|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
1-205 |
3.22e-132 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 369.50 E-value: 3.22e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 1 MSTESINHELAHgSHEHGHHDAGANKVFGFWIYLMSDCILFACLFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFS 80
Cdd:PRK10663 1 MATDTLTHATAH-AHEHGHHDAGATKVFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 81 SITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFVAMEIYEFHHLIAEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVV 160
Cdd:PRK10663 80 SITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHHLIVEGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490522312 161 MMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMGAM 205
Cdd:PRK10663 160 LMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
26-205 |
3.63e-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: 302.64 E-value: 3.63e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 26 KVFGFWIYLMSDCILFACLFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLAL 105
Cdd:TIGR02842 1 TIFGFWLYLMSDCILFATLFATYAVLSNNTAGGPSGKEIFDLPFVLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 106 TFLFGAGFVAMEIYEFHHLIAEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFW 185
Cdd:TIGR02842 81 TFLLGLGFIGMEIYEFYHLIAEGNGPDRSAFLSAFFTLVGTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFW 160
|
170 180
....*....|....*....|
gi 490522312 186 HFLDVVWICVFSVVYLMGAM 205
Cdd:TIGR02842 161 HFLDIVWICVFTFVYLLGVL 180
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
18-203 |
3.25e-105 |
|
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: 300.31 E-value: 3.25e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 18 GHHDAGANKVFGFWIYLMSDCILFACLFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAMIAMNNNKQS 97
Cdd:cd02863 1 HHTNTGSKKILGFWIYLMSDCILFATLFATYAVLSGNTAGGPPGHELFELPLVFIETFLLLLSSFTCGLAMIAMNKNNKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 98 QVMSWLALTFLFGAGFVAMEIYEFHHLIAEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRAR 177
Cdd:cd02863 81 KVILWLIITFLLGLGFVGMEIYEFHHLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARR 160
|
170 180
....*....|....*....|....*.
gi 490522312 178 LMCLSMFWHFLDVVWICVFSVVYLMG 203
Cdd:cd02863 161 LFCLSLFWHFLDIVWIFVFTVVYLLG 186
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
11-202 |
1.28e-73 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 220.49 E-value: 1.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 11 AHGSHEHGHHDAGANKVFGFWIYLMSDCILFACLFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAMIA 90
Cdd:COG1845 1 AHDVEAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPDWPAGAELLDLPLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 91 MNNNKQSQVMSWLALTFLFGAGFVAMEIYEFHHLIAEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGL 170
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 490522312 171 THNNRARLMCLSMFWHFLDVVWICVFSVVYLM 202
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
17-203 |
1.28e-11 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 61.66 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 17 HGHHDAGANK--VFGFWIYLMSDCILFACLFATY---AVLVNGTAGG---PTGK---DIFELPfvLVETFLLLFSSITYG 85
Cdd:pfam00510 65 LGDHTFAVQKglNLGMILFIISEVFFFLGIFWAFfhsALSPTVELGAqwpPVGIhpvNPFEVP--LLNTIILLSSGVTVT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 86 MAMIAMNNNKQSQVMSWLALTFLFGAGFVAMEIYEFHHliaEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHV 165
Cdd:pfam00510 143 YAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTE---ASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRL 219
|
170 180 190
....*....|....*....|....*....|....*...
