|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 903.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00153 5 LFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00153 85 LGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00153 165 TIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00153 245 ILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00153 325 LHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMN 404
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00153 405 PKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRR 437
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
4-433 |
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: 798.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 4 TNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGA 83
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 84 PDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVI 163
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 164 NMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 243
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 244 GFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYG 323
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 324 TQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNTKM 403
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430
....*....|....*....|....*....|
gi 2449669701 404 LKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRR 430
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-433 |
4.90e-180 |
|
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: 511.77 E-value: 4.90e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMiGGFGNWLVPIM 80
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRR 431
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-433 |
3.14e-179 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 510.82 E-value: 3.14e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPIM 80
Cdd:COG0843 10 LTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:COG0843 89 IGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:COG0843 169 TILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYIL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:COG0843 249 ILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIAT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:COG0843 328 MWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLN 407
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:COG0843 408 ERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRR 440
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
8-433 |
7.92e-122 |
|
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: 361.12 E-value: 7.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 8 DIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPIMLGAPDMA 87
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 88 FPRMNNMSFWLLPPALTLLLVSSMvenGAGTGWTVYPPLssniahggASVDLAIFSLHLAGISSILGAVNFITTVINMRS 167
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 168 TGITFdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 247
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 248 ISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLN 327
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 328 -YSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNTKMLKS 406
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420
....*....|....*....|....*..
gi 2449669701 407 QFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRR 407
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 903.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00153 5 LFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00153 85 LGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00153 165 TIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00153 245 ILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00153 325 LHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMN 404
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00153 405 PKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRR 437
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
4-433 |
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: 798.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 4 TNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGA 83
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 84 PDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVI 163
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 164 NMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 243
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 244 GFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYG 323
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 324 TQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNTKM 403
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430
....*....|....*....|....*....|
gi 2449669701 404 LKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRR 430
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 765.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00167 7 LFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00167 87 IGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00167 167 TIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00167 247 ILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00167 327 LHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLN 406
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00167 407 ETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRR 439
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 757.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00223 4 LFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00223 84 LGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00223 164 TIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00223 244 ILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLAT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00223 324 IYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLH 403
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00223 404 RRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRR 436
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 756.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00116 7 LFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00116 87 IGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00116 167 TCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00116 247 ILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00116 327 LHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLH 406
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00116 407 QTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRR 439
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 748.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00142 5 LFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00142 85 LGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00142 165 TVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00142 245 ILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLAT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00142 325 LHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLN 404
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00142 405 PRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRR 437
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 685.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00103 7 LFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00103 87 IGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00103 167 TIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00103 247 ILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00103 327 LHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLN 406
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00103 407 DTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRR 439
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 677.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00037 7 LFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00037 87 IGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00037 167 TIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00037 247 ILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00037 327 LQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLH 406
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00037 407 PLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRR 439
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 677.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00183 7 FFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00183 87 IGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00183 167 TIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00183 247 ILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00183 327 LHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLH 406
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00183 407 STWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRR 439
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 673.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00007 4 LYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00007 84 LGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00007 164 TVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00007 244 ILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLAT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00007 324 IHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLH 403
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00007 404 DRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRR 436
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 669.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00077 7 LFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00077 87 IGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00077 167 TSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00077 247 ILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00077 327 MHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLH 406
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00077 407 STWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRR 439
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 626.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00182 9 VFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00182 89 IGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFIT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00182 169 TIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYIL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00182 249 ILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLAT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00182 329 IYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYN 408
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00182 409 ELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRR 441
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 624.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00079 8 LESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSnIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00079 88 LGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00079 167 TTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYIL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00079 247 ILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00079 327 LFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYD 406
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00079 407 KLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRK 439
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 612.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00184 9 LFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00184 89 IGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFIT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00184 169 TIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00184 249 ILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIAT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:MTH00184 329 IFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYN 408
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00184 409 EVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRR 441
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 548.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00026 8 FFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00026 88 IGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFIT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00026 168 TVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00026 248 ILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLAT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLN--YSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLT 398
Cdd:MTH00026 328 VSGSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYA 407
|
410 420 430
....*....|....*....|....*....|....*
gi 2449669701 399 LNTKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00026 408 YKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRR 442
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
6-433 |
0e+00 |
|
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: 538.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 6 HKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPiMLGAPD 85
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 86 MAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINM 165
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 166 RSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 245
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 246 GMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQ 325
Cdd:cd00919 240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 326 LNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNTKMLK 405
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420
....*....|....*....|....*...
