|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-385 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 662.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLSTMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVF 80
Cdd:MTH00079 110 LFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVF 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 81 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFG 160
Cdd:MTH00079 190 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFG 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 161 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFT 240
Cdd:MTH00079 270 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFT 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 241 IGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLH 320
Cdd:MTH00079 350 IGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLH 429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1546647470 321 FAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDYCVNSGPEY 385
Cdd:MTH00079 430 FAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEY 494
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-377 |
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: 618.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:cd01663 100 LLLLLLSALVEGGAGTGWTVYPPLSSiLAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:cd01663 180 LITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVF 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:cd01663 260 GYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLF 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:cd01663 340 TIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQ 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDY 377
Cdd:cd01663 420 HFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNV 477
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
3-367 |
5.26e-136 |
|
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: 397.75 E-value: 5.26e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 3 LILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFV 81
Cdd:TIGR02891 104 LLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 82 TVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISqSSLYLTGKKEVFGS 161
Cdd:TIGR02891 184 TSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIIS-EILPTFARKPIFGY 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 162 LGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTI 241
Cdd:TIGR02891 263 RAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVI 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 242 GGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHF 321
Cdd:TIGR02891 343 GGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHL 422
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1546647470 322 AGIHGYPRKYLDYPD--IYSVWNIVASYGSMVSVFALFLFIYVLLESF 367
Cdd:TIGR02891 423 LGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSL 470
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
9-368 |
7.15e-131 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 385.63 E-value: 7.15e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 9 FVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFVTVFLLV 87
Cdd:COG0843 119 FVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILIL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 88 LSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSsLYLTGKKEVFGSLGMVYA 167
Cdd:COG0843 199 LAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI-IPTFSRKPLFGYKAMVLA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 168 ILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTIGGLTGV 247
Cdd:COG0843 278 TVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 248 MLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGY 327
Cdd:COG0843 358 MLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGM 437
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1546647470 328 PRKYLDYP--DIYSVWNIVASYGSMVSVFALFLFIYVLLESFL 368
Cdd:COG0843 438 PRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLR 480
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
12-351 |
4.38e-87 |
|
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: 270.21 E-value: 4.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 12 MGCGTSWTVYPPLStmghpgsSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLeHMSLFVWTVFVTVFLLVLSLP 91
Cdd:pfam00115 103 GGATTGWTEYPPLV-------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 92 VLAGAITMLLTDRNLNTSffdpstGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKeVFGSLGMVYAILSI 171
Cdd:pfam00115 175 VLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 172 GLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVF-QPLLLWVTGFIFLFTIGGLTGVMLS 250
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 251 NSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGYPRK 330
Cdd:pfam00115 328 LPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRR 407
|
330 340
....*....|....*....|....*
gi 1546647470 331 Y----LDYPDIYSVWNIVASYGSMV 351
Cdd:pfam00115 408 YappfIETVPAFQPLNWIRTIGGVL 432
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-385 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 662.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLSTMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVF 80
Cdd:MTH00079 110 LFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVF 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 81 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFG 160
Cdd:MTH00079 190 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFG 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 161 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFT 240
Cdd:MTH00079 270 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFT 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 241 IGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLH 320
Cdd:MTH00079 350 IGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLH 429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1546647470 321 FAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDYCVNSGPEY 385
Cdd:MTH00079 430 FAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEY 494
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-377 |
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: 618.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:cd01663 100 LLLLLLSALVEGGAGTGWTVYPPLSSiLAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:cd01663 180 LITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVF 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:cd01663 260 GYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLF 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:cd01663 340 TIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQ 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDY 377
Cdd:cd01663 420 HFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNV 477
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-385 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 598.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00153 107 LTLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00153 187 LITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETF 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00153 267 GTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLF 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00153 347 TIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQ 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDYCVNSGPEY 385
Cdd:MTH00153 427 HFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEW 492
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-385 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 544.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00223 106 LYLLLSSSAVESGVGTGWTVYPPLSsNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00223 186 KVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVF 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00223 266 GTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLF 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00223 346 TVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQ 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDYCVNSGPEY 385
Cdd:MTH00223 426 HFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEW 491
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-385 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 542.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00167 109 LLLLLASSGVEAGAGTGWTVYPPLAgNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSI 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00167 189 LVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPF 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00167 269 GYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLF 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00167 349 TVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQ 428
