|
Name |
Accession |
Description |
Interval |
E-value |
| CyoA |
COG1622 |
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion]; |
14-261 |
2.29e-89 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
Pssm-ID: 441229 [Multi-domain] Cd Length: 229 Bit Score: 269.01 E-value: 2.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 14 LILIGFAAPAISAERSLNMTPGVTEISGKVYHLHMLIFYICVAIALVVFGAMFYAIFKHRKSKG-AVAAHFHESTKVEII 92
Cdd:COG1622 3 RLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGdADPAQFHHNTKLEIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 93 WTIIPIVILVAMAIPATKTLVAMEDTSQSDLTIKITGSQWKWHYSYFDEGVEfysllatsqkqidgieakgahylleVDQ 172
Cdd:COG1622 83 WTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA-------------------------TVN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 173 PLVVPVHRKIRFLLTSDDVIHSWWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYD 252
Cdd:COG1622 138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217
|
....*....
gi 2029777874 253 QWLNDKKAE 261
Cdd:COG1622 218 AWLAEQKAS 226
|
|
| CcO_II_C |
cd13912 |
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ... |
121-254 |
3.06e-62 |
|
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: 195.87 E-value: 3.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 121 SDLTIKITGSQWKWHYSYFD-EGVEFYSLLATSQKQidgieAKGAHYLLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVPA 199
Cdd:cd13912 1 PSLTIKAIGHQWYWSYEYSDfNDLEFDSYMIPEDDL-----EKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2029777874 200 FAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQW 254
Cdd:cd13912 76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
|
|
| CoxB |
TIGR02866 |
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ... |
37-256 |
1.02e-48 |
|
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: 163.71 E-value: 1.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 37 TEISGKVYHLHMLIFYICVAIALVVFGAMFYAIFKHR-KSKGAVAAHFHESTKVEIIWTIIPIVILVAMAIP-ATKTLVA 114
Cdd:TIGR02866 3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRrKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAAtAKGLLYL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 115 MEDTSQSDLTIKITGSQWKWHYSYfdegvefysllatsqkqidgieakgAHYLLEVDQPLVVPVHRKIRFLLTSDDVIHS 194
Cdd:TIGR02866 83 ERPIPKDALKVKVTGYQWWWDFEY-------------------------PESGFTTVNELVLPAGTPVELQVTSKDVIHS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2029777874 195 WWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLN 256
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
|
|
| COX2 |
MTH00140 |
cytochrome c oxidase subunit II; Provisional |
43-256 |
4.64e-47 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214430 [Multi-domain] Cd Length: 228 Bit Score: 160.10 E-value: 4.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 43 VYHLH--MLIFYICVAIALVVFGAMFYAIFKHrkskgavaaHFHESTKVEIIWTIIPIVILVAMAIPATKTLVAMEDTSQ 120
Cdd:MTH00140 22 FFHDHamVVLVLIFSFVMYMLVLLLFNKFSCR---------TILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 121 SDLTIKITGSQWKWHYSYFD-EGVEFYSLLatsqkqIDGIEAKGAHY-LLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVP 198
Cdd:MTH00140 93 PLLTVKAIGHQWYWSYEYSDfSVIEFDSYM------VPENELELGDFrLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2029777874 199 AFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLN 256
Cdd:MTH00140 167 SLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
|
|
| COX2 |
pfam00116 |
Cytochrome C oxidase subunit II, periplasmic domain; |
123-245 |
8.19e-43 |
|
Cytochrome C oxidase subunit II, periplasmic domain;
Pssm-ID: 395066 [Multi-domain] Cd Length: 120 Bit Score: 145.63 E-value: 8.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 123 LTIKITGSQWKWHYSYFD-EGVEFYSLLATSQKQidgieAKGAHYLLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVPAFA 201
Cdd:pfam00116 1 LTIKAIGHQWYWSYEYTDfGDLEFDSYMIPTEDL-----EEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2029777874 202 VKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQA 245
Cdd:pfam00116 76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
|
|
| CccA |
COG2010 |
Cytochrome c, mono- and diheme variants [Energy production and conversion]; |
195-363 |
6.36e-27 |
|
Cytochrome c, mono- and diheme variants [Energy production and conversion];
Pssm-ID: 441613 [Multi-domain] Cd Length: 169 Bit Score: 105.42 E-value: 6.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 195 WWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLNDKKAEVALAKQEAEKALQ 274
Cdd:COG2010 1 GGLLGGALGALLGGGGLSDEGAGAAGAGGVAAAGAGLAGALVDGAAAAAALGAAAAAAAAAAALALALLLALLLAAAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 275 SSMSLDELMTLGEKVYLDRCAVCHQPTGLGIPGAFPAMKGSPVTTGDVHQHIATVVDGRSGTAMQAFGNQLSEKELAAVI 354
Cdd:COG2010 81 APAADAEALARGKALYEQNCAACHGADGKGGLGAAPNLTDDALYGGDPEALVETILNGRPGGAMPAFGGQLSDEEIAALA 160
|
....*....
