|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
5-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 806.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 5 LGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNLS 84
Cdd:MTH00153 20 FGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 85 FWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKV 164
Cdd:MTH00153 100 FWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRM 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 165 PLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISAS 244
Cdd:MTH00153 180 PLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 245 VGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWC 324
Cdd:MTH00153 260 SGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 325 IGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGV 404
Cdd:MTH00153 340 LGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGV 419
|
410
....*....|....*
gi 223403388 405 NMTFFPQHFLGLNGM 419
Cdd:MTH00153 420 NLTFFPQHFLGLAGM 434
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
4-419 |
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: 746.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 4 YLGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNL 83
Cdd:cd01663 12 IFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 84 SFWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEK 163
Cdd:cd01663 92 SFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 164 VPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISA 243
Cdd:cd01663 172 MPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIIST 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 244 SVGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMW 323
Cdd:cd01663 252 FSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLW 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 324 CIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLG 403
Cdd:cd01663 332 ALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIG 411
|
410
....*....|....*.
gi 223403388 404 VNMTFFPQHFLGLNGM 419
Cdd:cd01663 412 VNLTFFPQHFLGLAGM 427
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
11-419 |
3.66e-169 |
|
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: 483.26 E-value: 3.66e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 11 MVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILiGGFGNWLVPLMLGAPDMAFPRMNNLSFWLLPP 90
Cdd:TIGR02891 22 LVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 91 SLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKVPLFVWS 170
Cdd:TIGR02891 101 GGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 171 VLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISASVGKReP 250
Cdd:TIGR02891 181 ILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-I 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 251 FGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWCIGFVFL 330
Cdd:TIGR02891 260 FGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 331 FTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGVNMTFFP 410
Cdd:TIGR02891 340 FVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFP 419
|
....*....
gi 223403388 411 QHFLGLNGM 419
Cdd:TIGR02891 420 MHLLGLLGM 428
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
11-419 |
5.03e-167 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 479.24 E-value: 5.03e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 11 MVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPIlIGGFGNWLVPLMLGAPDMAFPRMNNLSFWLLPP 90
Cdd:COG0843 31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 91 SLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKVPLFVWS 170
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 171 VLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISASVGKReP 250
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-L 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 251 FGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWCIGFVFL 330
Cdd:COG0843 269 FGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIIL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 331 FTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGVNMTFFP 410
Cdd:COG0843 349 FVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFP 428
|
....*....
gi 223403388 411 QHFLGLNGM 419
Cdd:COG0843 429 MHILGLLGM 437
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
11-419 |
7.28e-115 |
|
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: 342.63 E-value: 7.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 11 MVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPIlIGGFGNWLVPLMLGAPDMAFPRMNNLSFWLLPP 90
Cdd:pfam00115 15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 91 SLMLLFISSMaevGVGAGWTVYPPLAAsmghsgssVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMeKVPLFVWS 170
Cdd:pfam00115 94 GAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 171 VLITAVLLLLSLPVLAGAITMLLTDRNFNtsffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISASVGKReP 250
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-L 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 251 FGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKL-ESPLMWCIGFVF 329
Cdd:pfam00115 235 FGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 330 LFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGVNMTFF 409
Cdd:pfam00115 315 LFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFF 394
|
410
....*....|
gi 223403388 410 PQHFLGLNGM 419
Cdd:pfam00115 395 PMHILGLLGM 404
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
5-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 806.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 5 LGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNLS 84
Cdd:MTH00153 20 FGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 85 FWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKV 164
Cdd:MTH00153 100 FWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRM 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 165 PLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISAS 244
Cdd:MTH00153 180 PLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 245 VGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWC 324
Cdd:MTH00153 260 SGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 325 IGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGV 404
Cdd:MTH00153 340 LGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGV 419
|
410
....*....|....*
gi 223403388 405 NMTFFPQHFLGLNGM 419
Cdd:MTH00153 420 NLTFFPQHFLGLAGM 434
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
4-419 |
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: 746.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 4 YLGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNL 83
Cdd:cd01663 12 IFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 84 SFWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEK 163
Cdd:cd01663 92 SFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 164 VPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISA 243
Cdd:cd01663 172 MPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIIST 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 244 SVGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMW 323
Cdd:cd01663 252 FSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLW 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 324 CIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLG 403
Cdd:cd01663 332 ALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIG 411
|
410
....*....|....*.