gi 490522312 166 SRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMG 203
Cdd:pfam00510 220 LKYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYWWG 257
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10663 |
PRK10663 |
cytochrome o ubiquinol oxidase subunit III; Provisional |
1-205 |
3.22e-132 |
|
cytochrome o ubiquinol oxidase subunit III; Provisional
Pssm-ID: 182628 Cd Length: 204 Bit Score: 369.50 E-value: 3.22e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 1 MSTESINHELAHgSHEHGHHDAGANKVFGFWIYLMSDCILFACLFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFS 80
Cdd:PRK10663 1 MATDTLTHATAH-AHEHGHHDAGATKVFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 81 SITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFVAMEIYEFHHLIAEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVV 160
Cdd:PRK10663 80 SITYGMAAIAMYKNNKSQVISWLALTFLFGAGFIGMEIYEFHHLIVEGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490522312 161 MMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMGAM 205
Cdd:PRK10663 160 LMVQVARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM 204
|
|
| CyoC |
TIGR02842 |
cytochrome o ubiquinol oxidase, subunit III; Cytochrome o terminal oxidase complex is the ... |
26-205 |
3.63e-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: 302.64 E-value: 3.63e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 26 KVFGFWIYLMSDCILFACLFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLAL 105
Cdd:TIGR02842 1 TIFGFWLYLMSDCILFATLFATYAVLSNNTAGGPSGKEIFDLPFVLVETFLLLLSSITFGFAMLAMNKKNKKMVILWLAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 106 TFLFGAGFVAMEIYEFHHLIAEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFW 185
Cdd:TIGR02842 81 TFLLGLGFIGMEIYEFYHLIAEGNGPDRSAFLSAFFTLVGTHGLHVTSGLIWIIVMIIQVYKYGLTKINRRRLACLSLFW 160
|
170 180
....*....|....*....|
gi 490522312 186 HFLDVVWICVFSVVYLMGAM 205
Cdd:TIGR02842 161 HFLDIVWICVFTFVYLLGVL 180
|
|
| Ubiquinol_oxidase_III |
cd02863 |
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ... |
18-203 |
3.25e-105 |
|
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: 300.31 E-value: 3.25e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 18 GHHDAGANKVFGFWIYLMSDCILFACLFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAMIAMNNNKQS 97
Cdd:cd02863 1 HHTNTGSKKILGFWIYLMSDCILFATLFATYAVLSGNTAGGPPGHELFELPLVFIETFLLLLSSFTCGLAMIAMNKNNKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 98 QVMSWLALTFLFGAGFVAMEIYEFHHLIAEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRAR 177
Cdd:cd02863 81 KVILWLIITFLLGLGFVGMEIYEFHHLIAEGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLKKRGLTPDTARR 160
|
170 180
....*....|....*....|....*.
gi 490522312 178 LMCLSMFWHFLDVVWICVFSVVYLMG 203
Cdd:cd02863 161 LFCLSLFWHFLDIVWIFVFTVVYLLG 186
|
|
| CyoC |
COG1845 |
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion]; |
11-202 |
1.28e-73 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
Pssm-ID: 441450 Cd Length: 192 Bit Score: 220.49 E-value: 1.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 11 AHGSHEHGHHDAGANKVFGFWIYLMSDCILFACLFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAMIA 90
Cdd:COG1845 1 AHDVEAPHAPERRSPGKLGMWLFLASEVMLFAALFAAYFVLRASAPDWPAGAELLDLPLPLINTLLLLLSSFTVALAVRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 91 MNNNKQSQVMSWLALTFLFGAGFVAMEIYEFHHLIAEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGL 170
Cdd:COG1845 81 ARRGDRKGLRLWLLLTLLLGLAFLGLQAYEYSHLIAEGLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRALRGGF 160
|
170 180 190
....*....|....*....|....*....|..
