|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-431 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 810.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
410 420 430
....*....|....*....|....*....|.
gi 188501834 401 IYPIQLCSSIEWYQNTPPAEHSYSELPLLTN 431
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-412 |
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: 680.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:cd01663 74 VPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:cd01663 154 NFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:cd01663 234 VYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:cd01663 314 WLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITG 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:cd01663 394 LSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKV 473
|
410
....*....|...
gi 188501834 401 IYPI-QLCSSIEW 412
Cdd:cd01663 474 IFNVgEGSTSLEW 486
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-430 |
2.00e-154 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 447.65 E-value: 2.00e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQR 398
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
410 420 430
....*....|....*....|....*....|...
gi 188501834 399 QV-IYPIQlCSSIEWYQNTPPAEHSYSELPLLT 430
Cdd:COG0843 484 KAgGNPWG-ARTLEWATPSPPPLYNFASIPVVR 515
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-423 |
5.15e-151 |
|
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: 437.81 E-value: 5.15e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:TIGR02891 76 LPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:TIGR02891 156 NFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:TIGR02891 236 VYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFN 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:TIGR02891 315 WIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTTWNVISTIGSSISLLGILFFFYIIWESLVSQR 398
Cdd:TIGR02891 395 RMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP 474
|
410 420
....*....|....*....|....*
gi 188501834 399 QVIYPIQLCSSIEWYQNTPPAEHSY 423
Cdd:TIGR02891 475 KAGANPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-378 |
1.04e-101 |
|
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: 309.50 E-value: 1.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMvenGAGTGWTVYPPLssgiahggASVDLAIFSLHLAGISSILGAV 80
Cdd:pfam00115 69 VPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTsff*******************HPE 160
Cdd:pfam00115 138 NFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:pfam00115 211 VYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLS-YSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFT 319
Cdd:pfam00115 290 WLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLT 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 188501834 320 GLTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTTWNVISTIGSSI 378
Cdd:pfam00115 370 GRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-431 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 810.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
410 420 430
....*....|....*....|....*....|.
gi 188501834 401 IYPIQLCSSIEWYQNTPPAEHSYSELPLLTN 431
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-412 |
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: 680.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:cd01663 74 VPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:cd01663 154 NFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:cd01663 234 VYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:cd01663 314 WLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITG 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:cd01663 394 LSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKV 473
|
410
....*....|...
gi 188501834 401 IYPI-QLCSSIEW 412
Cdd:cd01663 474 IFNVgEGSTSLEW 486
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-429 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 655.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00167 83 VPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00167 163 NFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00167 243 VYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00167 323 WLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00167 403 LTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKL 482
|
410 420
....*....|....*....|....*....
gi 188501834 401 IYPIQLCSSIEWYQNTPPAEHSYSELPLL 429
Cdd:MTH00167 483 LPVELTSTNVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-431 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 655.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00142 81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00142 161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00142 241 VYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00142 321 WLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00142 401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLV 480
|
410 420 430
....*....|....*....|....*....|.
gi 188501834 401 IYPIQLCSSIEWYQNTPPAEHSYSELPLLTN 431
Cdd:MTH00142 481 MWSSHLSTSLEWSHRLPPDFHTYDELPILVV 511
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-427 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 654.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00223 80 VPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00223 160 NFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00223 240 VYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00223 320 WLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTG 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00223 400 VTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSV 479
|
410 420
....*....|....*....|....*..
gi 188501834 401 IYPIQLCSSIEWYQNTPPAEHSYSELP 427
Cdd:MTH00223 480 VWSGHLSTSLEWDNLLPADFHNNSETG 506
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-431 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 646.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00116 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00116 163 NFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00116 243 VYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00116 323 WLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00116 403 YTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKV 482
|
410 420 430
....*....|....*....|....*....|.
gi 188501834 401 IYPIQLCSSIEWYQNTPPAEHSYSELPLLTN 431
Cdd:MTH00116 483 LQPELTTTNIEWIHGCPPPYHTFEEPAFVQV 513
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-428 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 587.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00037 83 IPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00037 163 NFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00037 243 VYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00037 323 WMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSG 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00037 403 VSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREV 482
|
410 420
....*....|....*....|....*....
