|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
3.82e-179 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 502.86 E-value: 3.82e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00153 66 FMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00153 146 FSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00153 226 PILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTS 305
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00153 306 ATMIIAVPTGIKIFSWLATLHGSQINYSPSLLW 338
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-273 |
3.49e-168 |
|
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: 474.28 E-value: 3.49e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:cd01663 59 FMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:cd01663 139 FSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:cd01663 219 PILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTA 298
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:cd01663 299 ATMIIAVPTGIKVFSWLATMWGGSIKFETPMLW 331
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-273 |
5.40e-105 |
|
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: 313.78 E-value: 5.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILiGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:TIGR02891 62 LFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:TIGR02891 141 LGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKRePFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:TIGR02891 221 PLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSA 299
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:TIGR02891 300 ATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLF 332
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-273 |
1.65e-101 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 305.90 E-value: 1.65e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPIlIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:COG0843 71 FFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:COG0843 150 LGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGD 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKRePFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:COG0843 230 PLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSI 308
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:COG0843 309 ATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLF 341
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-273 |
3.86e-63 |
|
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: 204.34 E-value: 3.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPIlIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMvemGVGAGWTVYPPLASsvghmgssMDFAI 80
Cdd:pfam00115 55 WFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMeKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTsffdpsGGGD 160
Cdd:pfam00115 123 IGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKRePFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:pfam00115 196 PLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSV 274
|
250 260 270
....*....|....*....|....*....|....
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKM-SSPLMW 273
Cdd:pfam00115 275 FSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLF 308
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
3.82e-179 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 502.86 E-value: 3.82e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00153 66 FMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00153 146 FSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00153 226 PILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTS 305
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00153 306 ATMIIAVPTGIKIFSWLATLHGSQINYSPSLLW 338
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-273 |
3.49e-168 |
|
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: 474.28 E-value: 3.49e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:cd01663 59 FMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:cd01663 139 FSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:cd01663 219 PILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTA 298
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:cd01663 299 ATMIIAVPTGIKVFSWLATMWGGSIKFETPMLW 331
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
2.36e-155 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 442.49 E-value: 2.36e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00223 65 FLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00223 145 FSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGD 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00223 225 PILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTA 304
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00223 305 ATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLW 337
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
2.47e-152 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 434.87 E-value: 2.47e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00167 68 FMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00167 148 FSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00167 228 PILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTS 307
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00167 308 ATMIIAVPTGIKVFSWLATLHGGKIKWETPMLW 340
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
1.37e-149 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 427.99 E-value: 1.37e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00142 66 FMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00142 146 FSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGD 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00142 226 PILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTA 305
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00142 306 ATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLW 338
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
1.57e-148 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 425.28 E-value: 1.57e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00116 68 FMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00116 148 FSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00116 228 PILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTS 307
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00116 308 ATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLW 340
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
1.25e-137 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 397.66 E-value: 1.25e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00037 68 FMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00037 148 FSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00037 228 PILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTA 307
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00037 308 ATMIIAVPTGIKVFSWMATLQGSNLRWETPLLW 340
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-273 |
1.32e-137 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 397.35 E-value: 1.32e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00007 65 FLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00007 145 FSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGD 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00007 225 PILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTA 304
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00007 305 ATMIIAVPTGIKVFSWLATIHGSPIKYETPMLW 337
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-273 |
1.78e-132 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 384.62 E-value: 1.78e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00103 68 FMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00103 148 FSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00103 228 PILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTS 307
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00103 308 ATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLW 340
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
1.00e-131 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 382.73 E-value: 1.00e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00183 68 FMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00183 148 FSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00183 228 PILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTS 307
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00183 308 ATMIIAIPTGVKVFSWLATLHGGSIKWETPLLW 340
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
2.18e-131 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 381.72 E-value: 2.18e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLaSSVGHMGSSMDFAI 80
