|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-224 |
1.97e-112 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 331.06 E-value: 1.97e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:MTH00153 18 FIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:MTH00153 98 MSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00153 178 RMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-224 |
5.94e-103 |
|
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: 306.33 E-value: 5.94e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:cd01663 11 LIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:cd01663 91 LSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:cd01663 171 KMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-224 |
3.54e-59 |
|
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: 193.59 E-value: 3.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLgfsmSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPvMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:TIGR02891 18 FAFFLVGGVL----ALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:TIGR02891 93 FSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:TIGR02891 173 RMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEV 236
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-224 |
1.28e-56 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 187.64 E-value: 1.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPvMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:COG0843 23 LVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:COG0843 102 LSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLM 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:COG0843 182 RMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-224 |
1.13e-30 |
|
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: 116.90 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPvMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:pfam00115 7 LVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLIlstFIIVGVGTGWTVYPPLslilghggMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:pfam00115 86 LSFWLVVLGAVLLL---ASFGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 mMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTsffvpsGGGDPILYQHLFWFFGHPVV 224
Cdd:pfam00115 155 -MPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEV 211
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-224 |
1.97e-112 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 331.06 E-value: 1.97e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:MTH00153 18 FIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:MTH00153 98 MSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00153 178 RMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-224 |
5.94e-103 |
|
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: 306.33 E-value: 5.94e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:cd01663 11 LIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:cd01663 91 LSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:cd01663 171 KMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 234
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-224 |
9.76e-98 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 293.51 E-value: 9.76e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:MTH00167 20 FIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:MTH00167 100 MSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQY 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00167 180 QTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-224 |
1.47e-94 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 285.33 E-value: 1.47e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:MTH00223 17 LIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:MTH00223 97 MSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00223 177 RLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-224 |
2.07e-92 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 280.05 E-value: 2.07e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:MTH00116 20 LIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:MTH00116 100 MSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQY 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00116 180 QTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-224 |
1.04e-90 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 275.45 E-value: 1.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:MTH00142 18 FLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:MTH00142 98 MSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00142 178 RVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-224 |
2.79e-85 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 261.76 E-value: 2.79e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:MTH00007 17 FILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:MTH00007 97 MSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00007 177 RIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-224 |
1.15e-83 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 257.84 E-value: 1.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:MTH00037 20 LIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:MTH00037 100 MSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00037 180 RLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
3-224 |
6.81e-81 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 250.61 E-value: 6.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 3 LGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNIMS 82
Cdd:MTH00183 22 FGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 83 FWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMDMM 162
Cdd:MTH00183 102 FWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2257466763 163 SLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00183 182 PLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-224 |
1.17e-80 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 249.80 E-value: 1.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:MTH00103 20 LLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:MTH00103 100 MSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQY 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00103 180 QTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
3-224 |
2.23e-80 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 249.09 E-value: 2.23e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 3 LGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNIMS 82
Cdd:MTH00077 22 FGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 83 FWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMDMM 162
Cdd:MTH00077 102 FWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2257466763 163 SLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00077 182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-224 |
3.38e-80 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 248.44 E-value: 3.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:MTH00079 21 FLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLiLGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:MTH00079 101 LSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00079 180 HMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEV 243
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
4-224 |
3.26e-77 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 241.26 E-value: 3.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 4 GLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNIMSF 83
Cdd:MTH00182 25 GAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 84 WLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMDMMS 163
Cdd:MTH00182 105 WLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLP 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2257466763 164 LFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00182 185 LFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEV 245
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-224 |
4.91e-77 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 240.50 E-value: 4.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:MTH00184 22 LLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:MTH00184 102 ISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00184 182 RMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 245
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
3-224 |
5.89e-69 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 220.27 E-value: 5.89e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 3 LGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNIMS 82
Cdd:MTH00026 23 FGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNIS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 83 FWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMDMM 162
Cdd:MTH00026 103 FWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRI 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2257466763 163 SLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00026 183 PLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 244
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-224 |
1.28e-61 |
|
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: 199.29 E-value: 1.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPlMLGSPDMSFPRMNI 80
Cdd:cd00919 9 LIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:cd00919 88 LSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:cd00919 168 KMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEV 231
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-224 |
3.54e-59 |
|
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: 193.59 E-value: 3.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLgfsmSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPvMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:TIGR02891 18 FAFFLVGGVL----ALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:TIGR02891 93 FSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:TIGR02891 173 RMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEV 236
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-224 |
1.28e-56 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 187.64 E-value: 1.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPvMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:COG0843 23 LVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:COG0843 102 LSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLM 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:COG0843 182 RMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-224 |
7.79e-55 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 182.57 E-value: 7.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:MTH00048 21 TLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLILSTFIivGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILfIMD 160
Cdd:MTH00048 101 LSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN-VFS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 MMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:MTH00048 178 RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEV 241
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
10-224 |
9.53e-46 |
|
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: 158.51 E-value: 9.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 10 LGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGgFGNWLIPLMLGSPDMSFPRMNIMSFWLLIPS 89
Cdd:cd01662 24 RGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 90 LLLLILSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMDMMSLFSWSV 169
Cdd:cd01662 103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2257466763 170 FITAILLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:cd01662 183 LVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-224 |
1.13e-30 |
|
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: 116.90 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 1 FFLGLWSGMLGFSMSLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPvMIGGFGNWLIPLMLGSPDMSFPRMNI 80
Cdd:pfam00115 7 LVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 81 MSFWLLIPSLLLLIlstFIIVGVGTGWTVYPPLslilghggMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMD 160
Cdd:pfam00115 86 LSFWLVVLGAVLLL---ASFGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257466763 161 mMSLFSWSVFITAILLLLSLPVLAGAITMLLTVRIMNTsffvpsGGGDPILYQHLFWFFGHPVV 224
Cdd:pfam00115 155 -MPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEV 211
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
15-224 |
8.09e-27 |
|
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: 107.63 E-value: 8.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 15 SLIIRLELGMPGSLIGIVQIYITIVTSHAFIMIFFMVMPVMIGgFGNWLIPLMLGSPDMSFPRMNIMSFWLLIPSLLLLI 94
Cdd:TIGR02882 72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 95 LSTFIIVGVGTGWTVYPPLSLILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMDMMSLFSWSVFITAI 174
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2257466763 175 LLLLSLPVLAGAITMLLTVRIMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEV 280
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
35-224 |
2.31e-25 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 103.48 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 35 YITIVTSHAFIMIFFMVMPVMIGgFGNWLIPLMLGSPDMSFPRMNIMSFWLLIPSLLLLILSTFIIVGVGTGWTVYPPLS 114
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257466763 115 LILGHGGMSVVLGIFSLHLAGASSIMGAVNFITTIMNMRSILFIMDMMSLFSWSVFITAILLLLSLPVLAGAITMLLTVR 194
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180 190
....*....|....*....|....*....|
gi 2257466763 195 IMNTSFFVPSGGGDPILYQHLFWFFGHPVV 224
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEV 287
|
|
|