|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
1-204 |
4.64e-132 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 369.11 E-value: 4.64e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 1 MATDTLTHATAHAHEHGHHDAGGTKIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSS 80
Cdd:PRK10663 1 MATDTLTHATAHAHEHGHHDAGATKVFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 81 ITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVL 160
Cdd:PRK10663 81 ITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHHLIVEGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16128415 161 MVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
Cdd:PRK10663 161 MVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
25-204 |
2.54e-106 |
|
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131889 Cd Length: 180 Bit Score: 303.02 E-value: 2.54e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 25 KIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLAL 104
Cdd:TIGR02842 1 TIFGFWLYLMSDCILFATLFATYAVLSNNTAGGPSGKEIFDLPFVLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 105 TWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFW 184
Cdd:TIGR02842 81 TFLLGLGFIGMEIYEFYHLIAEGNGPDRSAFLSAFFTLVGTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFW 160
|
170 180
....*....|....*....|
gi 16128415 185 HFLDVVWICVFTVVYLMGAM 204
Cdd:TIGR02842 161 HFLDIVWICVFTFVYLLGVL 180
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
17-202 |
1.55e-103 |
|
Ubiquinol oxidase subunit III subfamily. 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. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.
Pssm-ID: 239214 Cd Length: 186 Bit Score: 296.07 E-value: 1.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 17 GHHDAGGTKIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKS 96
Cdd:cd02863 1 HHTNTGSKKILGFWIYLMSDCILFATLFATYAVLSGNTAGGPPGHELFELPLVFIETFLLLLSSFTCGLAMIAMNKNNKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 97 QVISWLALTWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTR 176
Cdd:cd02863 81 KVILWLIITFLLGLGFVGMEIYEFHHLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARR 160
|
170 180
....*....|....*....|....*.
gi 16128415 177 IMCLSLFWHFLDVVWICVFTVVYLMG 202
Cdd:cd02863 161 LFCLSLFWHFLDIVWIFVFTVVYLLG 186
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
11-201 |
6.25e-71 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 213.56 E-value: 6.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 11 AHAHEHGH-HDAGGTKIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIA 89
Cdd:COG1845 1 AHDVEAPHaPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPDWPAGAELLDLPLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 90 MYKNNKSQVISWLALTWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGL 169
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 16128415 170 TSTNRTRIMCLSLFWHFLDVVWICVFTVVYLM 201
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
16-202 |
1.17e-11 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 62.04 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 16 HGHHDAGGTK--IFGFWIYLMSDCILFSILFATY---AVLVNGTAGG---PTGK---DIFELPfvLVETFLLLFSSITYG 84
Cdd:pfam00510 65 LGDHTFAVQKglNLGMILFIISEVFFFLGIFWAFfhsALSPTVELGAqwpPVGIhpvNPFEVP--LLNTIILLSSGVTVT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 85 MAAIAMYKNNKSQVISWLALTWLFGAGFIGMEIYEFHhliVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQI 164
Cdd:pfam00510 143 YAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYT---EASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRL 219
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128415 165 ARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
Cdd:pfam00510 220 LKYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYWWG 257
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
1-204 |
4.64e-132 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 369.11 E-value: 4.64e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 1 MATDTLTHATAHAHEHGHHDAGGTKIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSS 80
Cdd:PRK10663 1 MATDTLTHATAHAHEHGHHDAGATKVFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 81 ITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVL 160
Cdd:PRK10663 81 ITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHHLIVEGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16128415 161 MVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
Cdd:PRK10663 161 MVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
25-204 |
2.54e-106 |
|
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131889 Cd Length: 180 Bit Score: 303.02 E-value: 2.54e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 25 KIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLAL 104
Cdd:TIGR02842 1 TIFGFWLYLMSDCILFATLFATYAVLSNNTAGGPSGKEIFDLPFVLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 105 TWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFW 184
Cdd:TIGR02842 81 TFLLGLGFIGMEIYEFYHLIAEGNGPDRSAFLSAFFTLVGTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFW 160
|
170 180
....*....|....*....|
gi 16128415 185 HFLDVVWICVFTVVYLMGAM 204
Cdd:TIGR02842 161 HFLDIVWICVFTFVYLLGVL 180
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
17-202 |
1.55e-103 |
|
Ubiquinol oxidase subunit III subfamily. 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. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.