gi 223403388 404 VNMTFFPQHFLGLNGM 419
Cdd:cd01663 412 VNLTFFPQHFLGLAGM 427
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
5-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 701.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 5 LGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNLS 84
Cdd:MTH00167 22 FGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 85 FWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKV 164
Cdd:MTH00167 102 FWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 165 PLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISAS 244
Cdd:MTH00167 182 PLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 245 VGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWC 324
Cdd:MTH00167 262 SGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 325 IGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGV 404
Cdd:MTH00167 342 LGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGV 421
|
410
....*....|....*
gi 223403388 405 NMTFFPQHFLGLNGM 419
Cdd:MTH00167 422 NLTFFPQHFLGLAGM 436
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
4-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 697.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 4 YLGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNL 83
Cdd:MTH00223 18 IFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 84 SFWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEK 163
Cdd:MTH00223 98 SFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLER 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 164 VPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISA 243
Cdd:MTH00223 178 LPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSH 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 244 SVGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMW 323
Cdd:MTH00223 258 YSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLW 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 324 CIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLG 403
Cdd:MTH00223 338 ALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLG 417
|
410
....*....|....*.
gi 223403388 404 VNMTFFPQHFLGLNGM 419
Cdd:MTH00223 418 VNLTFFPQHFLGLAGM 433
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
6-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 690.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 6 GAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNLSF 85
Cdd:MTH00116 23 GAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 86 WLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKVP 165
Cdd:MTH00116 103 WLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 166 LFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISASV 245
Cdd:MTH00116 183 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 246 GKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWCI 325
Cdd:MTH00116 263 GKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWAL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 326 GFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGVN 405
Cdd:MTH00116 343 GFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVN 422
|
410
....*....|....
gi 223403388 406 MTFFPQHFLGLNGM 419
Cdd:MTH00116 423 LTFFPQHFLGLAGM 436
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
3-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 677.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 3 YYLGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNN 82
Cdd:MTH00142 18 FLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 83 LSFWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTME 162
Cdd:MTH00142 98 MSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 163 KVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIIS 242
Cdd:MTH00142 178 RVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 243 ASVGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLM 322
Cdd:MTH00142 258 HYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPML 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 323 WCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFL 402
Cdd:MTH00142 338 WALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFI 417
|
410
....*....|....*..
gi 223403388 403 GVNMTFFPQHFLGLNGM 419
Cdd:MTH00142 418 GVNLTFFPQHFLGLAGM 434
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
6-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 625.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 6 GAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNLSF 85
Cdd:MTH00037 23 GAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 86 WLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKVP 165
Cdd:MTH00037 103 WLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 166 LFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISASV 245
Cdd:MTH00037 183 LFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 246 GKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWCI 325
Cdd:MTH00037 263 GKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWAL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 326 GFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGVN 405
Cdd:MTH00037 343 GFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVN 422
|
410
....*....|....
gi 223403388 406 MTFFPQHFLGLNGM 419
Cdd:MTH00037 423 LTFFPQHFLGLAGM 436
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
3-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 622.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 3 YYLGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNN 82
Cdd:MTH00007 17 FILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 83 LSFWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTME 162
Cdd:MTH00007 97 MSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 163 KVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIIS 242
Cdd:MTH00007 177 RIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 243 ASVGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLM 322
Cdd:MTH00007 257 HYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPML 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 323 WCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFL 402
Cdd:MTH00007 337 WALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFL 416
|
410
....*....|....*..
