|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 551.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00153 56 VTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00153 136 HSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00153 216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGM 295
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00153 296 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 324
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-269 |
0e+00 |
|
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 518.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:cd01663 49 VTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:cd01663 129 HSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:cd01663 209 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGL 288
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:cd01663 289 DVDTRAYFTAATMIIAVPTGIKVFSWLAT 317
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-269 |
2.53e-113 |
|
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: 334.96 E-value: 2.53e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMiGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:TIGR02891 52 FTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:TIGR02891 131 SPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:TIGR02891 211 HFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGM 289
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:TIGR02891 290 PPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-269 |
1.13e-112 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 334.40 E-value: 1.13e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:COG0843 61 FTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:COG0843 140 SPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:COG0843 220 HFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGI 298
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:COG0843 299 SPLVKAFFSIATMLIAVPTGVKVFNWIAT 327
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-269 |
7.60e-70 |
|
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: 221.29 E-value: 7.60e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSfieKGAGTGWTVYPPLssnia 80
Cdd:pfam00115 45 RTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 hegASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMlSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINt 160
Cdd:pfam00115 116 ---VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-TLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 sffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:pfam00115 191 -----AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGL 264
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:pfam00115 265 PPWLQALFSVFSMLIAVPSGVKVFNWLAT 293
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 551.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00153 56 VTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00153 136 HSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00153 216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGM 295
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00153 296 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 324
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-269 |
0e+00 |
|
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 518.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:cd01663 49 VTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:cd01663 129 HSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:cd01663 209 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGL 288
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:cd01663 289 DVDTRAYFTAATMIIAVPTGIKVFSWLAT 317
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
3.74e-172 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 484.95 E-value: 3.74e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00167 58 VTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00167 138 HAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00167 218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 297
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00167 298 DVDTRAYFTSATMIIAVPTGIKVFSWLAT 326
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
2.27e-171 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 482.94 E-value: 2.27e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00223 55 VTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00223 135 HAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00223 215 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGM 294
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00223 295 DVDTRAYFTAATMIIAVPTGIKVFSWLAT 323
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
1.11e-168 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 476.51 E-value: 1.11e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00116 58 VTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00116 138 HAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00116 218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGM 297
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00116 298 DVDTRAYFTSATMIIAIPTGIKVFSWLAT 326
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
2.17e-166 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 470.36 E-value: 2.17e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00142 56 VTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00142 136 HSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00142 216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGM 295
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00142 296 DVDTRAYFTAATMVIAVPTGIKVFSWLAT 324
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-269 |
1.47e-150 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 430.48 E-value: 1.47e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00007 55 VTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00007 135 HAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00007 215 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGM 294
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00007 295 DVDTRAYFTAATMIIAVPTGIKVFSWLAT 323
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
3.93e-149 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 427.03 E-value: 3.93e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00183 58 VTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00183 138 HAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00183 218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 297
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00183 298 DVDTRAYFTSATMIIAIPTGVKVFSWLAT 326
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-269 |
1.41e-147 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 422.75 E-value: 1.41e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00103 58 VTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00103 138 HAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00103 218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGM 297
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00103 298 DVDTRAYFTSATMIIAIPTGVKVFSWLAT 326
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
7.12e-147 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 421.16 E-value: 7.12e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00037 58 VTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00037 138 HAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00037 218 TFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGM 297
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00037 298 DVDTRAYFTAATMIIAVPTGIKVFSWMAT 326
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
2.68e-145 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 416.77 E-value: 2.68e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSnIA 80
