|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-258 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 517.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00153 247 PGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00153 327 GSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPK 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSANM 240
Cdd:MTH00153 407 WLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNL 486
|
250
....*....|....*...
gi 737509794 241 SSSTEWLQNNPPAEHSYS 258
Cdd:MTH00153 487 SSSIEWLQNLPPAEHSYS 504
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-248 |
1.96e-149 |
|
Cytochrome C oxidase subunit I. 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, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. 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 I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 426.13 E-value: 1.96e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:cd01663 240 PGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMW 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:cd01663 320 GGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNET 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSAN- 239
Cdd:cd01663 400 LGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGe 479
|
....*....
gi 737509794 240 MSSSTEWLQ 248
Cdd:cd01663 480 GSTSLEWTL 488
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-255 |
1.99e-88 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 271.62 E-value: 1.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:COG0843 251 PAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMW 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:COG0843 330 RGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNER 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVmfSA 238
Cdd:COG0843 410 LGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA--GG 487
|
250
....*....|....*....
gi 737509794 239 N--MSSSTEWLQNNPPAEH 255
Cdd:COG0843 488 NpwGARTLEWATPSPPPLY 506
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-257 |
7.02e-88 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 269.48 E-value: 7.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:TIGR02891 242 PAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSA 238
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANP 480
|
250
....*....|....*....
gi 737509794 239 NMSSSTEWLQNNPPAEHSY 257
Cdd:TIGR02891 481 WGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-194 |
1.22e-63 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 205.11 E-value: 1.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:pfam00115 217 PAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLW 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFN-PPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNN 159
Cdd:pfam00115 296 GGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSE 375
|
170 180 190
....*....|....*....|....*....|....*
gi 737509794 160 TWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSD 194
Cdd:pfam00115 376 KLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-258 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 517.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00153 247 PGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLH 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00153 327 GSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPK 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSANM 240
Cdd:MTH00153 407 WLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNL 486
|
250
....*....|....*...
gi 737509794 241 SSSTEWLQNNPPAEHSYS 258
Cdd:MTH00153 487 SSSIEWLQNLPPAEHSYS 504
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-248 |
1.96e-149 |
|
Cytochrome C oxidase subunit I. 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, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. 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 I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 426.13 E-value: 1.96e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:cd01663 240 PGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMW 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:cd01663 320 GGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNET 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSAN- 239
Cdd:cd01663 400 LGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGe 479
|
....*....
gi 737509794 240 MSSSTEWLQ 248
Cdd:cd01663 480 GSTSLEWTL 488
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-258 |
2.39e-144 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 413.99 E-value: 2.39e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00223 246 PGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIY 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00223 326 GSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRR 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSANM 240
Cdd:MTH00223 406 WAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHL 485
|
250
....*....|....*...
gi 737509794 241 SSSTEWLQNNPPAEHSYS 258
Cdd:MTH00223 486 STSLEWDNLLPADFHNNS 503
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-257 |
9.91e-144 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 412.53 E-value: 9.91e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00167 249 PGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLH 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00167 329 GGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNET 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSANM 240
Cdd:MTH00167 409 WTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELT 488
|
250
....*....|....*..
gi 737509794 241 SSSTEWLQNNPPAEHSY 257
Cdd:MTH00167 489 STNVEWLHGCPPPHHTW 505
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-258 |
5.86e-143 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 410.27 E-value: 5.86e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00142 247 PGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLH 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00142 327 GSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSANM 240
Cdd:MTH00142 407 WLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHL 486
|
250
....*....|....*...
gi 737509794 241 SSSTEWLQNNPPAEHSYS 258
Cdd:MTH00142 487 STSLEWSHRLPPDFHTYD 504
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-257 |
8.56e-143 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 410.25 E-value: 8.56e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00116 249 PGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLH 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00116 329 GGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSANM 240
Cdd:MTH00116 409 WTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELT 488
|
250
....*....|....*..
gi 737509794 241 SSSTEWLQNNPPAEHSY 257
Cdd:MTH00116 489 TTNIEWIHGCPPPYHTF 505
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-257 |
1.64e-126 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 368.83 E-value: 1.64e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00103 249 PGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLH 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00103 329 GGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSANM 240
Cdd:MTH00103 409 WAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELT 488
|
250
....*....|....*..