gi 490522312 171 THNNRARLMCLSMFWHFLDVVWICVFSVVYLM 202
Cdd:COG1845 161 TPENHTGVEAAALYWHFVDVVWIFLFALVYLL 192
|
|
| Heme_Cu_Oxidase_III_like |
cd00386 |
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
19-202 |
2.10e-54 |
|
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: 171.62 E-value: 2.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 19 HHDAGANKVFGFWIYLMSDCILFACLFATYAVLVNGTAGGP-TGKDIFELPFVLVETFLLLFSSITYGMAMIAMNNNKQS 97
Cdd:cd00386 2 TASVRSGGRLGMWLFILSEVMLFGSFFWAYFHSRLSPPVEFgAGLDPLDLPLLNTNTLLLSGSSVTWAHASLAARRGNRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 98 QVMSWLALTFLFGAGFVAMEIYEFHHLIaegFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRAR 177
Cdd:cd00386 82 KARLWLLLTILLGLAFLGLQAYEYSHLI---FTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRLRRGHFTPRHHLG 158
|
170 180
....*....|....*....|....*
gi 490522312 178 LMCLSMFWHFLDVVWICVFSVVYLM 202
Cdd:cd00386 159 LEAAALYWHFVDVVWLFLFPLVYLW 183
|
|
| QoxC |
TIGR02897 |
cytochrome aa3 quinol oxidase, subunit III; This family (QoxC) encodes subunit III of the ... |
27-203 |
1.01e-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: 165.03 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 27 VFGFWIYLMSDCILFACLFATYAVLVN-GTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLAL 105
Cdd:TIGR02897 11 ILGFWIFLGAEIALFATLFATYLVLQHgGDYAGKMPAELFELPLVLIMTFLLLFSSFTCGIAIYEMRKENQKLMMFWMII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 106 TFLFGAGFVAMEIYEFHHLIAEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFW 185
Cdd:TIGR02897 91 TLLLGAGFVGFEIYEFAHYASEGVTPQIGSYWSSFFVLLGTHGCHVTLGIVWAICLLIQIQRRGLTPYTAPKVFIVSLYW 170
|
170
....*....|....*...
gi 490522312 186 HFLDVVWICVFSVVYLMG 203
Cdd:TIGR02897 171 HFLDVVWVFIFTAVYLIG 188
|
|
| NorE_like |
cd02862 |
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ... |
28-202 |
8.02e-28 |
|
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: 103.47 E-value: 8.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 28 FGFWIYLMSDCILFACLFATYAV-LVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLALT 106
Cdd:cd02862 11 LGMWVFILSELLAFGALFIAYAVyRALYPELFAAGSAHLDLLLGALNTLVLLTSSFTVALAVRAARAGRRRRARRWLAAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 107 FLFGAGFVAMEIYEFHHLIAEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWH 186
Cdd:cd02862 91 VLLGLVFLVIKYFEYAHKIAAGIDPDAGLFFTLYFLLTGFHLLHVLIGLGILLWVAWRARRGRYSARDYEGVEAAALYWH 170
|
170
....*....|....*.
gi 490522312 187 FLDVVWICVFSVVYLM 202
Cdd:cd02862 171 MVDLVWIVLFPLLYLV 186
|
|
| Heme_Cu_Oxidase_III_1 |
cd02864 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
28-202 |
2.16e-24 |
|
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: 94.88 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 28 FGFWIYLMSDCILFACLFATYA-VLVNGTAGGPTGKDIFELP---------FVLVETFLLLFSSITYGMAMIAMNNNKQS 97
Cdd:cd02864 11 AMMWFFLLSDAFIFSSFLIAYMtARISTTEPWPLPSDVFALRighfniplvLIAIMTFILITSSGTMAMAVNFGYRGNRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 98 QVMSWLALTFLFGAGFVAMEIYEFHHLIAEG--------FGPDKsgFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRG 169
Cdd:cd02864 91 AAARLMLATALLGATFVGMQAFEWTKLIVEEgvrpwgnpWGAAQ--FGASFFMITGFHGTHVTIGVIYLIIIARKVWRGK 168
|
170 180 190
....*....|....*....|....*....|....
gi 490522312 170 LTHNNRARLM-CLSMFWHFLDVVWICVFSVVYLM 202
Cdd:cd02864 169 YQRIGRYEIVeIAGLYWHFVDLVWVFIFAFFYLW 202
|
|
| Cyt_c_Oxidase_III |
cd01665 |
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
28-200 |
3.07e-20 |
|
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: 84.87 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 28 FGFWIYLMSDCILFACLFAT--YAVLVNGTAGG----PTG---KDIFELPfvLVETFLLLFSSITYGMAMIAMNNNKQSQ 98
Cdd:cd01665 65 LGMILFILSEVMFFFSFFWAffHSSLSPSVELGgtwpPVGiepLNPFGIP--LLNTIILLSSGATVTWAHHALLLGNRKK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 99 VMSWLALTFLFGAGFVAMEIYEFHHLiaeGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARL 178
Cdd:cd01665 143 AILGLILTILLGVYFTGLQAYEYYEA---SFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLLKGHFSSNHHLGF 219
|
170 180
....*....|....*....|..