gi 2029777874 355 TYERNAWGN 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 |
8.52e-09 |
|
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: 52.16 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 286 GEKVYLDRCAVCHQPTGLGIPGAFPAMKGSPVTTG---------DVHQHIATVVD---GRSGTAMQAFgNQLSEKELAAV 353
Cdd:pfam00034 3 GKKLFAANCAACHGVNGEGAGAGGPDLAGLAARYPgdalgaireNKHAIGGGGVDragGPPGTGMPAF-DGLTDEEIADL 81
|
....*...
gi 2029777874 354 ITYERNAW 361
Cdd:pfam00034 82 VAYLLSLS 89
|
|
| ccoP |
TIGR00782 |
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ... |
281-356 |
6.54e-04 |
|
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: 41.03 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 281 ELMTLGEKVYLDRCAVCHQPTGLGIPGafpamKGSPVTTGDVHQH-------IATVVDGRSGTaMQAFGNQLSEKELAAV 353
Cdd:TIGR00782 201 ALAAKGQELFADNCTTCHGEDGKGLQE-----LGAPNLTDDVWLYggdlktiTTTITNGRGGV-MPAWGPRLSEAQIKAL 274
|
...
gi 2029777874 354 ITY 356
Cdd:TIGR00782 275 AAY 277
|
|
| PRK14486 |
PRK14486 |
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional |
268-359 |
5.66e-03 |
|
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional
Pssm-ID: 184704 [Multi-domain] Cd Length: 294 Bit Score: 38.26 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 268 EAEKALQSSMSLdelMTLGEKVYLDRCAVCHQPTGLGIPGAFPAMKGSPVTTGDVHqhIATVVDGRSGTAMQAFGNQLSE 347
Cdd:PRK14486 203 ELPNPFATDVAA---IAKGKALYDANCAACHGDEAQGQEGVALNDIDDGDLPDAAY--FGMIKGGSDAKGMPGFGGDLSD 277
|
90
....*....|..
gi 2029777874 348 KELAAVITYERN 359
Cdd:PRK14486 278 DDIWAIVAYIRS 289
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CyoA |
COG1622 |
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion]; |
14-261 |
2.29e-89 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
Pssm-ID: 441229 [Multi-domain] Cd Length: 229 Bit Score: 269.01 E-value: 2.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 14 LILIGFAAPAISAERSLNMTPGVTEISGKVYHLHMLIFYICVAIALVVFGAMFYAIFKHRKSKG-AVAAHFHESTKVEII 92
Cdd:COG1622 3 RLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGdADPAQFHHNTKLEIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 93 WTIIPIVILVAMAIPATKTLVAMEDTSQSDLTIKITGSQWKWHYSYFDEGVEfysllatsqkqidgieakgahylleVDQ 172
Cdd:COG1622 83 WTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA-------------------------TVN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 173 PLVVPVHRKIRFLLTSDDVIHSWWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYD 252
Cdd:COG1622 138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217
|
....*....
