|
Name |
Accession |
Description |
Interval |
E-value |
| CyoA |
COG1622 |
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion]; |
11-260 |
2.89e-97 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
Pssm-ID: 441229 [Multi-domain] Cd Length: 229 Bit Score: 288.65 E-value: 2.89e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 11 LGLSAVFGQAQAAWDVNMRSGATDVSRSVFDLHMTIFWICVVIGVLVFGVMIYSMIAHRRSK-RQQSANFHENTRVEVLW 89
Cdd:COG1622 4 LLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKgDADPAQFHHNTKLEIVW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 90 TVIPLLILVGMAIPATRTLIHIYDSSESDVDVQITGYQWKWHYKYLGEDVEffsnlttpreqinnqspkgehylleVDEP 169
Cdd:COG1622 84 TVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA-------------------------TVNE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 170 LVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYAS 249
Cdd:COG1622 139 LVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDA 218
|
250
....*....|.
gi 515814187 250 WLGEKKAEAAK 260
Cdd:COG1622 219 WLAEQKASAAT 229
|
|
| CcO_II_C |
cd13912 |
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ... |
117-250 |
1.76e-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: 196.25 E-value: 1.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 117 SDVDVQITGYQWKWHYKYL-GEDVEFFSNLTTPREQinnqsPKGEHYLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPD 195
Cdd:cd13912 1 PSLTIKAIGHQWYWSYEYSdFNDLEFDSYMIPEDDL-----EKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 515814187 196 LAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASW 250
Cdd:cd13912 76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
|
|
| COX2 |
MTH00140 |
cytochrome c oxidase subunit II; Provisional |
50-252 |
1.01e-59 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214430 [Multi-domain] Cd Length: 228 Bit Score: 192.85 E-value: 1.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 50 CVVIGVLVFGVMIYSMIAHRRSKrQQSANFHENTRVEVLWTVIPLLILVGMAIPATRTLihiYDSSE---SDVDVQITGY 126
Cdd:MTH00140 27 AMVVLVLIFSFVMYMLVLLLFNK-FSCRTILEAQKLETIWTIVPALILVFLALPSLRLL---YLLDEtnnPLLTVKAIGH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 127 QWKWHYKYLGEDVEFFSNLTTPREQINnqspKGEHYLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGF 206
Cdd:MTH00140 103 QWYWSYEYSDFSVIEFDSYMVPENELE----LGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515814187 207 INESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWLG 252
Cdd:MTH00140 179 LNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
|
|
| CoxB |
TIGR02866 |
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ... |
32-251 |
3.90e-54 |
|
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: 177.19 E-value: 3.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 32 ATDVSRSVFDLHMTIFWICVVIGVLVFGVMIYSMIAHRRSKRQQS-ANFHENTRVEVLWTVIPLLILVGMAIPATRTLIH 110
Cdd:TIGR02866 2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGDEEKpSQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 111 IYDSSESD-VDVQITGYQWKWHYKYlgedveffsnlttpreqinnqspkgEHYLLEVDEPLVIPAGAKVRFLITAADVIH 189
Cdd:TIGR02866 82 LERPIPKDaLKVKVTGYQWWWDFEY-------------------------PESGFTTVNELVLPAGTPVELQVTSKDVIH 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515814187 190 SWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWL 251
Cdd:TIGR02866 137 SFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
|
|
| COX2 |
pfam00116 |
Cytochrome C oxidase subunit II, periplasmic domain; |
125-240 |
6.48e-41 |
|
Cytochrome C oxidase subunit II, periplasmic domain;
Pssm-ID: 395066 [Multi-domain] Cd Length: 120 Bit Score: 140.24 E-value: 6.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 125 GYQWKWHYKYLG-EDVEFFSnLTTPREQINnqspKGEHYLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAI 203
Cdd:pfam00116 7 GHQWYWSYEYTDfGDLEFDS-YMIPTEDLE----EGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81
|
90 100 110
....*....|....*....|....*....|....*..
