|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-355 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 716.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00153 128 PPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITML 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00153 208 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00153 288 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHD 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00153 368 TYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTS 447
|
330 340 350
....*....|....*....|....*....|....*
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQTIMF 355
Cdd:MTH00153 448 WNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-355 |
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: 637.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:cd01663 121 PPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITML 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:cd01663 201 LTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:cd01663 281 HHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHD 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:cd01663 361 TYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAG 440
|
330 340 350
....*....|....*....|....*....|....*
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQTIMF 355
Cdd:cd01663 441 WNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIF 475
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-347 |
1.06e-146 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 424.93 E-value: 1.06e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:COG0843 132 PPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:COG0843 212 LLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:COG0843 291 HHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHD 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAY 318
Cdd:COG0843 371 TYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGW 450
|
330 340
....*....|....*....|....*....
gi 970839841 319 MSWNVMSSMGSTISIVGILMFIFIVWESM 347
Cdd:COG0843 451 QPLNLISTIGAFILAVGFLLFLINLVVSL 479
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-347 |
4.05e-145 |
|
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: 419.71 E-value: 4.05e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:TIGR02891 123 PPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:TIGR02891 203 LLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:TIGR02891 282 HHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHD 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDA--Y 318
Cdd:TIGR02891 362 TYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgF 441
|
330 340
....*....|....*....|....*....
gi 970839841 319 MSWNVMSSMGSTISIVGILMFIFIVWESM 347
Cdd:TIGR02891 442 ATLNLISTIGAFILAAGFLVFLWNLIWSL 470
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
14-331 |
7.33e-96 |
|
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: 291.40 E-value: 7.33e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 14 VDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLdQTPLFVWSVMITALLLLLSLPVLAGAITMLLTDRNLNtsffdp 93
Cdd:pfam00115 118 VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 94 AGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTR 173
Cdd:pfam00115 191 AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 174 AYFTSATMIIAVPTGIKVFSWLATLYGTKFKFN-PPLLWAIGFIFLFTIGGLTGLILANSSLDIILHDTYYVVAHFHYVL 252
Cdd:pfam00115 270 ALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 253 SMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYS----DYPDAYMSWNVMSSMG 328
Cdd:pfam00115 350 FGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIG 429
|
...
gi 970839841 329 STI 331
Cdd:pfam00115 430 GVL 432
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-355 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 716.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00153 128 PPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITML 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00153 208 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00153 288 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHD 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00153 368 TYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTS 447
|
330 340 350
....*....|....*....|....*....|....*
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQTIMF 355
Cdd:MTH00153 448 WNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-355 |
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: 637.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:cd01663 121 PPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITML 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:cd01663 201 LTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:cd01663 281 HHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHD 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:cd01663 361 TYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAG 440
|
330 340 350
....*....|....*....|....*....|....*
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQTIMF 355
Cdd:cd01663 441 WNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIF 475
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-354 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 602.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00116 130 PPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITML 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00116 210 LTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00116 290 HHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00116 370 TYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL 449
|
330 340 350
....*....|....*....|....*....|....
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQTIM 354
Cdd:MTH00116 450 WNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVL 483
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-355 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 601.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00223 127 PPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITML 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00223 207 LTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00223 287 HHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHD 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00223 367 TYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTK 446
|
330 340 350
....*....|....*....|....*....|....*
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQTIMF 355
Cdd:MTH00223 447 WNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-351 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 598.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00167 130 PPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITML 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00167 210 LTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00167 290 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00167 370 TYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL 449
|
330 340 350
....*....|....*....|....*....|.
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQ 351
Cdd:MTH00167 450 WNVVSSIGSLISLVAVILFLFIIWEAFSSKR 480
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-355 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 594.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00142 128 PPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITML 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00142 208 LTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00142 288 HHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHD 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00142 368 TYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTT 447
|
330 340 350
....*....|....*....|....*....|....*
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQTIMF 355
Cdd:MTH00142 448 WNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMW 482
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-354 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 534.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00007 127 PPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITML 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00007 207 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00007 287 HHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHD 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00007 367 TYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTK 446
|
330 340 350
....*....|....*....|....*....|....
