|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-360 |
0e+00 |
|
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: 648.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQIfmGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:cd01663 32 LSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:cd01663 110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:cd01663 190 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPVFGYLGMVYAML 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:cd01663 270 SIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVL 349
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:cd01663 350 ANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPK 390
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-357 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 613.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00153 39 LGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00153 117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00153 197 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKETFGTLGMIYAML 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00153 277 AIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVL 356
|
330 340 350
....*....|....*....|....*....|....*...
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:MTH00153 357 ANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHW 394
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-360 |
4.20e-160 |
|
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: 457.84 E-value: 4.20e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQiFMGNhQLYNVVVTAHAFIMVFFLVMPaLIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:TIGR02891 35 LATPGNT-FMDA-ETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:TIGR02891 112 GGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKKNVFGYLGMVYAMLS 240
Cdd:TIGR02891 192 FPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 241 IGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAMS 320
Cdd:TIGR02891 272 IGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLA 351
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2442382042 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:TIGR02891 352 SVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPK 391
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-360 |
7.79e-158 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 453.43 E-value: 7.79e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQIFmgNHQLYNVVVTAHAFIMVFFLVMPaLIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:COG0843 44 LAGPGLGLL--SPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:COG0843 121 GGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKKNVFGYLGMVYAMLS 240
Cdd:COG0843 201 FPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 241 IGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAMS 320
Cdd:COG0843 281 IAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLA 360
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2442382042 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:COG0843 361 SVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPK 400
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-360 |
1.29e-104 |
|
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: 314.13 E-value: 1.29e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQIFmgNHQLYNVVVTAHAFIMVFFLVMPAlIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAiv 80
Cdd:pfam00115 28 LAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 eSGAGTGWTVYPPLssvqahsgPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFhRLPLFVWSVLITAFLLLLT 160
Cdd:pfam00115 103 -GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTsfydpsGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKKNVFGYLGMVYAMLS 240
Cdd:pfam00115 173 FPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 241 IGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKF-ETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVML 326
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPK 367
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-360 |
0e+00 |
|
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: 648.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQIfmGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:cd01663 32 LSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:cd01663 110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:cd01663 190 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPVFGYLGMVYAML 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:cd01663 270 SIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVL 349
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:cd01663 350 ANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPK 390
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-357 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 613.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00153 39 LGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00153 117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00153 197 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKETFGTLGMIYAML 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00153 277 AIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVL 356
|
330 340 350
....*....|....*....|....*....|....*...
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:MTH00153 357 ANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHW 394
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-357 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 569.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGnqIFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00223 38 LGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00223 116 ESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00223 196 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSsKKEVFGTLGMIYAML 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00223 276 SIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIIL 355
|
330 340 350
....*....|....*....|....*....|....*...
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:MTH00223 356 SNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHW 393
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-357 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 562.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQIfmGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00167 41 LSQPGSLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00167 119 EAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00167 199 LPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00167 279 AIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVL 358
|
330 340 350
....*....|....*....|....*....|....*...
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:MTH00167 359 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHW 396
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-357 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 554.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00116 41 LGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00116 119 EAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00116 199 LPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAML 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00116 279 SIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVL 358
|
330 340 350
....*....|....*....|....*....|....*...
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:MTH00116 359 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHW 396
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-357 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 547.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00142 39 LGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00142 117 ESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00142 197 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAML 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00142 277 SIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVL 356
|
330 340 350
....*....|....*....|....*....|....*...
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:MTH00142 357 ANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHW 394
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-360 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 518.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQIfmGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00182 43 LSAPGAML--GDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00182 121 EQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAF-AKKNVFGYLGMVYAML 239
Cdd:MTH00182 201 LPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFvAKKQIFGYLGMVYAML 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00182 281 SIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVL 360
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:MTH00182 361 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-360 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 513.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00184 43 LSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00184 121 EQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAF-AKKNVFGYLGMVYAML 239
Cdd:MTH00184 201 LPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFaAKKQIFGYLGMVYAMV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00184 281 SIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVL 360
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:MTH00184 361 ANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-357 |
1.61e-179 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 507.68 E-value: 1.61e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGnqIFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00079 42 LSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSvQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00079 120 DMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00079 199 LPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTgKKEVFGSLGMVYAIL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00079 279 SIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVIL 358
|
330 340 350
....*....|....*....|....*....|....*...