gi 2029777874 253 QWLNDKKAE 261
Cdd:COG1622 218 AWLAEQKAS 226
|
|
| CcO_II_C |
cd13912 |
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ... |
121-254 |
3.06e-62 |
|
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: 195.87 E-value: 3.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 121 SDLTIKITGSQWKWHYSYFD-EGVEFYSLLATSQKQidgieAKGAHYLLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVPA 199
Cdd:cd13912 1 PSLTIKAIGHQWYWSYEYSDfNDLEFDSYMIPEDDL-----EKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2029777874 200 FAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQW 254
Cdd:cd13912 76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
|
|
| CoxB |
TIGR02866 |
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ... |
37-256 |
1.02e-48 |
|
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: 163.71 E-value: 1.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 37 TEISGKVYHLHMLIFYICVAIALVVFGAMFYAIFKHR-KSKGAVAAHFHESTKVEIIWTIIPIVILVAMAIP-ATKTLVA 114
Cdd:TIGR02866 3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRrKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAAtAKGLLYL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 115 MEDTSQSDLTIKITGSQWKWHYSYfdegvefysllatsqkqidgieakgAHYLLEVDQPLVVPVHRKIRFLLTSDDVIHS 194
Cdd:TIGR02866 83 ERPIPKDALKVKVTGYQWWWDFEY-------------------------PESGFTTVNELVLPAGTPVELQVTSKDVIHS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2029777874 195 WWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLN 256
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
|
|
| COX2 |
MTH00140 |
cytochrome c oxidase subunit II; Provisional |
43-256 |
4.64e-47 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214430 [Multi-domain] Cd Length: 228 Bit Score: 160.10 E-value: 4.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 43 VYHLH--MLIFYICVAIALVVFGAMFYAIFKHrkskgavaaHFHESTKVEIIWTIIPIVILVAMAIPATKTLVAMEDTSQ 120
Cdd:MTH00140 22 FFHDHamVVLVLIFSFVMYMLVLLLFNKFSCR---------TILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 121 SDLTIKITGSQWKWHYSYFD-EGVEFYSLLatsqkqIDGIEAKGAHY-LLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVP 198
Cdd:MTH00140 93 PLLTVKAIGHQWYWSYEYSDfSVIEFDSYM------VPENELELGDFrLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2029777874 199 AFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLN 256
Cdd:MTH00140 167 SLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
|
|
| COX2 |
MTH00139 |
cytochrome c oxidase subunit II; Provisional |
44-258 |
5.11e-45 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214429 [Multi-domain] Cd Length: 226 Bit Score: 154.88 E-value: 5.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 44 YHLHMLIfyICVAIALVVFGAMFYAIFKHRKSKGAVaahfhESTKVEIIWTIIPIVILVAMAIPATKTLVAMEDTSQSDL 123
Cdd:MTH00139 23 FHDHAMV--ILIMILSFVGYISLSLMSNKFTSRSLL-----ESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 124 TIKITGSQWKWHYSYFD-EGVEFYSLLATSQKQidgieAKGAHYLLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVPAFAV 202
Cdd:MTH00139 96 TFKAVGHQWYWSYEYSDfKNLSFDSYMIPTEDL-----SSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2029777874 203 KKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLNDK 258
Cdd:MTH00139 171 KIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
|
|
| COX2 |
MTH00168 |
cytochrome c oxidase subunit II; Provisional |
29-256 |
2.35e-43 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177223 [Multi-domain] Cd Length: 225 Bit Score: 150.52 E-value: 2.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 29 SLNMTPGVTEISGKVYHLHMLIFYICVAIALVVFgAMFYAIfkhrKSKGAVAAHFHESTKVEIIWTIIPIVILVAMAIPA 108
Cdd:MTH00168 6 QLGLQDAASPVMEELILFHDHALLILVLILTLVL-YSLLVL----VTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 109 TKTLVAMEDTSQSDLTIKITGSQWKWHYSYFD-EGVEFYSLLATSQKQIDGieakgAHYLLEVDQPLVVPVHRKIRFLLT 187
Cdd:MTH00168 81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDyNDLEFDSYMVPTQDLSPG-----QFRLLEVDNRLVLPMDSKIRVLVT 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2029777874 188 SDDVIHSWWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLN 256
Cdd:MTH00168 156 SADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
|
|
| COX2 |
MTH00038 |
cytochrome c oxidase subunit II; Provisional |
44-257 |
3.05e-43 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177113 [Multi-domain] Cd Length: 229 Bit Score: 150.24 E-value: 3.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 44 YHLHMLIFYICVAIaLVVFG--AMFYAIFKHRKskgavaahFHESTKVEIIWTIIPIVILVAMAIPATKTLVAMEDTSQS 121
Cdd:MTH00038 23 FHDYALIILTLITI-LVFYGlaSLLFSSPTNRF--------FLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 122 DLTIKITGSQWKWHYSYFD-EGVEFYS-LLATSQKQIdgieakGAHYLLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVPA 199
Cdd:MTH00038 94 FLTIKAIGHQWYWSYEYTDyNDLEFDSyMVPTSDLST------GLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2029777874 200 FAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLND 257
