|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 601.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00153 52 YNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00153 132 SNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00153 212 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMF 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00153 292 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGG 350
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-299 |
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: 560.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:cd01663 45 YNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:cd01663 125 SILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:cd01663 205 NFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMF 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:cd01663 285 TVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGG 343
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-299 |
5.52e-125 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 367.15 E-value: 5.52e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:COG0843 57 YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:COG0843 136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:COG0843 216 SLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMF 294
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:COG0843 295 TPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGG 353
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-299 |
3.06e-124 |
|
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: 364.24 E-value: 3.06e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMiGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:TIGR02891 48 YNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:TIGR02891 127 STSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:TIGR02891 207 LFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMF 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:TIGR02891 286 TTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGG 344
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-299 |
2.88e-77 |
|
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: 241.71 E-value: 2.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSfieKGAGTGWTVYPPLs 80
Cdd:pfam00115 41 YNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 sniahegASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMlSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:pfam00115 116 -------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-TLRMPLFVWAILATAILILLAFPVLAAALLLLLLDR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:pfam00115 188 SLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLF 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARIT-YSPTSLWSLGFIFLFTIGG 299
Cdd:pfam00115 261 TTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGG 320
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 601.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00153 52 YNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00153 132 SNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00153 212 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMF 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00153 292 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGG 350
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-299 |
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: 560.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:cd01663 45 YNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:cd01663 125 SILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:cd01663 205 NFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMF 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:cd01663 285 TVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGG 343
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 524.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00167 54 YNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00167 134 GNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00167 214 NLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMF 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00167 294 TVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGG 352
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 521.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00223 51 YNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00223 131 SNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00223 211 NFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMF 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00223 291 TVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGG 349
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 513.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00116 54 YNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00116 134 GNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00116 214 NLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMF 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00116 294 TVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGG 352
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 508.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00142 52 YNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00142 132 SNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00142 212 NFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMF 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00142 292 TVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGG 350
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-299 |
4.60e-165 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 468.61 E-value: 4.60e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00007 51 YNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00007 131 SNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00007 211 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMF 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00007 291 TVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGG 349
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-299 |
2.18e-162 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 461.66 E-value: 2.18e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00103 54 YNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00103 134 GNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00103 214 NLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMF 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00103 294 TVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGG 352
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
8.57e-162 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 460.16 E-value: 8.57e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00183 54 YNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00183 134 GNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00183 214 NLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMF 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00183 294 TVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGG 352
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
2.53e-159 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 453.75 E-value: 2.53e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00079 55 YNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SnIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00079 135 T-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00079 214 NLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMY 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00079 294 TVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGG 352
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
5.85e-159 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 453.13 E-value: 5.85e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00037 54 YNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00037 134 SNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00037 214 NINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMF 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00037 294 TVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGG 352
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
4.79e-158 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 450.55 E-value: 4.79e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00077 54 YNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00077 134 GNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00077 214 NLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMF 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00077 294 TVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGG 352
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
2.48e-152 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 436.56 E-value: 2.48e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00182 56 YNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00182 136 SIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00182 216 NFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMF 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00182 296 TVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGG 354
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
2.28e-149 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 428.86 E-value: 2.28e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00184 56 YNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00184 136 SIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00184 216 NFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMF 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00184 296 TVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGG 354
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
3.69e-135 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 393.22 E-value: 3.69e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00026 55 YNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00026 135 SIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00026 215 NFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMY 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGA--RITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00026 295 VVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGG 355
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-299 |
5.38e-129 |
|
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: 374.95 E-value: 5.38e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPlMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:cd00919 43 YNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:cd00919 122 TLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:cd00919 202 NFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMF 280
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:cd00919 281 TVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGG 339
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-299 |
5.52e-125 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 367.15 E-value: 5.52e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:COG0843 57 YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:COG0843 136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:COG0843 216 SLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMF 294
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:COG0843 295 TPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGG 353
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-299 |
3.06e-124 |
|
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: 364.24 E-value: 3.06e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMiGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:TIGR02891 48 YNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:TIGR02891 127 STSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:TIGR02891 207 LFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMF 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:TIGR02891 286 TTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGG 344
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-299 |
1.61e-119 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 352.44 E-value: 1.61e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIekGAGTGWTVYPPLS 80
Cdd:MTH00048 55 YNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGmLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00048 133 SSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN-VFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00048 212 NFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMF 291
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYS-PTSLWSLGFIFLFTIGG 299
Cdd:MTH00048 292 TVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGG 351
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-299 |
8.01e-111 |
|
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: 329.93 E-value: 8.01e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:cd01662 49 YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:cd01662 128 GLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:cd01662 208 YFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMF 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:cd01662 287 TTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGG 345
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-299 |
2.88e-77 |
|
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: 241.71 E-value: 2.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSfieKGAGTGWTVYPPLs 80
Cdd:pfam00115 41 YNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 sniahegASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMlSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:pfam00115 116 -------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-TLRMPLFVWAILATAILILLAFPVLAAALLLLLLDR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:pfam00115 188 SLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLF 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARIT-YSPTSLWSLGFIFLFTIGG 299
Cdd:pfam00115 261 TTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGG 320
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-299 |
1.52e-75 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 243.30 E-value: 1.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESgKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFF 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:PRK15017 337 TMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGG 395
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-299 |
3.85e-73 |
|
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: 236.67 E-value: 3.85e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:TIGR02882 92 YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:TIGR02882 171 GPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDR 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESgKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:TIGR02882 251 IFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFF 329
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911482 241 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:TIGR02882 330 TMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGG 388
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
1-278 |
4.12e-04 |
|
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: 41.50 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 1 YNTIVTAHAFIM-IFFMVMPIMigGFGNWLIPLMLGAPDMAfPRLNNMSFWLLPPSLTLLLMSSFIEKgAGTGWTVYPPL 79
Cdd:cd01660 44 YYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN-RRLAWAGFWLMVIGTVMAAVPILLGQ-ASVLYTFYPPL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 80 ssnIAHEGASVDLAIFSLHmagiSSILGAINFITTA-YNMRPSGmlsERMTLFIWAVSITAIL-LLFSLPVlagAITMLL 157
Cdd:cd01660 120 ---QAHPLFYIGAALVVVG----SWISGFAMFVTLWrWKKANPG---KKVPLATFMVVTTMILwLVASLGV---ALEVLF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911482 158 tdRNINTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAH 237
Cdd:cd01660 187 --QLLPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGK-LFSDPLARLAFILFLLFSTPVGFH 262
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2315911482 238 HMFT-VGMDVDTRAYFTSATMIIAVPTGIKIFSWLATF-HGAR 278
Cdd:cd01660 263 HQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeIAGR 305
|
|
|