gi 515814187 204 PGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVE 240
Cdd:pfam00116 82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
|
|
| CccA |
COG2010 |
Cytochrome c, mono- and diheme variants [Energy production and conversion]; |
261-355 |
4.26e-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: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 261 LAELTSKEWTLEELSERGQKVYQTACASCHQAGGEGIPPMFPALKGSAIATGDVEAHIDIVVNGKPGTAMAAFGKQLSEV 340
Cdd:COG2010 75 AAAAADAPAADAEALARGKALYEQNCAACHGADGKGGLGAAPNLTDDALYGGDPEALVETILNGRPGGAMPAFGGQLSDE 154
|
90
....*....|....*
gi 515814187 341 DLAAVITYERNAWGN 355
Cdd:COG2010 155 EIAALAAYLRSLSGN 169
|
|
| Cytochrom_C |
pfam00034 |
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ... |
276-353 |
1.07e-14 |
|
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: 69.10 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 276 ERGQKVYQTACASCHQAGGEGIPPMFPALKGSAIATGDVEAHIDIV------------VNGKPGTAMAAFGkQLSEVDLA 343
Cdd:pfam00034 1 ARGKKLFAANCAACHGVNGEGAGAGGPDLAGLAARYPGDALGAIREnkhaiggggvdrAGGPPGTGMPAFD-GLTDEEIA 79
|
90
....*....|
gi 515814187 344 AVITYERNAW 353
Cdd:pfam00034 80 DLVAYLLSLS 89
|
|
| PRK13697 |
PRK13697 |
cytochrome c6; Provisional |
278-348 |
1.79e-07 |
|
cytochrome c6; Provisional
Pssm-ID: 184253 [Multi-domain] Cd Length: 111 Bit Score: 49.01 E-value: 1.79e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515814187 278 GQKVYQTACASCHqAGGEGIPPMFPALKGSAI---ATGDVEAHIDIVVNGKpgTAMAAFGKQLSEVDLAAVITY 348
Cdd:PRK13697 31 GEQVFSANCASCH-AGGKNLVNAGKTLKKADLekyGMYSLEAITAQVTNGK--NAMPAFKDRLSPDQIEDVAAY 101
|
|
| ccoP |
TIGR00782 |
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ... |
251-348 |
9.88e-06 |
|
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: 46.81 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 251 LGEK--KAEAAKLAELTSKEWTLEELSERGQKVYQTACASCHQAGGEGIPPM-FPALKGSAIATGDVEAHIDIVVNGKPG 327
Cdd:TIGR00782 177 LEEAdiKDVASYVMSLSSGKPKDEALAAKGQELFADNCTTCHGEDGKGLQELgAPNLTDDVWLYGGDLKTITTTITNGRG 256
|
90 100
....*....|....*....|.
gi 515814187 328 TAMAAFGKQLSEVDLAAVITY 348
Cdd:TIGR00782 257 GVMPAWGPRLSEAQIKALAAY 277
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CyoA |
COG1622 |
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion]; |
11-260 |
2.89e-97 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
Pssm-ID: 441229 [Multi-domain] Cd Length: 229 Bit Score: 288.65 E-value: 2.89e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 11 LGLSAVFGQAQAAWDVNMRSGATDVSRSVFDLHMTIFWICVVIGVLVFGVMIYSMIAHRRSK-RQQSANFHENTRVEVLW 89
Cdd:COG1622 4 LLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKgDADPAQFHHNTKLEIVW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 90 TVIPLLILVGMAIPATRTLIHIYDSSESDVDVQITGYQWKWHYKYLGEDVEffsnlttpreqinnqspkgehylleVDEP 169
Cdd:COG1622 84 TVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA-------------------------TVNE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 170 LVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYAS 249
Cdd:COG1622 139 LVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDA 218
|
250
....*....|.
gi 515814187 250 WLGEKKAEAAK 260
Cdd:COG1622 219 WLAEQKASAAT 229
|
|
| CcO_II_C |
cd13912 |
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ... |
117-250 |
1.76e-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: 196.25 E-value: 1.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 117 SDVDVQITGYQWKWHYKYL-GEDVEFFSNLTTPREQinnqsPKGEHYLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPD 195
Cdd:cd13912 1 PSLTIKAIGHQWYWSYEYSdFNDLEFDSYMIPEDDL-----EKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 515814187 196 LAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASW 250
Cdd:cd13912 76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
|
|
| COX2 |
MTH00140 |
cytochrome c oxidase subunit II; Provisional |
50-252 |
1.01e-59 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214430 [Multi-domain] Cd Length: 228 Bit Score: 192.85 E-value: 1.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 50 CVVIGVLVFGVMIYSMIAHRRSKrQQSANFHENTRVEVLWTVIPLLILVGMAIPATRTLihiYDSSE---SDVDVQITGY 126
Cdd:MTH00140 27 AMVVLVLIFSFVMYMLVLLLFNK-FSCRTILEAQKLETIWTIVPALILVFLALPSLRLL---YLLDEtnnPLLTVKAIGH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 127 QWKWHYKYLGEDVEFFSNLTTPREQINnqspKGEHYLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGF 206
Cdd:MTH00140 103 QWYWSYEYSDFSVIEFDSYMVPENELE----LGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515814187 207 INESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWLG 252
Cdd:MTH00140 179 LNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
|
|
| CoxB |
TIGR02866 |
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ... |
32-251 |
3.90e-54 |
|
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: 177.19 E-value: 3.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 32 ATDVSRSVFDLHMTIFWICVVIGVLVFGVMIYSMIAHRRSKRQQS-ANFHENTRVEVLWTVIPLLILVGMAIPATRTLIH 110
