|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-252 |
1.01e-173 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 488.22 E-value: 1.01e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00153 248 GFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00153 328 SQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKW 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00153 408 LKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLS 487
|
250
....*....|..
gi 78103097 241 SSIEWFQNTPPA 252
Cdd:MTH00153 488 SSIEWLQNLPPA 499
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-245 |
5.06e-144 |
|
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: 411.88 E-value: 5.06e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPI-QL 239
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEG 480
|
....*.
gi 78103097 240 NSSIEW 245
Cdd:cd01663 481 STSLEW 486
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-251 |
1.96e-79 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 248.50 E-value: 1.96e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:COG0843 252 AFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:COG0843 331 GRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLV-MYPI 237
Cdd:COG0843 411 GKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAgGNPW 490
|
250
....*....|....
gi 78103097 238 QLNsSIEWFQNTPP 251
Cdd:COG0843 491 GAR-TLEWATPSPP 503
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-251 |
3.63e-78 |
|
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: 244.05 E-value: 3.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:TIGR02891 243 AFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:TIGR02891 322 GSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERL 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQ 238
Cdd:TIGR02891 402 GRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPW 481
|
250
....*....|...
gi 78103097 239 LNSSIEWFQNTPP 251
Cdd:TIGR02891 482 GATTLEWTTSSPP 494
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-193 |
2.59e-54 |
|
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: 180.46 E-value: 2.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:pfam00115 218 AFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQL-IYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSI 159
Cdd:pfam00115 297 GWIrFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEK 376
|
170 180 190
....*....|....*....|....*....|....
gi 78103097 160 YLKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSD 193
Cdd:pfam00115 377 LGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-252 |
1.01e-173 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 488.22 E-value: 1.01e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00153 248 GFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00153 328 SQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKW 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00153 408 LKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLS 487
|
250
....*....|..
gi 78103097 241 SSIEWFQNTPPA 252
Cdd:MTH00153 488 SSIEWLQNLPPA 499
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-245 |
5.06e-144 |
|
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: 411.88 E-value: 5.06e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPI-QL 239
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEG 480
|
....*.
gi 78103097 240 NSSIEW 245
Cdd:cd01663 481 STSLEW 486
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-252 |
9.74e-138 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 396.74 E-value: 9.74e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00167 250 GFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00167 330 GKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETW 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00167 410 TKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTS 489
|
250
....*....|..
gi 78103097 241 SSIEWFQNTPPA 252
Cdd:MTH00167 490 TNVEWLHGCPPP 501
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-252 |
1.46e-137 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 396.40 E-value: 1.46e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00142 248 GFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHG 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00142 328 SKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRW 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00142 408 LKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLS 487
|
250
....*....|..
gi 78103097 241 SSIEWFQNTPPA 252
Cdd:MTH00142 488 TSLEWSHRLPPD 499
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-252 |
2.99e-136 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 393.19 E-value: 2.99e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00223 247 GFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00223 327 SKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRW 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00223 407 AKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLS 486
|
250
....*....|..
gi 78103097 241 SSIEWFQNTPPA 252
Cdd:MTH00223 487 TSLEWDNLLPAD 498
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-251 |
5.41e-136 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 392.53 E-value: 5.41e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00116 250 GFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00116 330 GTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTW 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00116 410 TKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTT 489
|
250
....*....|.
gi 78103097 241 SSIEWFQNTPP 251
Cdd:MTH00116 490 TNIEWIHGCPP 500
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-251 |
2.63e-121 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 355.34 E-value: 2.63e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00103 250 GFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00103 330 GNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTW 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00103 410 AKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTT 489
|
250
....*....|.
gi 78103097 241 SSIEWFQNTPP 251
Cdd:MTH00103 490 TNLEWLHGCPP 500
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-251 |
2.80e-120 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 352.59 E-value: 2.80e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00037 250 GFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00037 330 SNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLW 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00037 410 SKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSS 489
|
250
....*....|.
gi 78103097 241 SSIEWFQNTPP 251
Cdd:MTH00037 490 SSLEWQYSSFP 500
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-250 |
5.72e-119 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 349.20 E-value: 5.72e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00007 247 GFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00007 327 SPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRW 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00007 407 AKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMS 486
|
250
....*....|
gi 78103097 241 SSIEWFQNTP 250
Cdd:MTH00007 487 SSLEWQDTLP 496
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-251 |
9.08e-119 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 348.84 E-value: 9.08e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00183 250 GFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00183 330 GSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTW 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00183 410 TKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTS 489
|
250
....*....|.
gi 78103097 241 SSIEWFQNTPP 251
Cdd:MTH00183 490 TNVEWLHGCPP 500
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-251 |
2.82e-116 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 342.31 E-value: 2.82e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00077 250 GFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00077 330 GAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTW 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00077 410 SKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTS 489
|
250
....*....|.