Pssm-ID: 239214 Cd Length: 186 Bit Score: 296.07 E-value: 1.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 17 GHHDAGGTKIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKS 96
Cdd:cd02863 1 HHTNTGSKKILGFWIYLMSDCILFATLFATYAVLSGNTAGGPPGHELFELPLVFIETFLLLLSSFTCGLAMIAMNKNNKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 97 QVISWLALTWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTR 176
Cdd:cd02863 81 KVILWLIITFLLGLGFVGMEIYEFHHLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARR 160
|
170 180
....*....|....*....|....*.
gi 16128415 177 IMCLSLFWHFLDVVWICVFTVVYLMG 202
Cdd:cd02863 161 LFCLSLFWHFLDIVWIFVFTVVYLLG 186
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
11-201 |
6.25e-71 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 213.56 E-value: 6.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 11 AHAHEHGH-HDAGGTKIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIA 89
Cdd:COG1845 1 AHDVEAPHaPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPDWPAGAELLDLPLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 90 MYKNNKSQVISWLALTWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGL 169
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 16128415 170 TSTNRTRIMCLSLFWHFLDVVWICVFTVVYLM 201
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
18-201 |
1.14e-52 |
|
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.
Pssm-ID: 238227 Cd Length: 183 Bit Score: 167.00 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 18 HHDAGGTKIFGFWIYLMSDCILFSILFATYAVLVNGTAGGP-TGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKS 96
Cdd:cd00386 2 TASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFgAGLDPLDLPLLNTNTLLLSGSSVTWAHASLAARRGNRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 97 QVISWLALTWLFGAGFIGMEIYEFHHLIVngmGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTR 176
Cdd:cd00386 82 KARLWLLLTILLGLAFLGLQAYEYSHLIF---TISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFTPRHHLG 158
|
170 180
....*....|....*....|....*
gi 16128415 177 IMCLSLFWHFLDVVWICVFTVVYLM 201
Cdd:cd00386 159 LEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
22-202 |
5.31e-51 |
|
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III 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: 131943 Cd Length: 190 Bit Score: 163.10 E-value: 5.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 22 GGTKIFGFWIYLMSDCILFSILFATYAVLVN-GTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVIS 100
Cdd:TIGR02897 7 GRLNILGFWIFLGAEIALFATLFATYLVLQHgGDYAGKMPAELFELPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 101 WLALTWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCL 180
Cdd:TIGR02897 87 WMIITLLLGAGFVGFEIYEFAHYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIV 166
|
170 180
....*....|....*....|..
gi 16128415 181 SLFWHFLDVVWICVFTVVYLMG 202
Cdd:TIGR02897 167 SLYWHFLDVVWVFIFTAVYLIG 188
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
27-201 |
2.92e-26 |
|
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.
Pssm-ID: 239213 Cd Length: 186 Bit Score: 99.23 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 27 FGFWIYLMSDCILFSILFATYAV-LVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALT 105
Cdd:cd02862 11 LGMWVFILSELLAFGALFIAYAVyRALYPELFAAGSAHLDLLLGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 106 WLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWH 185
Cdd:cd02862 91 VLLGLVFLVIKYFEYAHKIAAGIDPDAGLFFTLYFLLTGFHLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWH 170
|
170
....*....|....*.
gi 16128415 186 FLDVVWICVFTVVYLM 201
Cdd:cd02862 171 MVDLVWIVLFPLLYLV 186
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
27-201 |
4.34e-26 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239215 Cd Length: 202 Bit Score: 99.50 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 27 FGFWIYLMSDCILFSILFATYA-VLVNGTAGGPTGKDIFELP---------FVLVETFLLLFSSITYGMAAIAMYKNNKS 96
Cdd:cd02864 11 AMMWFFLLSDAFIFSSFLIAYMtARISTTEPWPLPSDVFALRighfniplvLIAIMTFILITSSGTMAMAVNFGYRGNRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 97 QVISWLALTWLFGAGFIGMEIYEFHHLIVN-GMGP-----DRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLT 170
Cdd:cd02864 91 AAARLMLATALLGATFVGMQAFEWTKLIVEeGVRPwgnpwGAAQFGASFFMITGFHGTHVTIGVIYLIIIARKVWRGKYQ 170
|
170 180 190
....*....|....*....|....*....|..
gi 16128415 171 STNRTRIM-CLSLFWHFLDVVWICVFTVVYLM 201
Cdd:cd02864 171 RIGRYEIVeIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
57-199 |
1.56e-18 |
|
Cytochrome c oxidase subunit III. 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. CcO 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, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. 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 III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.