Cdd:TIGR02866 2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGDEEKpSQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 111 IYDSSESD-VDVQITGYQWKWHYKYlgedveffsnlttpreqinnqspkgEHYLLEVDEPLVIPAGAKVRFLITAADVIH 189
Cdd:TIGR02866 82 LERPIPKDaLKVKVTGYQWWWDFEY-------------------------PESGFTTVNELVLPAGTPVELQVTSKDVIH 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515814187 190 SWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWL 251
Cdd:TIGR02866 137 SFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
|
|
| COX2 |
MTH00154 |
cytochrome c oxidase subunit II; Provisional |
49-251 |
2.53e-52 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214438 [Multi-domain] Cd Length: 227 Bit Score: 173.48 E-value: 2.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 49 ICVVIGVLVFGVMIYSMI---AHRrskrqqsaNFHENTRVEVLWTVIPLLILVGMAIPATRTLIHIYDSSESDVDVQITG 125
Cdd:MTH00154 30 ILIMITILVGYMMISLLFnkfTNR--------FLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 126 YQWKWHYKY-LGEDVEFFSNLTtPREQINNQSPKgehyLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIP 204
Cdd:MTH00154 102 HQWYWSYEYsDFKNIEFDSYMI-PTNELENNGFR----LLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515814187 205 GFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWL 251
Cdd:MTH00154 177 GRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
|
|
| COX2 |
MTH00139 |
cytochrome c oxidase subunit II; Provisional |
22-254 |
6.03e-51 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214429 [Multi-domain] Cd Length: 226 Bit Score: 169.90 E-value: 6.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 22 AAWD-VNMRSGATDVSRSVFDLHMTIFWICVVIGVLVFGVMIYSMIAHRRSKrqqsaNFHENTRVEVLWTVIPLLILVGM 100
Cdd:MTH00139 2 AYWGqLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSR-----SLLESQEVETIWTVLPAFILLFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 101 AIPATRTLIHIYDSSESDVDVQITGYQWKWHYKYLG-EDVEFFSNLTTPREQInnqspKGEHYLLEVDEPLVIPAGAKVR 179
Cdd:MTH00139 77 ALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDfKNLSFDSYMIPTEDLS-----SGEFRLLEVDNRLVLPYKSNIR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515814187 180 FLITAADVIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWLGEK 254
Cdd:MTH00139 152 ALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
|
|
| COX2 |
MTH00051 |
cytochrome c oxidase subunit II; Provisional |
24-258 |
3.63e-50 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177126 [Multi-domain] Cd Length: 234 Bit Score: 168.42 E-value: 3.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 24 WDVNMRSGATDVSRSVFDLHMTIFWICVVIGVLVFGVMIYSMIAHRRSKrqqsaNFHENTRVEVLWTVIPLLILVGMAIP 103
Cdd:MTH00051 7 WQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHK-----YLFEGTLIEIIWTLIPAAILIFIAFP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 104 ATRTLIHIYDSSESDVDVQITGYQWKWHYKY--LGEDVEFFSNLTTPREQINNqspkGEHYLLEVDEPLVIPAGAKVRFL 181
Cdd:MTH00051 82 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYsdYGTDTIEFDSYMIPTSDLNS----GDLRLLEVDNRLIVPIQTQVRVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515814187 182 ITAADVIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWLGEKKAEA 258
Cdd:MTH00051 158 VTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
|
|
| COX2 |
MTH00023 |
cytochrome c oxidase subunit II; Validated |
23-251 |
5.76e-50 |
|
cytochrome c oxidase subunit II; Validated
Pssm-ID: 214402 [Multi-domain] Cd Length: 240 Bit Score: 168.00 E-value: 5.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 23 AWDVNMRSGATDVSRSVFDLHMTIFWICVVIGVLVFGVMIYSMiahrrSKRQQSANFHENTRVEVLWTVIPLLILVGMAI 102
Cdd:MTH00023 13 PWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEAL-----NGKFYDRFLVDGTFLEIVWTIIPAVILVFIAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 103 PATRTLIHIYDSSESDVDVQITGYQWKWHYKY---LGEDVEFFSNLTtPREQINnqspKGEHYLLEVDEPLVIPAGAKVR 179
Cdd:MTH00023 88 PSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYsdyEGETLEFDSYMV-PTSDLN----SGDFRLLEVDNRLVVPINTHVR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515814187 180 FLITAADVIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWL 251
Cdd:MTH00023 163 ILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
|
|
| COX2 |
MTH00027 |
cytochrome c oxidase subunit II; Provisional |
11-254 |
1.33e-47 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214405 [Multi-domain] Cd Length: 262 Bit Score: 162.50 E-value: 1.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 11 LGLSAVFGQAQAAWDVNMRSGATDVSRSVFDLHMTIFWICVVIGVLVFGVMIYSMIAHrrSKRQQSANFHENTRVEVLWT 90
Cdd:MTH00027 20 MNVASMIKDANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGN--NYYSYYWNKLDGSLIEVIWT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 91 VIPLLILVGMAIPATRtLIHIYDSS--ESDVDVQITGYQWKWHYKY--LGEDVEFFSNLTTPREQINnqspKGEHYLLEV 166
Cdd:MTH00027 98 LIPAFILILIAFPSLR-LLYIMDECgfSANITIKVTGHQWYWSYSYedYGEKNIEFDSYMIPTADLE----FGDLRLLEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 167 DEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQED 246
Cdd:MTH00027 173 DNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSK 252
|
....*...
