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Conserved domains on  [gi|5834891|ref|NP_006961|]
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cytochrome c oxidase subunit I (mitochondrion) [Caenorhabditis elegans]

Protein Classification

cytochrome-c oxidase subunit 1( domain architecture ID 10009556)

cytochrome-c oxidase subunit 1 is the catalytic subunit of cytochrome c oxidase, which is the component of the respiratory chain that catalyzes the reduction of oxygen to water

Graphical summary

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List of domain hits

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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