|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 628.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00153 10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00153 90 MAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00153 170 RSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00153 250 GMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQ 329
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00153 330 INYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYV 371
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-362 |
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: 601.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:cd01663 3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:cd01663 83 MAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:cd01663 163 RAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:cd01663 243 GIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGS 322
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:cd01663 323 IKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYV 364
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-362 |
1.04e-134 |
|
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: 393.51 E-value: 1.04e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPfMIGGFGNFLIPLMLGSPD 80
Cdd:TIGR02891 6 HKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:TIGR02891 85 MAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:TIGR02891 165 RAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:TIGR02891 245 GIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGS 323
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:TIGR02891 324 IRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFV 365
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-362 |
4.25e-128 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 377.55 E-value: 4.25e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPD 80
Cdd:COG0843 15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:COG0843 94 MAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:COG0843 174 RAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:COG0843 254 GIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGR 332
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:COG0843 333 IRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFV 374
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
3-362 |
4.35e-89 |
|
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: 274.45 E-value: 4.35e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 3 DIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPDMA 82
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 83 YPRMNNMSFWLLPPSLILLIMSnfiSTGTGAGWTLYPPLtsnmfhsgPSVDMTIFSLHIAGMSSILGAINFISTIFNMHQ 162
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLAS---FGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 163 KKISMdKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTtffdpsGGGDPILYQHLFWFFGHPEVYILILPGFGL 242
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 243 ISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMKIN 322
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1938538769 323 -YNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFV 341
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 628.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00153 10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00153 90 MAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00153 170 RSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00153 250 GMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQ 329
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00153 330 INYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYV 371
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-362 |
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: 601.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:cd01663 3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:cd01663 83 MAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:cd01663 163 RAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:cd01663 243 GIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGS 322
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:cd01663 323 IKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYV 364
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 554.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00167 12 HKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00167 92 MAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00167 172 KPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00167 252 GMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGK 331
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00167 332 IKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYV 373
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 544.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00223 9 HKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00223 89 MAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00223 169 RSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00223 249 GMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSK 328
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00223 329 IKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYV 370
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 543.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00116 12 HKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00116 92 MAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00116 172 KPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00116 252 GIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGT 331
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00116 332 IKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYV 373
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 529.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00142 10 HKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00142 90 MAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00142 170 RAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00142 250 GMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSK 329
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00142 330 VKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYV 371
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-362 |
9.40e-174 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 493.27 E-value: 9.40e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00007 9 HKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00007 89 MAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00007 169 RWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00007 249 GAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSP 328
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00007 329 IKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYV 370
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-362 |
5.19e-172 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 489.01 E-value: 5.19e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00103 12 HKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00103 92 MAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00103 172 KPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00103 252 GMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGN 331
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00103 332 IKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYV 373
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
6.29e-171 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 486.35 E-value: 6.29e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00183 12 HKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00183 92 MAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00183 172 KPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00183 252 GMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGS 331
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00183 332 IKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYV 373
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
2.28e-170 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 484.72 E-value: 2.28e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00037 12 HKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00037 92 MAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00037 172 RTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00037 252 GMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSN 331
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00037 332 LRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYV 373
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
2.40e-169 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 481.87 E-value: 2.40e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00079 13 HKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLtSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00079 93 MSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00079 172 RSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00079 252 GIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMK 331
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00079 332 MKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYV 373
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