gi 2449669701 406 SQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRR 426
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-433 |
4.90e-180 |
|
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: 511.77 E-value: 4.90e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMiGGFGNWLVPIM 80
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRR 431
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-433 |
3.14e-179 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 510.82 E-value: 3.14e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPIM 80
Cdd:COG0843 10 LTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:COG0843 89 IGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:COG0843 169 TILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYIL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:COG0843 249 ILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIAT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:COG0843 328 MWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLN 407
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:COG0843 408 ERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRR 440
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-433 |
5.66e-164 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 471.08 E-value: 5.66e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIM 80
Cdd:MTH00048 8 LFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVenGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:MTH00048 88 LGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFIC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:MTH00048 166 TIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:MTH00048 245 ILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYS-PATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTL 399
Cdd:MTH00048 325 LLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSL 404
|
410 420 430
....*....|....*....|....*....|....
gi 2449669701 400 NTKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:MTH00048 405 NKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRR 438
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
3-433 |
3.28e-155 |
|
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: 448.57 E-value: 3.28e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 3 STNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPIMLG 82
Cdd:cd01662 4 TVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 83 APDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTV 162
Cdd:cd01662 83 ARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 163 INMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILIL 242
Cdd:cd01662 163 LKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILIL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 243 PGFGMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLY 322
Cdd:cd01662 243 PAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 323 GTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNTK 402
Cdd:cd01662 322 RGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNER 401
|
410 420 430
....*....|....*....|....*....|.
gi 2449669701 403 MLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:cd01662 402 LGKWSFWLWFIGFNLTFFPMHILGLMGMPRR 432
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
8-433 |
7.92e-122 |
|
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: 361.12 E-value: 7.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 8 DIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPIMLGAPDMA 87
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 88 FPRMNNMSFWLLPPALTLLLVSSMvenGAGTGWTVYPPLssniahggASVDLAIFSLHLAGISSILGAVNFITTVINMRS 167
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 168 TGITFdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 247
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 248 ISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLN 327
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 328 -YSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLNTKMLKS 406
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420
....*....|....*....|....*..
gi 2449669701 407 QFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRR 407
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-433 |
2.79e-105 |
|
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: 325.27 E-value: 2.79e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPIM 80
Cdd:TIGR02882 45 LTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 81 LGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFIT 160
Cdd:TIGR02882 124 IGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 161 TVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 240
Cdd:TIGR02882 204 TILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 241 ILPGFGMISHIISQESgKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 320
Cdd:TIGR02882 284 ILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 LYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTLN 400
Cdd:TIGR02882 363 LYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLN 442
|
410 420 430
....*....|....*....|....*....|...
gi 2449669701 401 TKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:TIGR02882 443 ERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRR 475
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-433 |
6.13e-99 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 309.56 E-value: 6.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 1 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIR-----AELGHPGALigDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNW 75
Cdd:PRK15017 49 LTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRsqqalASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 76 LVPIMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGA 155
Cdd:PRK15017 126 VVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 156 VNFITTVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHP 235
Cdd:PRK15017 206 INFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 236 EVYILILPGFGMISHIISQESgKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIF 315
Cdd:PRK15017 286 EVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 316 SWLATLYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFT 395
Cdd:PRK15017 365 NWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAF 444
|
410 420 430
....*....|....*....|....*....|....*...
gi 2449669701 396 GLTLNTKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:PRK15017 445 GFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRR 482
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
9-433 |
6.08e-16 |
|
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: 79.64 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 9 IGTLYFIFGAWAGMvgtsLSILIRAELGhpgALIGDDQIYNVIVTAHAFIM-IFFMVMPIMigGFGNWLVPIMLGAPDMA 87
Cdd:cd01660 12 VAFLALLLGGLFGL----LQVLVRTGVF---PLPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 88 fPRMNNMSFWLLPPALTLLLVSsMVENGAGTGWTVYPPLssnIAHGGASVDLAIFSLHlagiSSILGAVNFITTVINMRS 167
Cdd:cd01660 83 -RRLAWAGFWLMVIGTVMAAVP-ILLGQASVLYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLWRWKKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 168 tgITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLtdrnINTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 247
Cdd:cd01660 154 --NPGKKVPLATFMVVTTMILWLVASLGVALEVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 248 ISHIISQESGKKETFGSLGMIyAMLAIGLLGFIVWAHHMFT-VGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT------ 320
Cdd:cd01660 227 WYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASleiagr 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449669701 321 ------LYG--TQLNYSPATLWALGFVFL-FTVGGLTGVVLANSSVDIILHDTYYVVAHFHyvLSMGAVFAIMA-GFVHW 390
Cdd:cd01660 306 lrggkgLFGwiRALPWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAYW 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2449669701 391 Y-PLFTGLTLNTKMLKS-QFTIMFMGVNLTFFPQHFLGLAGMPRR 433
Cdd:cd01660 384 LvPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRR 428
|
|
| |