Pssm-ID: 238834 Cd Length: 243 Bit Score: 80.25 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 57 GPTGKDIFELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIGMEIYEFHHlivNGMGPDRSGFL 136
Cdd:cd01665 104 GIEPLNPFGIP--LLNTIILLSSGATVTWAHHALLLGNRKKAILGLILTILLGVYFTGLQAYEYYE---ASFTISDSVYG 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128415 137 SAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVY 199
Cdd:cd01665 179 STFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGFEAAIWYWHFVDVVWLFLFVFVY 241
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
19-199 |
3.67e-18 |
|
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). 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. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.
Pssm-ID: 239216 Cd Length: 184 Bit Score: 78.18 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 19 HDAGGTKIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPtGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKSQV 98
Cdd:cd02865 3 AGARSPGWWGLWVFMAVEGTLFALLISAYFMRMTSGDWQP-GAPLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 99 ISWLALTWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIM 178
Cdd:cd02865 82 RLGLALAGALALAFLAGQLLAWHALNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVE 161
|
170 180
....*....|....*....|.
gi 16128415 179 CLSLFWHFLDVVWICVFTVVY 199
Cdd:cd02865 162 LCALYWHFLLLVWLVLLALLY 182
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
57-203 |
3.55e-12 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 63.24 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 57 GPTGKDIFELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFI---GMEIYEFHHLIVNGMgpdrs 133
Cdd:MTH00130 120 GITTLDPFEVP--LLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTflqAMEYYEAPFTIADGV----- 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 134 gFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
Cdd:MTH00130 193 -YGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
26-200 |
8.83e-12 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 61.47 E-value: 8.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 26 IFGFWIYLMSDCILFSILFATYAVLVNGTAGgpTGKDIFELPFVlvETFLLLFSSITygmaaIAMYKNNKSQVISW--LA 103
Cdd:MTH00049 54 ESAFWLFILSEVIIFGSLLVCCLWFDDWSYI--SLSSSLEIPFV--GCFLLLGSSIT-----VTAYHHLLGWKYCDlfLY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 104 LTWLFGAGFIGMEIYEFHHLIVNGMgpdRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQiarrGLTSTNRTRIMCLSLF 183
Cdd:MTH00049 125 LTILLGLLFVVLQVFEFEESGVNSL---DSSYYASCFCTVGLHFSHVVLGVVGLSTLLLV----GSSSFGVYRSTVLTWY 197
|
170
....*....|....*..
gi 16128415 184 WHFLDVVWICVFTVVYL 200
Cdd:MTH00049 198 WHFVDYIWLLVYLIVYV 214
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
16-202 |
1.17e-11 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 62.04 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 16 HGHHDAGGTK--IFGFWIYLMSDCILFSILFATY---AVLVNGTAGG---PTGK---DIFELPfvLVETFLLLFSSITYG 84
Cdd:pfam00510 65 LGDHTFAVQKglNLGMILFIISEVFFFLGIFWAFfhsALSPTVELGAqwpPVGIhpvNPFEVP--LLNTIILLSSGVTVT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 85 MAAIAMYKNNKSQVISWLALTWLFGAGFIGMEIYEFHhliVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQI 164
Cdd:pfam00510 143 YAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYT---EASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRL 219
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128415 165 ARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
Cdd:pfam00510 220 LKYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
64-202 |
2.75e-10 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 57.98 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIG---MEIYEFHHLIVNGMgpdrsgFLSAFF 140
Cdd:MTH00141 125 FQVP--LLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTFlqaGEYYEASFSIADGV------YGSTFF 196
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128415 141 ALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
Cdd:MTH00141 197 VLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 258
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
93-203 |
1.11e-09 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 56.61 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 93 NNKSQVISWLALTWLFGAGFIGMEIYEFHHlivNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTST 172
Cdd:MTH00028 190 DFRTNAVIGLLMTILLGIIFTGLQAFEYKE---ASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQFTNS 266
|
90 100 110
....*....|....*....|....*....|.