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:MTH00079 359 SNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLW 396
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-357 |
5.38e-177 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 501.67 E-value: 5.38e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00037 41 LAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00037 119 ESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00037 199 LPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSgKQEPFGYLGMVYAMI 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00037 279 AIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVL 358
|
330 340 350
....*....|....*....|....*....|....*...
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:MTH00037 359 ANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHW 396
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-357 |
1.40e-176 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 500.20 E-value: 1.40e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00007 38 LGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00007 116 EKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKK-NVFGYLGMVYAML 239
Cdd:MTH00007 196 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKlEPFGTLGMIYAML 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00007 276 GIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVL 355
|
330 340 350
....*....|....*....|....*....|....*...
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:MTH00007 356 SNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHW 393
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-357 |
7.56e-175 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 495.98 E-value: 7.56e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00183 41 LSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00183 119 EAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00183 199 LPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00183 279 AIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVL 358
|
330 340 350
....*....|....*....|....*....|....*...
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:MTH00183 359 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHW 396
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-357 |
2.79e-173 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 492.15 E-value: 2.79e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00077 41 LSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00077 119 EAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00077 199 LPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00077 279 SIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVL 358
|
330 340 350
....*....|....*....|....*....|....*...
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:MTH00077 359 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHW 396
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-357 |
2.05e-171 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 487.08 E-value: 2.05e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00103 41 LGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00103 119 EAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00103 199 LPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:MTH00103 279 SIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVL 358
|
330 340 350
....*....|....*....|....*....|....*...
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:MTH00103 359 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHW 396
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-360 |
4.20e-160 |
|
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: 457.84 E-value: 4.20e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQiFMGNhQLYNVVVTAHAFIMVFFLVMPaLIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:TIGR02891 35 LATPGNT-FMDA-ETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:TIGR02891 112 GGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKKNVFGYLGMVYAMLS 240
Cdd:TIGR02891 192 FPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 241 IGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAMS 320
Cdd:TIGR02891 272 IGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLA 351
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2442382042 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:TIGR02891 352 SVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPK 391
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-360 |
5.92e-160 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 459.09 E-value: 5.92e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNqiFMGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00026 42 LSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00026 120 EQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00026 200 LPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAML 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 240 SIGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGG--SLKFETPLLFVLGFILLFVMGGVTGV 317
Cdd:MTH00026 280 AIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGI 359
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2442382042 318 AMSNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:MTH00026 360 VLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGK 402
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-360 |
4.90e-159 |
|
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: 453.91 E-value: 4.90e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQIfmGNHQLYNVVVTAHAFIMVFFLVMPALIGGFGNWFVPlMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:cd00919 30 LATPGSLF--LDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:cd00919 107 GGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKKNVFGYLGMVYAMLS 240
Cdd:cd00919 187 LPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKPLFGYKLMVYAFLA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 241 IGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAMS 320
Cdd:cd00919 267 IGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLA 346
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2442382042 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:cd00919 347 NVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPK 386
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-360 |
7.79e-158 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 453.43 E-value: 7.79e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQIFmgNHQLYNVVVTAHAFIMVFFLVMPaLIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:COG0843 44 LAGPGLGLL--SPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:COG0843 121 GGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKKNVFGYLGMVYAMLS 240
Cdd:COG0843 201 FPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 241 IGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAMS 320
Cdd:COG0843 281 IAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLA 360
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2442382042 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:COG0843 361 SVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPK 400
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-357 |
7.38e-141 |
|
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: 408.89 E-value: 7.38e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQiFMGNHQlYNVVVTAHAFIMVFFLVMPALIGgFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:cd01662 36 LALPGND-FLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:cd01662 113 GGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKKNVFGYLGMVYAMLS 240
Cdd:cd01662 193 FPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 241 IGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAMS 320
Cdd:cd01662 273 IGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLA 352
|
330 340 350
....*....|....*....|....*....|....*..