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQTIM 354
Cdd:MTH00007 447 WNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVI 480
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-355 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 532.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00103 130 PPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITML 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00103 210 LTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00103 290 HHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00103 370 TYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTT 449
|
330 340 350
....*....|....*....|....*....|....*
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQTIMF 355
Cdd:MTH00103 450 WNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLT 484
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-355 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 527.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00183 130 PPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITML 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00183 210 LTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00183 290 HHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00183 370 TYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL 449
|
330 340 350
....*....|....*....|....*....|....*
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQTIMF 355
Cdd:MTH00183 450 WNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-355 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 527.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00037 130 PPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITML 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00037 210 LTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00037 290 HHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00037 370 TYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL 449
|
330 340 350
....*....|....*....|....*....|....*
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQTIMF 355
Cdd:MTH00037 450 WNTVSSIGSTISLVATLFFLFLIWEAFASQREVIS 484
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-353 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 522.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00077 130 PPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITML 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00077 210 LTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00077 290 HHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00077 370 TYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL 449
|
330 340 350
....*....|....*....|....*....|...
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQTI 353
Cdd:MTH00077 450 WNTVSSIGSLISLVAVIMMMFIIWEAFSSKREV 482
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-354 |
3.44e-176 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 498.82 E-value: 3.44e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSgAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00079 131 PPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITML 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00079 210 LTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00079 290 HHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00079 370 TYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSV 449
|
330 340 350
....*....|....*....|....*....|....
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMISNQTIM 354
Cdd:MTH00079 450 WNVISSYGSMISVFALFLFIYVLLESFFSYRLVL 483
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-349 |
4.00e-172 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 489.33 E-value: 4.00e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00182 132 PPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITML 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00182 212 LTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00182 292 HHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00182 372 TYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAG 451
|
330 340
....*....|....*....|....*....
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESMIS 349
Cdd:MTH00182 452 WNLVSSLGSIISIVGVVWFIYIIYDAYVR 480
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-346 |
3.83e-168 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 478.94 E-value: 3.83e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00184 132 PPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITML 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00184 212 LTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:MTH00184 292 HHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:MTH00184 372 TYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAG 451
|
330 340
....*....|....*....|....*.
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWES 346
Cdd:MTH00184 452 WNQISSLGSVISIVGVVWFIYIVYDA 477
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-347 |
1.89e-156 |
|
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: 446.98 E-value: 1.89e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:cd00919 118 PPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVML 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:cd00919 198 LLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:cd00919 277 HHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHD 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYMS 320
Cdd:cd00919 357 TYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAP 436
|
330 340
....*....|....*....|....*..
gi 970839841 321 WNVMSSMGSTISIVGILMFIFIVWESM 347
Cdd:cd00919 437 WNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-347 |
1.06e-146 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 424.93 E-value: 1.06e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:COG0843 132 PPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:COG0843 212 LLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:COG0843 291 HHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHD 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAY 318
Cdd:COG0843 371 TYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGW 450
|
330 340
....*....|....*....|....*....
gi 970839841 319 MSWNVMSSMGSTISIVGILMFIFIVWESM 347
Cdd:COG0843 451 QPLNLISTIGAFILAVGFLLFLINLVVSL 479
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-347 |
4.05e-145 |
|
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: 419.71 E-value: 4.05e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:TIGR02891 123 PPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:TIGR02891 203 LLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:TIGR02891 282 HHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHD 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDA--Y 318
Cdd:TIGR02891 362 TYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgF 441
|
330 340
....*....|....*....|....*....
gi 970839841 319 MSWNVMSSMGSTISIVGILMFIFIVWESM 347
Cdd:TIGR02891 442 ATLNLISTIGAFILAAGFLVFLWNLIWSL 470
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-346 |
7.27e-145 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 420.19 E-value: 7.27e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00026 131 PPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITML 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00026 211 LTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGT--KFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIIL 238
Cdd:MTH00026 291 HHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 239 HDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAY 318
Cdd:MTH00026 371 HDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNF 450
|
330 340
....*....|....*....|....*...
