|
Name |
Accession |
Description |
Interval |
E-value |
| CyoA |
COG1622 |
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion]; |
13-264 |
6.70e-90 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
Pssm-ID: 441229 [Multi-domain] Cd Length: 229 Bit Score: 270.93 E-value: 6.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 13 KSFVVLLVSPLVHASSDYNMTQGVTEISGKVYELHMLIFYICCAIAFVVFGVMFYSILRHRKSKG-AVAAHFHESTKVEI 91
Cdd:COG1622 2 KRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGdADPAQFHHNTKLEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 92 VWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTVKITGSQWKWHYSYFGEDVEffsllatsdkeieglevkgahylleVD 171
Cdd:COG1622 82 VWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA-------------------------TV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 172 KPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEF 251
Cdd:COG1622 137 NELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEF 216
|
250
....*....|...
gi 518661713 252 DAWLAEQKELAIA 264
Cdd:COG1622 217 DAWLAEQKASAAT 229
|
|
| CcO_II_C |
cd13912 |
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ... |
121-254 |
1.21e-61 |
|
C-terminal domain of Cytochrome c Oxidase subunit II; 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.
Pssm-ID: 259979 [Multi-domain] Cd Length: 130 Bit Score: 194.71 E-value: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 121 SDLTVKITGSQWKWHYSYF-GEDVEFFS-LLATSDKEieglevKGAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVP 198
Cdd:cd13912 1 PSLTIKAIGHQWYWSYEYSdFNDLEFDSyMIPEDDLE------KGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVP 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 518661713 199 AFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAW 254
Cdd:cd13912 75 SLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
|
|
| CoxB |
TIGR02866 |
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ... |
37-256 |
6.15e-52 |
|
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]
Pssm-ID: 274329 [Multi-domain] Cd Length: 199 Bit Score: 172.18 E-value: 6.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 37 TEISGKVYELHMLIFYICCAIAFVVFGVMFYSILRHR-KSKGAVAAHFHESTKVEIVWTIIPII-ILIAMAIPATKTLIA 114
Cdd:TIGR02866 3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRrKGDEEKPSQIHGNRRLEYVWTVIPLIiVVGLFAATAKGLLYL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 115 MEDTSQSDLTVKITGSQWKWHYSYfgedveffsllatsdkeieglevkgAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHS 194
Cdd:TIGR02866 83 ERPIPKDALKVKVTGYQWWWDFEY-------------------------PESGFTTVNELVLPAGTPVELQVTSKDVIHS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518661713 195 WWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWLA 256
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
|
|
| COX2 |
MTH00140 |
cytochrome c oxidase subunit II; Provisional |
49-255 |
3.54e-45 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214430 [Multi-domain] Cd Length: 228 Bit Score: 155.48 E-value: 3.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 49 LIFY--ICCAIAFVVFGVMFYSILRHRKSKgAVAAHFHESTKVEIVWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTVK 126
Cdd:MTH00140 20 LIFFhdHAMVVLVLIFSFVMYMLVLLLFNK-FSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 127 ITGSQWKWHYSYFGEDVEFFSLLATSDKEIEglevKGAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKDT 206
Cdd:MTH00140 99 AIGHQWYWSYEYSDFSVIEFDSYMVPENELE----LGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518661713 207 IPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWL 255
Cdd:MTH00140 175 IPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWL 223
|
|
| COX2 |
pfam00116 |
Cytochrome C oxidase subunit II, periplasmic domain; |
123-245 |
1.16e-42 |
|
Cytochrome C oxidase subunit II, periplasmic domain;
Pssm-ID: 395066 [Multi-domain] Cd Length: 120 Bit Score: 145.25 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 123 LTVKITGSQWKWHYSY--FGeDVEFFS-LLATSDKEieglevKGAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPA 199
Cdd:pfam00116 1 LTIKAIGHQWYWSYEYtdFG-DLEFDSyMIPTEDLE------EGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPS 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 518661713 200 FAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHA 245
Cdd:pfam00116 74 LGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
|
|
| CccA |
COG2010 |
Cytochrome c, mono- and diheme variants [Energy production and conversion]; |
195-363 |
1.20e-28 |
|
Cytochrome c, mono- and diheme variants [Energy production and conversion];
Pssm-ID: 441613 [Multi-domain] Cd Length: 169 Bit Score: 110.04 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 195 WWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWLAEQKELAIAEQQAAKDALD 274
Cdd:COG2010 1 GGLLGGALGALLGGGGLSDEGAGAAGAGGVAAAGAGLAGALVDGAAAAAALGAAAAAAAAAAALALALLLALLLAAAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 275 ASLSLAELNTIGEEVYKTRCAVCHQANGEGIPGAFPAIKGSPIALGDVDVHIDTIVYGRGGTAMQAFDNQLTEKEIAAVV 354
Cdd:COG2010 81 APAADAEALARGKALYEQNCAACHGADGKGGLGAAPNLTDDALYGGDPEALVETILNGRPGGAMPAFGGQLSDEEIAALA 160
|
....*....
gi 518661713 355 TYQRNAWGN 363
Cdd:COG2010 161 AYLRSLSGN 169
|
|
| Cytochrom_C |
pfam00034 |
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ... |
286-361 |
4.34e-12 |
|
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.