Cdd:MTH00038 168 LGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225
|
|
| COX2 |
pfam00116 |
Cytochrome C oxidase subunit II, periplasmic domain; |
123-245 |
8.19e-43 |
|
Cytochrome C oxidase subunit II, periplasmic domain;
Pssm-ID: 395066 [Multi-domain] Cd Length: 120 Bit Score: 145.63 E-value: 8.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 123 LTIKITGSQWKWHYSYFD-EGVEFYSLLATSQKQidgieAKGAHYLLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVPAFA 201
Cdd:pfam00116 1 LTIKAIGHQWYWSYEYTDfGDLEFDSYMIPTEDL-----EEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2029777874 202 VKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQA 245
Cdd:pfam00116 76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
|
|
| COX2 |
MTH00023 |
cytochrome c oxidase subunit II; Validated |
46-261 |
1.49e-42 |
|
cytochrome c oxidase subunit II; Validated
Pssm-ID: 214402 [Multi-domain] Cd Length: 240 Bit Score: 148.74 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 46 LHMLIFYICVAIALVVFGAMFYAI---FKHRkskgavaaHFHESTKVEIIWTIIPIVILVAMAIPATKTLVAMEDTSQSD 122
Cdd:MTH00023 32 FHDQIMFLLIIIITVVLWLIVEALngkFYDR--------FLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 123 LTIKITGSQWKWHYSYFD---EGVEFYS-LLATSQKQidgieaKGAHYLLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVP 198
Cdd:MTH00023 104 LTIKAIGHQWYWSYEYSDyegETLEFDSyMVPTSDLN------SGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2029777874 199 AFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLNDKKAE 261
Cdd:MTH00023 178 SLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSND 240
|
|
| COX2 |
MTH00051 |
cytochrome c oxidase subunit II; Provisional |
30-262 |
1.69e-42 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177126 [Multi-domain] Cd Length: 234 Bit Score: 148.39 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 30 LNMTPGVTEISGKVYHLHMLIFYICVAIALVVFGAMFYAIfkhrkskgaVAAHFH----ESTKVEIIWTIIPIVILVAMA 105
Cdd:MTH00051 9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRAL---------TTKYYHkylfEGTLIEIIWTLIPAAILIFIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 106 IPATKTLVAMEDTSQSDLTIKITGSQWKWHYSYFDEG---VEFYS-LLATSQKQidgieaKGAHYLLEVDQPLVVPVHRK 181
Cdd:MTH00051 80 FPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGtdtIEFDSyMIPTSDLN------SGDLRLLEVDNRLIVPIQTQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 182 IRFLLTSDDVIHSWWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLNDKKAE 261
Cdd:MTH00051 154 VRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
|
.
gi 2029777874 262 V 262
Cdd:MTH00051 234 I 234
|
|
| COX2 |
MTH00185 |
cytochrome c oxidase subunit II; Provisional |
45-262 |
6.52e-42 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 164736 [Multi-domain] Cd Length: 230 Bit Score: 146.95 E-value: 6.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 45 HLHMLIFYICVAIaLVVFGAMFYAIFKHRkskgavaaHFHESTKVEIIWTIIPIVILVAMAIPATKTLVAMEDTSQSDLT 124
Cdd:MTH00185 26 HTLMIVFLISTLV-LYIIVAMVTTKLTNK--------YILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 125 IKITGSQWKWHYSYFD-EGVEFYSLLATSQKQidgieAKGAHYLLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVPAFAVK 203
Cdd:MTH00185 97 IKAMGHQWYWSYEYTDyEQLEFDSYMTPTQDL-----TPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVK 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2029777874 204 KDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLNDKKAEV 262
Cdd:MTH00185 172 MDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEEA 230
|
|
| COX2 |
MTH00117 |
cytochrome c oxidase subunit II; Provisional |
101-256 |
1.40e-41 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177178 [Multi-domain] Cd Length: 227 Bit Score: 145.83 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 101 LVAMAIPATKTLVAMEDTSQSDLTIKITGSQWKWHYSYFD-EGVEFYSLLATSQKQidgieAKGAHYLLEVDQPLVVPVH 179
Cdd:MTH00117 73 LILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDyKDLSFDSYMIPTQDL-----PNGHFRLLEVDHRMVIPME 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2029777874 180 RKIRFLLTSDDVIHSWWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLN 256
Cdd:MTH00117 148 SPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSS 224
|
|
| COX2 |
MTH00154 |
cytochrome c oxidase subunit II; Provisional |
101-256 |
1.98e-41 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214438 [Multi-domain] Cd Length: 227 Bit Score: 145.36 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 101 LVAMAIPATKTLVAMEDTSQSDLTIKITGSQWKWHYSYFD-EGVEFYS-LLATSQKQIDGIEakgahyLLEVDQPLVVPV 178
Cdd:MTH00154 73 LIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDfKNIEFDSyMIPTNELENNGFR------LLDVDNRLVLPM 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2029777874 179 HRKIRFLLTSDDVIHSWWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLN 256
Cdd:MTH00154 147 NTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
|
|
| COX2 |
MTH00076 |
cytochrome c oxidase subunit II; Provisional |