gi 16128415 173 NRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
Cdd:MTH00028 267 HHLGLEAAIWYWHFVDVVWLFLYVFVYWWGS 297
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
57-203 |
2.18e-09 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 55.52 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 57 GPTGKDIFELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFI---GMEIYEFHHLIVNGMgpdrs 133
Cdd:MTH00075 120 GITPLDPFEVP--LLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTllqAMEYYEAPFTIADGV----- 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 134 gFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
Cdd:MTH00075 193 -YGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
64-203 |
6.24e-09 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 54.19 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIG---MEIYEFHHLIVNGMgpdrsgFLSAFF 140
Cdd:MTH00118 127 FEVP--LLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTAlqaMEYYEAPFTISDSV------YGSTFF 198
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128415 141 ALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
Cdd:MTH00118 199 VATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
70-203 |
1.23e-08 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 53.22 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIG---MEIYEFHHLIVNgmgpdrSGFLSAFFALVGTH 146
Cdd:MTH00024 131 LLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGlqaIEYYEAPFAISD------SVYGSTFFVATGFH 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128415 147 GLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
Cdd:MTH00024 205 GLHVIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
70-202 |
1.26e-08 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 53.19 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIGMEIYEFhhlIVNGMGPDRSGFLSAFFALVGTHGLH 149
Cdd:MTH00039 130 LLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEY---YDAPFTIADSVYGSTFFVATGFHGLH 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 16128415 150 VTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
Cdd:MTH00039 207 VIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVDVVWLFLYVCIYWWG 259
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
62-202 |
1.35e-08 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 53.05 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 62 DIFELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIG---MEIYEFHHLIVNGMgpdrsgFLSA 138
Cdd:MTH00189 124 NPFEVP--LLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLlqaMEYYEAPFTIADSV------YGST 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128415 139 FFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMG 202
Cdd:MTH00189 196 FFVATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 259
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
64-199 |
1.51e-08 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 52.88 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 64 FELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIGMEIYEFHHLIVNgmgPDRSGFLSAFFALV 143
Cdd:MTH00155 125 FQIP--LLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEAPFT---IADSVYGSTFFMAT 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128415 144 GTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVY 199
Cdd:MTH00155 200 GFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
62-203 |
5.34e-08 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 51.33 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 62 DIFELPfvLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFI---GMEIYEFHHLIVNgmgpdrSGFLSA 138
Cdd:MTH00052 126 NPFSVP--LLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTglqAMEYYEAPFTISD------SVYGST 197
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128415 139 FFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
Cdd:MTH00052 198 FFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
70-203 |
1.12e-07 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 50.61 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIGMEIYEFhhlIVNGMGPDRSGFLSAFFALVGTHGLH 149
Cdd:MTH00009 129 LLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEY---IEAPFTIADSVYGSTFFVATGFHGLH 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 16128415 150 VTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
Cdd:MTH00009 206 VLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFVDVVWIFLYLCIYWWGS 259
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
70-203 |
1.38e-07 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 50.50 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFI---GMEIYEFHHLIVNGMgpdrsgFLSAFFALVGTH 146
Cdd:MTH00099 131 LLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTllqASEYYEAPFTISDGI------YGSTFFMATGFH 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128415 147 GLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
Cdd:MTH00099 205 GLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
70-199 |
4.41e-07 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 48.80 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISwLALTWLFGAGFIGMEIYEFHHlivNGMGPDRSGFLSAFFALVGTHGLH 149
Cdd:MTH00083 127 LLNTIILLSSGVSVTWSHHSLCLSNKSCTNS-LLLTCFLGLYFTSFQLMEYKE---ASFSISDSIYGSIFYLGTGFHGIH 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 16128415 150 VTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVY 199
Cdd:MTH00083 203 VLCGGLFLLFNLLRLLKSHFNYNHHLGLEFAILYWHFVDVVWLFLFVFVY 252
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
70-203 |
1.42e-06 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 47.47 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 70 LVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFI---GMEIYEFHHLIVNgmgpdrSGFLSAFFALVGTH 146
Cdd:MTH00219 132 LLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTmlqGMEYLEASFSISD------SVYGTTFFVATGFH 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128415 147 GLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGA 203
Cdd:MTH00219 206 GLHVIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 262
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
62-204 |
1.78e-06 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 46.97 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128415 62 DIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKS--QVISWLALTWLFgAGFIGMEIYEFHHLIVNGMgpdrsgFLSAF 139
Cdd:PLN02194 128 DPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAvyALVATVLLALVF-TGFQGMEYYQAPFTISDSI------YGSTF 200
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128415 140 FALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
Cdd:PLN02194 201 FLATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWWGGI 265
|
|
| |