Pssm-ID: 459641 [Multi-domain] Cd Length: 89 Bit Score: 61.79 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 286 GEEVYKTRCAVCHQANGEGIPGAFPAIKGSPIALG----DVDVHI--------DTIVYGRGGTAMQAFDnQLTEKEIAAV 353
Cdd:pfam00034 3 GKKLFAANCAACHGVNGEGAGAGGPDLAGLAARYPgdalGAIRENkhaiggggVDRAGGPPGTGMPAFD-GLTDEEIADL 81
|
....*...
gi 518661713 354 VTYQRNAW 361
Cdd:pfam00034 82 VAYLLSLS 89
|
|
| PRK14486 |
PRK14486 |
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional |
286-359 |
3.17e-04 |
|
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional
Pssm-ID: 184704 [Multi-domain] Cd Length: 294 Bit Score: 42.11 E-value: 3.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518661713 286 GEEVYKTRCAVCHQANGEGIPGAFPaikgSPIALGDV--DVHIDTIVYGRGGTAMQAFDNQLTEKEIAAVVTYQRN 359
Cdd:PRK14486 218 GKALYDANCAACHGDEAQGQEGVAL----NDIDDGDLpdAAYFGMIKGGSDAKGMPGFGGDLSDDDIWAIVAYIRS 289
|
|
| ccoP |
TIGR00782 |
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ... |
269-367 |
3.55e-03 |
|
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of approximately 26 kDa of the cbb3 type copper and heme-containing cytochrome oxidase. [Energy metabolism, Electron transport]
Pssm-ID: 129864 [Multi-domain] Cd Length: 285 Bit Score: 39.11 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 269 AKDALDASLSLAElntiGEEVYKTRCAVCHQANGEGIPGaFPAIKGSPIALG-DVDVHIDTIVYGR-----GGTA---MQ 339
Cdd:TIGR00782 97 AKDPELKQYARNA----GAAIFRTWCAQCHGSGAGGAKG-FPNLLDNDWLWGgTLEGIHTTIKHGIrdpddGDTYvgeMP 171
|
90 100
....*....|....*....|....*...
gi 518661713 340 AFDNQLTEKEIAAVVTYQRNAWGNDTGD 367
Cdd:TIGR00782 172 AFGPLLEEADIKDVASYVMSLSSGKPKD 199
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CyoA |
COG1622 |
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion]; |
13-264 |
6.70e-90 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
Pssm-ID: 441229 [Multi-domain] Cd Length: 229 Bit Score: 270.93 E-value: 6.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 13 KSFVVLLVSPLVHASSDYNMTQGVTEISGKVYELHMLIFYICCAIAFVVFGVMFYSILRHRKSKG-AVAAHFHESTKVEI 91
Cdd:COG1622 2 KRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGdADPAQFHHNTKLEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 92 VWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTVKITGSQWKWHYSYFGEDVEffsllatsdkeieglevkgahylleVD 171
Cdd:COG1622 82 VWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA-------------------------TV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 172 KPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEF 251
Cdd:COG1622 137 NELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEF 216
|
250
....*....|...
gi 518661713 252 DAWLAEQKELAIA 264
Cdd:COG1622 217 DAWLAEQKASAAT 229
|
|
| CcO_II_C |
cd13912 |
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ... |
121-254 |
1.21e-61 |
|
C-terminal domain of Cytochrome c Oxidase subunit II; 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.
