|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-287 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 569.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00153 30 SLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00153 110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00153 190 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTL 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00153 270 GMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 316
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-287 |
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: 546.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:cd01663 23 SLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:cd01663 103 LLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLIT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:cd01663 183 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYL 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:cd01663 263 GMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 309
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-287 |
3.15e-121 |
|
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: 355.76 E-value: 3.15e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMiGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:TIGR02891 26 VLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:TIGR02891 105 LLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYL 240
Cdd:TIGR02891 185 SILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYR 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:TIGR02891 264 AMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGV 310
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-287 |
2.60e-117 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 223913 [Multi-domain] Cd Length: 566 Bit Score: 348.13 E-value: 2.60e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQP-GSLLQDDQIYNVIVTAHALVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFL 79
Cdd:COG0843 36 ALALLMRLELATPsGSQFLDPQLYNQILTLHGVIMIFFFAMP-AIGGFANYLVPLMIGARDVAFPRLNAISFWLLVVGAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 80 LLLASAGVESGAG-TGWTIYPPLSSgLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVF 158
Cdd:COG0843 115 LLVTSFFVPGGAAdTGWTAYPPLSA-ISYSGPGVDLFILGLHLLGIGSLLGAINFIVTILNMRAPGMTMMKMPLFTWSIL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 159 VTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEpFG 238
Cdd:COG0843 194 ITAILILLAFPVLAAALTMLLLDRNFGTSFFTPAGGGDPLLYQHLFWFFGHPEVYILILPAFGIVSEIIPTFARKPL-FG 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 922668154 239 YLGMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:COG0843 273 YTSMVYAFVAIGILSFIVWAHHMFTTGLPADLRAFFSITTMIIAIPTGI 321
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; |
1-287 |
4.11e-80 |
|
Cytochrome C and Quinol oxidase polypeptide I;
Pssm-ID: 425471 Cd Length: 432 Bit Score: 248.64 E-value: 4.11e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:pfam00115 19 LLGLLIRLQLAFPGLNFLSPLTYNRLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGvesGAGTGWTIYPPLssglahagGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFdRLPLFVWSVFVT 160
Cdd:pfam00115 98 LLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNttffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYL 240
Cdd:pfam00115 166 AILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYR 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:pfam00115 239 LSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGV 285
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-287 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 569.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00153 30 SLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00153 110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00153 190 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTL 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00153 270 GMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 316
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-287 |
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: 546.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:cd01663 23 SLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:cd01663 103 LLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLIT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:cd01663 183 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYL 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:cd01663 263 GMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 309
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-287 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 527.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00167 32 ALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00167 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00167 192 TILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYM 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00167 272 GMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 318
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-287 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 521.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00037 32 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00037 112 LLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFIT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00037 192 AFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYL 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00037 272 GMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 318
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-287 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 520.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00116 32 ALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00116 112 LLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLIT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00116 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYM 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00116 272 GMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGI 318
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-287 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 514.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00223 29 SLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00223 109 LLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00223 189 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTL 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00223 269 GMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 315
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-287 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 507.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00142 30 GLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00142 110 LLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKIT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00142 190 AILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTL 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00142 270 GMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGI 316
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-287 |
5.12e-163 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 462.86 E-value: 5.12e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00183 32 ALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00183 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLIT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00183 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYM 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00183 272 GMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGV 318
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-287 |
1.44e-161 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 458.96 E-value: 1.44e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00103 32 ALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00103 112 LLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLIT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00103 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYM 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00103 272 GMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGV 318
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-287 |
