|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-264 |
1.27e-170 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 480.90 E-value: 1.27e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00153 15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00153 95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAI 278
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-264 |
2.95e-161 |
|
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: 456.17 E-value: 2.95e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:cd01663 8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:cd01663 88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:cd01663 168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:cd01663 248 IISTFSGKKPVFGYLGMVYAMLSI 271
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-264 |
4.98e-96 |
|
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: 290.66 E-value: 4.98e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMiGGFGNWLIPLMIGAPDMAFPR 80
Cdd:TIGR02891 11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:TIGR02891 90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKePFGTLGMIYALMAI 264
Cdd:TIGR02891 250 ILPTFARKP-IFGYRAMVYATVAI 272
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-264 |
1.13e-94 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 288.18 E-value: 1.13e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 2 LYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRM 81
Cdd:COG0843 21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 82 NNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGMT 161
Cdd:COG0843 100 NALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 162 MERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISHI 241
Cdd:COG0843 180 LMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI 259
|
250 260
....*....|....*....|...
gi 1220321659 242 ISHYSGKKePFGTLGMIYALMAI 264
Cdd:COG0843 260 IPTFSRKP-LFGYKAMVLATVAI 281
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-264 |
7.36e-60 |
|
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: 195.48 E-value: 7.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 2 LYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRM 81
Cdd:pfam00115 5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 82 NNLSFWLLIPSIFFLLFSSMasmGVGTGWTVYPPLssinfhsgAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGMT 161
Cdd:pfam00115 84 NALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 162 MeRIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTsffdplGGGDPILYQHLFWFFGHPEVYILILPGFGMISHI 241
Cdd:pfam00115 153 L-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225
|
250 260
....*....|....*....|...
gi 1220321659 242 ISHYSGKKePFGTLGMIYALMAI 264
Cdd:pfam00115 226 LPKFAGRP-LFGYKLSVLAFWLI 247
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-264 |
1.27e-170 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 480.90 E-value: 1.27e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00153 15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00153 95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAI 278
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-264 |
2.95e-161 |
|
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: 456.17 E-value: 2.95e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:cd01663 8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:cd01663 88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:cd01663 168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:cd01663 248 IISTFSGKKPVFGYLGMVYAMLSI 271
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-264 |
3.31e-151 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 431.71 E-value: 3.31e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00223 14 TLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00223 94 LNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00223 174 QLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 253
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00223 254 IVSHYSSKKEVFGTLGMIYAMLSI 277
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-264 |
1.02e-149 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 427.94 E-value: 1.02e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00167 17 TLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00167 97 MNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00167 177 TQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00167 257 IVVYYSGKKEPFGYMGMVWAMMAI 280
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-264 |
2.43e-145 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 416.80 E-value: 2.43e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00116 17 TLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00116 97 MNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00116 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 256
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00116 257 IVTYYAGKKEPFGYMGMVWAMLSI 280
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-264 |
5.81e-145 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 415.66 E-value: 5.81e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00142 15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00142 95 MNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00142 175 KFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00142 255 IINHYSGKKEVFGTLGMIYAMLSI 278
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-264 |
1.77e-129 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 376.48 E-value: 1.77e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00037 17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00037 97 MNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00037 177 TFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISH 256
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00037 257 VIAHYSGKQEPFGYLGMVYAMIAI 280
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-264 |
3.81e-129 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 375.76 E-value: 3.81e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00103 17 TLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00103 97 MNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00103 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00103 257 IVTYYSGKKEPFGYMGMVWAMMSI 280
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-264 |
5.65e-128 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 372.72 E-value: 5.65e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00183 17 TLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00183 97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00183 177 SQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00183 257 IVAYYSGKKEPFGYMGMVWAMMAI 280
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-264 |
2.60e-127 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 370.77 E-value: 2.60e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00007 14 TLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00007 94 LNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00007 174 RLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISH 253
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00007 254 IVTHYAGKLEPFGTLGMIYAMLGI 277
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-264 |
2.68e-127 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 370.81 E-value: 2.68e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00077 17 TLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00077 97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00077 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 256
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00077 257 IVTYYSAKKEPFGYMGMVWAMMSI 280
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-264 |
6.41e-124 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 362.60 E-value: 6.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00182 19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00182 99 LNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00182 179 TFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQ 258
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00182 259 IIPTFVAKKQIFGYLGMVYAMLSI 282
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-264 |
1.33e-121 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 356.44 E-value: 1.33e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00184 19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00184 99 LNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00184 179 TMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 258
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00184 259 IIPTFAAKKQIFGYLGMVYAMVSI 282
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-264 |
5.52e-117 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 344.36 E-value: 5.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00079 18 TLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINfHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00079 98 LNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLG-HPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00079 177 SLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQ 256
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00079 257 STLYLTGKKEVFGSLGMVYAILSI 280
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-264 |
4.12e-114 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 338.14 E-value: 4.12e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 80
Cdd:MTH00026 18 SLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:MTH00026 98 LNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00026 178 TMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 257
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00026 258 ILSLFSYKKQIFGYLGMVYAMLAI 281
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-264 |
3.34e-100 |
|
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: 300.22 E-value: 3.34e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPlMIGAPDMAFPR 80
Cdd:cd00919 6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:cd00919 85 LNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:cd00919 165 TLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISE 244
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKePFGTLGMIYALMAI 264
Cdd:cd00919 245 IIPTFSGKP-LFGYKLMVYAFLAI 267
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-264 |
4.98e-96 |
|
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: 290.66 E-value: 4.98e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 1 TLYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMiGGFGNWLIPLMIGAPDMAFPR 80
Cdd:TIGR02891 11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:TIGR02891 90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKePFGTLGMIYALMAI 264
Cdd:TIGR02891 250 ILPTFARKP-IFGYRAMVYATVAI 272
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-264 |
1.13e-94 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 288.18 E-value: 1.13e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 2 LYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRM 81
Cdd:COG0843 21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 82 NNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGMT 161
Cdd:COG0843 100 NALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 162 MERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISHI 241
Cdd:COG0843 180 LMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI 259
|
250 260
....*....|....*....|...