Pssm-ID: 259979 [Multi-domain] Cd Length: 130 Bit Score: 194.71 E-value: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 121 SDLTVKITGSQWKWHYSYF-GEDVEFFS-LLATSDKEieglevKGAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVP 198
Cdd:cd13912 1 PSLTIKAIGHQWYWSYEYSdFNDLEFDSyMIPEDDLE------KGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVP 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 518661713 199 AFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAW 254
Cdd:cd13912 75 SLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
|
|
| CoxB |
TIGR02866 |
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ... |
37-256 |
6.15e-52 |
|
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]
Pssm-ID: 274329 [Multi-domain] Cd Length: 199 Bit Score: 172.18 E-value: 6.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 37 TEISGKVYELHMLIFYICCAIAFVVFGVMFYSILRHR-KSKGAVAAHFHESTKVEIVWTIIPII-ILIAMAIPATKTLIA 114
Cdd:TIGR02866 3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRrKGDEEKPSQIHGNRRLEYVWTVIPLIiVVGLFAATAKGLLYL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 115 MEDTSQSDLTVKITGSQWKWHYSYfgedveffsllatsdkeieglevkgAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHS 194
Cdd:TIGR02866 83 ERPIPKDALKVKVTGYQWWWDFEY-------------------------PESGFTTVNELVLPAGTPVELQVTSKDVIHS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518661713 195 WWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWLA 256
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
|
|
| COX2 |
MTH00140 |
cytochrome c oxidase subunit II; Provisional |
49-255 |
3.54e-45 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214430 [Multi-domain] Cd Length: 228 Bit Score: 155.48 E-value: 3.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 49 LIFY--ICCAIAFVVFGVMFYSILRHRKSKgAVAAHFHESTKVEIVWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTVK 126
Cdd:MTH00140 20 LIFFhdHAMVVLVLIFSFVMYMLVLLLFNK-FSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 127 ITGSQWKWHYSYFGEDVEFFSLLATSDKEIEglevKGAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKDT 206
Cdd:MTH00140 99 AIGHQWYWSYEYSDFSVIEFDSYMVPENELE----LGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518661713 207 IPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWL 255
Cdd:MTH00140 175 IPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWL 223
|
|
| COX2 |
pfam00116 |
Cytochrome C oxidase subunit II, periplasmic domain; |
123-245 |
1.16e-42 |
|
Cytochrome C oxidase subunit II, periplasmic domain;
Pssm-ID: 395066 [Multi-domain] Cd Length: 120 Bit Score: 145.25 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 123 LTVKITGSQWKWHYSY--FGeDVEFFS-LLATSDKEieglevKGAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPA 199
Cdd:pfam00116 1 LTIKAIGHQWYWSYEYtdFG-DLEFDSyMIPTEDLE------EGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPS 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 518661713 200 FAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHA 245
Cdd:pfam00116 74 LGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
|
|
| COX2 |
MTH00168 |
cytochrome c oxidase subunit II; Provisional |
48-257 |
3.84e-42 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177223 [Multi-domain] Cd Length: 225 Bit Score: 147.43 E-value: 3.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 48 MLIF--YICCAIAFVVFGVMFYSILRhrKSKGAVAAHFHESTKVEIVWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTV 125
Cdd:MTH00168 20 LILFhdHALLILVLILTLVLYSLLVL--VTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 126 KITGSQWKWHYSY--FGeDVEFFS-LLATSDKEIeglevkGAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAV 202
Cdd:MTH00168 98 KAVGHQWYWSYEYtdYN-DLEFDSyMVPTQDLSP------GQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518661713 203 KKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWLAE 257
Cdd:MTH00168 171 KMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
|
|
| COX2 |
MTH00051 |
cytochrome c oxidase subunit II; Provisional |
35-260 |
6.75e-42 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177126 [Multi-domain] Cd Length: 234 Bit Score: 147.23 E-value: 6.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 35 GVTEISGKVYELHMLIFYICCAIAFVVFGVMFYSILRHRKSKgavaaHFHESTKVEIVWTIIPIIILIAMAIPATKTLIA 114
Cdd:MTH00051 14 AASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHK-----YLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 115 MEDTSQSDLTVKITGSQWKWHYSYF---GEDVEFFS-LLATSDKEIEGLEvkgahyLLEVDKPLVLPVDRKVRFLMTSDD 190
Cdd:MTH00051 89 MDEVIDPALTIKAIGHQWYWSYEYSdygTDTIEFDSyMIPTSDLNSGDLR------LLEVDNRLIVPIQTQVRVLVTAAD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 191 VIHSWWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWLAEQKE 260
Cdd:MTH00051 163 VLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSE 232
|
|
| COX2 |
MTH00139 |
cytochrome c oxidase subunit II; Provisional |
47-257 |
8.29e-41 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214429 [Multi-domain] Cd Length: 226 Bit Score: 144.09 E-value: 8.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 47 HMLIFYIccAIAFVVFGVMFYSILRHRKSKGAVaahfhESTKVEIVWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTVK 126