gi 737509794 241 SSSTEWLQNNPPAEHSY 257
Cdd:MTH00103 489 TTNLEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-257 |
3.86e-126 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 367.71 E-value: 3.86e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00183 249 PGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLH 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00183 329 GGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHST 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSANM 240
Cdd:MTH00183 409 WTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELT 488
|
250
....*....|....*..
gi 737509794 241 SSSTEWLQNNPPAEHSY 257
Cdd:MTH00183 489 STNVEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-258 |
1.90e-124 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 363.45 E-value: 1.90e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00007 246 PGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIH 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00007 326 GSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDR 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSANM 240
Cdd:MTH00007 406 WAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHM 485
|
250
....*....|....*...
gi 737509794 241 SSSTEWLQNNPPAEHSYS 258
Cdd:MTH00007 486 SSSLEWQDTLPLDFHNLP 503
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-257 |
3.88e-123 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 360.30 E-value: 3.88e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00037 249 PGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQ 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00037 329 GSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPL 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSANM 240
Cdd:MTH00037 409 WSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFS 488
|
250
....*....|....*...
gi 737509794 241 SSSTEWLQNN-PPAEHSY 257
Cdd:MTH00037 489 SSSLEWQYSSfPPSHHTF 506
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-257 |
4.51e-122 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 357.33 E-value: 4.51e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00077 249 PGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMH 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00077 329 GGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHST 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSANM 240
Cdd:MTH00077 409 WSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELT 488
|
250
....*....|....*..
gi 737509794 241 SSSTEWLQNNPPAEHSY 257
Cdd:MTH00077 489 STNIEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-257 |
2.71e-112 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 332.03 E-value: 2.71e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00079 249 PAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLF 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00079 329 GMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKL 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSANM 240
Cdd:MTH00079 409 MMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYI 488
|
250
....*....|....*..
gi 737509794 241 SSSTEWLQNNPPAEHSY 257
Cdd:MTH00079 489 NSSPEYSLSSYVFGHSY 505
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-257 |
2.35e-107 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 320.23 E-value: 2.35e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00182 251 PGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIY 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00182 331 GGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSANM 240
Cdd:MTH00182 411 YGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEG 490
|
250 260
....*....|....*....|.
gi 737509794 241 S----SSTEWLQNNPPAEHSY 257
Cdd:MTH00182 491 TgeswASLEWVHSSPPLFHTY 511
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-257 |
3.18e-104 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 312.15 E-value: 3.18e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00184 251 PGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIF 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:MTH00184 331 GGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESM---ISNRTVMFS 237
Cdd:MTH00184 411 YGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYvreIKFVGWVED 490
|
250 260
....*....|....*....|
gi 737509794 238 ANMSSSTEWLQNNPPAEHSY 257
Cdd:MTH00184 491 SGHYPSLEWAQTSPPAHHTY 510
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-228 |
1.18e-97 |
|
Heme-copper oxidase subunit I. 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 three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.
Pssm-ID: 238461 Cd Length: 463 Bit Score: 293.28 E-value: 1.18e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:cd00919 237 PAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLW 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:cd00919 316 GGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEK 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESM 228
Cdd:cd00919 396 LGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-255 |
1.99e-88 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 271.62 E-value: 1.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:COG0843 251 PAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMW 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:COG0843 330 RGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNER 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVmfSA 238
Cdd:COG0843 410 LGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA--GG 487
|
250
....*....|....*....
gi 737509794 239 N--MSSSTEWLQNNPPAEH 255
Cdd:COG0843 488 NpwGARTLEWATPSPPPLY 506
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-257 |
7.02e-88 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 269.48 E-value: 7.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:TIGR02891 242 PAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSA 238
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANP 480
|
250
....*....|....*....
gi 737509794 239 NMSSSTEWLQNNPPAEHSY 257
Cdd:TIGR02891 481 WGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-258 |
1.55e-84 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 261.87 E-value: 1.55e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00026 250 PGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVS 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GT--KFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMN 158
Cdd:MTH00026 330 GSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYK 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 159 NTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWES----------- 227
Cdd:MTH00026 410 DIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAyyreepfdini 489
|
250 260 270
....*....|....*....|....*....|...
gi 737509794 228 MISNRTVMFSANMS--SSTEWLQNNPPAEHSYS 258
Cdd:MTH00026 490 MAKGPLIPFSCQPAhfDTLEWSLTSPPEHHTYN 522
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-257 |
2.36e-79 |
|
Ubiquinol oxidase subunit I. 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. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.