gi 223403388 403 GVNMTFFPQHFLGLNGM 419
Cdd:MTH00007 417 GVNLTFFPQHFLGLSGM 433
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
5-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 618.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 5 LGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNLS 84
Cdd:MTH00103 22 FGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 85 FWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKV 164
Cdd:MTH00103 102 FWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 165 PLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISAS 244
Cdd:MTH00103 182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 245 VGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWC 324
Cdd:MTH00103 262 SGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 325 IGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGV 404
Cdd:MTH00103 342 LGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGV 421
|
410
....*....|....*
gi 223403388 405 NMTFFPQHFLGLNGM 419
Cdd:MTH00103 422 NMTFFPQHFLGLSGM 436
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
5-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 611.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 5 LGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNLS 84
Cdd:MTH00183 22 FGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 85 FWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKV 164
Cdd:MTH00183 102 FWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 165 PLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISAS 244
Cdd:MTH00183 182 PLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 245 VGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWC 324
Cdd:MTH00183 262 SGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 325 IGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGV 404
Cdd:MTH00183 342 LGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGV 421
|
410
....*....|....*
gi 223403388 405 NMTFFPQHFLGLNGM 419
Cdd:MTH00183 422 NLTFFPQHFLGLAGM 436
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
5-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 608.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 5 LGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNLS 84
Cdd:MTH00077 22 FGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 85 FWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKV 164
Cdd:MTH00077 102 FWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 165 PLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISAS 244
Cdd:MTH00077 182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 245 VGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWC 324
Cdd:MTH00077 262 SAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 325 IGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGV 404
Cdd:MTH00077 342 LGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGV 421
|
410
....*....|....*
gi 223403388 405 NMTFFPQHFLGLNGM 419
Cdd:MTH00077 422 NLTFFPQHFLGLAGM 436
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
6-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 590.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 6 GAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNLSF 85
Cdd:MTH00182 25 GAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 86 WLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKVP 165
Cdd:MTH00182 105 WLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 166 LFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISASV 245
Cdd:MTH00182 185 LFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 246 GKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWCI 325
Cdd:MTH00182 265 AKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAM 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 326 GFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGVN 405
Cdd:MTH00182 345 GFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVN 424
|
410
....*....|....
gi 223403388 406 MTFFPQHFLGLNGM 419
Cdd:MTH00182 425 LTFFPQHFLGLAGF 438
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
5-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 578.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 5 LGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNLS 84
Cdd:MTH00184 24 FGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNIS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 85 FWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKV 164
Cdd:MTH00184 104 FWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 165 PLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISAS 244
Cdd:MTH00184 184 PLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 245 VGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWC 324
Cdd:MTH00184 264 AAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 325 IGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGV 404
Cdd:MTH00184 344 IGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGV 423
|
410
....*....|....*
gi 223403388 405 NMTFFPQHFLGLNGM 419
Cdd:MTH00184 424 NLTFFPQHFLGLAGL 438
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 573.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 1 YIYYLGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRM 80
Cdd:MTH00079 19 LYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 81 NNLSFWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAaSMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMT 160
Cdd:MTH00079 99 NNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSIS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 161 MEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHI 240
Cdd:MTH00079 178 LEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 241 ISASVGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESP 320
Cdd:MTH00079 258 TLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 321 LMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIM 400
Cdd:MTH00079 338 LLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLM 417
|
410
....*....|....*....
gi 223403388 401 FLGVNMTFFPQHFLGLNGM 419
Cdd:MTH00079 418 FVGVNLTFFPLHFAGLHGM 436
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
5-419 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 519.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 5 LGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNLS 84
Cdd:MTH00026 23 FGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNIS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 85 FWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKV 164
Cdd:MTH00026 103 FWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 165 PLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISAS 244
Cdd:MTH00026 183 PLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 245 VGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKL--ESPLM 322
Cdd:MTH00026 263 SYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNLifTTPMA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 323 WCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFL 402
Cdd:MTH00026 343 WALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFI 422
|
410
....*....|....*..
gi 223403388 403 GVNMTFFPQHFLGLNGM 419
Cdd:MTH00026 423 GVNITFFPQHFLGLAGL 439
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
4-419 |
1.74e-175 |
|
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: 498.21 E-value: 1.74e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 4 YLGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPlMLGAPDMAFPRMNNL 83
Cdd:cd00919 10 IFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 84 SFWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEK 163
Cdd:cd00919 89 SFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 164 VPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISA 243
Cdd:cd00919 169 MPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 244 SVGKRePFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMW 323
Cdd:cd00919 249 FSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 324 CIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLG 403
Cdd:cd00919 328 ALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIG 407
|
410
....*....|....*.