gi 188501834 401 IYPIQLCSSIEW-YQNTPPAEHSYSELPL 428
Cdd:MTH00037 483 ISPEFSSSSLEWqYSSFPPSHHTFDETPS 511
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-430 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 584.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00007 80 VPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00007 160 NFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00007 240 VYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00007 320 WLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTG 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00007 400 LTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGV 479
|
410 420 430
....*....|....*....|....*....|
gi 188501834 401 IYPIQLCSSIEWYQNTPPAEHSYSELPLLT 430
Cdd:MTH00007 480 IASPHMSSSLEWQDTLPLDFHNLPETGIIT 509
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-425 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 578.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00103 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00103 163 NFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00103 243 VYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00103 323 WLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00103 403 YTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREV 482
|
410 420
....*....|....*....|....*
gi 188501834 401 IYPIQLCSSIEWYQNTPPAEHSYSE 425
Cdd:MTH00103 483 LTVELTTTNLEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-425 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 572.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00183 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00183 163 NFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00183 243 VYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00183 323 WLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSG 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00183 403 YTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREV 482
|
410 420
....*....|....*....|....*
gi 188501834 401 IYPIQLCSSIEWYQNTPPAEHSYSE 425
Cdd:MTH00183 483 LSVELTSTNVEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-431 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 565.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00077 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00077 163 NFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00077 243 VYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00077 323 WLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00077 403 YTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREV 482
|
410 420 430
....*....|....*....|....*....|.
gi 188501834 401 IYPIQLCSSIEWYQNTPPAEHSYSELPLLTN 431
Cdd:MTH00077 483 LTTELTSTNIEWLHGCPPPYHTFEEPSFVQT 513
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-429 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 531.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00182 85 VPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAI 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00182 165 NFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00182 245 VYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00182 325 WLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00182 405 YCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKF 484
|
410 420 430
....*....|....*....|....*....|...
gi 188501834 401 I----YPIQLCSSIEWYQNTPPAEHSYSELPLL 429
Cdd:MTH00182 485 IgwkeGTGESWASLEWVHSSPPLFHTYNELPFV 517
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-425 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 526.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSgIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00079 84 LPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGI 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00079 163 NFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00079 243 VYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00079 323 WLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTG 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00079 403 IVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLV 482
|
410 420
....*....|....*....|....*
gi 188501834 401 IYPIQLCSSIEWYQNTPPAEHSYSE 425
Cdd:MTH00079 483 LHDNYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-429 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 519.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00184 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00184 165 NFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00184 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:MTH00184 325 WIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQV 400
Cdd:MTH00184 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKF 484
|
410 420 430
....*....|....*....|....*....|..
gi 188501834 401 IYPIQ---LCSSIEWYQNTPPAEHSYSELPLL 429
Cdd:MTH00184 485 VGWVEdsgHYPSLEWAQTSPPAHHTYNELPYV 516
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-394 |
8.49e-166 |
|
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: 473.94 E-value: 8.49e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:cd00919 71 LPPLIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:cd00919 151 NFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:cd00919 231 VYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:cd00919 310 WLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTG 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESL 394
Cdd:cd00919 390 RMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-429 |
1.97e-155 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 450.23 E-value: 1.97e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00026 84 VPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAM 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00026 164 NFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00026 244 VYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGT--QLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLF 318
Cdd:MTH00026 324 WLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKI 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 319 TGLTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVsqR 398
Cdd:MTH00026 404 TGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYY--R 481
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 188501834 399 QVIYPIQLCS---------------SIEWYQNTPPAEHSYSELPLL 429
Cdd:MTH00026 482 EEPFDINIMAkgplipfscqpahfdTLEWSLTSPPEHHTYNELPYI 527
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-430 |
2.00e-154 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 447.65 E-value: 2.00e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQR 398
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
410 420 430
....*....|....*....|....*....|...
gi 188501834 399 QV-IYPIQlCSSIEWYQNTPPAEHSYSELPLLT 430
Cdd:COG0843 484 KAgGNPWG-ARTLEWATPSPPPLYNFASIPVVR 515
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-423 |
5.15e-151 |
|
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: 437.81 E-value: 5.15e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:TIGR02891 76 LPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:TIGR02891 156 NFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:TIGR02891 236 VYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFN 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:TIGR02891 315 WIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTTWNVISTIGSSISLLGILFFFYIIWESLVSQR 398
Cdd:TIGR02891 395 RMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP 474
|
410 420
....*....|....*....|....*
gi 188501834 399 QVIYPIQLCSSIEWYQNTPPAEHSY 423
Cdd:TIGR02891 475 KAGANPWGATTLEWTTSSPPPAHNF 499
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-423 |
8.67e-134 |
|
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: 393.87 E-value: 8.67e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:cd01662 77 VPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:cd01662 157 NFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:cd01662 237 VYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFN 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:cd01662 316 WLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVISTIGSSISLLGILFFFY-IIWESLVSQ 397
Cdd:cd01662 396 RMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLInVIVSIRKGK 475
|
410 420
....*....|....*....|....*.