Cdd:MTH00139 26 HAMVILI--MILSFVGYISLSLMSNKFTSRSLL-----ESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 127 ITGSQWKWHYSYFG-EDVEFFS-LLATSDKeiegleVKGAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKK 204
Cdd:MTH00139 99 AVGHQWYWSYEYSDfKNLSFDSyMIPTEDL------SSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518661713 205 DTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWLAE 257
Cdd:MTH00139 173 DAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
|
|
| COX2 |
MTH00023 |
cytochrome c oxidase subunit II; Validated |
85-255 |
2.91e-40 |
|
cytochrome c oxidase subunit II; Validated
Pssm-ID: 214402 [Multi-domain] Cd Length: 240 Bit Score: 142.97 E-value: 2.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 85 ESTKVEIVWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTVKITGSQWKWHYSY---FGEDVEFFS-LLATSDKEiegle 160
Cdd:MTH00023 66 DGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYsdyEGETLEFDSyMVPTSDLN----- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 161 vKGAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMP 240
Cdd:MTH00023 141 -SGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMP 219
|
170
....*....|....*
gi 518661713 241 IVVHAMEEDEFDAWL 255
Cdd:MTH00023 220 IVIEAVSLDKYINWL 234
|
|
| COX2 |
MTH00185 |
cytochrome c oxidase subunit II; Provisional |
57-254 |
3.95e-40 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 164736 [Multi-domain] Cd Length: 230 Bit Score: 142.33 E-value: 3.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 57 IAFVVFGVMFYSILRHRKSKgAVAAHFHESTKVEIVWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTVKITGSQWKWHY 136
Cdd:MTH00185 30 IVFLISTLVLYIIVAMVTTK-LTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 137 SYFG-EDVEFFSLLaTSDKEIEglevKGAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKDTIPGFINEAW 215
Cdd:MTH00185 109 EYTDyEQLEFDSYM-TPTQDLT----PGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQAT 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 518661713 216 TKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAW 254
Cdd:MTH00185 184 FIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
|
|
| COX2 |
MTH00154 |
cytochrome c oxidase subunit II; Provisional |
115-255 |
5.20e-39 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214438 [Multi-domain] Cd Length: 227 Bit Score: 139.19 E-value: 5.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 115 MEDTSQSDLTVKITGSQWKWHYSY--FgEDVEFFS-LLATSDKEIEGLEvkgahyLLEVDKPLVLPVDRKVRFLMTSDDV 191
Cdd:MTH00154 87 LDEVNNPSITLKTIGHQWYWSYEYsdF-KNIEFDSyMIPTNELENNGFR------LLDVDNRLVLPMNTQIRILITAADV 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518661713 192 IHSWWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWL 255
Cdd:MTH00154 160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
|
|
| COX2 |
MTH00038 |
cytochrome c oxidase subunit II; Provisional |
83-257 |
6.98e-39 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177113 [Multi-domain] Cd Length: 229 Bit Score: 139.07 E-value: 6.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 83 FHESTKVEIVWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTVKITGSQWKWHYSYFG-EDVEFFS-LLATSDKEIegle 160
Cdd:MTH00038 55 FLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDyNDLEFDSyMVPTSDLST---- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 161 vkGAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMP 240
Cdd:MTH00038 131 --GLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMP 208
|
170
....*....|....*..
gi 518661713 241 IVVHAMEEDEFDAWLAE 257
Cdd:MTH00038 209 IVIESVPFNTFENWVSN 225
|
|
| COX2 |
MTH00008 |
cytochrome c oxidase subunit II; Validated |
85-260 |
1.12e-38 |
|
cytochrome c oxidase subunit II; Validated
Pssm-ID: 164584 [Multi-domain] Cd Length: 228 Bit Score: 138.45 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 85 ESTKVEIVWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTVKITGSQWKWHYSYFG-EDVEFFS-LLATSDKEieglevK 162
Cdd:MTH00008 57 EAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDfSNLEFDSyMLPTSDLS------P 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 163 GAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIV 242
Cdd:MTH00008 131 GQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIV 210
|
170
....*....|....*...
gi 518661713 243 VHAMEEDEFDAWLAEQKE 260
Cdd:MTH00008 211 LEAVDTKSFMKWVSSFAE 228
|
|
| COX2 |
MTH00117 |
cytochrome c oxidase subunit II; Provisional |
89-256 |
2.29e-38 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177178 [Multi-domain] Cd Length: 227 Bit Score: 137.74 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 89 VEIVWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTVKITGSQWKWHYSYF-GEDVEFFS-LLATSDKEieglevKGAHY 166
Cdd:MTH00117 61 VELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTdYKDLSFDSyMIPTQDLP------NGHFR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 167 LLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAM 246
Cdd:MTH00117 135 LLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESV 214
|
170
....*....|