4.25e-160 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 455.55 E-value: 4.25e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00077 32 ALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00077 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLIT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00077 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYM 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00077 272 GMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGV 318
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-287 |
1.07e-157 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 449.35 E-value: 1.07e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00007 29 SMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00007 109 LVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVIT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00007 189 VVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTL 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00007 269 GMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 315
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-287 |
3.04e-156 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 445.81 E-value: 3.04e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00182 34 AFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALIL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00182 114 LLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILIT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00182 194 AFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYL 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00182 274 GMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-287 |
3.56e-154 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 440.42 E-value: 3.56e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00184 34 AFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00184 114 LLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00184 194 TFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYL 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00184 274 GMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-287 |
4.45e-147 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 422.17 E-value: 4.45e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00079 33 SLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSgLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00079 113 ILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00079 192 VFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSL 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00079 272 GMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGV 318
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-287 |
3.09e-135 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 392.84 E-value: 3.09e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00026 33 AFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00026 113 LLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFIT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00026 193 AILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYL 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00026 273 GMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGI 319
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-287 |
5.85e-126 |
|
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: 366.47 E-value: 5.85e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPlMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:cd00919 21 LLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:cd00919 100 LLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYL 240
Cdd:cd00919 180 AILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYK 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:cd00919 259 LMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGI 305
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-287 |
3.15e-121 |
|
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: 355.76 E-value: 3.15e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMiGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:TIGR02891 26 VLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:TIGR02891 105 LLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYL 240
Cdd:TIGR02891 185 SILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYR 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:TIGR02891 264 AMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGV 310
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-287 |
2.60e-117 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 223913 [Multi-domain] Cd Length: 566 Bit Score: 348.13 E-value: 2.60e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQP-GSLLQDDQIYNVIVTAHALVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFL 79
Cdd:COG0843 36 ALALLMRLELATPsGSQFLDPQLYNQILTLHGVIMIFFFAMP-AIGGFANYLVPLMIGARDVAFPRLNAISFWLLVVGAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 80 LLLASAGVESGAG-TGWTIYPPLSSgLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVF 158
Cdd:COG0843 115 LLVTSFFVPGGAAdTGWTAYPPLSA-ISYSGPGVDLFILGLHLLGIGSLLGAINFIVTILNMRAPGMTMMKMPLFTWSIL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 159 VTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEpFG 238
Cdd:COG0843 194 ITAILILLAFPVLAAALTMLLLDRNFGTSFFTPAGGGDPLLYQHLFWFFGHPEVYILILPAFGIVSEIIPTFARKPL-FG 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 922668154 239 YLGMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:COG0843 273 YTSMVYAFVAIGILSFIVWAHHMFTTGLPADLRAFFSITTMIIAIPTGI 321
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-287 |
1.50e-108 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 323.94 E-value: 1.50e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 2 MSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLLL 81
Cdd:MTH00048 34 LSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 82 LASagVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFdRLPLFVWSVFVTA 161
Cdd:MTH00048 114 LLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 162 FLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLG 241
Cdd:MTH00048 191 ILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYG 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 922668154 242 MVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00048 271 LVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGI 316
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-287 |
5.44e-102 |
|
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: 306.81 E-value: 5.44e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:cd01662 27 VDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:cd01662 106 LNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYL 240
Cdd:cd01662 186 SILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYR 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:cd01662 265 SMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGV 311
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; |
1-287 |
4.11e-80 |
|
Cytochrome C and Quinol oxidase polypeptide I;
Pssm-ID: 425471 Cd Length: 432 Bit Score: 248.64 E-value: 4.11e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:pfam00115 19 LLGLLIRLQLAFPGLNFLSPLTYNRLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 81 LLASAGvesGAGTGWTIYPPLssglahagGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFdRLPLFVWSVFVT 160
Cdd:pfam00115 98 LLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNttffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYL 240
Cdd:pfam00115 166 AILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYR 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:pfam00115 239 LSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGV 285
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
23-287 |
1.03e-63 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 211.72 E-value: 1.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 23 YNVIVTAHALVMIFFMVMPIMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLLLLASAGVESGAGTGWTIYPPLS 102
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 103 SGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDR 182
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 183 NVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSgKSEPFGYLGMVYAIVSIGILGFLVWAHHMF 262
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFF 336
|
250 260
....*....|....*....|....*
gi 922668154 263 TVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:PRK15017 337 TMGAGANVNAFFGITTMIIAIPTGV 361
|
|
|