gi 188501834 398 RQVIYPIQLCSSIEWYQNTPPAEHSY 423
Cdd:cd01662 476 RDATGDPWGARTLEWATSSPPPAYNF 501
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-422 |
3.37e-129 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 382.49 E-value: 3.37e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVenGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:MTH00048 84 LPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:MTH00048 162 NFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:MTH00048 241 VYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYS-PAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFT 319
Cdd:MTH00048 321 WLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLIT 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 320 GLTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQ 399
Cdd:MTH00048 401 GLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNE 480
|
410 420
....*....|....*....|...
gi 188501834 400 VIYPIQLCSSIEWYQNTPPAEHS 422
Cdd:MTH00048 481 VLGLWGSSSCVVNVLMSPVPYHN 503
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-378 |
1.04e-101 |
|
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: 309.50 E-value: 1.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMvenGAGTGWTVYPPLssgiahggASVDLAIFSLHLAGISSILGAV 80
Cdd:pfam00115 69 VPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTsff*******************HPE 160
Cdd:pfam00115 138 NFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:pfam00115 211 VYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFN 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLS-YSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFT 319
Cdd:pfam00115 290 WLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLT 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 188501834 320 GLTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTTWNVISTIGSSI 378
Cdd:pfam00115 370 GRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-427 |
1.46e-90 |
|
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: 287.14 E-value: 1.46e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:TIGR02882 120 VPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:TIGR02882 200 NFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESgKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:TIGR02882 280 VYIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFN 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:TIGR02882 359 WLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFG 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTTWNVISTIGSSISLLGILFFFY-IIWESLVSQ 397
Cdd:TIGR02882 439 YKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKSP 518
|
410 420 430
....*....|....*....|....*....|
gi 188501834 398 RQVIYPIQLCSSIEWYQNTPPAEHSYSELP 427
Cdd:TIGR02882 519 REATGDPWNGRTLEWATASPPPKYNFAVTP 548
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-427 |
2.18e-89 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 284.52 E-value: 2.18e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 1 VPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSGIAHGGASVDLAIFSLHLAGISSILGAV 80
Cdd:PRK15017 127 VPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 81 NFIATVINMRSSGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFF*******************HPE 160
Cdd:PRK15017 207 NFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 161 VYILILPGFGMISHIISQESgKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 240
Cdd:PRK15017 287 VYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFN 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 241 WLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTG 320
Cdd:PRK15017 366 WLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFG 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 321 LTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA-YTTWNVISTIGSSISLLGIL---FFFYIIWESLVS 396
Cdd:PRK15017 446 FKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPqFHTMLMIAASGAALIALGILcqvIQMYVSIRDRDQ 525
|
410 420 430
....*....|....*....|....*....|.
gi 188501834 397 QRQVIYPIQLCSSIEWYQNTPPAEHSYSELP 427
Cdd:PRK15017 526 NRDLTGDPWGGRTLEWATSSPPPFYNFAVVP 556
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
158-395 |
8.99e-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: 78.87 E-value: 8.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 158 HPEVYILILPGFGMISHIISQESGKKETFGSLGMIyAMLAIGLLGFIVWAHHMFT-VGMDVDTRAYFTSATMIIAVPTGI 236
Cdd:cd01660 213 HPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 237 KIFSWLATL-------HG-------TQLSYSPAILWALGFVFL-FTVGGLTGVVLANSSIDIILHDTYYVVAHFHyvLSM 301
Cdd:cd01660 292 TAFTVFASLeiagrlrGGkglfgwiRALPWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTV 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188501834 302 GAVFAIMA-GFIHWY-PLFTGLTLNNKWLKS-QFIIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDAY-----TTWNVI 371
Cdd:cd01660 370 GGAVALTFmAVAYWLvPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQL 449
|
250 260
....*....|....*....|....
gi 188501834 372 STIGSSISLLGILFFFYIIWESLV 395
Cdd:cd01660 450 MAIGGTILFVSGALFLYILFRTLL 473
|
|
| |
