|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
8-515 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 875.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 8 QGGLAVWLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFG 87
Cdd:MTH00079 1 QGGLSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 88 NWLLPLMLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTMGHPGSSVDLAIFSLHAAGLSSILG 167
Cdd:MTH00079 81 NWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 168 GINFMCTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGH 247
Cdd:MTH00079 161 GINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 248 PEVYILILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKV 327
Cdd:MTH00079 241 PEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 328 FSWLATLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFI 407
Cdd:MTH00079 321 FSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 408 TGYVLDKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYR 487
Cdd:MTH00079 401 TGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYR 480
|
490 500
....*....|....*....|....*...
gi 5834891 488 LVISDYYSNSSPEYCMSNYVFGHSYQSE 515
Cdd:MTH00079 481 LVLHDNYINSSPEYSLSSYVFGHSYQSE 508
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-503 |
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: 820.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 19 NHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPLMLGAP 98
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 99 DMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHAAGLSSILGGINFMCTTKN 177
Cdd:cd01663 82 DMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSiLAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 178 LRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPA 257
Cdd:cd01663 162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 258 FGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLATLFGM 337
Cdd:cd01663 242 FGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 338 KMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVLDKLMM 417
Cdd:cd01663 322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 418 SAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISDY-YSN 496
Cdd:cd01663 402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEGS 481
|
....*..
gi 5834891 497 SSPEYCM 503
Cdd:cd01663 482 TSLEWTL 488
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
15-485 |
0e+00 |
|
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: 524.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 15 LESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPtMIGGFGNWLLPLM 94
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 95 LGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHAAGLSSILGGINFMC 173
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 174 TTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYIL 253
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 254 ILPAFGIVSqSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLAT 333
Cdd:TIGR02891 240 FLPAFGIIS-EILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 334 LFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVLD 413
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5834891 414 KLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPD--VYSVWNIIASYGSIISTAGLFLFIYVLLESFFS 485
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRK 472
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
14-484 |
2.75e-179 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 514.68 E-value: 2.75e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPtMIGGFGNWLLPL 93
Cdd:COG0843 9 WLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 94 MLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHAAGLSSILGGINFM 172
Cdd:COG0843 88 QIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 173 CTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYI 252
Cdd:COG0843 168 VTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 253 LILPAFGIVSQSTLYLTGKKeVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLA 332
Cdd:COG0843 248 LILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 333 TLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVL 412
Cdd:COG0843 327 TMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRML 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5834891 413 DKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYS--VWNIIASYGSIISTAGLFLFIYVLLESFF 484
Cdd:COG0843 407 NERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGwqPLNLISTIGAFILAVGFLLFLINLVVSLR 480
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
22-467 |
1.55e-122 |
|
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: 366.13 E-value: 1.55e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 22 DIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPtMIGGFGNWLLPLMLGAPDMS 101
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 102 FPRLNNLSFWLLPTSMLLILdacFVDMGCGTSWTVYPPLStmghpgsSVDLAIFSLHAAGLSSILGGINFMCTTKNLRSS 181
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLL---ASFGGATTGWTEYPPLV-------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 182 SISLeHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSffdpstGGNPLIYQHLFWFFGHPEVYILILPAFGIV 261
Cdd:pfam00115 150 GMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAFGII 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 262 SQSTLYLTGKKeVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLATLFGMKMVF 341
Cdd:pfam00115 223 YYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 342 N-PLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVLDKLMMSAV 420
Cdd:pfam00115 302 RtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLH 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 5834891 421 FILLFIGVNLTFFPLHFAGLHGFPRKY----LDYPDVYSVWNIIASYGSII 467
Cdd:pfam00115 382 FWLLFIGFNLTFFPMHILGLLGMPRRYappfIETVPAFQPLNWIRTIGGVL 432
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
8-515 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 875.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 8 QGGLAVWLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFG 87
Cdd:MTH00079 1 QGGLSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 88 NWLLPLMLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTMGHPGSSVDLAIFSLHAAGLSSILG 167
Cdd:MTH00079 81 NWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 168 GINFMCTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGH 247
Cdd:MTH00079 161 GINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 248 PEVYILILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKV 327
Cdd:MTH00079 241 PEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 328 FSWLATLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFI 407
Cdd:MTH00079 321 FSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 408 TGYVLDKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYR 487
Cdd:MTH00079 401 TGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYR 480
|
490 500
....*....|....*....|....*...