gi 518661713 247 EEDEFDAWLA 256
Cdd:MTH00117 215 PLKHFENWSS 224
|
|
| COX2 |
MTH00080 |
cytochrome c oxidase subunit II; Provisional |
39-255 |
5.94e-38 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177149 [Multi-domain] Cd Length: 231 Bit Score: 136.68 E-value: 5.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 39 ISGKVYELHM--------LIFYICCAIAFVVF-GVMFYSILRHRKSKgavaahFHESTKVEIVWTIIPIIILIAMAIPAT 109
Cdd:MTH00080 10 FSNSLFSSYMdwfhnfncSLLFGEFVLAFVVFlFLYLISNNFYFKSK------KIEYQFGELLCSVFPVLILLMQMVPSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 110 KTLIAMEDTS-QSDLTVKITGSQWKWHYSyFGED--VEFFSLLatsdKEIEGLEVkGAHYLLEVDKPLVLPVDRKVRFLM 186
Cdd:MTH00080 84 SLLYYYGLMNlDSNLTVKVTGHQWYWSYE-FSDIpgLEFDSYM----KSLDQLRL-GEPRLLEVDNRCVLPCDTNIRFCI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518661713 187 TSDDVIHSWWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWL 255
Cdd:MTH00080 158 TSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
|
|
| COX2 |
MTH00129 |
cytochrome c oxidase subunit II; Provisional |
82-254 |
1.58e-37 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177187 [Multi-domain] Cd Length: 230 Bit Score: 135.61 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 82 HFHESTKVEIVWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTVKITGSQWKWHYSYFG-EDVEFFS-LLATSDKeiegl 159
Cdd:MTH00129 54 YILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDyEDLGFDSyMIPTQDL----- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 160 eVKGAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFM 239
Cdd:MTH00129 129 -TPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFM 207
|
170
....*....|....*
gi 518661713 240 PIVVHAMEEDEFDAW 254
Cdd:MTH00129 208 PIVVEAVPLEHFENW 222
|
|
| COX2 |
MTH00076 |
cytochrome c oxidase subunit II; Provisional |
85-260 |
1.82e-37 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 164646 [Multi-domain] Cd Length: 228 Bit Score: 135.29 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 85 ESTKVEIVWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTVKITGSQWKWHYSYFG-EDVEFFSLLATSDKEIeglevKG 163
Cdd:MTH00076 57 DAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDyEDLSFDSYMIPTQDLT-----PG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 164 AHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVV 243
Cdd:MTH00076 132 QFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVV 211
|
170
....*....|....*..
gi 518661713 244 HAMEEDEFDAWLAEQKE 260
Cdd:MTH00076 212 EATPLNNFLNWSSSMLE 228
|
|
| COX2 |
MTH00027 |
cytochrome c oxidase subunit II; Provisional |
46-258 |
1.97e-37 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214405 [Multi-domain] Cd Length: 262 Bit Score: 136.31 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 46 LHMLIFYICCaiafVVFGVMFYSILRHRKSKGAVAAHFH--ESTKVEIVWTIIPIIILIAMAIPATKTLIAMEDTS-QSD 122
Cdd:MTH00027 51 LHDQILFILT----IIVGVVLWLIIRILLGNNYYSYYWNklDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSAN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 123 LTVKITGSQWKWHYSY--FGE-DVEFFS-LLATSDKEIEGLEvkgahyLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVP 198
Cdd:MTH00027 127 ITIKVTGHQWYWSYSYedYGEkNIEFDSyMIPTADLEFGDLR------LLEVDNRLILPVDTNVRVLITAADVLHSWTVP 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 199 AFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWLAEQ 258
Cdd:MTH00027 201 SLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGRE 260
|
|
| COX2 |
MTH00098 |
cytochrome c oxidase subunit II; Validated |
48-256 |
4.45e-37 |
|
cytochrome c oxidase subunit II; Validated
Pssm-ID: 177160 [Multi-domain] Cd Length: 227 Bit Score: 134.46 E-value: 4.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 48 MLIFYICCAIAFVVFgVMFYSILRHRKSKGAvaahfhesTKVEIVWTIIPIIILIAMAIPATKTLIAMEDTSQSDLTVKI 127
Cdd:MTH00098 29 MIVFLISSLVLYIIS-LMLTTKLTHTSTMDA--------QEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 128 TGSQWKWHYSYFG-EDVEFFS-LLATSDKEieglevKGAHYLLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKD 205
Cdd:MTH00098 100 MGHQWYWSYEYTDyEDLSFDSyMIPTSDLK------PGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518661713 206 TIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWLA 256
Cdd:MTH00098 174 AIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSA 224
|
|
| CuRO_HCO_II_like_5 |
cd13919 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
122-246 |
1.26e-35 |
|
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.
Pssm-ID: 259986 [Multi-domain] Cd Length: 107 Bit Score: 126.60 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 122 DLTVKITGSQWKWHYSYFGEDVEFfsllaTSDKEIEGLEvkgahyllevdkpLVLPVDRKVRFLMTSDDVIHSWWVPAFA 201
Cdd:cd13919 1 ALVVEVTAQQWAWTFRYPGGDGKL-----GTDDDVTSPE-------------LHLPVGRPVLFNLRSKDVIHSFWVPEFR 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 518661713 202 VKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAM 246
Cdd:cd13919 63 VKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKVV 107
|
|
| CuRO_CcO_Caa3_II |
cd04213 |
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ... |
122-246 |
6.76e-34 |
|
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.
