18 E-value: 2.84e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00037 74 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00037 154 GASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQH 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00037 234 LFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWA 289
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
4.07e-132 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 380.95 E-value: 4.07e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00167 74 MIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00167 154 GVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQH 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00167 234 LFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWA 289
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
4.37e-132 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 380.98 E-value: 4.37e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00116 74 MIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00116 154 GVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00116 234 LFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWA 289
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
3.59e-130 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 376.24 E-value: 3.59e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00223 71 MIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00223 151 GVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00223 231 LFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWA 286
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
6.77e-129 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 372.90 E-value: 6.77e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00142 72 MIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00142 152 GVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQH 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00142 232 LFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWA 287
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
9.07e-116 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 339.59 E-value: 9.07e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00183 74 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00183 154 GVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00183 234 LFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWA 289
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
3.01e-114 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 335.76 E-value: 3.01e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00077 74 MIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00077 154 GVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQH 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00077 234 LFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWA 289
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-216 |
3.99e-114 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 335.31 E-value: 3.99e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00103 74 MIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00103 154 GVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00103 234 LFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWA 289
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-216 |
1.01e-112 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 331.48 E-value: 1.01e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00007 71 FIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00007 151 GVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQH 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00007 231 LFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWA 286
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
9.20e-111 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 327.16 E-value: 9.20e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00182 76 MIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00182 156 GVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQH 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00182 236 LFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWA 291
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
6.73e-109 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 322.16 E-value: 6.73e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00184 76 MIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00184 156 GISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQH 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00184 236 LFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWA 291
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
1.66e-102 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 305.45 E-value: 1.66e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSgLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00079 75 MIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00079 154 GISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQH 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00079 234 LFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWA 289
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
2.20e-96 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 290.76 E-value: 2.20e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00026 75 MIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00026 155 GLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQH 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00026 235 LFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWA 290
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-216 |
5.51e-89 |
|
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: 270.25 E-value: 5.51e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:TIGR02891 67 ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:TIGR02891 147 GISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQH 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:TIGR02891 227 LFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWA 281
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-216 |
6.57e-88 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 268.53 E-value: 6.57e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:COG0843 76 FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:COG0843 156 GVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQH 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:COG0843 236 LFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWA 290
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-216 |
1.84e-87 |
|
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: 265.55 E-value: 1.84e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPlMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:cd00919 63 IFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:cd00919 142 GVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQH 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:cd00919 222 LFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWA 276
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-216 |
2.15e-76 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 238.42 E-value: 2.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASagVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:MTH00048 75 LIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFdRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:MTH00048 153 GVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQH 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:MTH00048 232 MFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWA 287
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-216 |
1.58e-72 |
|
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: 228.23 E-value: 1.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLA 80
Cdd:cd01662 68 LVFGLMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQH 160
Cdd:cd01662 148 GIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQH 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:cd01662 228 LFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWV 282
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-216 |
1.20e-53 |
|
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: 177.38 E-value: 1.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 1 MIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGvesGAGTGWTIYPPLssglahagGSVDLAIFSLHLA 80
Cdd:pfam00115 60 FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 81 GASSILASINFITTVINMRTPGISFdRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNttffdpAGGGDPILFQH 160
Cdd:pfam00115 129 GVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQH 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 922668165 161 LFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVWA 216
Cdd:pfam00115 202 LFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWA 256
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
4-215 |
1.29e-44 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 157.40 E-value: 1.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 4 GFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGAS 83
Cdd:PRK15017 121 GLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 84 SILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFW 163
Cdd:PRK15017 201 TTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 922668165 164 FFGHPEVYILILPGFGMISHVIAHYSgKSEPFGYLGMVYAIVSIGILGFLVW 215
Cdd:PRK15017 281 AWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVW 331
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-215 |
7.46e-43 |
|
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: 152.32 E-value: 7.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 2 IGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLVASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAG 81
Cdd:TIGR02882 112 IIGLMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668165 82 ASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHL 161
Cdd:TIGR02882 192 IGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANL 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 922668165 162 FWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYLGMVYAIVSIGILGFLVW 215
Cdd:TIGR02882 272 FWIWGHPEVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVW 324
|
|
|