gi 490522312 179 MCLSMFWHFLDVVWICVFSVVY 200
Cdd:cd01665 220 EAAIWYWHFVDVVWLFLFVFVY 241
|
|
| Heme_Cu_Oxidase_III_2 |
cd02865 |
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ... |
20-200 |
1.25e-19 |
|
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: 82.03 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 20 HDAGANKVFGFWIYLMSDCILFACLFATYAVLVNGTAGGPtGKDIFELPFVLVETFLLLFSSITYGMAMIAMNNNKQSQV 99
Cdd:cd02865 3 AGARSPGWWGLWVFMAVEGTLFALLISAYFMRMTSGDWQP-GAPLPLPNLLSLNTAVLAASSVAMQWARRAARRNRRVLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 100 MSWLALTFLFGAGFVAMEIYEFHHLIAEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLM 179
Cdd:cd02865 82 RLGLALAGALALAFLAGQLLAWHALNDAGYGPTSNPAGSFFYLLTGLHGLHVIGGLVALAIVLAGLIRGHYGPRRRLPVE 161
|
170 180
....*....|....*....|.
gi 490522312 180 CLSMFWHFLDVVWICVFSVVY 200
Cdd:cd02865 162 LCALYWHFLLLVWLVLLALLY 182
|
|
| COX3 |
pfam00510 |
Cytochrome c oxidase subunit III; |
17-203 |
1.28e-11 |
|
Cytochrome c oxidase subunit III;
Pssm-ID: 395410 Cd Length: 258 Bit Score: 61.66 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 17 HGHHDAGANK--VFGFWIYLMSDCILFACLFATY---AVLVNGTAGG---PTGK---DIFELPfvLVETFLLLFSSITYG 85
Cdd:pfam00510 65 LGDHTFAVQKglNLGMILFIISEVFFFLGIFWAFfhsALSPTVELGAqwpPVGIhpvNPFEVP--LLNTIILLSSGVTVT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 86 MAMIAMNNNKQSQVMSWLALTFLFGAGFVAMEIYEFHHliaEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHV 165
Cdd:pfam00510 143 YAHHSLIEGNRKQALQGLILTILLAVYFTGLQAMEYTE---ASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRL 219
|
170 180 190
....*....|....*....|....*....|....*...
gi 490522312 166 SRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMG 203
Cdd:pfam00510 220 LKYHLTDNHHFGFEAAILYWHFVDVVWLFLYVSVYWWG 257
|
|
| COX3 |
MTH00049 |
cytochrome c oxidase subunit III; Validated |
28-201 |
6.06e-11 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177124 Cd Length: 215 Bit Score: 59.16 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 28 FGFWIYLMSDCILFACLFATYAVLVNGTAGgpTGKDIFELPFVlvETFLLLFSSITygmaMIAMNNNKQSQVMSW-LALT 106
Cdd:MTH00049 55 SAFWLFILSEVIIFGSLLVCCLWFDDWSYI--SLSSSLEIPFV--GCFLLLGSSIT----VTAYHHLLGWKYCDLfLYLT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 107 FLFGAGFVAMEIYEFHHLIAEGFgpdKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHvsrrGLTHNNRARLMCLSMFWH 186
Cdd:MTH00049 127 ILLGLLFVVLQVFEFEESGVNSL---DSSYYASCFCTVGLHFSHVVLGVVGLSTLLLV----GSSSFGVYRSTVLTWYWH 199
|
170
....*....|....*
gi 490522312 187 FLDVVWICVFSVVYL 201
Cdd:MTH00049 200 FVDYIWLLVYLIVYV 214
|
|
| COX3 |
MTH00130 |
cytochrome c oxidase subunit III; Provisional |
58-204 |
6.85e-11 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177188 Cd Length: 261 Bit Score: 59.78 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 58 GPTGKDIFELPfvLVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFV---AMEIYEFHHLIAEGFgpdks 134
Cdd:MTH00130 120 GITTLDPFEVP--LLNTAVLLASGVTVTWAHHSIMEGERKQAIQSLTLTILLGFYFTflqAMEYYEAPFTIADGV----- 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 135 gFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMGA 204