Pssm-ID: 259875 [Multi-domain] Cd Length: 103 Bit Score: 121.57 E-value: 6.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 122 DLTVKITGSQWKWHYSYFGEDVEffsLLATSDKeieglevkgahyllevdkpLVLPVDRKVRFLMTSDDVIHSWWVPAFA 201
Cdd:cd04213 1 ALTIEVTGHQWWWEFRYPDEPGR---GIVTANE-------------------LHIPVGRPVRLRLTSADVIHSFWVPSLA 58
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 518661713 202 VKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAM 246
Cdd:cd04213 59 GKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
|
|
| CccA |
COG2010 |
Cytochrome c, mono- and diheme variants [Energy production and conversion]; |
195-363 |
1.20e-28 |
|
Cytochrome c, mono- and diheme variants [Energy production and conversion];
Pssm-ID: 441613 [Multi-domain] Cd Length: 169 Bit Score: 110.04 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 195 WWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWLAEQKELAIAEQQAAKDALD 274
Cdd:COG2010 1 GGLLGGALGALLGGGGLSDEGAGAAGAGGVAAAGAGLAGALVDGAAAAAALGAAAAAAAAAAALALALLLALLLAAAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 275 ASLSLAELNTIGEEVYKTRCAVCHQANGEGIPGAFPAIKGSPIALGDVDVHIDTIVYGRGGTAMQAFDNQLTEKEIAAVV 354
Cdd:COG2010 81 APAADAEALARGKALYEQNCAACHGADGKGGLGAAPNLTDDALYGGDPEALVETILNGRPGGAMPAFGGQLSDEEIAALA 160
|
....*....
gi 518661713 355 TYQRNAWGN 363
Cdd:COG2010 161 AYLRSLSGN 169
|
|
| CuRO_HCO_II_like |
cd13842 |
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ... |
123-243 |
6.49e-28 |
|
Cupredoxin domain of Heme-copper oxidase subunit II; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.
Pssm-ID: 259911 [Multi-domain] Cd Length: 95 Bit Score: 105.46 E-value: 6.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 123 LTVKITGSQWKWHYSYFGedveffsllatsdkeieglevkgahylLEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAV 202
Cdd:cd13842 1 LTVYVTGVQWSWTFIYPN---------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGV 53
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 518661713 203 KKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVV 243
Cdd:cd13842 54 KVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKV 94
|
|
| PTZ00047 |
PTZ00047 |
cytochrome c oxidase subunit II; Provisional |
168-253 |
7.07e-28 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 240243 [Multi-domain] Cd Length: 162 Bit Score: 107.60 E-value: 7.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 168 LEVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAME 247
Cdd:PTZ00047 69 LEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVS 148
|
....*.
gi 518661713 248 EDEFDA 253
Cdd:PTZ00047 149 PEAYAA 154
|
|
| CuRO_HCO_II_like_2 |
cd13915 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
122-243 |
1.71e-27 |
|
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.
Pssm-ID: 259982 [Multi-domain] Cd Length: 98 Bit Score: 104.63 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 122 DLTVKITGSQWKWHYSYFGEDVEffsllatsdkeieglevkgahyllevDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFA 201
Cdd:cd13915 1 ALEIQVTGRQWMWEFTYPNGKRE--------------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFR 54
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 518661713 202 VKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVV 243
Cdd:cd13915 55 IKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
|
|
| COX2 |
MTH00047 |
cytochrome c oxidase subunit II; Provisional |
44-250 |
2.29e-27 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214412 [Multi-domain] Cd Length: 194 Bit Score: 107.35 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 44 YELHMLIFYICCAIAFVVFGVMFYSIlrhrKSKGAVAAHFHESTKVEIVWTIIPIIILIAMAIPATKTLIAMEDTSQSDl 123
Cdd:MTH00047 8 YDIVCYILALCVFIPCWVYIMLCWQV----VSGNGSVNFGSENQVLELLWTVVPTLLVLVLCFLNLNFITSDLDCFSSE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 124 TVKITGSQWKWHYSYFGEDvEFFSLLAtsdKEIEGlevkgahylleVDKPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVK 203
Cdd:MTH00047 83 TIKVIGHQWYWSYEYSFGG-SYDSFMT---DDIFG-----------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518661713 204 KDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDE 250
Cdd:MTH00047 148 MDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
|
|
| CuRO_HCO_II_like_3 |
cd13914 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
124-255 |
1.12e-26 |
|
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.
Pssm-ID: 259981 [Multi-domain] Cd Length: 108 Bit Score: 102.49 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 124 TVKITGSQWKWHYSYFGEDVEffsllaTSDkeieglevkgahyllevdkPLVLPVDRKVRFLMTSDDVIHSWWVPAFAVK 203
Cdd:cd13914 2 EIEVEAYQWGWEFSYPEANVT------TSE-------------------QLVIPADRPVYFRITSRDVIHAFHVPELGLK 56
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 518661713 204 KDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWL 255
Cdd:cd13914 57 QDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
|
|
| CuRO_HCO_II_like_6 |
cd13918 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
122-255 |
5.42e-24 |
|
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.