gi 515814187 247 YASWLGEK 254
Cdd:MTH00027 253 YIDWIGRE 260
|
|
| COX2 |
MTH00008 |
cytochrome c oxidase subunit II; Validated |
51-251 |
3.78e-47 |
|
cytochrome c oxidase subunit II; Validated
Pssm-ID: 164584 [Multi-domain] Cd Length: 228 Bit Score: 160.02 E-value: 3.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 51 VVIGVLVFGVMIYSMIAHRRSKrQQSANFHENTRVEVLWTVIPLLILVGMAIPATRTLIHIYDSSESDVDVQITGYQWKW 130
Cdd:MTH00008 28 LLILTLVLTVVGYAMTSLMFNK-LSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYW 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 131 HYKYLG-EDVEFFSNLTtPREQInnqSPkGEHYLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGFINE 209
Cdd:MTH00008 107 SYEYSDfSNLEFDSYML-PTSDL---SP-GQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQ 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515814187 210 SWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWL 251
Cdd:MTH00008 182 IGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
|
|
| COX2 |
MTH00168 |
cytochrome c oxidase subunit II; Provisional |
49-251 |
5.24e-47 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177223 [Multi-domain] Cd Length: 225 Bit Score: 159.76 E-value: 5.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 49 ICVVIGVLVFgVMIYSMIAHRRSKRqqsaNFHENTRVEVLWTVIPLLILVGMAIPATRTLIHIYDSSESDVDVQITGYQW 128
Cdd:MTH00168 30 ILVLILTLVL-YSLLVLVTSKYTNR----FLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 129 KWHYKYLG-EDVEFFSNLTtPREQINNqspkGEHYLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGFI 207
Cdd:MTH00168 105 YWSYEYTDyNDLEFDSYMV-PTQDLSP----GQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515814187 208 NESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWL 251
Cdd:MTH00168 180 NQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
|
|
| COX2 |
MTH00038 |
cytochrome c oxidase subunit II; Provisional |
49-253 |
2.76e-46 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177113 [Multi-domain] Cd Length: 229 Bit Score: 157.94 E-value: 2.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 49 ICVVIGVLVF---GVMIYSMIAHRRskrqqsanFHENTRVEVLWTVIPLLILVGMAIPATRTLIHIYDSSESDVDVQITG 125
Cdd:MTH00038 30 ILTLITILVFyglASLLFSSPTNRF--------FLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 126 YQWKWHYKYLG-EDVEFFSNLTtPREQINNQSPKgehyLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIP 204
Cdd:MTH00038 102 HQWYWSYEYTDyNDLEFDSYMV-PTSDLSTGLPR----LLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515814187 205 GFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWLGE 253
Cdd:MTH00038 177 GRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225
|
|
| COX2 |
MTH00076 |
cytochrome c oxidase subunit II; Provisional |
55-251 |
2.52e-45 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 164646 [Multi-domain] Cd Length: 228 Bit Score: 155.32 E-value: 2.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 55 VLVFGVMIYSMIAHRRSKRQQSANFHENTRVEVLWTVIPLLILVGMAIPATRTLIHIYDSSESDVDVQITGYQWKWHYKY 134
Cdd:MTH00076 31 VFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 135 LG-EDVEFFSNLTTPreqiNNQSPkGEHYLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGFINESWTR 213
Cdd:MTH00076 111 TDyEDLSFDSYMIPT----QDLTP-GQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFI 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 515814187 214 VEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWL 251
Cdd:MTH00076 186 ASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWS 223
|
|
| COX2 |
MTH00117 |
cytochrome c oxidase subunit II; Provisional |
80-251 |
3.04e-45 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177178 [Multi-domain] Cd Length: 227 Bit Score: 155.07 E-value: 3.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 80 HENT----RVEVLWTVIPLLILVGMAIPATRTLIHIYDSSESDVDVQITGYQWKWHYKYL-GEDVEFFSNLTTPREQinn 154
Cdd:MTH00117 52 HTNTvdaqEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTdYKDLSFDSYMIPTQDL--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 155 qsPKGEHYLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGF 234
Cdd:MTH00117 129 --PNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSF 206
|
170
....*....|....*..
gi 515814187 235 MPVVVEVKSQEDYASWL 251
Cdd:MTH00117 207 MPIVVESVPLKHFENWS 223
|
|
| COX2 |
MTH00080 |
cytochrome c oxidase subunit II; Provisional |
35-251 |
3.36e-45 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177149 [Multi-domain] Cd Length: 231 Bit Score: 155.17 E-value: 3.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 35 VSRSVFDLHMtiFWI----CVVI---GVLVFGVMIYsMIAHRRSKRQQSANFHENTrVEVLWTVIPLLILVGMAIPatrT 107
Cdd:MTH00080 10 FSNSLFSSYM--DWFhnfnCSLLfgeFVLAFVVFLF-LYLISNNFYFKSKKIEYQF-GELLCSVFPVLILLMQMVP---S 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 108 LIHIYDS----SESDVDVQITGYQWKWHYKYlGED--VEFFSNLttpreQINNQSPKGEHYLLEVDEPLVIPAGAKVRFL 181
Cdd:MTH00080 83 LSLLYYYglmnLDSNLTVKVTGHQWYWSYEF-SDIpgLEFDSYM-----KSLDQLRLGEPRLLEVDNRCVLPCDTNIRFC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 182 ITAADVIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWL 251