gi 223403388 404 VNMTFFPQHFLGLNGM 419
Cdd:cd00919 408 FNLTFFPMHFLGLLGM 423
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
11-419 |
3.66e-169 |
|
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: 483.26 E-value: 3.66e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 11 MVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILiGGFGNWLVPLMLGAPDMAFPRMNNLSFWLLPP 90
Cdd:TIGR02891 22 LVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 91 SLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKVPLFVWS 170
Cdd:TIGR02891 101 GGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 171 VLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISASVGKReP 250
Cdd:TIGR02891 181 ILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-I 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 251 FGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWCIGFVFL 330
Cdd:TIGR02891 260 FGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 331 FTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGVNMTFFP 410
Cdd:TIGR02891 340 FVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFP 419
|
....*....
gi 223403388 411 QHFLGLNGM 419
Cdd:TIGR02891 420 MHLLGLLGM 428
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
11-419 |
5.03e-167 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 479.24 E-value: 5.03e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 11 MVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPIlIGGFGNWLVPLMLGAPDMAFPRMNNLSFWLLPP 90
Cdd:COG0843 31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 91 SLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKVPLFVWS 170
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 171 VLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISASVGKReP 250
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-L 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 251 FGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWCIGFVFL 330
Cdd:COG0843 269 FGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIIL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 331 FTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGVNMTFFP 410
Cdd:COG0843 349 FVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFP 428
|
....*....
gi 223403388 411 QHFLGLNGM 419
Cdd:COG0843 429 MHILGLLGM 437
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
5-419 |
5.88e-152 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 440.27 E-value: 5.88e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 5 LGAWSAMVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRMNNLS 84
Cdd:MTH00048 23 LGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 85 FWLLPPSLMLLFISSMaeVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTmEKV 164
Cdd:MTH00048 103 AWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 165 PLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISAS 244
Cdd:MTH00048 180 SIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 245 VGKREPFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLM-W 323
Cdd:MTH00048 260 SNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwW 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 324 CIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLG 403
Cdd:MTH00048 340 VVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIG 419
|
410
....*....|....*.
gi 223403388 404 VNMTFFPQHFLGLNGM 419
Cdd:MTH00048 420 FNLCFFPMHYFGLCGL 435
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-419 |
1.00e-144 |
|
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: 421.22 E-value: 1.00e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 2 IYYLGAWSAM--VGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPILIGgFGNWLVPLMLGAPDMAFPR 79
Cdd:cd01662 12 IMYIITAFVFflRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 80 MNNLSFWLLPPSLMLLFISSMAEVGVGAGWTVYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGM 159
Cdd:cd01662 91 LNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 160 TMEKVPLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 239
Cdd:cd01662 171 TLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 240 IISASVGKRePFGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLES 319
Cdd:cd01662 251 IVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFET 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 320 PLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFII 399
Cdd:cd01662 330 PMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWL 409
|
410 420
....*....|....*....|
gi 223403388 400 MFLGVNMTFFPQHFLGLNGM 419
Cdd:cd01662 410 WFIGFNLTFFPMHILGLMGM 429
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
11-419 |
7.28e-115 |
|
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: 342.63 E-value: 7.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 11 MVGTAMSVLIRIELGQPGSLLGDDHLYNVIVTAHAFVMIFFMVMPIlIGGFGNWLVPLMLGAPDMAFPRMNNLSFWLLPP 90