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDYCVNSGPEY 385
Cdd:MTH00167 429 HFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEW 494
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-374 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 520.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00116 109 FLLLLASSTVEAGAGTGWTVYPPLAgNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00116 189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPF 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00116 269 GYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLF 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00116 349 TIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQ 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFL 374
Cdd:MTH00116 429 HFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVL 483
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-385 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 514.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00142 107 LLLLLSSAAVESGAGTGWTVYPPLSSnLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00142 187 KITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVF 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00142 267 GTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLF 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00142 347 TVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQ 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFLFDYCVNSGPEY 385
Cdd:MTH00142 427 HFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEW 492
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-371 |
2.46e-166 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 475.16 E-value: 2.46e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPL-STMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00007 106 LILLVSSAAVEKGVGTGWTVYPPLaSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00007 186 VITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPF 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00007 266 GTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLF 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00007 346 TTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQ 425
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHR 371
Cdd:MTH00007 426 HFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQR 477
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
3-371 |
6.22e-161 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 461.99 E-value: 6.22e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 3 LILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFV 81
Cdd:MTH00037 111 LLLASAGVESGAGTGWTIYPPLSSnIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 82 TVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFGS 161
Cdd:MTH00037 191 TAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGY 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 162 LGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTI 241
Cdd:MTH00037 271 LGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTI 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 242 GGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHF 321
Cdd:MTH00037 351 GGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHF 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1546647470 322 AGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHR 371
Cdd:MTH00037 431 LGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQR 480
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
2-371 |
2.34e-160 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 460.12 E-value: 2.34e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 2 FLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVF 80
Cdd:MTH00103 110 LLLLASSMVEAGAGTGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 81 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFG 160
Cdd:MTH00103 190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFG 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 161 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFT 240
Cdd:MTH00103 270 YMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFT 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 241 IGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLH 320
Cdd:MTH00103 350 VGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQH 429
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1546647470 321 FAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHR 371
Cdd:MTH00103 430 FLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKR 480
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-371 |
7.20e-159 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 456.69 E-value: 7.20e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00183 109 FLLLLASSGVEAGAGTGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00183 189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPF 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00183 269 GYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLF 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00183 349 TVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQ 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHR 371
Cdd:MTH00183 429 HFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKR 480
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-374 |
1.31e-158 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 456.21 E-value: 1.31e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00182 111 LILLLGSAFVEQGAGTGWTVYPPLSSIqAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00182 191 LITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIF 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00182 271 GYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLF 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00182 351 TLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQ 430
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFL 374
Cdd:MTH00182 431 HFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFI 485
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-374 |
2.46e-158 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 455.17 E-value: 2.46e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00077 109 FLLLLASSGVEAGAGTGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00077 189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPF 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:MTH00077 269 GYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLF 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00077 349 TVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQ 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLFL 374
Cdd:MTH00077 429 HFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVL 483
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
3-373 |
1.49e-156 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 450.82 E-value: 1.49e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 3 LILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFV 81
Cdd:MTH00184 113 LLLGSAFVEQGAGTGWTVYPPLSSiQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 82 TVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFGS 161
Cdd:MTH00184 193 TTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 162 LGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTI 241
Cdd:MTH00184 273 LGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTM 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 242 GGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHF 321
Cdd:MTH00184 353 GGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHF 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1546647470 322 AGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESFLGHRLF 373
Cdd:MTH00184 433 LGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKF 484
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-367 |
8.38e-146 |
|
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: 421.17 E-value: 8.38e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLSTMG-HPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:cd00919 97 LLLLLSSVLVGGGAGTGWTFYPPLSTLSySSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKeVF 159
Cdd:cd00919 177 LVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LF 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLF 239
Cdd:cd00919 256 GYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLF 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:cd00919 336 TIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPM 415
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESF 367
Cdd:cd00919 416 HFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-367 |
2.82e-140 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 409.79 E-value: 2.82e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 1 MFLILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTV 79
Cdd:MTH00026 110 LFLLLGSSLVEQGAGTGWTVYPPLASIqAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 80 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVF 159