Cdd:MTH00080 157 ITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
|
|
| COX2 |
MTH00185 |
cytochrome c oxidase subunit II; Provisional |
28-250 |
1.92e-43 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 164736 [Multi-domain] Cd Length: 230 Bit Score: 150.42 E-value: 1.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 28 MRSGATDVSRSVFDLHMTIFWICVVIGVLVFgVMIYSMIAHRRSKRQqsanFHENTRVEVLWTVIPLLILVGMAIPATRT 107
Cdd:MTH00185 9 LQDAASPVMEELIHFHDHTLMIVFLISTLVL-YIIVAMVTTKLTNKY----ILDSQEIEIVWTILPAIILIMIALPSLRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 108 LIHIYDSSESDVDVQITGYQWKWHYKYLG-EDVEFFSNLTtpreQINNQSPkGEHYLLEVDEPLVIPAGAKVRFLITAAD 186
Cdd:MTH00185 84 LYLMDEINDPHLTIKAMGHQWYWSYEYTDyEQLEFDSYMT----PTQDLTP-GQFRLLETDHRMVVPMESPIRVLITAED 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515814187 187 VIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASW 250
Cdd:MTH00185 159 VLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
|
|
| COX2 |
MTH00098 |
cytochrome c oxidase subunit II; Validated |
80-250 |
6.27e-42 |
|
cytochrome c oxidase subunit II; Validated
Pssm-ID: 177160 [Multi-domain] Cd Length: 227 Bit Score: 146.40 E-value: 6.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 80 HENT----RVEVLWTVIPLLILVGMAIPATRTLIHIYDSSESDVDVQITGYQWKWHYKYLG-EDVEFFSNLTTPREQinn 154
Cdd:MTH00098 52 HTSTmdaqEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDyEDLSFDSYMIPTSDL--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 155 qSPkGEHYLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGF 234
Cdd:MTH00098 129 -KP-GELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSF 206
|
170
....*....|....*.
gi 515814187 235 MPVVVEVKSQEDYASW 250
Cdd:MTH00098 207 MPIVLELVPLKYFEKW 222
|
|
| COX2 |
MTH00129 |
cytochrome c oxidase subunit II; Provisional |
80-250 |
1.50e-41 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177187 [Multi-domain] Cd Length: 230 Bit Score: 145.63 E-value: 1.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 80 HENTRVEVLWTVIPLLILVGMAIPATRTLIHIYDSSESDVDVQITGYQWKWHYKYLG-EDVEFFSNLTtPREQInnqSPk 158
Cdd:MTH00129 56 LDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDyEDLGFDSYMI-PTQDL---TP- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 159 GEHYLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVV 238
Cdd:MTH00129 131 GQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIV 210
|
170
....*....|..
gi 515814187 239 VEVKSQEDYASW 250
Cdd:MTH00129 211 VEAVPLEHFENW 222
|
|
| COX2 |
pfam00116 |
Cytochrome C oxidase subunit II, periplasmic domain; |
125-240 |
6.48e-41 |
|
Cytochrome C oxidase subunit II, periplasmic domain;
Pssm-ID: 395066 [Multi-domain] Cd Length: 120 Bit Score: 140.24 E-value: 6.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 125 GYQWKWHYKYLG-EDVEFFSnLTTPREQINnqspKGEHYLLEVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAI 203
Cdd:pfam00116 7 GHQWYWSYEYTDfGDLEFDS-YMIPTEDLE----EGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81
|
90 100 110
....*....|....*....|....*....|....*..
gi 515814187 204 PGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVE 240
Cdd:pfam00116 82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
|
|
| COX2 |
MTH00047 |
cytochrome c oxidase subunit II; Provisional |
40-241 |
3.29e-34 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214412 [Multi-domain] Cd Length: 194 Bit Score: 125.07 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 40 FDLHMTIFWICVVIGVLVFGVMIYSMIAhrrskRQQSANF-HENTRVEVLWTVIPLLILVGMAIPATRTLIHIYDSSESD 118
Cdd:MTH00047 8 YDIVCYILALCVFIPCWVYIMLCWQVVS-----GNGSVNFgSENQVLELLWTVVPTLLVLVLCFLNLNFITSDLDCFSSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 119 VdVQITGYQWKWHYKYLGEDvEFFSNLTtprEQINNqspkgehylleVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAV 198
Cdd:MTH00047 83 T-IKVIGHQWYWSYEYSFGG-SYDSFMT---DDIFG-----------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515814187 199 KKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEV 241
Cdd:MTH00047 147 KMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEV 189
|
|
| CuRO_CcO_Caa3_II |
cd04213 |
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ... |
118-235 |
2.70e-30 |
|
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: 111.56 E-value: 2.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 118 DVDVQITGYQWKWHYKYLGEDVEffsNLTTPREqinnqspkgehyllevdepLVIPAGAKVRFLITAADVIHSWWVPDLA 197
Cdd:cd04213 1 ALTIEVTGHQWWWEFRYPDEPGR---GIVTANE-------------------LHIPVGRPVRLRLTSADVIHSFWVPSLA 58
|
90 100 110
....*....|....*....|....*....|....*...
gi 515814187 198 VKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFM 235
Cdd:cd04213 59 GKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
|
|
| PTZ00047 |
PTZ00047 |
cytochrome c oxidase subunit II; Provisional |
164-249 |
2.98e-30 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 240243 [Multi-domain] Cd Length: 162 Bit Score: 113.76 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 164 LEVDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKS 243
Cdd:PTZ00047 69 LEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVS 148
|
....*.