gi 970839841 319 MSWNVMSSMGSTISIVGILMFIFIVWES 346
Cdd:MTH00026 451 EDFNQISSFGSIISIIAVIWFIVVIFDA 478
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-349 |
1.85e-131 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 385.18 E-value: 1.85e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLdQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:MTH00048 129 PPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITML 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:MTH00048 208 LFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLL-WAIGFIFLFTIGGLTGLILANSSLDIILH 239
Cdd:MTH00048 288 HHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLH 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 240 DTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYM 319
Cdd:MTH00048 368 DTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYY 447
|
330 340 350
....*....|....*....|....*....|
gi 970839841 320 SWNVMSSMGSTISIVGILMFIFIVWESMIS 349
Cdd:MTH00048 448 WINVVCTVGSFISAFSGCFFVFILWESLVV 477
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-347 |
8.27e-127 |
|
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: 373.07 E-value: 8.27e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:cd01662 124 PPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:cd01662 204 ELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:cd01662 283 HHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHD 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAY 318
Cdd:cd01662 363 TYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGW 442
|
330 340
....*....|....*....|....*....
gi 970839841 319 MSWNVMSSMGSTISIVGILMFIFIVWESM 347
Cdd:cd01662 443 DPLNLISTIGAFLIAAGVLLFLINVIVSI 471
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
14-331 |
7.33e-96 |
|
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: 291.40 E-value: 7.33e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 14 VDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLdQTPLFVWSVMITALLLLLSLPVLAGAITMLLTDRNLNtsffdp 93
Cdd:pfam00115 118 VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 94 AGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTR 173
Cdd:pfam00115 191 AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 174 AYFTSATMIIAVPTGIKVFSWLATLYGTKFKFN-PPLLWAIGFIFLFTIGGLTGLILANSSLDIILHDTYYVVAHFHYVL 252
Cdd:pfam00115 270 ALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 253 SMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYS----DYPDAYMSWNVMSSMG 328
Cdd:pfam00115 350 FGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIG 429
|
...
gi 970839841 329 STI 331
Cdd:pfam00115 430 GVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-346 |
2.44e-78 |
|
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131928 Cd Length: 643 Bit Score: 252.47 E-value: 2.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 2 PLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITMLL 81
Cdd:TIGR02882 168 PLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMT 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 82 TDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAH 161
Cdd:TIGR02882 248 TDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVH 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 162 HMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHDT 241
Cdd:TIGR02882 327 HFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNT 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 242 YYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDY--PDAYM 319
Cdd:TIGR02882 407 YFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWF 486
|
330 340
....*....|....*....|....*..
gi 970839841 320 SWNVMSSMGSTISIVGILMFIFIVWES 346
Cdd:TIGR02882 487 PLNLISTIGALLMAIGFIFLVYNIYYS 513
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-347 |
1.39e-75 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 245.62 E-value: 1.39e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 1 PPLSGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTAINMRSKKMTLDQTPLFVWSVMITALLLLLSLPVLAGAITML 80
Cdd:PRK15017 174 PPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 81 LTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWA 160
Cdd:PRK15017 254 TLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 161 HHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHD 240
Cdd:PRK15017 333 HHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 241 TYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLIMNNKWLKIQFMIMFIGVNMTFFPQHFLGLAGMPRRYSDYPD-AYM 319
Cdd:PRK15017 413 SLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFH 492
|
330 340
....*....|....*....|....*...
gi 970839841 320 SWNVMSSMGSTISIVGILMFIFIVWESM 347
Cdd:PRK15017 493 TMLMIAASGAALIALGILCQVIQMYVSI 520
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
98-347 |
1.42e-18 |
|
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: 86.57 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 98 DPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIgLMGFIVWAHHMFT-VGMDVDTRAYF 176
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFAdPGIGPGWKFIH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 177 TSATMIIAVPTGIKVFSWLAT------------LYGTKFKF---NPPLLWAIGFIFLFTIGGLTGLILANSSLDIILHDT 241
Cdd:cd01660 279 MVLTFMVALPSLLTAFTVFASleiagrlrggkgLFGWIRALpwgDPMFLALFLAMLMFIPGGAGGIINASYQLNYVVHNT 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839841 242 YYVVAHFHyvLSMGAVFAIMG-GIIQWY-PLFTGLIMNNKWL-KIQFMIMFIGVNMTFFPQHFLGLAGMPRR--YSDYPD 316
Cdd:cd01660 359 AWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGG 436
|
250 260 270
....*....|....*....|....*....|....*.
gi 970839841 317 AYM-----SWNVMSSMGSTISIVGILMFIFIVWESM 347
Cdd:cd01660 437 LPAagewaPYQQLMAIGGTILFVSGALFLYILFRTL 472
|
|
|