Pssm-ID: 259985 [Multi-domain] Cd Length: 139 Bit Score: 96.37 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 122 DLTVKITGSQWKWHYSYFGEdveffsllatsdkeiegleVKGAHYLlevdkplVLPVDRKVRFLMTSDDVIHSWWVPAFA 201
Cdd:cd13918 32 ALEVEVEGFQFGWQFEYPNG-------------------VTTGNTL-------RVPADTPIALRVTSTDVFHTFGIPELR 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 518661713 202 VKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFMPIVVHAMEEDEFDAWL 255
Cdd:cd13918 86 VKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
|
|
| CuRO_UO_II |
cd04212 |
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ... |
123-246 |
3.52e-14 |
|
The cupredoxin domain of Ubiquinol oxidase subunit II; 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. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.
Pssm-ID: 259874 [Multi-domain] Cd Length: 99 Bit Score: 67.96 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 123 LTVKITGSQWKWHYSYFGEDVeffsllATSDKeieglevkgahyllevdkpLVLPVDRKVRFLMTSDDVIHSWWVPAFAV 202
Cdd:cd04212 1 LEIQVVSLDWKWLFIYPEQGI------ATVNE-------------------LVIPVGRPVNFRLTSDSVMNSFFIPQLGG 55
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 518661713 203 KKDTIPGFINEAWTKIDEPGVYRGQCAELCGraHGF--MPIVVHAM 246
Cdd:cd04212 56 QIYAMAGMQTQLHLIADKPGTYQGLSANYSG--EGFsdMKFKVLAV 99
|
|
| ba3_CcO_II_C |
cd13913 |
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ... |
173-239 |
2.40e-13 |
|
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; 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.
Pssm-ID: 259980 [Multi-domain] Cd Length: 99 Bit Score: 65.67 E-value: 2.40e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518661713 173 PLVLPVDRKVRFLMTSDDVIHSWWVPAFAVKKDTIPGFINEAWTKIDEPGVYRGQCAELCGRAHGFM 239
Cdd:cd13913 26 EIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
|
|
| Cytochrom_C |
pfam00034 |
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ... |
286-361 |
4.34e-12 |
|
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.
Pssm-ID: 459641 [Multi-domain] Cd Length: 89 Bit Score: 61.79 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 286 GEEVYKTRCAVCHQANGEGIPGAFPAIKGSPIALG----DVDVHI--------DTIVYGRGGTAMQAFDnQLTEKEIAAV 353
Cdd:pfam00034 3 GKKLFAANCAACHGVNGEGAGAGGPDLAGLAARYPgdalGAIRENkhaiggggVDRAGGPPGTGMPAFD-GLTDEEIADL 81
|
....*...
gi 518661713 354 VTYQRNAW 361
Cdd:pfam00034 82 VAYLLSLS 89
|
|
| TsdA |
COG3258 |
Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion ... |
286-356 |
1.82e-09 |
|
Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion transport and metabolism];
Pssm-ID: 442489 [Multi-domain] Cd Length: 216 Bit Score: 57.17 E-value: 1.82e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518661713 286 GEEVYKTRCAVCHQANGEGIPGA-----FPAIKGSP-IALGDVDVHIDTIVYGRGGTAMQAFDNQ-LTEKEIAAVVTY 356
Cdd:COG3258 120 GKALYAERCASCHGADGEGQGRAdgqygFPPLWGGDsYNDGAGMARLGTLADFIKGRNMPLGKPGsLSDDEAWDVAAY 197
|
|
| CytC553 |
COG2863 |
Cytochrome c553 [Energy production and conversion]; |
270-356 |
5.34e-09 |
|
Cytochrome c553 [Energy production and conversion];
Pssm-ID: 442110 [Multi-domain] Cd Length: 98 Bit Score: 53.19 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 270 KDALDASLSLAELNTIGEEvYKTRCAVCHQANGEG-IPGAFPAIKGspialgdvdVHIDTIVY--------GRGGTAMQA 340
Cdd:COG2863 2 KLALLAAPAAAGDAARGKA-YAAACAACHGADGEGnPGGGAPRLAG---------QHAEYLVAqlkafrsgARKNGVMPA 71
|
90
....*....|....*.
gi 518661713 341 FDNQLTEKEIAAVVTY 356
Cdd:COG2863 72 IAKGLSDEDIKALAAY 87
|
|
| Cytochrome_CBB3 |
pfam13442 |
Cytochrome C oxidase, cbb3-type, subunit III; |
286-356 |
1.96e-07 |
|
Cytochrome C oxidase, cbb3-type, subunit III;
Pssm-ID: 463879 [Multi-domain] Cd Length: 67 Bit Score: 47.79 E-value: 1.96e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518661713 286 GEEVYKTRCAVCHqanGEGIPGafPAIKGSPIALGDVdvhIDTIVYGRGgtAMQAFDNQLTEKEIAAVVTY 356
Cdd:pfam13442 6 GEALYAANCASCH---GTGGAG--PSLAGRALPPEAL---VDIIRNGKG--AMPAFGGDLSDEELEALAAY 66
|
|
| CuRO_HCO_II_like_1 |
cd13916 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
160-239 |
8.56e-07 |
|
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.