gi 515814187 244 QEDYAS 249
Cdd:PTZ00047 149 PEAYAA 154
|
|
| CuRO_HCO_II_like_5 |
cd13919 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
118-240 |
1.57e-29 |
|
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: 110.04 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 118 DVDVQITGYQWKWHYKYLGEDVEFfsnlttpreqinnqspkGEHYLLEVDEpLVIPAGAKVRFLITAADVIHSWWVPDLA 197
Cdd:cd13919 1 ALVVEVTAQQWAWTFRYPGGDGKL-----------------GTDDDVTSPE-LHLPVGRPVLFNLRSKDVIHSFWVPEFR 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 515814187 198 VKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFM--PVVVE 240
Cdd:cd13919 63 VKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
|
|
| CccA |
COG2010 |
Cytochrome c, mono- and diheme variants [Energy production and conversion]; |
261-355 |
4.26e-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: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 261 LAELTSKEWTLEELSERGQKVYQTACASCHQAGGEGIPPMFPALKGSAIATGDVEAHIDIVVNGKPGTAMAAFGKQLSEV 340
Cdd:COG2010 75 AAAAADAPAADAEALARGKALYEQNCAACHGADGKGGLGAAPNLTDDALYGGDPEALVETILNGRPGGAMPAFGGQLSDE 154
|
90
....*....|....*
gi 515814187 341 DLAAVITYERNAWGN 355
Cdd:COG2010 155 EIAALAAYLRSLSGN 169
|
|
| CuRO_HCO_II_like |
cd13842 |
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ... |
119-240 |
2.45e-26 |
|
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: 100.83 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 119 VDVQITGYQWKWHYKYLgedveffsNLTTPREqinnqspkgehyllevdepLVIPAGAKVRFLITAADVIHSWWVPDLAV 198
Cdd:cd13842 1 LTVYVTGVQWSWTFIYP--------NVRTPNE-------------------IVVPAGTPVRFRVTSPDVIHGFYIPNLGV 53
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 515814187 199 KKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVE 240
Cdd:cd13842 54 KVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
|
|
| CuRO_HCO_II_like_3 |
cd13914 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
119-251 |
4.30e-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: 100.56 E-value: 4.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 119 VDVQITGYQWKWHYKYLGEdveffsNLTTpreqinnqspkgehyllevDEPLVIPAGAKVRFLITAADVIHSWWVPDLAV 198
Cdd:cd13914 1 VEIEVEAYQWGWEFSYPEA------NVTT-------------------SEQLVIPADRPVYFRITSRDVIHAFHVPELGL 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 515814187 199 KKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASWL 251
Cdd:cd13914 56 KQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
|
|
| CuRO_HCO_II_like_2 |
cd13915 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
120-241 |
1.12e-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: 259982 [Multi-domain] Cd Length: 98 Bit Score: 96.54 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 120 DVQITGYQWKWHYKYLGEDVEffsnlttpreqinnqspkgehyllevDEPLVIPAGAKVRFLITAADVIHSWWVPDLAVK 199
Cdd:cd13915 3 EIQVTGRQWMWEFTYPNGKRE--------------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIK 56
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 515814187 200 KDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEV 241
Cdd:cd13915 57 QDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
|
|
| CuRO_HCO_II_like_6 |
cd13918 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
95-251 |
1.93e-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: 91.75 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 95 LILVGMAIPATRTLIHIYDS----SESDVDVQITGYQWKWHYKYLGEDveffsnlttprEQINNqspkgehyllevdepL 170
Cdd:cd13918 5 IIVISLIVWTYGMLLYVEDPpdeaDEDALEVEVEGFQFGWQFEYPNGV-----------TTGNT---------------L 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 171 VIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVKSQEDYASW 250
Cdd:cd13918 59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
|
.
gi 515814187 251 L 251
Cdd:cd13918 139 Y 139
|
|
| Cytochrom_C |
pfam00034 |
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ... |
276-353 |
1.07e-14 |
|
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: 69.10 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 276 ERGQKVYQTACASCHQAGGEGIPPMFPALKGSAIATGDVEAHIDIV------------VNGKPGTAMAAFGkQLSEVDLA 343
Cdd:pfam00034 1 ARGKKLFAANCAACHGVNGEGAGAGGPDLAGLAARYPGDALGAIREnkhaiggggvdrAGGPPGTGMPAFD-GLTDEEIA 79
|
90
....*....|
gi 515814187 344 AVITYERNAW 353
Cdd:pfam00034 80 DLVAYLLSLS 89
|
|
| ba3_CcO_II_C |
cd13913 |
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ... |
169-242 |
2.68e-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: 65.28 E-value: 2.68e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515814187 169 PLVIPAGAKVRFLITAADVIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFMPVVVEVK 242
Cdd:cd13913 26 EIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
|
|
| CuRO_UO_II |
cd04212 |
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ... |
119-234 |
5.30e-12 |
|
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: 61.80 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 119 VDVQITGYQWKWHYKYLGEDVEffsnlttpreqinnqspkgehyllEVDEpLVIPAGAKVRFLITAADVIHSWWVPDLAV 198
Cdd:cd04212 1 LEIQVVSLDWKWLFIYPEQGIA------------------------TVNE-LVIPVGRPVNFRLTSDSVMNSFFIPQLGG 55
|
90 100 110
....*....|....*....|....*....|....*.
