|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-228 |
3.03e-131 |
|
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: 378.36 E-value: 3.03e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:cd01663 8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:cd01663 86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:cd01663 166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 233
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-228 |
2.05e-127 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 369.58 E-value: 2.05e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00153 15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00153 93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00153 173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-228 |
2.95e-81 |
|
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: 250.99 E-value: 2.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNHLLlgNHQVYNVLITAHAILMIFFMVMPvMIGGFGNWFVPIMIGSPDMAF 80
Cdd:TIGR02891 11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:TIGR02891 88 PRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:TIGR02891 168 GMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPE 235
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-228 |
1.59e-78 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 245.04 E-value: 1.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 2 LYLIFGAFSGVLGGCMSMFIRMELAQPGNHLLLGNHqvYNVLITAHAILMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFP 81
Cdd:COG0843 21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 82 RLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNPG 161
Cdd:COG0843 98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812622738 162 QTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:COG0843 178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-228 |
3.23e-48 |
|
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: 163.51 E-value: 3.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 2 LYLIFGAFSGVLGGCMSMFIRMELAQPGNHLLlgNHQVYNVLITAHAILMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFP 81
Cdd:pfam00115 5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 82 RLNNISFWLLPPSLCLLLLSSiveVGVGTGWTVYPPLssiqshsgAAVDLAIFSLHLSGASSILGAINFMSTIINMRNPG 161
Cdd:pfam00115 82 RLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812622738 162 QTFyRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTaffdpsGGGDPVLYQHLFWFFGHPE 228
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPE 210
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-228 |
3.03e-131 |
|
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: 378.36 E-value: 3.03e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:cd01663 8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:cd01663 86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:cd01663 166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 233
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-228 |
2.05e-127 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 369.58 E-value: 2.05e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00153 15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00153 93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00153 173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-228 |
1.01e-114 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 337.42 E-value: 1.01e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00167 17 TLYFIFGAWAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00167 95 PRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00167 175 GITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-228 |
1.11e-112 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 332.06 E-value: 1.11e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00116 17 TLYLIFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00116 95 PRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00116 175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-228 |
1.37e-111 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 329.25 E-value: 1.37e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGnhLLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00223 14 TLYLIFGMWSGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00223 92 PRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00223 172 GMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-228 |
5.28e-109 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 322.44 E-value: 5.28e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00142 15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00142 93 PRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00142 173 GMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-228 |
1.58e-102 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 306.36 E-value: 1.58e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00182 19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00182 97 PRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00182 177 GVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-228 |
5.66e-101 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 302.13 E-value: 5.66e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00037 17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00037 95 PRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00037 175 GMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPE 242
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-228 |
1.91e-100 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 300.98 E-value: 1.91e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00184 19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00184 97 PRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00184 177 GITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-228 |
2.59e-99 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 297.95 E-value: 2.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00103 17 TLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00103 95 PRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00103 175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-228 |
1.01e-98 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 296.47 E-value: 1.01e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00077 17 TLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00077 95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00077 175 SMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 242
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-228 |
1.08e-98 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 296.45 E-value: 1.08e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00183 17 TLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00183 95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00183 175 AISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-228 |
5.85e-98 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 294.28 E-value: 5.85e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGnhLLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00079 18 TLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSiQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00079 96 PRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00079 175 SISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPE 242
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-228 |
1.96e-97 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 292.96 E-value: 1.96e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00007 14 TLYFILGVWGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00007 92 PRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00007 172 GLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-228 |
1.77e-92 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 281.13 E-value: 1.77e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAF 80
Cdd:MTH00026 18 SLYLVFGALSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:MTH00026 96 PRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00026 176 GMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 243
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-228 |
3.37e-83 |
|
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: 255.15 E-value: 3.37e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNhlLLGNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPiMIGSPDMAF 80
Cdd:cd00919 6 LLYLIFAFVALLLGGLLALLIRLELATPGS--LFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:cd00919 83 PRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:cd00919 163 GMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPE 230
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-228 |
2.95e-81 |
|
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: 250.99 E-value: 2.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 1 TLYLIFGAFSGVLGGCMSMFIRMELAQPGNHLLlgNHQVYNVLITAHAILMIFFMVMPvMIGGFGNWFVPIMIGSPDMAF 80
Cdd:TIGR02891 11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 81 PRLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNP 160
Cdd:TIGR02891 88 PRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1812622738 161 GQTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:TIGR02891 168 GMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPE 235
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-228 |
1.59e-78 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 245.04 E-value: 1.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 2 LYLIFGAFSGVLGGCMSMFIRMELAQPGNHLLLGNHqvYNVLITAHAILMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFP 81
Cdd:COG0843 21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 82 RLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNPG 161
Cdd:COG0843 98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812622738 162 QTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:COG0843 178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-228 |
3.71e-66 |
|
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: 212.06 E-value: 3.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 2 LYLIFGAFSGVLGGCMSMFIRMELAQPGNHLLLGNHqvYNVLITAHAILMIFFMVMPVMIGgFGNWFVPIMIGSPDMAFP 81
Cdd:cd01662 13 MYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 82 RLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNPG 161
Cdd:cd01662 90 RLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812622738 162 QTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:cd01662 170 MTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPE 236
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-228 |
1.49e-65 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 210.69 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 2 LYLIFGAFSGVLGGCMSMFIRMELAQPGNHLLlgNHQVYNVLITAHAILMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFP 81
Cdd:MTH00048 19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 82 RLNNISFWLLPPSLCLLLLSSIVevGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNPg 161
Cdd:MTH00048 97 RLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMT- 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812622738 162 QTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:MTH00048 174 NVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPE 240
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-228 |
3.23e-48 |
|
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: 163.51 E-value: 3.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 2 LYLIFGAFSGVLGGCMSMFIRMELAQPGNHLLlgNHQVYNVLITAHAILMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFP 81
Cdd:pfam00115 5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 82 RLNNISFWLLPPSLCLLLLSSiveVGVGTGWTVYPPLssiqshsgAAVDLAIFSLHLSGASSILGAINFMSTIINMRNPG 161
Cdd:pfam00115 82 RLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812622738 162 QTFyRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTaffdpsGGGDPVLYQHLFWFFGHPE 228
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPE 210
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-228 |
2.31e-40 |
|
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: 145.77 E-value: 2.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 2 LYLIFGAFSGVLGGCMSMFIRMELAQPGNHLLLGNHqvYNVLITAHAILMIFFMVMPVMIGgFGNWFVPIMIGSPDMAFP 81
Cdd:TIGR02882 56 MYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 82 RLNNISFWLLPPSLCLLLLSSIVEVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNPG 161
Cdd:TIGR02882 133 VLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPG 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1812622738 162 QTFYRIPLFVWAIFVTAFLLLLAVPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:TIGR02882 213 MKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPE 279
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
25-228 |
8.56e-38 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 138.92 E-value: 8.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 25 LAQPGNHLLLGNHQvYNVLITAHAILMIFFMVMPVMIGgFGNWFVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLLSSIV 104
Cdd:PRK15017 85 LASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812622738 105 EVGVGTGWTVYPPLSSIQSHSGAAVDLAIFSLHLSGASSILGAINFMSTIINMRNPGQTFYRIPLFVWAIFVTAFLLLLA 184
Cdd:PRK15017 163 GEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIAS 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1812622738 185 VPVLAGAITMLLTDRNFNTAFFDPSGGGDPVLYQHLFWFFGHPE 228
Cdd:PRK15017 243 FPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPE 286
|
|
|