gi 5834891 488 LVISDYYSNSSPEYCMSNYVFGHSYQSE 515
Cdd:MTH00079 481 LVLHDNYINSSPEYSLSSYVFGHSYQSE 508
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
19-503 |
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: 820.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 19 NHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPLMLGAP 98
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 99 DMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHAAGLSSILGGINFMCTTKN 177
Cdd:cd01663 82 DMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSiLAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 178 LRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPA 257
Cdd:cd01663 162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 258 FGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLATLFGM 337
Cdd:cd01663 242 FGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 338 KMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVLDKLMM 417
Cdd:cd01663 322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 418 SAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISDY-YSN 496
Cdd:cd01663 402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEGS 481
|
....*..
gi 5834891 497 SSPEYCM 503
Cdd:cd01663 482 TSLEWTL 488
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
14-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 802.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPL 93
Cdd:MTH00153 4 WLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 94 MLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHAAGLSSILGGINFM 172
Cdd:MTH00153 84 MLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 173 CTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYI 252
Cdd:MTH00153 164 TTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 253 LILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLA 332
Cdd:MTH00153 244 LILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 333 TLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVL 412
Cdd:MTH00153 324 TLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 413 DKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISD 492
Cdd:MTH00153 404 NPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFS 483
|
490 500
....*....|....*....|
gi 5834891 493 YYSNSSPEYCMSNYVFGHSY 512
Cdd:MTH00153 484 LNLSSSIEWLQNLPPAEHSY 503
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
14-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 731.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPL 93
Cdd:MTH00223 3 WLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 94 MLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHAAGLSSILGGINFM 172
Cdd:MTH00223 83 MLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSsNLAHAGPSVDLAIFSLHLAGVSSILGAINFI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 173 CTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYI 252
Cdd:MTH00223 163 TTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 253 LILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLA 332
Cdd:MTH00223 243 LILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 333 TLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVL 412
Cdd:MTH00223 323 TIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 413 DKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISD 492
Cdd:MTH00223 403 HRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWS 482
|
....*....
gi 5834891 493 YYSNSSPEY 501
Cdd:MTH00223 483 GHLSTSLEW 491
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
14-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 729.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPL 93
Cdd:MTH00167 6 WLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 94 MLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHAAGLSSILGGINFM 172
Cdd:MTH00167 86 MIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAgNLAHAGASVDLAIFSLHLAGVSSILGSINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 173 CTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYI 252
Cdd:MTH00167 166 TTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 253 LILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLA 332
Cdd:MTH00167 246 LILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 333 TLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVL 412
Cdd:MTH00167 326 TLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 413 DKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISD 492
Cdd:MTH00167 406 NETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPV 485
|
490 500
....*....|....*....|
gi 5834891 493 YYSNSSPEYCMSNYVFGHSY 512
Cdd:MTH00167 486 ELTSTNVEWLHGCPPPHHTW 505
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
14-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 703.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPL 93
Cdd:MTH00116 6 WLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 94 MLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHAAGLSSILGGINFM 172
Cdd:MTH00116 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAgNLAHAGASVDLAIFSLHLAGVSSILGAINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 173 CTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYI 252
Cdd:MTH00116 166 TTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 253 LILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLA 332
Cdd:MTH00116 246 LILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 333 TLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVL 412
Cdd:MTH00116 326 TLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 413 DKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISD 492
Cdd:MTH00116 406 HQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQP 485
|
....*....
gi 5834891 493 YYSNSSPEY 501
Cdd:MTH00116 486 ELTTTNIEW 494
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
14-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 692.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPL 93
Cdd:MTH00142 4 WLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 94 MLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHAAGLSSILGGINFM 172
Cdd:MTH00142 84 MLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSnLAHSGGSVDLAIFSLHLAGVSSILGAINFI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 173 CTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYI 252
Cdd:MTH00142 164 TTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 253 LILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLA 332
Cdd:MTH00142 244 LILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 333 TLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVL 412
Cdd:MTH00142 324 TLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 413 DKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISD 492
Cdd:MTH00142 404 NPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWS 483
|
....*....