gi 515814187 199 KKDAIPGFINESWTRVEQPGIYRGQCTELCGkdHGF 234
Cdd:cd04212 56 QIYAMAGMQTQLHLIADKPGTYQGLSANYSG--EGF 89
|
|
| Cytochrome_CBB3 |
pfam13442 |
Cytochrome C oxidase, cbb3-type, subunit III; |
276-348 |
7.87e-12 |
|
Cytochrome C oxidase, cbb3-type, subunit III;
Pssm-ID: 463879 [Multi-domain] Cd Length: 67 Bit Score: 60.11 E-value: 7.87e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515814187 276 ERGQKVYQTACASCHQAGGEGippmfPALKGSAIATgdvEAHIDIVVNGKpgTAMAAFGKQLSEVDLAAVITY 348
Cdd:pfam13442 4 AAGEALYAANCASCHGTGGAG-----PSLAGRALPP---EALVDIIRNGK--GAMPAFGGDLSDEELEALAAY 66
|
|
| CytC553 |
COG2863 |
Cytochrome c553 [Energy production and conversion]; |
276-348 |
1.48e-10 |
|
Cytochrome c553 [Energy production and conversion];
Pssm-ID: 442110 [Multi-domain] Cd Length: 98 Bit Score: 57.43 E-value: 1.48e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515814187 276 ERGQKvYQTACASCHQAGGEG-IPPMFPALKGsaIATGDVEAHIDIVVNGK-PGTAMAAFGKQLSEVDLAAVITY 348
Cdd:COG2863 16 ARGKA-YAAACAACHGADGEGnPGGGAPRLAG--QHAEYLVAQLKAFRSGArKNGVMPAIAKGLSDEDIKALAAY 87
|
|
| COX2_TM |
pfam02790 |
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ... |
24-103 |
2.78e-10 |
|
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: 56.57 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 24 WDVNMRSGATDVSRSVFDLHMTIFWICVVIGVLVFGVMIYSMIAHRRSKRQQSA-NFHENTRVEVLWTVIPLLILVGMAI 102
Cdd:pfam02790 5 WGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITArYTTHGQTIEIIWTIIPAVILILIAL 84
|
.
gi 515814187 103 P 103
Cdd:pfam02790 85 P 85
|
|
| CuRO_HCO_II_like_1 |
cd13916 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
121-235 |
3.92e-09 |
|
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: 53.15 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 121 VQITGYQWKWhykylgedveffsnlttpreqinnqspkgehyllEVDePLVIPAGAKVRFLITAADVIHSWWVPD----L 196
Cdd:cd13916 3 VAVTGHQWYW----------------------------------ELS-RTEIPAGKPVEFRVTSADVNHGFGIYDpdmrL 47
|
90 100 110
....*....|....*....|....*....|....*....
gi 515814187 197 AVKKDAIPGFINESWTRVEQPGIYRGQCTELCGKDHGFM 235
Cdd:cd13916 48 LAQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
|
|
| TsdA |
COG3258 |
Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion ... |
240-348 |
1.12e-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: 54.86 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 240 EVKSQEDYASWLGEKKAEAAKLAELTSKEWTLEELS---ERGQKVYQTACASCHQAGGEGIP-----PMFPALKG-SAIA 310
Cdd:COG3258 79 EMKALVAYLRWLSRGLPVGVKLDGRGLPKLPKPAASadvERGKALYAERCASCHGADGEGQGradgqYGFPPLWGgDSYN 158
|
90 100 110
....*....|....*....|....*....|....*....
gi 515814187 311 TGDVEAHIDIVVNGKPGTAMAAF-GKQLSEVDLAAVITY 348
Cdd:COG3258 159 DGAGMARLGTLADFIKGRNMPLGkPGSLSDDEAWDVAAY 197
|
|
| PRK13697 |
PRK13697 |
cytochrome c6; Provisional |
278-348 |
1.79e-07 |
|
cytochrome c6; Provisional
Pssm-ID: 184253 [Multi-domain] Cd Length: 111 Bit Score: 49.01 E-value: 1.79e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515814187 278 GQKVYQTACASCHqAGGEGIPPMFPALKGSAI---ATGDVEAHIDIVVNGKpgTAMAAFGKQLSEVDLAAVITY 348
Cdd:PRK13697 31 GEQVFSANCASCH-AGGKNLVNAGKTLKKADLekyGMYSLEAITAQVTNGK--NAMPAFKDRLSPDQIEDVAAY 101
|
|
| petJ |
CHL00183 |
cytochrome c553; Provisional |
276-348 |
8.17e-07 |
|
cytochrome c553; Provisional
Pssm-ID: 177085 Cd Length: 108 Bit Score: 47.08 E-value: 8.17e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515814187 276 ERGQKVYQTACASCHQAGGEGIPPMfPALKGSAIATGD---VEAHIDIVVNGKpgTAMAAFGKQLSEVDLAAVITY 348
Cdd:CHL00183 27 DNGEQIFSANCAACHAGGNNVIMPE-KTLKKDALEANSmnsIEAITYQVTNGK--NAMPAFGGRLSDEDIEDVANY 99
|
|
| ccoP |
TIGR00782 |
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ... |
251-348 |
9.88e-06 |
|
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: 46.81 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 251 LGEK--KAEAAKLAELTSKEWTLEELSERGQKVYQTACASCHQAGGEGIPPM-FPALKGSAIATGDVEAHIDIVVNGKPG 327
Cdd:TIGR00782 177 LEEAdiKDVASYVMSLSSGKPKDEALAAKGQELFADNCTTCHGEDGKGLQELgAPNLTDDVWLYGGDLKTITTTITNGRG 256
|
90 100
....*....|....*....|.