Cdd:MTH00026 190 FITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIF 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 160 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATL--FGMKMVFQPLLLWVTGFIF 237
Cdd:MTH00026 270 GYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVsgSGRNLIFTTPMAWALGFIF 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 238 LFTIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFF 317
Cdd:MTH00026 350 LFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFF 429
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1546647470 318 PLHFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESF 367
Cdd:MTH00026 430 PQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAY 479
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
3-367 |
5.26e-136 |
|
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: 397.75 E-value: 5.26e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 3 LILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFV 81
Cdd:TIGR02891 104 LLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 82 TVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISqSSLYLTGKKEVFGS 161
Cdd:TIGR02891 184 TSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIIS-EILPTFARKPIFGY 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 162 LGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTI 241
Cdd:TIGR02891 263 RAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVI 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 242 GGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHF 321
Cdd:TIGR02891 343 GGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHL 422
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1546647470 322 AGIHGYPRKYLDYPD--IYSVWNIVASYGSMVSVFALFLFIYVLLESF 367
Cdd:TIGR02891 423 LGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSL 470
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
9-368 |
7.15e-131 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 385.63 E-value: 7.15e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 9 FVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFVTVFLLV 87
Cdd:COG0843 119 FVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILIL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 88 LSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSsLYLTGKKEVFGSLGMVYA 167
Cdd:COG0843 199 LAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI-IPTFSRKPLFGYKAMVLA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 168 ILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTIGGLTGV 247
Cdd:COG0843 278 TVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 248 MLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGY 327
Cdd:COG0843 358 MLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGM 437
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1546647470 328 PRKYLDYP--DIYSVWNIVASYGSMVSVFALFLFIYVLLESFL 368
Cdd:COG0843 438 PRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLR 480
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-367 |
3.41e-124 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 367.85 E-value: 3.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 2 FLILDACFvdmGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHmSLFVWTVF 80
Cdd:MTH00048 112 FLLLSMCL---GAGVGWTFYPPLSSsLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRT-SIILWSYL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 81 VTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFG 160
Cdd:MTH00048 188 FTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 161 SLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKM-VFQPLLLWVTGFIFLF 239
Cdd:MTH00048 268 YYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVrKSDPVVWWVVSFIVLF 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 240 TIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPL 319
Cdd:MTH00048 348 TIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPM 427
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1546647470 320 HFAGIHGYPRKYLDYPDIYSVWNIVASYGSMVSVFALFLFIYVLLESF 367
Cdd:MTH00048 428 HYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESL 475
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
9-367 |
5.21e-119 |
|
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: 354.19 E-value: 5.21e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 9 FVDMGCGTSWTVYPPLSTMGH-PGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFVTVFLLV 87
Cdd:cd01662 111 LIGGFPDAGWFAYPPLSGLEYsPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILIL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 88 LSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISqSSLYLTGKKEVFGSLGMVYA 167
Cdd:cd01662 191 FAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFS-EIVPTFSRKPLFGYRSMVYA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 168 ILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTIGGLTGV 247
Cdd:cd01662 270 TVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGV 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 248 MLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGY 327
Cdd:cd01662 350 MLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGM 429
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1546647470 328 PRKYLDYP--DIYSVWNIVASYGSMVSVFALFLFIYVLLESF 367
Cdd:cd01662 430 PRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSI 471
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
12-351 |
4.38e-87 |
|
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: 270.21 E-value: 4.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 12 MGCGTSWTVYPPLStmghpgsSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLeHMSLFVWTVFVTVFLLVLSLP 91
Cdd:pfam00115 103 GGATTGWTEYPPLV-------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 92 VLAGAITMLLTDRNLNTSffdpstGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKeVFGSLGMVYAILSI 171
Cdd:pfam00115 175 VLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 172 GLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVF-QPLLLWVTGFIFLFTIGGLTGVMLS 250
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 251 NSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGYPRK 330
Cdd:pfam00115 328 LPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRR 407
|
330 340
....*....|....*....|....*
gi 1546647470 331 Y----LDYPDIYSVWNIVASYGSMV 351
Cdd:pfam00115 408 YappfIETVPAFQPLNWIRTIGGVL 432
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
16-330 |
6.99e-73 |
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cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 239.45 E-value: 6.99e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 16 TSWTVYPPLSTMGH-PGSSVDLAIFSLHCAGISSILGAINFMTTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLA 94
Cdd:PRK15017 168 TGWLAYPPLSGIEYsPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILT 247
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 95 GAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTgKKEVFGSLGMVYAILSIGLI 174
Cdd:PRK15017 248 VTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVL 326
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 175 GCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMVFQPLLLWVTGFIFLFTIGGLTGVMLSNSSL 254
Cdd:PRK15017 327 SFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGA 406
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250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1546647470 255 DIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGFVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGYPRK 330
Cdd:PRK15017 407 DFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRR 482
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| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
118-368 |
2.89e-13 |
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ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.
Pssm-ID: 238830 Cd Length: 473 Bit Score: 70.78 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 118 NPLIYQHLFWFFGHPEVYILILPAFGIISQSSLYLTGKKEVFGSLGMVYAILSIgLIGCVVWAHHMYT-VGMDLDSRAYF 196
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFAdPGIGPGWKFIH 278
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 197 TAATMVIAVPT-------------------GVKVFSWLATLFGMKMVFQPLLLwvtGFIFlFTIGGLTGVMLSNSSLDII 257
Cdd:cd01660 279 MVLTFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALFL---AMLM-FIPGGAGGIINASYQLNYV 354
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546647470 258 LHDTYYVVSHFHYVLSlGAVFGIFTGVTLW-WSFITG-FVYDKMMMSSVFVLMFVGVNLTFFPLHFAGIHGYPRK--YLD 333
Cdd:cd01660 355 VHNTAWVPGHFHLTVG-GAVALTFMAVAYWlVPHLTGrELAAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQ 433
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250 260 270 280
....*....|....*....|....*....|....*....|
gi 1546647470 334 YPDIY-----SVWNIVASYGSMVSVFALFLFIYVLLESFL 368
Cdd:cd01660 434 YGGLPaagewAPYQQLMAIGGTILFVSGALFLYILFRTLL 473
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