Cdd:pfam00115 15 LVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 91 SLMLLFISSMaevGVGAGWTVYPPLAAsmghsgssVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMeKVPLFVWS 170
Cdd:pfam00115 94 GAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 171 VLITAVLLLLSLPVLAGAITMLLTDRNFNtsffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISASVGKReP 250
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-L 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 251 FGSLGMIYAMAGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKL-ESPLMWCIGFVF 329
Cdd:pfam00115 235 FGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 330 LFTLGGITGVVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGVNMTFF 409
Cdd:pfam00115 315 LFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFF 394
|
410
....*....|
gi 223403388 410 PQHFLGLNGM 419
Cdd:pfam00115 395 PMHILGLLGM 404
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
35-419 |
3.33e-108 |
|
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131890 Cd Length: 646 Bit Score: 332.41 E-value: 3.33e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 35 HLYNVIVTAHAFVMIFFMVMPILIGGFgNWLVPLMLGAPDMAFPRMNNLSFWLLPPSLMLLFISsmaeVGVG----AGWT 110
Cdd:TIGR02843 96 HHYDQIFTAHGVIMIFFVAMPFVFGLM-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVS----LGVGefaqTGWL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 111 VYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKVPLFVWSVLITAVLLLLSLPVLAGAIT 190
Cdd:TIGR02843 171 AYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 191 MLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISASVGKREpFGSLGMIYAMAGIGGMGFVV 270
Cdd:TIGR02843 251 LLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRL-FGYTSMVWATIAITVLSFIV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 271 WAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWCIGFVFLFTLGGITGVVLSNSSLDIVL 350
Cdd:TIGR02843 330 WLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVL 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223403388 351 HDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGVNMTFFPQHFLGLNGM 419
Cdd:TIGR02843 410 HNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGM 478
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
35-419 |
1.60e-92 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 292.22 E-value: 1.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 35 HLYNVIVTAHAFVMIFFMVMPILIGgFGNWLVPLMLGAPDMAFPRMNNLSFWLLPPSLMLLFISsmaeVGVG----AGWT 110
Cdd:PRK15017 97 HHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVS----LGVGefaqTGWL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 111 VYPPLAASMGHSGSSVDFAIFSLHLAGASSIMGAINFISTILNMRSFGMTMEKVPLFVWSVLITAVLLLLSLPVLAGAIT 190
Cdd:PRK15017 172 AYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 191 MLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIiSASVGKREPFGSLGMIYAMAGIGGMGFVV 270
Cdd:PRK15017 252 LLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEI-AATFSRKRLFGYTSLVWATVCITVLSFIV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 271 WAHHMFSVGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLHGSYFKLESPLMWCIGFVFLFTLGGITGVVLSNSSLDIVL 350
Cdd:PRK15017 331 WLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVL 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223403388 351 HDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGVIINESKSKLQFIIMFLGVNMTFFPQHFLGLNGM 419
Cdd:PRK15017 411 HNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGM 479
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
30-419 |
1.69e-11 |
|
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: 65.77 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 30 LLGDDHLYNVIVTAHAFVMIFfmVMPIL-IGGFGNWLVPLMLGAPDMAfPRMNNLSFWllppslMLLFISSMAEVGVGAG 108
Cdd:cd01660 37 LPSSGILYYQGLTLHGVLLAI--VFTTFfIMGFFYAIVARALLRSLFN-RRLAWAGFW------LMVIGTVMAAVPILLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 109 -----WTVYPPLAASmghsgssVDFAIFSLHLAGASSIMGAINFIsTILNMRSfGMTMEKVPLFVWSVLITAVLLLLSLP 183
Cdd:cd01660 108 qasvlYTFYPPLQAH-------PLFYIGAALVVVGSWISGFAMFV-TLWRWKK-ANPGKKVPLATFMVVTTMILWLVASL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 184 VLAGAITMLLTDRNFNTsffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHIISASVGKR---EPFGSLGMIYAM 260
Cdd:cd01660 179 GVALEVLFQLLPWSLGL-----VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKlfsDPLARLAFILFL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 261 AGIGGMGFvvwaHHMFS-VGMDVDTRAYFTAATMVIAIPTGIKVFSWMATLH------------GSYFKLE--SPLMWCI 325
Cdd:cd01660 254 LFSTPVGF----HHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLEiagrlrggkglfGWIRALPwgDPMFLAL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403388 326 GFVFL-FTLGGITGVVLSNSSLDIVLHDTYYVVAHFHyvLSMGAVFAILA-GITYWF-PLFFG-VIINESKSKLQFIIMF 401
Cdd:cd01660 330 FLAMLmFIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGrELAAKRLALAQPWLWF 407
|
410
....*....|....*...
gi 223403388 402 LGVNMTFFPQHFLGLNGM 419
Cdd:cd01660 408 VGMTIMSTAMHVAGLLGA 425
|
|
| |