Cdd:MTH00079 59 ITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00079 138 HPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00079 218 SFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGM 297
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00079 298 DLDSRAYFTAATMVIAVPTGVKVFSWLAT 326
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
4.95e-145 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 416.26 E-value: 4.95e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00077 58 VTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00077 138 HAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00077 218 TFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDL 297
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00077 298 NVDTRAYFTSATMIIAIPTGVKVFSWLAT 326
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
3.93e-142 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 409.21 E-value: 3.93e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00182 60 VTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00182 140 HSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00182 220 TFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGM 299
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00182 300 DVDTRAYFTAATMIIAVPTGIKVFSWLAT 328
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
8.10e-140 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 403.05 E-value: 8.10e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00184 60 VTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00184 140 HSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00184 220 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGM 299
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00184 300 DVDTRAYFTAATMIIAVPTGIKIFSWIAT 328
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
5.35e-127 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 371.27 E-value: 5.35e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00026 59 VTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00026 139 HSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00026 219 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGM 298
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00026 299 DVDTRAYFTAATMIIAVPTGIKIFSWLAT 327
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-269 |
7.55e-117 |
|
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: 342.59 E-value: 7.55e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPlMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:cd00919 47 VTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:cd00919 126 SSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:cd00919 206 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGL 284
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:cd00919 285 PVDTRAYFTAATMIIAVPTGIKVFNWLAT 313
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-269 |
2.53e-113 |
|
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: 334.96 E-value: 2.53e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMiGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:TIGR02891 52 FTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:TIGR02891 131 SPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:TIGR02891 211 HFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGM 289
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:TIGR02891 290 PPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-269 |
1.13e-112 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 334.40 E-value: 1.13e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:COG0843 61 FTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:COG0843 140 SPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:COG0843 220 HFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGI 298
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:COG0843 299 SPLVKAFFSIATMLIAVPTGVKVFNWIAT 327
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-267 |
6.46e-112 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 331.64 E-value: 6.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIekGAGTGWTVYPPLSSNIA 80
Cdd:MTH00048 59 ITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGmLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00048 137 SSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN-VFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00048 216 AFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGL 295
|
250 260
....*....|....*....|....*..
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWL 267
Cdd:MTH00048 296 DVKTAVFFSSVTMIIGVPTGIKVFSWL 322
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-269 |
1.56e-99 |
|
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: 299.88 E-value: 1.56e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 2 TAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIAH 81
Cdd:cd01662 54 TMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 82 EGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINTS 161
Cdd:cd01662 133 PGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 162 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGMD 241
Cdd:cd01662 213 FFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAG 291
|
250 260
....*....|....*....|....*...
gi 1100876513 242 VDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:cd01662 292 ALVNAFFSIATMIIAVPTGVKIFNWLFT 319
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-269 |
7.60e-70 |
|
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: 221.29 E-value: 7.60e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 1 VTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSfieKGAGTGWTVYPPLssnia 80
Cdd:pfam00115 45 RTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 81 hegASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMlSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINt 160
Cdd:pfam00115 116 ---VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-TLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 161 sffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:pfam00115 191 -----AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGL 264
|
250 260
....*....|....*....|....*....
gi 1100876513 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:pfam00115 265 PPWLQALFSVFSMLIAVPSGVKVFNWLAT 293
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
2-269 |
1.22e-66 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 218.65 E-value: 1.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 2 TAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIAH 81
Cdd:PRK15017 104 TAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 82 EGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINTS 161
Cdd:PRK15017 183 PGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTH 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 162 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESgKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGMD 241
Cdd:PRK15017 263 FFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAG 341
|
250 260
....*....|....*....|....*...
gi 1100876513 242 VDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:PRK15017 342 ANVNAFFGITTMIIAIPTGVKIFNWLFT 369
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-269 |
6.27e-64 |
|
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: 211.25 E-value: 6.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 2 TAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIAH 81
Cdd:TIGR02882 97 TTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 82 EGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINTS 161
Cdd:TIGR02882 176 PGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876513 162 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESgKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGMD 241
Cdd:TIGR02882 256 FFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNG 334
|
250 260
....*....|....*....|....*...
gi 1100876513 242 VDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:TIGR02882 335 ALINSFFSITTMAIAIPTGVKIFNWLLT 362
|
|
|