Pssm-ID: 259983 [Multi-domain] Cd Length: 93 Bit Score: 46.61 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 160 EVKGAHYLLEVDkPLVLPVDRKVRFLMTSDDVIHswwvpAFAVKKD---------TIPGFINEAWTKIDEPGVYRGQCAE 230
Cdd:cd13916 4 AVTGHQWYWELS-RTEIPAGKPVEFRVTSADVNH-----GFGIYDPdmrllaqtqAMPGYTNVLRYTFDKPGTYTILCLE 77
|
....*....
gi 518661713 231 LCGRAHGFM 239
Cdd:cd13916 78 YCGLAHHVM 86
|
|
| CytC5 |
COG3245 |
Cytochrome c5 [Energy production and conversion]; |
261-356 |
1.57e-04 |
|
Cytochrome c5 [Energy production and conversion];
Pssm-ID: 442476 [Multi-domain] Cd Length: 108 Bit Score: 40.82 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 261 LAIAEQQAAKDALDASLSLAELNTiGEEVYKTRCAVCHQANGEGIPGAF-PAIKGSPIALGDvDVHIDTIVYGRGgtAM- 338
Cdd:COG3245 11 LALRIAPVGAVALAAAAAAAAARS-GEAVYNATCAACHATGVAGAPKLGdKAAWAPRIAKGM-DTLLKHAINGFN--AMp 86
|
90 100
....*....|....*....|.
gi 518661713 339 ---QAFDnqLTEKEIAAVVTY 356
Cdd:COG3245 87 pkgGCAD--LSDDEVKAAVDY 105
|
|
| PRK14486 |
PRK14486 |
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional |
286-359 |
3.17e-04 |
|
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional
Pssm-ID: 184704 [Multi-domain] Cd Length: 294 Bit Score: 42.11 E-value: 3.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518661713 286 GEEVYKTRCAVCHQANGEGIPGAFPaikgSPIALGDV--DVHIDTIVYGRGGTAMQAFDNQLTEKEIAAVVTYQRN 359
Cdd:PRK14486 218 GKALYDANCAACHGDEAQGQEGVAL----NDIDDGDLpdAAYFGMIKGGSDAKGMPGFGGDLSDDDIWAIVAYIRS 289
|
|
| COX2_TM |
pfam02790 |
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ... |
31-95 |
7.77e-04 |
|
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.
Pssm-ID: 397083 [Multi-domain] Cd Length: 89 Bit Score: 38.08 E-value: 7.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518661713 31 NMTQGVTEISGKVYELHMLIFYICCAIAFVVFGVMFYSILRHRKSKGAVAA-HFHESTKVEIVWTI 95
Cdd:pfam02790 8 GFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITArYTTHGQTIEIIWTI 73
|
|
| ccoP |
TIGR00782 |
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ... |
269-367 |
3.55e-03 |
|
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of approximately 26 kDa of the cbb3 type copper and heme-containing cytochrome oxidase. [Energy metabolism, Electron transport]
Pssm-ID: 129864 [Multi-domain] Cd Length: 285 Bit Score: 39.11 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 269 AKDALDASLSLAElntiGEEVYKTRCAVCHQANGEGIPGaFPAIKGSPIALG-DVDVHIDTIVYGR-----GGTA---MQ 339
Cdd:TIGR00782 97 AKDPELKQYARNA----GAAIFRTWCAQCHGSGAGGAKG-FPNLLDNDWLWGgTLEGIHTTIKHGIrdpddGDTYvgeMP 171
|
90 100
....*....|....*....|....*...
gi 518661713 340 AFDNQLTEKEIAAVVTYQRNAWGNDTGD 367
Cdd:TIGR00782 172 AFGPLLEEADIKDVASYVMSLSSGKPKD 199
|
|
| ccoP |
TIGR00782 |
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ... |
261-356 |
3.99e-03 |
|
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of approximately 26 kDa of the cbb3 type copper and heme-containing cytochrome oxidase. [Energy metabolism, Electron transport]
Pssm-ID: 129864 [Multi-domain] Cd Length: 285 Bit Score: 38.72 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518661713 261 LAIAEQQAAKDALDASLSL-------AELNTIGEEVYKTRCAVCHQANGEGIPGafpaiKGSPIALGDVDVH-------I 326
Cdd:TIGR00782 174 GPLLEEADIKDVASYVMSLssgkpkdEALAAKGQELFADNCTTCHGEDGKGLQE-----LGAPNLTDDVWLYggdlktiT 248
|
90 100 110
....*....|....*....|....*....|
gi 518661713 327 DTIVYGRGGTaMQAFDNQLTEKEIAAVVTY 356
Cdd:TIGR00782 249 TTITNGRGGV-MPAWGPRLSEAQIKALAAY 277
|
|
| |