gi 5834891 493 YYSNSSPEY 501
Cdd:MTH00142 484 SHLSTSLEW 492
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
14-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 640.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPL 93
Cdd:MTH00007 3 WLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 94 MLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPL-STMGHPGSSVDLAIFSLHAAGLSSILGGINFM 172
Cdd:MTH00007 83 MLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLaSNLAHAGPSVDLAIFSLHLAGVSSILGAINFI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 173 CTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYI 252
Cdd:MTH00007 163 TTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 253 LILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLA 332
Cdd:MTH00007 243 LILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 333 TLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVL 412
Cdd:MTH00007 323 TIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 413 DKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISD 492
Cdd:MTH00007 403 HDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIAS 482
|
....*....
gi 5834891 493 YYSNSSPEY 501
Cdd:MTH00007 483 PHMSSSLEW 491
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
11-524 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 638.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 11 LAVWLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWL 90
Cdd:MTH00037 3 LSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 91 LPLMLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHAAGLSSILGGI 169
Cdd:MTH00037 83 IPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSnIAHAGGSVDLAIFSLHLAGASSILASI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 170 NFMCTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPE 249
Cdd:MTH00037 163 NFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 250 VYILILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFS 329
Cdd:MTH00037 243 VYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 330 WLATLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITG 409
Cdd:MTH00037 323 WMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 410 YVLDKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLV 489
Cdd:MTH00037 403 VSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREV 482
|
490 500 510
....*....|....*....|....*....|....*
gi 5834891 490 ISDYYSNSSPEYCMSNYVFGHSYQSEIYFSTTSLK 524
Cdd:MTH00037 483 ISPEFSSSSLEWQYSSFPPSHHTFDETPSTVILIK 517
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
14-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 624.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPL 93
Cdd:MTH00103 6 WLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 94 MLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHAAGLSSILGGINFM 172
Cdd:MTH00103 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 173 CTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYI 252
Cdd:MTH00103 166 TTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 253 LILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLA 332
Cdd:MTH00103 246 LILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 333 TLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVL 412
Cdd:MTH00103 326 TLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 413 DKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISD 492
Cdd:MTH00103 406 NDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTV 485
|
....*....
gi 5834891 493 YYSNSSPEY 501
Cdd:MTH00103 486 ELTTTNLEW 494
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
14-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 618.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPL 93
Cdd:MTH00183 6 WFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 94 MLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHAAGLSSILGGINFM 172
Cdd:MTH00183 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 173 CTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYI 252
Cdd:MTH00183 166 TTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 253 LILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLA 332
Cdd:MTH00183 246 LILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 333 TLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVL 412
Cdd:MTH00183 326 TLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 413 DKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISD 492
Cdd:MTH00183 406 HSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSV 485
|
....*....
gi 5834891 493 YYSNSSPEY 501
Cdd:MTH00183 486 ELTSTNVEW 494
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
14-521 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 616.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPL 93
Cdd:MTH00077 6 WLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 94 MLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLS-TMGHPGSSVDLAIFSLHAAGLSSILGGINFM 172
Cdd:MTH00077 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAgNLAHAGASVDLTIFSLHLAGVSSILGAINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 173 CTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYI 252
Cdd:MTH00077 166 TTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 253 LILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLA 332
Cdd:MTH00077 246 LILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 333 TLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVL 412
Cdd:MTH00077 326 TMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 413 DKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISD 492
Cdd:MTH00077 406 HSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTT 485
|
490 500
....*....|....*....|....*....
gi 5834891 493 YYSNSSPEYCMSNYVFGHSYQSEIYFSTT 521
Cdd:MTH00077 486 ELTSTNIEWLHGCPPPYHTFEEPSFVQTR 514
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
11-491 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 602.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 11 LAVWLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWL 90
Cdd:MTH00182 5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 91 LPLMLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHAAGLSSILGGI 169
Cdd:MTH00182 85 VPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIqAHSGGAVDMAIFSLHLAGVSSILGAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 170 NFMCTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPE 249
Cdd:MTH00182 165 NFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 250 VYILILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFS 329
Cdd:MTH00182 245 VYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 330 WLATLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITG 409
Cdd:MTH00182 325 WLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 410 YVLDKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLV 489
Cdd:MTH00182 405 YCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKF 484
|
..