1.33e-167 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 477.90 E-value: 1.33e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00077 12 HKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00077 92 MAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00077 172 KPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00077 252 GMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGA 331
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00077 332 IKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYV 373
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
8.77e-162 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 463.14 E-value: 8.77e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00184 14 HKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00184 94 MAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00184 174 RAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00184 254 GIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGS 333
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00184 334 LRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYV 375
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
1.04e-159 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 458.13 E-value: 1.04e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00182 14 HKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00182 94 MAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00182 174 RAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00182 254 GMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGT 333
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00182 334 LRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYV 375
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-362 |
5.92e-145 |
|
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: 418.09 E-value: 5.92e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPlMLGSPD 80
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:cd00919 240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYV 360
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
2.18e-141 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 411.71 E-value: 2.18e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSPD 80
Cdd:MTH00026 13 HKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:MTH00026 93 MAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00026 173 RTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:MTH00026 253 GIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSG 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1938538769 321 IN--YNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00026 333 RNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYV 376
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-362 |
1.04e-134 |
|
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: 393.51 E-value: 1.04e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPfMIGGFGNFLIPLMLGSPD 80
Cdd:TIGR02891 6 HKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:TIGR02891 85 MAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:TIGR02891 165 RAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:TIGR02891 245 GIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGS 323
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:TIGR02891 324 IRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFV 365
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-362 |
1.22e-130 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 383.64 E-value: 1.22e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGS-CNNLINNDqIYNSLITSHAFIMIFFMVMPFMIGGFGNFLIPLMLGSP 79
Cdd:MTH00048 13 HKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDpYYNVISLD-VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 80 DMAYPRMNNMSFWLLPPSLILLIMSNFIstGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFN 159
Cdd:MTH00048 92 DLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 160 MHQKKISMdKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPG 239
Cdd:MTH00048 170 AFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 240 FGLISHIIMNESGKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGM 319
Cdd:MTH00048 249 FGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNS 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1938538769 320 KIN-YNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:MTH00048 329 RVRkSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFV 372
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-362 |
4.25e-128 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 377.55 E-value: 4.25e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPD 80
Cdd:COG0843 15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:COG0843 94 MAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:COG0843 174 RAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:COG0843 254 GIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGR 332
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:COG0843 333 IRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFV 374
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-362 |
1.96e-113 |
|
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: 339.17 E-value: 1.96e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGgFGNFLIPLMLGSPD 80
Cdd:cd01662 7 HKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:cd01662 86 VAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:cd01662 166 RAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:cd01662 246 GIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGR 324
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:cd01662 325 IRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFV 366
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
3-362 |
4.35e-89 |
|
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: 274.45 E-value: 4.35e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 3 DIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFmIGGFGNFLIPLMLGSPDMA 82
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 83 YPRMNNMSFWLLPPSLILLIMSnfiSTGTGAGWTLYPPLtsnmfhsgPSVDMTIFSLHIAGMSSILGAINFISTIFNMHQ 162
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLAS---FGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 163 KKISMdKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTtffdpsGGGDPILYQHLFWFFGHPEVYILILPGFGL 242
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 243 ISHIIMNESGKKeTFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMKIN 322
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1938538769 323 -YNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFV 341
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-362 |
1.74e-76 |
|
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: 247.84 E-value: 1.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLELGSCNNLINNDQIYNSLITSHAFIMIFFMVMPFMIGgFGNFLIPLMLGSPD 80
Cdd:TIGR02882 50 HKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 81 MAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTIFNM 160
Cdd:TIGR02882 129 VAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKM 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 161 HQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILILPGF 240
Cdd:TIGR02882 209 RAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 241 GLISHIIMNESgKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLHGMK 320
Cdd:TIGR02882 289 GIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGK 367
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1938538769 321 INYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:TIGR02882 368 IRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFL 409
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-362 |
5.27e-74 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 241.76 E-value: 5.27e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 1 HKDIGILYFLLAIWSGMIGSAMSMIIRLE--LGSCNNL-INNDQIYNSLITSHAFIMIFFMVMPFMIGgFGNFLIPLMLG 77
Cdd:PRK15017 54 HKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAgFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 78 SPDMAYPRMNNMSFWLLPPSLILLIMSNFISTGTGAGWTLYPPLTSNMFHSGPSVDMTIFSLHIAGMSSILGAINFISTI 157
Cdd:PRK15017 133 ARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 158 FNMHQKKISMDKIPLLVWSILITTILLLLSLPVLAGAITMLLTDRNLNTTFFDPSGGGDPILYQHLFWFFGHPEVYILIL 237
Cdd:PRK15017 213 LKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILIL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 238 PGFGLISHIIMNESgKKETFGSLGMIYAMITIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWISTLH 317
Cdd:PRK15017 293 PVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMY 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1938538769 318 GMKINYNPTLWWSMGFIFLFSMGGFTGIMLSNSSIDIILHDTYYV 362
Cdd:PRK15017 372 QGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFL 416
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
216-362 |
7.89e-04 |
|
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: 41.12 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 216 DPILYQHLFWFFGHPEVYILILPGFGLISHIIMNESGKKETFGSLGMIyAMITIGFLGFIVWAHHMFT-IGLDVDTRAYF 294
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938538769 295 TSATMIIAIPTGIKIFSWISTL-------HGMK-INYNPTLWWS----MGFIF---LFSMGGFTGIMLSNSSIDIILHDT 359
Cdd:cd01660 279 MVLTFMVALPSLLTAFTVFASLeiagrlrGGKGlFGWIRALPWGdpmfLALFLamlMFIPGGAGGIINASYQLNYVVHNT 358
|
...
gi 1938538769 360 YYV 362
Cdd:cd01660 359 AWV 361
|
|
|