Cdd:MTH00079 69 FMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00079 148 FSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGN 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00079 228 PLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTA 307
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00079 308 ATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLW 340
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
7.30e-130 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 378.40 E-value: 7.30e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00182 70 FLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00182 150 FSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGD 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00182 230 PILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTA 309
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00182 310 ATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLW 342
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
7.55e-130 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 377.74 E-value: 7.55e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00077 68 FMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00077 148 FSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00077 228 PVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTS 307
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00077 308 ATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLW 340
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
6.80e-127 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 370.31 E-value: 6.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00184 70 FLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00184 150 FSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGD 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00184 230 PILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTA 309
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00184 310 ATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLW 342
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
2.88e-114 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 338.91 E-value: 2.88e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00026 69 FLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00026 149 FSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00026 229 PILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTA 308
|
250 260 270
....*....|....*....|....*....|....*
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKM--SSPLMW 273
Cdd:MTH00026 309 ATMIIAVPTGIKIFSWLATVSGSGRNLifTTPMAW 343
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-273 |
5.40e-105 |
|
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: 313.78 E-value: 5.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILiGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:TIGR02891 62 LFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:TIGR02891 141 LGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKRePFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:TIGR02891 221 PLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSA 299
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:TIGR02891 300 ATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLF 332
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-273 |
8.26e-105 |
|
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: 312.16 E-value: 8.26e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPlMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:cd00919 57 FFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:cd00919 136 LGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKRePFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:cd00919 216 PVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTA 294
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:cd00919 295 ATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLF 327
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-273 |
1.65e-101 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 305.90 E-value: 1.65e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPIlIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:COG0843 71 FFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:COG0843 150 LGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGD 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKRePFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:COG0843 230 PLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSI 308
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:COG0843 309 ATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLF 341
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
2.78e-101 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 304.68 E-value: 2.78e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSsmVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:MTH00048 69 FFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSmEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:MTH00048 147 FSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGD 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:MTH00048 226 PVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSS 305
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:MTH00048 306 VTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVW 338
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-273 |
1.11e-89 |
|
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: 274.84 E-value: 1.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGgFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:cd01662 63 LFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:cd01662 142 LGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKRePFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:cd01662 222 PMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSI 300
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:cd01662 301 ATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLW 333
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-273 |
3.86e-63 |
|
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: 204.34 E-value: 3.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPIlIGGFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMvemGVGAGWTVYPPLASsvghmgssMDFAI 80
Cdd:pfam00115 55 WFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMeKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTsffdpsGGGD 160
Cdd:pfam00115 123 IGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKRePFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:pfam00115 196 PLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSV 274
|
250 260 270
....*....|....*....|....*....|....
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKM-SSPLMW 273
Cdd:pfam00115 275 FSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLF 308
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-273 |
1.53e-60 |
|
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: 202.39 E-value: 1.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGgFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:TIGR02882 106 FMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:TIGR02882 185 IALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGM 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKRePFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:TIGR02882 265 PMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKR-LFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSI 343
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:TIGR02882 344 TTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLF 376
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-273 |
1.32e-57 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 194.77 E-value: 1.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 1 FMVMPILIGgFGNWLVPLMLGAPDMSFPRMNNLSFWLLPPSLFLLFMSSMVEMGVGAGWTVYPPLASSVGHMGSSMDFAI 80
Cdd:PRK15017 113 FVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWI 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 81 FSLHLAGASSIMGAVNFISTIINMRGVGMSMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGD 160
Cdd:PRK15017 192 WSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGN 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76881416 161 PILFQHLFWFFGHPEVYILILPGFGIVSHVISSFSGKREpFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTA 240
Cdd:PRK15017 272 MMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRL-FGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGI 350
|
250 260 270
....*....|....*....|....*....|...
gi 76881416 241 ATMIIAVPTGIKVFSWMATLHGSYFKMSSPLMW 273
Cdd:PRK15017 351 TTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLW 383
|
|
|