101-256 |
7.39e-40 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 164646 [Multi-domain] Cd Length: 228 Bit Score: 141.46 E-value: 7.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 101 LVAMAIPATKTLVAMEDTSQSDLTIKITGSQWKWHYSYFD-EGVEFYSLLATSQKQIdgieaKGAHYLLEVDQPLVVPVH 179
Cdd:MTH00076 73 LIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDyEDLSFDSYMIPTQDLT-----PGQFRLLEVDNRMVVPME 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2029777874 180 RKIRFLLTSDDVIHSWWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLN 256
Cdd:MTH00076 148 SPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSS 224
|
|
| COX2 |
MTH00008 |
cytochrome c oxidase subunit II; Validated |
44-255 |
2.28e-39 |
|
cytochrome c oxidase subunit II; Validated
Pssm-ID: 164584 [Multi-domain] Cd Length: 228 Bit Score: 139.99 E-value: 2.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 44 YHLHMLIFYICVaiaLVVFGAMFYAIFKHRKSKGAVAahfhESTKVEIIWTIIPIVILVAMAIPATKTLVAMEDTSQSDL 123
Cdd:MTH00008 23 FHDHALLILTLV---LTVVGYAMTSLMFNKLSNRYIL----EAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 124 TIKITGSQWKWHYSYFD-EGVEFYS-LLATSQKqidgieAKGAHYLLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVPAFA 201
Cdd:MTH00008 96 TLKTIGHQWYWSYEYSDfSNLEFDSyMLPTSDL------SPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2029777874 202 VKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWL 255
Cdd:MTH00008 170 VKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
|
|
| COX2 |
MTH00080 |
cytochrome c oxidase subunit II; Provisional |
48-255 |
2.64e-39 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177149 [Multi-domain] Cd Length: 231 Bit Score: 140.15 E-value: 2.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 48 MLIFYICVaIALVVFGAMFYAI----FKHRKSkgavaahfhESTKVEIIWTIIPIVILVAMAIPATKTLVAMEDTS-QSD 122
Cdd:MTH00080 28 SLLFGEFV-LAFVVFLFLYLISnnfyFKSKKI---------EYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 123 LTIKITGSQWKWHYSYFD-EGVEFYSLLatsqKQIDGIEAkGAHYLLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVPAFA 201
Cdd:MTH00080 98 LTVKVTGHQWYWSYEFSDiPGLEFDSYM----KSLDQLRL-GEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2029777874 202 VKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWL 255
Cdd:MTH00080 173 IKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
|
|
| COX2 |
MTH00129 |
cytochrome c oxidase subunit II; Provisional |
82-254 |
3.92e-39 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177187 [Multi-domain] Cd Length: 230 Bit Score: 139.46 E-value: 3.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 82 HFHESTKVEIIWTIIPIVILVAMAIPATKTLVAMEDTSQSDLTIKITGSQWKWHYSYFD-EGVEFYSLLATSQKQidgie 160
Cdd:MTH00129 54 YILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDyEDLGFDSYMIPTQDL----- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 161 AKGAHYLLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMP 240
Cdd:MTH00129 129 TPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMP 208
|
170
....*....|....
gi 2029777874 241 IVVQAMAEDDYDQW 254
Cdd:MTH00129 209 IVVEAVPLEHFENW 222
|
|
| COX2 |
MTH00027 |
cytochrome c oxidase subunit II; Provisional |
101-255 |
4.62e-37 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214405 [Multi-domain] Cd Length: 262 Bit Score: 135.15 E-value: 4.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 101 LVAMAIPATKTLVAMEDTS-QSDLTIKITGSQWKWHYSYFDEG---VEFYS-LLATSQKQIdgieakGAHYLLEVDQPLV 175
Cdd:MTH00027 104 LILIAFPSLRLLYIMDECGfSANITIKVTGHQWYWSYSYEDYGeknIEFDSyMIPTADLEF------GDLRLLEVDNRLI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 176 VPVHRKIRFLLTSDDVIHSWWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWL 255
Cdd:MTH00027 178 LPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
|
|
| COX2 |
MTH00098 |
cytochrome c oxidase subunit II; Validated |
101-254 |
5.85e-37 |
|
cytochrome c oxidase subunit II; Validated
Pssm-ID: 177160 [Multi-domain] Cd Length: 227 Bit Score: 133.69 E-value: 5.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 101 LVAMAIPATKTLVAMEDTSQSDLTIKITGSQWKWHYSYFD-EGVEFYSLLATSQKQidgieAKGAHYLLEVDQPLVVPVH 179
Cdd:MTH00098 73 LILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDyEDLSFDSYMIPTSDL-----KPGELRLLEVDNRVVLPME 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2029777874 180 RKIRFLLTSDDVIHSWWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQW 254
Cdd:MTH00098 148 MPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
|
|
| CuRO_HCO_II_like_5 |
cd13919 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
122-239 |
3.68e-32 |
|
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: 116.97 E-value: 3.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 122 DLTIKITGSQWKWHYSYFDEGVEFysllatsqkqidgieakGAHYLLEVDQpLVVPVHRKIRFLLTSDDVIHSWWVPAFA 201
Cdd:cd13919 1 ALVVEVTAQQWAWTFRYPGGDGKL-----------------GTDDDVTSPE-LHLPVGRPVLFNLRSKDVIHSFWVPEFR 62
|
90 100 110
....*....|....*....|....*....|....*...