gi 5834891 490 IS 491
Cdd:MTH00182 485 IG 486
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
11-483 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 600.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 11 LAVWLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWL 90
Cdd:MTH00184 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 91 LPLMLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHAAGLSSILGGI 169
Cdd:MTH00184 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSiQAHSGGSVDMAIFSLHLAGISSILGAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 170 NFMCTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPE 249
Cdd:MTH00184 165 NFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 250 VYILILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFS 329
Cdd:MTH00184 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 330 WLATLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITG 409
Cdd:MTH00184 325 WIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5834891 410 YVLDKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESF 483
Cdd:MTH00184 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAY 478
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
20-483 |
0e+00 |
|
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: 553.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 20 HKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLlPLMLGAPD 99
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLL-PPLIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 100 MSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTMG-HPGSSVDLAIFSLHAAGLSSILGGINFMCTTKNL 178
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSySSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 179 RSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAF 258
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 259 GIVSQSTLYLTGKKeVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLATLFGMK 338
Cdd:cd00919 240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 339 MVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVLDKLMMS 418
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5834891 419 AVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESF 483
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
14-484 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 543.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPL 93
Cdd:MTH00026 7 WFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 94 MLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHAAGLSSILGGINFM 172
Cdd:MTH00026 87 MIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIqAHSGGSVDMAIFSLHLAGLSSILGAMNFI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 173 CTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYI 252
Cdd:MTH00026 167 TTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 253 LILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLA 332
Cdd:MTH00026 247 LILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 333 TL--FGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGY 410
Cdd:MTH00026 327 TVsgSGRNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGY 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5834891 411 VLDKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFF 484
Cdd:MTH00026 407 AYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYY 480
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
15-485 |
0e+00 |
|
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: 524.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 15 LESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPtMIGGFGNWLLPLM 94
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 95 LGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHAAGLSSILGGINFMC 173
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 174 TTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYIL 253
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 254 ILPAFGIVSqSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLAT 333
Cdd:TIGR02891 240 FLPAFGIIS-EILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 334 LFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVLD 413
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5834891 414 KLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPD--VYSVWNIIASYGSIISTAGLFLFIYVLLESFFS 485
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRK 472
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
14-484 |
2.75e-179 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 514.68 E-value: 2.75e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPtMIGGFGNWLLPL 93
Cdd:COG0843 9 WLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 94 MLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTM-GHPGSSVDLAIFSLHAAGLSSILGGINFM 172
Cdd:COG0843 88 QIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 173 CTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYI 252
Cdd:COG0843 168 VTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 253 LILPAFGIVSQSTLYLTGKKeVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLA 332
Cdd:COG0843 248 LILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 333 TLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVL 412
Cdd:COG0843 327 TMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRML 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5834891 413 DKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYS--VWNIIASYGSIISTAGLFLFIYVLLESFF 484
Cdd:COG0843 407 NERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGwqPLNLISTIGAFILAVGFLLFLINLVVSLR 480
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
10-511 |
3.35e-171 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 493.43 E-value: 3.35e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 10 GLAVWLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNW 89
Cdd:MTH00048 3 SLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 90 LLPLMLGAPDMSFPRLNNLSFWLL-PTSMLLILDACFvdmGCGTSWTVYPPLST-MGHPGSSVDLAIFSLHAAGLSSILG 167
Cdd:MTH00048 83 LLPLLLGLSDLNLPRLNALSAWLLvPSIVFLLLSMCL---GAGVGWTFYPPLSSsLFSSSWGVDFLMFSLHLAGVSSLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 168 GINFMCTTKNLRSSSISLEHmTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGH 247