Cdd:MTH00130 193 -YGSTFFVATGFHGLHVIIGSTFLAVCLLRQIQYHFTSEHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00028 |
cytochrome c oxidase subunit III; Provisional |
103-204 |
1.71e-10 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214406 Cd Length: 297 Bit Score: 58.92 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 103 LALTFLFGAGFVAMEIYEFHHliaEGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLS 182
Cdd:MTH00028 199 LLMTILLGIIFTGLQAFEYKE---ASFAISDSVYGSTFFMLTGTHGLHVLVGTTFLIVCFIRLLSNQFTNSHHLGLEAAI 275
|
90 100
....*....|....*....|..
gi 490522312 183 MFWHFLDVVWICVFSVVYLMGA 204
Cdd:MTH00028 276 WYWHFVDVVWLFLYVFVYWWGS 297
|
|
| COX3 |
MTH00141 |
cytochrome c oxidase subunit III; Provisional |
65-203 |
2.30e-10 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177199 Cd Length: 259 Bit Score: 58.36 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 65 FELPfvLVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFV---AMEIYEFHHLIAEG-FGpdksgflSAF 140
Cdd:MTH00141 125 FQVP--LLNTAVLLASGVTVTWAHHSLMEGDYKSALQGLGLTIILGVYFTflqAGEYYEASFSIADGvYG-------STF 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490522312 141 FTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMG 203
Cdd:MTH00141 196 FVLTGFHGLHVIIGTTFLLVCLVRLLLGHFSTNHHFGFEAAAWYWHFVDVVWLFLYLSIYWWG 258
|
|
| COX3 |
MTH00155 |
cytochrome c oxidase subunit III; Provisional |
65-200 |
5.94e-09 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214439 Cd Length: 255 Bit Score: 54.03 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 65 FELPfvLVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFVAMEIYEFHHLiaeGFGPDKSGFLSAFFTLV 144
Cdd:MTH00155 125 FQIP--LLNTIILLSSGVTVTWAHHSLMENNYKQATQSLFFTIILGIYFTMLQAYEYYEA---PFTIADSVYGSTFFMAT 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 490522312 145 GTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVY 200
Cdd:MTH00155 200 GFHGLHVIIGTTFLLVCLIRHLNNHFSSNHHFGFEAAAWYWHFVDVVWLFLYISIY 255
|
|
| COX3 |
MTH00075 |
cytochrome c oxidase subunit III; Provisional |
58-204 |
7.85e-09 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177146 Cd Length: 261 Bit Score: 53.98 E-value: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 58 GPTGKDIFELPfvLVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFV---AMEIYEFHHLIAEGFgpdks 134
Cdd:MTH00075 120 GITPLDPFEVP--LLNTAVLLASGVTVTWAHHSIMQGNRKEAIQSLALTIILGLYFTllqAMEYYEAPFTIADGV----- 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 135 gFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMGA 204
Cdd:MTH00075 193 -YGSTFFVATGFHGLHVIIGSLFLLVCLLRQINFHFTSQHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00052 |
cytochrome c oxidase subunit III; Provisional |
63-204 |
1.00e-08 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 164623 Cd Length: 262 Bit Score: 53.64 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 63 DIFELPfvLVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFV---AMEIYEFHHLIAEgfgpdkSGFLSA 139
Cdd:MTH00052 126 NPFSVP--LLNTAVLLSSGATVTWAHHGIISGKRKEAIIGLALTVALGLLFTglqAMEYYEAPFTISD------SVYGST 197
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490522312 140 FFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMGA 204