gi 78103097 241 SSIEWFQNTPP 251
Cdd:MTH00077 490 TNIEWLHGCPP 500
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
2-251 |
7.96e-105 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 312.77 E-value: 7.96e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 2 FGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 81
Cdd:MTH00079 251 FGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGM 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 82 QLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIYL 161
Cdd:MTH00079 331 KMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMM 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 162 KTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLNS 241
Cdd:MTH00079 411 SAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINS 490
|
250
....*....|
gi 78103097 242 SIEWFQNTPP 251
Cdd:MTH00079 491 SPEYSLSSYV 500
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-252 |
1.45e-101 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 305.21 E-value: 1.45e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00182 252 GFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYG 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00182 332 GTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELY 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00182 412 GKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEGT 491
|
250
....*....|....*.
gi 78103097 241 ----SSIEWFQNTPPA 252
Cdd:MTH00182 492 geswASLEWVHSSPPL 507
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-252 |
1.87e-98 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 296.74 E-value: 1.87e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00184 252 GFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFG 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00184 332 GSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVY 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLV---MYPI 237
Cdd:MTH00184 412 GKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFvgwVEDS 491
|
250
....*....|....*
gi 78103097 238 QLNSSIEWFQNTPPA 252
Cdd:MTH00184 492 GHYPSLEWAQTSPPA 506
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-227 |
1.38e-89 |
|
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: 272.48 E-value: 1.38e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:cd00919 238 AFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWG 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:cd00919 317 GRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKL 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESI 227
Cdd:cd00919 397 GKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-226 |
3.33e-83 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 258.02 E-value: 3.33e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00026 251 GFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSG 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 T--QLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNS 158
Cdd:MTH00026 331 SgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKD 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78103097 159 IYLKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWES 226
Cdd:MTH00026 411 IYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDA 478
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-251 |
1.96e-79 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 248.50 E-value: 1.96e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:COG0843 252 AFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:COG0843 331 GRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLV-MYPI 237
Cdd:COG0843 411 GKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAgGNPW 490
|
250
....*....|....
gi 78103097 238 QLNsSIEWFQNTPP 251
Cdd:COG0843 491 GAR-TLEWATPSPP 503
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-251 |
3.63e-78 |
|
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: 244.05 E-value: 3.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:TIGR02891 243 AFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:TIGR02891 322 GSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERL 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQ 238
Cdd:TIGR02891 402 GRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPW 481
|
250
....*....|...
gi 78103097 239 LNSSIEWFQNTPP 251
Cdd:TIGR02891 482 GATTLEWTTSSPP 494
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-234 |
1.07e-73 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 233.03 E-value: 1.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00048 248 GFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLN 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQL-IYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSI 159
Cdd:MTH00048 328 SRVrKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKY 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78103097 160 YLKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVM 234
Cdd:MTH00048 408 LLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-227 |
9.42e-71 |
|
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: 225.15 E-value: 9.42e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 2 FGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 81
Cdd:cd01662 245 FGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRG 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 82 QLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIYL 161
Cdd:cd01662 324 RIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLG 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78103097 162 KTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNIISSIGSTISFLGILYFFFIIWESI 227
Cdd:cd01662 404 KWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSI 471
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-193 |
2.59e-54 |
|
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: 180.46 E-value: 2.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:pfam00115 218 AFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 81 TQL-IYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSI 159
Cdd:pfam00115 297 GWIrFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEK 376
|
170 180 190
....*....|....*....|....*....|....
gi 78103097 160 YLKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSD 193
Cdd:pfam00115 377 LGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
2-196 |
8.02e-43 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 153.94 E-value: 8.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 2 FGMISHIISHESgKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 81
Cdd:PRK15017 295 FGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 82 QLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIYL 161
Cdd:PRK15017 374 RIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWG 453
|
170 180 190
....*....|....*....|....*....|....*
gi 78103097 162 KTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPD 196
Cdd:PRK15017 454 KRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
60-223 |
1.24e-08 |
|
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: 54.98 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 60 TMIIAVPTGIKIFSWLATL-------HGTQLIYSPSTMW---------ALGFIFlFTVGGLTGVVLANSSIDIMLHDTYY 123
Cdd:cd01660 282 TFMVALPSLLTAFTVFASLeiagrlrGGKGLFGWIRALPwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103097 124 VVAHFHyvLSMGAVFAIMAGFIHWY--SLFTGLTLNSIYL-KTQFLIMFMGVNLTFFPQHFLGLAGMPRR--YSDYPDAY 198
Cdd:cd01660 361 VPGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLP 438
|
170 180 190
....*....|....*....|....*....|
gi 78103097 199 -----TSWNIISSIGSTISFLGILYFFFII 223
Cdd:cd01660 439 aagewAPYQQLMAIGGTILFVSGALFLYIL 468
|
|
|