gi 515814187 328 TAMAAFGKQLSEVDLAAVITY 348
Cdd:TIGR00782 257 GVMPAWGPRLSEAQIKALAAY 277
|
|
| thiosulf_SoxX |
TIGR04485 |
sulfur oxidation c-type cytochrome SoxX; Members of this family are SoxX, a c-type cytochrome ... |
286-348 |
1.59e-05 |
|
sulfur oxidation c-type cytochrome SoxX; Members of this family are SoxX, a c-type cytochrome with a CxxCH motif, part of a heterodimer with SoxA. SoxXA, SoxYZ, and SoxB contribute to thiosulfate oxidation to sulfate.
Pssm-ID: 275278 [Multi-domain] Cd Length: 78 Bit Score: 42.57 E-value: 1.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 286 CASCHQAGGEGIPP--MFPALKGSAIATGDVEAHIDIVVNGK---PGTAMAAFGKQ--LSEVDLAAVITY 348
Cdd:TIGR04485 5 CLACHQIPGSEVFPgnIGPSLTGYGARYPDEAYLRAKIADAKavnPCTVMPRFGKNgiLTEQEIEDVVAY 74
|
|
| Cyc7 |
COG3474 |
Cytochrome c2 [Energy production and conversion]; |
276-348 |
1.80e-05 |
|
Cytochrome c2 [Energy production and conversion];
Pssm-ID: 442697 [Multi-domain] Cd Length: 101 Bit Score: 42.95 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 276 ERGQKVYQTACASCHQAGGEGIPPMFPALKG----------------SAIATGDV--EAHID--IVVNGK--PGTAMAAF 333
Cdd:COG3474 4 AAGEKLFNRKCAACHSVDGGAGNRVGPNLNGvvgrkagsvegfaysdALKASGLVwdEETLDawLADPKAfvPGTKMPFA 83
|
90
....*....|....*.
gi 515814187 334 GkqLSEV-DLAAVITY 348
Cdd:COG3474 84 G--LKDPeDRADLIAY 97
|
|
| CxxCH_TIGR02603 |
TIGR02603 |
putative heme-binding domain, Pirellula/Verrucomicrobium type; This model represents a domain ... |
276-323 |
6.67e-05 |
|
putative heme-binding domain, Pirellula/Verrucomicrobium type; This model represents a domain limited to very few species but expanded into large paralogous families in some species that conain it. We find it in over 20 copies each in Pirellula sp. strain 1 (phylum Planctomycetes) and Verrucomicrobium spinosum DSM 4136 (phylum Verrucomicrobia), and no matches above trusted cutoff an any other species so far. This domain, about 140 amino acids long, contains an absolutely conserved motif CxxCH, the cytochrome c family heme-binding site signature (PS00190).
Pssm-ID: 274224 Cd Length: 133 Bit Score: 42.35 E-value: 6.67e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 515814187 276 ERGQKVYQTACASCHQAGGEGIpPMFPALKGsaIATGDVEAHIDIVVN 323
Cdd:TIGR02603 4 ARGKAVFAKVCYLCHRIGGQGV-DFGPNLTT--VGTKGKEYLLEAILD 48
|
|
| PRK14486 |
PRK14486 |
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional |
253-351 |
1.48e-03 |
|
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional
Pssm-ID: 184704 [Multi-domain] Cd Length: 294 Bit Score: 40.19 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814187 253 EKKAEAAKLAELTSKEWTLEELSERGQKVYQTACASCHQAGGEGipPMFPALkgSAIATGDV--EAHIDIVVNGKPGTAM 330
Cdd:PRK14486 193 RAAGGAEVDLELPNPFATDVAAIAKGKALYDANCAACHGDEAQG--QEGVAL--NDIDDGDLpdAAYFGMIKGGSDAKGM 268
|
90 100
....*....|....*....|.
gi 515814187 331 AAFGKQLSEVDLAAVITYERN 351
Cdd:PRK14486 269 PGFGGDLSDDDIWAIVAYIRS 289
|
|
| Cupredoxin_1 |
pfam13473 |
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ... |
170-237 |
4.56e-03 |
|
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel.
Pssm-ID: 379208 [Multi-domain] Cd Length: 104 Bit Score: 36.41 E-value: 4.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515814187 170 LVIPAGAKVRFLITAAD-VIHSWWVPDLAVKKDAIPGFINESWTRVEQPGIYRGQCtELCGKDHGFMPV 237
Cdd:pfam13473 37 ITVPAGTPVKLEFKNKDkTPAEFESPDLGIEKVLAPGKTSTITIPPLKPGEYDFFC-DMHMDAKGKLIV 104
|
|
| |