Cdd:MTH00052 198 FFVTTGAHGGHVLIGSSFLLVCLFRLINHQFTRHHHFGFEAAAWYWHFVDVVWLFLFIFMYWWGS 262
|
|
| COX3 |
MTH00039 |
cytochrome c oxidase subunit III; Validated |
71-203 |
1.13e-08 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177114 Cd Length: 260 Bit Score: 53.58 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 71 LVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFVAMEIYEFhhlIAEGFGPDKSGFLSAFFTLVGTHGIH 150
Cdd:MTH00039 130 LLNTAVLLSSGVTITWSHHSILEGNRTEAIQALFLTVLLGLYFTALQAWEY---YDAPFTIADSVYGSTFFVATGFHGLH 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 490522312 151 VTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMG 203
Cdd:MTH00039 207 VIIGTTFLAVCLFRLINHHFSNNHHFGFEAAAWYWHFVDVVWLFLYVCIYWWG 259
|
|
| COX3 |
MTH00083 |
cytochrome c oxidase subunit III; Provisional |
28-200 |
1.46e-08 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177150 Cd Length: 256 Bit Score: 53.04 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 28 FGFWIYLMSDCILFACLFATY---AVLVNGTAGG---PTG---KDIFELPfvLVETFLLLFS--SITYGMAMIAMNNNKQ 96
Cdd:MTH00083 77 FGMILFIFSEFMFFFSIFWTFfdaALVPVHELGGvwsPIGihlVNYLGVP--LLNTIILLSSgvSVTWSHHSLCLSNKSC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 97 SqvmSWLALTFLFGAGFVAMEIYEFHHLiaeGFGPDKSGFLSAFFTLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRA 176
Cdd:MTH00083 155 T---NSLLLTCFLGLYFTSFQLMEYKEA---SFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLLKSHFNYNHHL 228
|
170 180
....*....|....*....|....
gi 490522312 177 RLMCLSMFWHFLDVVWICVFSVVY 200
Cdd:MTH00083 229 GLEFAILYWHFVDVVWLFLFVFVY 252
|
|
| COX3 |
MTH00219 |
cytochrome c oxidase subunit III; Provisional |
71-204 |
1.72e-08 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 214464 Cd Length: 262 Bit Score: 52.87 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 71 LVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFVAMEIYEFhhlIAEGFGPDKSGFLSAFFTLVGTHGIH 150
Cdd:MTH00219 132 LLNTAVLLASGVTVTWAHHSLMESNHKEAQQGLLFTILLGLYFTMLQGMEY---LEASFSISDSVYGTTFFVATGFHGLH 208
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 490522312 151 VTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMGA 204
Cdd:MTH00219 209 VIIGTIFLFVCFMRGLMLHFSKNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 262
|
|
| COX3 |
MTH00099 |
cytochrome c oxidase subunit III; Validated |
71-204 |
9.12e-08 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177161 Cd Length: 261 Bit Score: 50.88 E-value: 9.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 71 LVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFV---AMEIYEFHHLIAEGFgpdksgFLSAFFTLVGTH 147
Cdd:MTH00099 131 LLNTSVLLASGVSITWAHHSLMEGNRKHMLQALFITILLGLYFTllqASEYYEAPFTISDGI------YGSTFFMATGFH 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 490522312 148 GIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMGA 204
Cdd:MTH00099 205 GLHVIIGSTFLIVCFLRQLKFHFTSNHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGS 261
|
|
| COX3 |
MTH00024 |
cytochrome c oxidase subunit III; Validated |
71-204 |