Cdd:MTH00048 160 SINFICTIYSAFMTNVFSRT-SIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 248 PEVYILILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKV 327
Cdd:MTH00048 239 PEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 328 FSWLATLFGMKM-VFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSF 406
Cdd:MTH00048 319 FSWLYMLLNSRVrKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 407 ITGYVLDKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSY 486
Cdd:MTH00048 399 ITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVK 478
|
490 500
....*....|....*....|....*
gi 5834891 487 RLVISDYYSNSSPEYCMSNYVFGHS 511
Cdd:MTH00048 479 NEVLGLWGSSSCVVNVLMSPVPYHN 503
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
14-483 |
1.14e-157 |
|
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: 458.58 E-value: 1.14e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGgFGNWLLPL 93
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 94 MLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTMGH-PGSSVDLAIFSLHAAGLSSILGGINFM 172
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYsPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 173 CTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYI 252
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 253 LILPAFGIVSqSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLA 332
Cdd:cd01662 240 LILPAFGIFS-EIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 333 TLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVL 412
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5834891 413 DKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDV--YSVWNIIASYGSIISTAGLFLFIYVLLESF 483
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGpgWDPLNLISTIGAFLIAAGVLLFLINVIVSI 471
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
22-467 |
1.55e-122 |
|
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: 366.13 E-value: 1.55e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 22 DIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPtMIGGFGNWLLPLMLGAPDMS 101
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 102 FPRLNNLSFWLLPTSMLLILdacFVDMGCGTSWTVYPPLStmghpgsSVDLAIFSLHAAGLSSILGGINFMCTTKNLRSS 181
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLL---ASFGGATTGWTEYPPLV-------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 182 SISLeHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSffdpstGGNPLIYQHLFWFFGHPEVYILILPAFGIV 261
Cdd:pfam00115 150 GMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAFGII 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 262 SQSTLYLTGKKeVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLATLFGMKMVF 341
Cdd:pfam00115 223 YYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 342 N-PLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVLDKLMMSAV 420
Cdd:pfam00115 302 RtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLH 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 5834891 421 FILLFIGVNLTFFPLHFAGLHGFPRKY----LDYPDVYSVWNIIASYGSII 467
Cdd:pfam00115 382 FWLLFIGFNLTFFPMHILGLLGMPRRYappfIETVPAFQPLNWIRTIGGVL 432
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
14-446 |
6.04e-96 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 304.94 E-value: 6.04e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 14 WLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIR----LELAKPGFFLSNGQlYNSVITAHAILMIFFMVMPTMIGgFGNW 89
Cdd:PRK15017 48 WLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRsqqaLASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 90 LLPLMLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTMGH-PGSSVDLAIFSLHAAGLSSILGG 168
Cdd:PRK15017 126 VVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYsPGVGVDYWIWSLQLSGIGTTLTG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 169 INFMCTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHP 248
Cdd:PRK15017 206 INFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 249 EVYILILPAFGIVSQSTLYLTgKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVF 328
Cdd:PRK15017 286 EVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 329 SWLATLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFIT 408
Cdd:PRK15017 365 NWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAF 444
|
410 420 430
....*....|....*....|....*....|....*...
gi 5834891 409 GYVLDKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRK 446
Cdd:PRK15017 445 GFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRR 482
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
27-484 |
1.01e-19 |
|
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: 91.96 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 27 YFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFfmVMPTM-IGGFGNWLLPLMLGAPDMSfPRL 105
Cdd:cd01660 9 HFVVAFLALLLGGLFGLLQVLVRTGVFPLPSSGILYYQGLTLHGVLLAI--VFTTFfIMGFFYAIVARALLRSLFN-RRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 106 NNLSFWLLPTSmlLILDACFVDMGCGTS-WTVYPPLstMGHPGSSVDLAIFSLHaaglSSILGGINFmcttKNLRS--SS 182
Cdd:cd01660 86 AWAGFWLMVIG--TVMAAVPILLGQASVlYTFYPPL--QAHPLFYIGAALVVVG----SWISGFAMF----VTLWRwkKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 183 ISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLtdrnLNTSFFDPSTGgNPLIYQHLFWFFGHPEVYILILPAFGIVS 262
Cdd:cd01660 154 NPGKKVPLATFMVVTTMILWLVASLGVALEVLFQL----LPWSLGLVDTV-DVLLSRTLFWWFGHPLVYFWLLPAYIAWY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 263 QSTLYLTGKKEVFGALGMVYAILSIgLIGCVVWAHHMYT-VGMDLDSRAYFSAATMVIAVPT------------------ 323
Cdd:cd01660 229 TILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSlltaftvfasleiagrlr 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 324 -GVKVFSWLATLFGMKMVFNPLLLWVLGFIflftLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSlGAVFGIFTGVTL 402
Cdd:cd01660 308 gGKGLFGWIRALPWGDPMFLALFLAMLMFI----PGGAGGIINASYQLNYVVHNTAWVPGHFHLTVG-GAVALTFMAVAY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5834891 403 W-WSFITGYVL-DKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRK--YLDYPDVY-----SVWNIIASYGSIISTAGLF 473
Cdd:cd01660 383 WlVPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGA 462
|
490
....*....|.
gi 5834891 474 LFIYVLLESFF 484
Cdd:cd01660 463 LFLYILFRTLL 473
|
|
|