gi 2029777874 202 VKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFM 239
Cdd:cd13919 63 VKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
|
|
| CuRO_CcO_Caa3_II |
cd04213 |
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ... |
122-246 |
1.12e-31 |
|
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: 115.79 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 122 DLTIKITGSQWKWHYSYFDEGVEfysLLATSQKqidgieakgahyllevdqpLVVPVHRKIRFLLTSDDVIHSWWVPAFA 201
Cdd:cd04213 1 ALTIEVTGHQWWWEFRYPDEPGR---GIVTANE-------------------LHIPVGRPVRLRLTSADVIHSFWVPSLA 58
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2029777874 202 VKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAM 246
Cdd:cd04213 59 GKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
|
|
| PTZ00047 |
PTZ00047 |
cytochrome c oxidase subunit II; Provisional |
168-251 |
7.81e-29 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 240243 [Multi-domain] Cd Length: 162 Bit Score: 109.91 E-value: 7.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 168 LEVDQPLVVPVHRKIRFLLTSDDVIHSWWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMA 247
Cdd:PTZ00047 69 LEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVS 148
|
....
gi 2029777874 248 EDDY 251
Cdd:PTZ00047 149 PEAY 152
|
|
| CccA |
COG2010 |
Cytochrome c, mono- and diheme variants [Energy production and conversion]; |
195-363 |
6.36e-27 |
|
Cytochrome c, mono- and diheme variants [Energy production and conversion];
Pssm-ID: 441613 [Multi-domain] Cd Length: 169 Bit Score: 105.42 E-value: 6.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 195 WWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWLNDKKAEVALAKQEAEKALQ 274
Cdd:COG2010 1 GGLLGGALGALLGGGGLSDEGAGAAGAGGVAAAGAGLAGALVDGAAAAAALGAAAAAAAAAAALALALLLALLLAAAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 275 SSMSLDELMTLGEKVYLDRCAVCHQPTGLGIPGAFPAMKGSPVTTGDVHQHIATVVDGRSGTAMQAFGNQLSEKELAAVI 354
Cdd:COG2010 81 APAADAEALARGKALYEQNCAACHGADGKGGLGAAPNLTDDALYGGDPEALVETILNGRPGGAMPAFGGQLSDEEIAALA 160
|
....*....
gi 2029777874 355 TYERNAWGN 363
Cdd:COG2010 161 AYLRSLSGN 169
|
|
| CuRO_HCO_II_like_3 |
cd13914 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
124-255 |
8.00e-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: 259981 [Multi-domain] Cd Length: 108 Bit Score: 102.87 E-value: 8.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 124 TIKITGSQWKWHYSYFDEGVEfysllatsqkqidgieakgahylleVDQPLVVPVHRKIRFLLTSDDVIHSWWVPAFAVK 203
Cdd:cd13914 2 EIEVEAYQWGWEFSYPEANVT-------------------------TSEQLVIPADRPVYFRITSRDVIHAFHVPELGLK 56
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2029777874 204 KDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWL 255
Cdd:cd13914 57 QDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
|
|
| CuRO_HCO_II_like |
cd13842 |
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ... |
123-243 |
9.86e-27 |
|
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: 102.37 E-value: 9.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 123 LTIKITGSQWKWHYSYFDegvefysllatsqkqidgieakgahylLEVDQPLVVPVHRKIRFLLTSDDVIHSWWVPAFAV 202
Cdd:cd13842 1 LTVYVTGVQWSWTFIYPN---------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGV 53
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2029777874 203 KKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVV 243
Cdd:cd13842 54 KVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKV 94
|
|
| CuRO_HCO_II_like_2 |
cd13915 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
122-243 |
1.91e-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: 259982 [Multi-domain] Cd Length: 98 Bit Score: 101.55 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 122 DLTIKITGSQWKWHYSYFDEGVEfysllatsqkqidgieakgahyllevDQPLVVPVHRKIRFLLTSDDVIHSWWVPAFA 201
Cdd:cd13915 1 ALEIQVTGRQWMWEFTYPNGKRE--------------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFR 54
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2029777874 202 VKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVV 243
Cdd:cd13915 55 IKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
|
|
| COX2 |
MTH00047 |
cytochrome c oxidase subunit II; Provisional |
44-244 |
1.40e-25 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214412 [Multi-domain] Cd Length: 194 Bit Score: 102.34 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 44 YHLHMLIFYICVAIALVVFGAMFYAIFkhrkSKGAVAAHFHESTKVEiiwtiipiviLVAMAIPATKTLV---------- 113