9.58e-08 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 214403 Cd Length: 261 Bit Score: 50.91 E-value: 9.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 71 LVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFVAMEIYEFHHliaEGFGPDKSGFLSAFFTLVGTHGIH 150
Cdd:MTH00024 131 LLNTAVLLSSGATVTWAHHAIISGKRKEAILGLFLTVFLGVLFTGLQAIEYYE---APFAISDSVYGSTFFVATGFHGLH 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 490522312 151 VTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMGA 204
Cdd:MTH00024 208 VIIGTTFLFVCLLRLLSNQFTRRQHVGFEAASWYWHFVDVVWLFLYLCIYWWGS 261
|
|
| COX3 |
MTH00189 |
cytochrome c oxidase subunit III; Provisional |
63-203 |
1.44e-07 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177238 Cd Length: 260 Bit Score: 50.36 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 63 DIFELPfvLVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFVAMEIYEFHHliaEGFGPDKSGFLSAFFT 142
Cdd:MTH00189 124 NPFEVP--LLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQALTLTVILGVYFTLLQAMEYYE---APFTIADSVYGSTFFV 198
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490522312 143 LVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMG 203
Cdd:MTH00189 199 ATGFHGLHVIIGSTFLLVCLLRQIQGHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWWG 259
|
|
| COX3 |
MTH00118 |
cytochrome c oxidase subunit III; Provisional |
65-204 |
2.48e-07 |
|
cytochrome c oxidase subunit III; Provisional
Pssm-ID: 177179 Cd Length: 261 Bit Score: 49.56 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 65 FELPfvLVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFVA---MEIYEFHHLIAEGFgpdksgFLSAFF 141
Cdd:MTH00118 127 FEVP--LLNTAVLLASGVTVTWAHHSIMEGNRKQAIQALTLTILLGLYFTAlqaMEYYEAPFTISDSV------YGSTFF 198
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490522312 142 TLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMGA 204
Cdd:MTH00118 199 VATGFHGLHVIIGSTFLIVCLLRLIKFHFTTNHHFGFEAAAWYWHFVDVVWLFLYISIYWWGS 261
|
|
| COX3 |
MTH00009 |
cytochrome c oxidase subunit III; Validated |
71-204 |
2.56e-07 |
|
cytochrome c oxidase subunit III; Validated
Pssm-ID: 177101 Cd Length: 259 Bit Score: 49.45 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 71 LVETFLLLFSSITYGMAMIAMNNNKQSQVMSWLALTFLFGAGFVAMEIYEFhhlIAEGFGPDKSGFLSAFFTLVGTHGIH 150
Cdd:MTH00009 129 LLNTAVLLASGVTVTWAHHSLIEGDRPEATQALILTVLLGAYFTFLQAGEY---IEAPFTIADSVYGSTFFVATGFHGLH 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 490522312 151 VTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMGA 204
Cdd:MTH00009 206 VLIGSSFLFVCLLRTWSHHFSTGHHFGFEAAAWYWHFVDVVWIFLYLCIYWWGS 259
|
|
| PLN02194 |
PLN02194 |
cytochrome-c oxidase |
63-205 |
8.97e-07 |
|
cytochrome-c oxidase
Pssm-ID: 177845 Cd Length: 265 Bit Score: 48.12 E-value: 8.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490522312 63 DIFELPFVLVETFLLLFSSITYGM-AMIAMNNNKQSQVMSWLALTFLFGAGFVAMEIYEFHHLIAEgfgpdkSGFLSAFF 141
Cdd:PLN02194 128 DPWEIPFLNTPILPSSGAAVTWAHhAILAGKEKRAVYALVATVLLALVFTGFQGMEYYQAPFTISD------SIYGSTFF 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490522312 142 TLVGTHGIHVTSGLIWMVVMMIHVSRRGLTHNNRARLMCLSMFWHFLDVVWICVFSVVYLMGAM 205
Cdd:PLN02194 202 LATGFHGFHVIIGTLFLIICGIRQYLGHLTKEHHVGFEAAAWYWHFVDVVWLFLFVSIYWWGGI 265
|
|
| |