gi 1220321659 242 ISHYSGKKePFGTLGMIYALMAI 264
Cdd:COG0843 260 IPTFSRKP-LFGYKAMVLATVAI 281
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-264 |
1.93e-91 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 279.25 E-value: 1.93e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 2 LYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRM 81
Cdd:MTH00048 19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 82 NNLSFWLLIPSIFFLLFSsmASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGMT 161
Cdd:MTH00048 99 NALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 162 mERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISHI 241
Cdd:MTH00048 177 -SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHI 255
|
250 260
....*....|....*....|...
gi 1220321659 242 ISHYSGKKEPFGTLGMIYALMAI 264
Cdd:MTH00048 256 CLSLSNNDDPFGYYGLVFAMFSI 278
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-264 |
4.61e-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: 247.11 E-value: 4.61e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 2 LYLIFGMWAGILGSALSIMIRIELGTP-TSFLGNDHlYNVIVTAHAFVMIFFMVMPIMIGgFGNWLIPLMIGAPDMAFPR 80
Cdd:cd01662 13 MYIITAFVFFLRGGVDALLMRTQLALPgNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 81 MNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGM 160
Cdd:cd01662 91 LNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 161 TMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:cd01662 171 TLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSE 250
|
250 260
....*....|....*....|....
gi 1220321659 241 IISHYSGKKePFGTLGMIYALMAI 264
Cdd:cd01662 251 IVPTFSRKP-LFGYRSMVYATVAI 273
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-264 |
7.36e-60 |
|
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: 195.48 E-value: 7.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 2 LYLIFGMWAGILGSALSIMIRIELGTPTSFLGNDHLYNVIVTAHAFVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRM 81
Cdd:pfam00115 5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 82 NNLSFWLLIPSIFFLLFSSMasmGVGTGWTVYPPLssinfhsgAAVDFAIFSLHIAGISSILGAINFITTILNMRTPGMT 161
Cdd:pfam00115 84 NALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 162 MeRIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTsffdplGGGDPILYQHLFWFFGHPEVYILILPGFGMISHI 241
Cdd:pfam00115 153 L-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225
|
250 260
....*....|....*....|...
gi 1220321659 242 ISHYSGKKePFGTLGMIYALMAI 264
Cdd:pfam00115 226 LPKFAGRP-LFGYKLSVLAFWLI 247
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
2-264 |
2.17e-50 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 175.12 E-value: 2.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 2 LYLIFGMWAGILGSALSIMIRIELGTPTS----FLGNDHlYNVIVTAHAFVMIFFMVMPIMIGgFGNWLIPLMIGAPDMA 77
Cdd:PRK15017 60 MYIIVAIVMLLRGFADAIMMRSQQALASAgeagFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 78 FPRMNNLSFWLLIPSIFFLLFSSMASMGVGTGWTVYPPLSSINFHSGAAVDFAIFSLHIAGISSILGAINFITTILNMRT 157
Cdd:PRK15017 138 FPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1220321659 158 PGMTMERIPLFIWSVLLTAILLLLSLPVLAGAITMLLLDRNFNTSFFDPLGGGDPILYQHLFWFFGHPEVYILILPGFGM 237
Cdd:PRK15017 218 PGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGV 297
|
250 260
....*....|....*....|....*..
gi 1220321659 238 ISHIISHYSgKKEPFGTLGMIYALMAI 264
Cdd:PRK15017 298 FSEIAATFS-RKRLFGYTSLVWATVCI 323
|
|
|