Cdd:MTH00047 8 YDIVCYILALCVFIPCWVYIMLCWQVV----SGNGSVNFGSENQVLE----------LLWTVVPTLLVLVlcflnlnfit 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 114 -AMEDTSQSdlTIKITGSQWKWHYSYFDEGveFYSLLATsqKQIDGieakgahylleVDQPLVVPVHRKIRFLLTSDDVI 192
Cdd:MTH00047 74 sDLDCFSSE--TIKVIGHQWYWSYEYSFGG--SYDSFMT--DDIFG-----------VDKPLRLVYGVPYHLLVTSSDVI 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2029777874 193 HSWWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQ 244
Cdd:MTH00047 137 HSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
|
|
| CuRO_HCO_II_like_6 |
cd13918 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
122-255 |
1.40e-22 |
|
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: 92.52 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 122 DLTIKITGSQWKWHYSYFDEGvefysllatsqKQIDGieakgahyllevdqpLVVPVHRKIRFLLTSDDVIHSWWVPAFA 201
Cdd:cd13918 32 ALEVEVEGFQFGWQFEYPNGV-----------TTGNT---------------LRVPADTPIALRVTSTDVFHTFGIPELR 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2029777874 202 VKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFMPIVVQAMAEDDYDQWL 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 |
1.01e-13 |
|
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: 66.42 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 123 LTIKITGSQWKWHYSYFDEGVefysllATsqkqidgieakgahylleVDQpLVVPVHRKIRFLLTSDDVIHSWWVPAFAV 202
Cdd:cd04212 1 LEIQVVSLDWKWLFIYPEQGI------AT------------------VNE-LVIPVGRPVNFRLTSDSVMNSFFIPQLGG 55
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2029777874 203 KKDSIPGFINEAWTRIEEPGVYRGQCAELCGraHGF--MPIVVQAM 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 |
1.38e-11 |
|
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: 60.66 E-value: 1.38e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2029777874 173 PLVVPVHRKIRFLLTSDDVIHSWWVPAFAVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGRAHGFM 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 |
8.52e-09 |
|
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: 52.16 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 286 GEKVYLDRCAVCHQPTGLGIPGAFPAMKGSPVTTG---------DVHQHIATVVD---GRSGTAMQAFgNQLSEKELAAV 353
Cdd:pfam00034 3 GKKLFAANCAACHGVNGEGAGAGGPDLAGLAARYPgdalgaireNKHAIGGGGVDragGPPGTGMPAF-DGLTDEEIADL 81
|
....*...
gi 2029777874 354 ITYERNAW 361
Cdd:pfam00034 82 VAYLLSLS 89
|
|
| TsdA |
COG3258 |
Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion ... |
286-356 |
2.83e-08 |
|
Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion transport and metabolism];
Pssm-ID: 442489 [Multi-domain] Cd Length: 216 Bit Score: 53.70 E-value: 2.83e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2029777874 286 GEKVYLDRCAVCHQPTGLGIPGA-----FPAMKGSPV-TTGDVHQHIATVVDGRSGTAMQAF-GNQLSEKELAAVITY 356
Cdd:COG3258 120 GKALYAERCASCHGADGEGQGRAdgqygFPPLWGGDSyNDGAGMARLGTLADFIKGRNMPLGkPGSLSDDEAWDVAAY 197
|
|
| Cytochrome_CBB3 |
pfam13442 |
Cytochrome C oxidase, cbb3-type, subunit III; |
286-356 |
1.88e-07 |
|
Cytochrome C oxidase, cbb3-type, subunit III;
Pssm-ID: 463879 [Multi-domain] Cd Length: 67 Bit Score: 47.79 E-value: 1.88e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2029777874 286 GEKVYLDRCAVCHQPTGLGipgafPAMKGSPVTTGDVHQHIAtvvDGRsgTAMQAFGNQLSEKELAAVITY 356
Cdd:pfam13442 6 GEALYAANCASCHGTGGAG-----PSLAGRALPPEALVDIIR---NGK--GAMPAFGGDLSDEELEALAAY 66
|
|
| CuRO_HCO_II_like_1 |
cd13916 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
159-239 |
8.06e-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: 46.99 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 159 IEAKGAHYLLEVDqPLVVPVHRKIRFLLTSDDVIHswwvpAFAVKKD---------SIPGFINEAWTRIEEPGVYRGQCA 229
Cdd:cd13916 3 VAVTGHQWYWELS-RTEIPAGKPVEFRVTSADVNH-----GFGIYDPdmrllaqtqAMPGYTNVLRYTFDKPGTYTILCL 76
|
90
....*....|
gi 2029777874 230 ELCGRAHGFM 239
Cdd:cd13916 77 EYCGLAHHVM 86
|
|
| CytC553 |
COG2863 |
Cytochrome c553 [Energy production and conversion]; |
272-356 |
1.34e-06 |
|
Cytochrome c553 [Energy production and conversion];
Pssm-ID: 442110 [Multi-domain] Cd Length: 98 Bit Score: 46.26 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 272 ALQSSMSLDELMTLGEKvYLDRCAVCHQPTGLG-IPGAFPAMKGspvttgdvhQH----IATVVDGRSG----TAMQAFG 342
Cdd:COG2863 4 ALLAAPAAAGDAARGKA-YAAACAACHGADGEGnPGGGAPRLAG---------QHaeylVAQLKAFRSGarknGVMPAIA 73
|
90
....*....|....