gi 2442382042 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:cd01662 353 SPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYW 389
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
16-357 |
1.67e-123 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 365.15 E-value: 1.67e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 16 YNVVVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIVesGAGTGWTVYPPLS 95
Cdd:MTH00048 55 YNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 96 SVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLsFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDR 175
Cdd:MTH00048 133 SSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV-FSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 176 NLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKKN-VFGYLGMVYAMLSIGLLGCIVWAHHMF 254
Cdd:MTH00048 212 NFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 255 TVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLL-FVLGFILLFVMGGVTGVAMSNSGLDIAIHDTYY 333
Cdd:MTH00048 292 TVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWF 371
|
330 340
....*....|....*....|....
gi 2442382042 334 IVGHFHYVLSMGAVFGIFTGFYFW 357
Cdd:MTH00048 372 VVAHFHYVLSLGSYSSVVIMFIWW 395
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-360 |
1.29e-104 |
|
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: 314.13 E-value: 1.29e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQIFmgNHQLYNVVVTAHAFIMVFFLVMPAlIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAiv 80
Cdd:pfam00115 28 LAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 eSGAGTGWTVYPPLssvqahsgPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFhRLPLFVWSVLITAFLLLLT 160
Cdd:pfam00115 103 -GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTsfydpsGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKKNVFGYLGMVYAMLS 240
Cdd:pfam00115 173 FPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 241 IGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKF-ETPLLFVLGFILLFVMGGVTGVAM 319
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVML 326
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2442382042 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPK 367
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-360 |
6.29e-95 |
|
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131928 Cd Length: 643 Bit Score: 295.99 E-value: 6.29e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQIFMGNHqlYNVVVTAHAFIMVFFLVMPALIGgFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:TIGR02882 79 LTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:TIGR02882 156 GGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKKNVFGYLGMVYAMLS 240
Cdd:TIGR02882 236 FPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 241 IGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAMS 320
Cdd:TIGR02882 316 IAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLA 395
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2442382042 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:TIGR02882 396 MASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPK 435
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-360 |
1.49e-92 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 290.30 E-value: 1.49e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 1 LAQPGNQIFMGNHQlYNVVVTAHAFIMVFFLVMPALIGgFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:PRK15017 85 LASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAIFSLHLTGISSILGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:PRK15017 163 GEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIAS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKKNVFGYLGMVYAMLS 240
Cdd:PRK15017 243 FPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVC 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 241 IGLLGCIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFVLGFILLFVMGGVTGVAMS 320
Cdd:PRK15017 323 ITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLA 402
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2442382042 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTGFYFWIGK 360
Cdd:PRK15017 403 VPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPK 442
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
9-357 |
3.31e-10 |
|
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: 61.15 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 9 FMGNHQLYNVVVTAHAFIMVffLVMPAL-IGGFGNWFVPLMIGAPDMAfPRMNNISFWLLPPALLLLVSsAIVESGAGTG 87
Cdd:cd01660 37 LPSSGILYYQGLTLHGVLLA--IVFTTFfIMGFFYAIVARALLRSLFN-RRLAWAGFWLMVIGTVMAAV-PILLGQASVL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 88 WTVYPPLssvQAHSGPSVDLAIFSLHltgiSSILGAINFI-STIYNMRAPGLsfhRLPLFVWSVLITAFLLLLTLPVLAg 166
Cdd:cd01660 113 YTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVtLWRWKKANPGK---KVPLATFMVVTTMILWLVASLGVA- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 167 aITMLLTDRNLNTSFYDPSgggDPVLYQHLFWFFGHPEVYILILPAFGIISQVAAAFAKKNVFGYLGMVYAMLSIGLLGC 246
Cdd:cd01660 182 -LEVLFQLLPWSLGLVDTV---DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFST 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2442382042 247 IVWAHHMFT-VGLDVDTRAYFSAATMIIAVPTGIKIFSWLATL--------------WGGSLKFETPLLFVLGF-ILLFV 310
Cdd:cd01660 258 PVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeiagrlrggkglfgWIRALPWGDPMFLALFLaMLMFI 337
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2442382042 311 MGGVTGVAMSNSGLDIAIHDTYYIVGHFHYVLSmGAVFGIFTGFYFW 357
Cdd:cd01660 338 PGGAGGIINASYQLNYVVHNTAWVPGHFHLTVG-GAVALTFMAVAYW 383
|
|
|