Pssm-ID: 238832 Cd Length: 501 Bit Score: 247.49 E-value: 2.36e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:cd01662 243 PAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMW 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:cd01662 322 RGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNER 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVISSIGSTISIVGIILFISIMWESmISNRTVMFSA 238
Cdd:cd01662 402 LGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVS-IRKGKRDATG 480
|
250 260
....*....|....*....|.
gi 737509794 239 NM--SSSTEWLQNNPPAEHSY 257
Cdd:cd01662 481 DPwgARTLEWATSSPPPAYNF 501
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-256 |
3.18e-78 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 244.97 E-value: 3.18e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:MTH00048 247 PGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLL-WALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNN 159
Cdd:MTH00048 327 NSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNK 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 160 TWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIILFISIMWESMISNRTVMFSAN 239
Cdd:MTH00048 407 YLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLGLWG 486
|
250
....*....|....*..
gi 737509794 240 MSSSTEWLQNNPPAEHS 256
Cdd:MTH00048 487 SSSCVVNVLMSPVPYHN 503
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-194 |
1.22e-63 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 205.11 E-value: 1.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:pfam00115 217 PAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLW 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFN-PPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNN 159
Cdd:pfam00115 296 GGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSE 375
|
170 180 190
....*....|....*....|....*....|....*
gi 737509794 160 TWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSD 194
Cdd:pfam00115 376 KLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-258 |
3.19e-52 |
|
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131928 Cd Length: 643 Bit Score: 179.28 E-value: 3.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:TIGR02882 286 PAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLY 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:TIGR02882 365 KGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTSWNVISSIGSTISIVG-IILFISIMWESMISNRTVMFS 237
Cdd:TIGR02882 445 LGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGfIFLVYNIYYSHRKSPREATGD 524
|
250 260
....*....|....*....|.
gi 737509794 238 ANMSSSTEWLQNNPPAEHSYS 258
Cdd:TIGR02882 525 PWNGRTLEWATASPPPKYNFA 545
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-258 |
1.04e-46 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 164.72 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 1 PGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLY 80
Cdd:PRK15017 293 PVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMY 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 81 GTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNT 160
Cdd:PRK15017 372 QGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNET 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 161 WLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTSWNVISSIGSTISIVGIILFISIMWESMIS---NRTVMF 236
Cdd:PRK15017 452 WGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDrdqNRDLTG 531
|
250 260
....*....|....*....|..
gi 737509794 237 SANMSSSTEWLQNNPPAEHSYS 258
Cdd:PRK15017 532 DPWGGRTLEWATSSPPPFYNFA 553
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
61-228 |
3.47e-13 |
|
ba3-like heme-copper oxidase subunit I. 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. For general information on the heme-copper oxidase superfamily, please see cd00919.
Pssm-ID: 238830 Cd Length: 473 Bit Score: 68.47 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 61 TMIIAVPTGIKVFSWLATL-YGTKFKFNPPLLW---------------ALGFIFlFTIGGLTGLILANSSLDIVLHDTYY 124
Cdd:cd01660 282 TFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737509794 125 VVAHFHyvLSMGAVFAIMG-GIIQWY-PLFTGLTMNNTWL-KIQFTIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDAY 199
Cdd:cd01660 361 VPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLP 438
|
170 180 190
....*....|....*....|....*....|....
gi 737509794 200 -----TSWNVISSIGSTISIVGIILFISIMWESM 228
Cdd:cd01660 439 aagewAPYQQLMAIGGTILFVSGALFLYILFRTL 472
|
|
|