gi 2029777874 343 NQLSEKELAAVITY 356
Cdd:COG2863 74 KGLSDEDIKALAAY 87
|
|
| PRK10525 |
PRK10525 |
cytochrome o ubiquinol oxidase subunit II; Provisional |
48-282 |
5.75e-06 |
|
cytochrome o ubiquinol oxidase subunit II; Provisional
Pssm-ID: 182518 [Multi-domain] Cd Length: 315 Bit Score: 47.87 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 48 MLIFYICVAIALVVFGamfyaiFKHRKS--KGAVAAHFHESTKVEIIWTIIPIVILVAMAIPATKTLVAME-----DTSQ 120
Cdd:PRK10525 51 MLIVVIPAILMAVGFA------WKYRASnkDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEpskplAHDE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 121 SDLTIKITGSQWKWHYSYFDEGVefysllATSQkqidgieakgahyllEVDQPLVVPVHRKIrfllTSDDVIHSWWVPAF 200
Cdd:PRK10525 125 KPITIEVVSMDWKWFFIYPEQGI------ATVN---------------EIAFPANVPVYFKV----TSNSVMNSFFIPRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 201 AVKKDSIPGFINEAWTRIEEPGVYRGQCAELCGraHGFMPIVVQAMA---EDDYDQWlndkkaeVALAKQEAeKALQSSM 277
Cdd:PRK10525 180 GSQIYAMAGMQTRLHLIANEPGTYDGISASYSG--PGFSGMKFKAIAtpdRAEFDQW-------VAKAKQSP-NTMNDMA 249
|
....*
gi 2029777874 278 SLDEL 282
Cdd:PRK10525 250 AFEKL 254
|
|
| ccoP |
TIGR00782 |
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ... |
281-356 |
6.54e-04 |
|
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: 41.03 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 281 ELMTLGEKVYLDRCAVCHQPTGLGIPGafpamKGSPVTTGDVHQH-------IATVVDGRSGTaMQAFGNQLSEKELAAV 353
Cdd:TIGR00782 201 ALAAKGQELFADNCTTCHGEDGKGLQE-----LGAPNLTDDVWLYggdlktiTTTITNGRGGV-MPAWGPRLSEAQIKAL 274
|
...
gi 2029777874 354 ITY 356
Cdd:TIGR00782 275 AAY 277
|
|
| Cyc7 |
COG3474 |
Cytochrome c2 [Energy production and conversion]; |
286-355 |
8.66e-04 |
|
Cytochrome c2 [Energy production and conversion];
Pssm-ID: 442697 [Multi-domain] Cd Length: 101 Bit Score: 38.32 E-value: 8.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 286 GEKVYLDRCAVCHQPTGLGIPGAFPAMKGspVttgdVHQHIATVVDGRSGTAMQAFGNQLSEKELAAVIT 355
Cdd:COG3474 6 GEKLFNRKCAACHSVDGGAGNRVGPNLNG--V----VGRKAGSVEGFAYSDALKASGLVWDEETLDAWLA 69
|
|
| PRK14486 |
PRK14486 |
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional |
268-359 |
5.66e-03 |
|
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional
Pssm-ID: 184704 [Multi-domain] Cd Length: 294 Bit Score: 38.26 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029777874 268 EAEKALQSSMSLdelMTLGEKVYLDRCAVCHQPTGLGIPGAFPAMKGSPVTTGDVHqhIATVVDGRSGTAMQAFGNQLSE 347
Cdd:PRK14486 203 ELPNPFATDVAA---IAKGKALYDANCAACHGDEAQGQEGVALNDIDDGDLPDAAY--FGMIKGGSDAKGMPGFGGDLSD 277
|
90
....*....|..
gi 2029777874 348 KELAAVITYERN 359
Cdd:PRK14486 278 DDIWAIVAYIRS 289
|
|
| |
