|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-402 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 794.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00153 13 IGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00153 93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00153 173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00153 253 SHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00153 333 SPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQF 412
|
..
gi 326417834 401 LV 402
Cdd:MTH00153 413 FI 414
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-402 |
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: 713.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:cd01663 6 IGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:cd01663 86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:cd01663 166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:cd01663 246 SHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:cd01663 326 ETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHF 405
|
..
gi 326417834 401 LV 402
Cdd:cd01663 406 WL 407
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-392 |
3.54e-154 |
|
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: 444.74 E-value: 3.54e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMiGGFGNWLVPLMLGAPDMAF 80
Cdd:TIGR02891 9 IGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:TIGR02891 88 PRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:TIGR02891 168 GMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGII 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQeSSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:TIGR02891 248 SEILPT-FARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRF 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLN 392
Cdd:TIGR02891 327 TTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-400 |
1.24e-153 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 444.57 E-value: 1.24e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMmIGGFGNWLVPLMLGAPDMAF 80
Cdd:COG0843 18 IGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:COG0843 97 PRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:COG0843 177 GMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQeSSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:COG0843 257 SEIIPT-FSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:COG0843 336 TTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHF 415
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-400 |
5.55e-107 |
|
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: 321.83 E-value: 5.55e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMmIGGFGNWLVPLMLGAPDMAF 80
Cdd:pfam00115 2 IGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMvnkGAGTGWTVYPPLSAniahegasVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:pfam00115 81 PRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTpERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:pfam00115 150 GMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGII 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQeSSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:pfam00115 223 YYILPK-FAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSS-LWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQ 399
Cdd:pfam00115 302 RTTPmLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLH 381
|
.
gi 326417834 400 F 400
Cdd:pfam00115 382 F 382
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-402 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 794.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00153 13 IGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00153 93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00153 173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00153 253 SHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00153 333 SPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQF 412
|
..
gi 326417834 401 LV 402
Cdd:MTH00153 413 FI 414
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-402 |
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: 713.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:cd01663 6 IGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:cd01663 86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:cd01663 166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:cd01663 246 SHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:cd01663 326 ETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHF 405
|
..
gi 326417834 401 LV 402
Cdd:cd01663 406 WL 407
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-402 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 672.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00167 15 IGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00167 95 PRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00167 175 GITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00167 255 SHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKW 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00167 335 ETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHF 414
|
..
gi 326417834 401 LV 402
Cdd:MTH00167 415 FV 416
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-402 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 670.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00223 12 IGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00223 92 PRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00223 172 GMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00223 252 SHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00223 332 EAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHF 411
|
..
gi 326417834 401 LV 402
Cdd:MTH00223 412 FL 413
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-402 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 664.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00116 15 IGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00116 95 PRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00116 175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00116 255 SHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKW 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00116 335 DPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQF 414
|
..
gi 326417834 401 LV 402
Cdd:MTH00116 415 GV 416
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-402 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 662.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00142 13 IGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00142 93 PRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00142 173 GMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00142 253 SHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00142 333 EPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHF 412
|
..
gi 326417834 401 LV 402
Cdd:MTH00142 413 YT 414
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-402 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 602.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00103 15 IGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00103 95 PRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00103 175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00103 255 SHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKW 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00103 335 SPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHF 414
|
..
gi 326417834 401 LV 402
Cdd:MTH00103 415 TI 416
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-402 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 599.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00007 12 IGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00007 92 PRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00007 172 GLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00007 252 SHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00007 332 ETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHF 411
|
..
gi 326417834 401 LV 402
Cdd:MTH00007 412 FL 413
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-402 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 596.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00183 15 IGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00183 95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00183 175 AISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00183 255 SHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKW 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00183 335 ETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHF 414
|
..
gi 326417834 401 LV 402
Cdd:MTH00183 415 GV 416
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-402 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 594.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00077 15 IGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00077 95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00077 175 SMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00077 255 SHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKW 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00077 335 DAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHF 414
|
..
gi 326417834 401 LV 402
Cdd:MTH00077 415 GV 416
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-402 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 590.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00037 15 IGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00037 95 PRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00037 175 GMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00037 255 SHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRW 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00037 335 ETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHF 414
|
..
gi 326417834 401 LV 402
Cdd:MTH00037 415 FL 416
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-402 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 558.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00079 16 IGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSaNIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00079 96 PRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00079 175 SISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGII 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00079 255 SQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKF 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00079 335 QPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVF 414
|
..
gi 326417834 401 LV 402
Cdd:MTH00079 415 FL 416
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-400 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 551.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00182 17 IGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00182 97 PRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00182 177 GVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00182 257 SQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00182 337 DTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHF 416
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-400 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 543.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00184 17 IGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00184 97 PRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00184 177 GITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00184 257 SQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:MTH00184 337 DTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHF 416
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-395 |
1.02e-173 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 495.69 E-value: 1.02e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00026 16 IGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00026 96 PRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00026 176 GMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGA--LI 318
Cdd:MTH00026 256 SQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNL 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326417834 319 SFSPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKY 395
Cdd:MTH00026 336 IFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIY 412
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-402 |
1.53e-167 |
|
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: 477.02 E-value: 1.53e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPlMLGAPDMAF 80
Cdd:cd00919 4 IGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:cd00919 83 PRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:cd00919 163 GMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQEsSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:cd00919 243 SEIIPTF-SGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:cd00919 322 DPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHF 401
|
..
gi 326417834 401 LV 402
Cdd:cd00919 402 WL 403
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-392 |
3.54e-154 |
|
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: 444.74 E-value: 3.54e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMiGGFGNWLVPLMLGAPDMAF 80
Cdd:TIGR02891 9 IGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:TIGR02891 88 PRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:TIGR02891 168 GMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGII 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQeSSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:TIGR02891 248 SEILPT-FARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRF 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLN 392
Cdd:TIGR02891 327 TTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-400 |
1.24e-153 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 444.57 E-value: 1.24e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMmIGGFGNWLVPLMLGAPDMAF 80
Cdd:COG0843 18 IGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:COG0843 97 PRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:COG0843 177 GMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQeSSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:COG0843 257 SEIIPT-FSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:COG0843 336 TTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHF 415
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-402 |
1.15e-144 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 421.01 E-value: 1.15e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGGFGNWLVPLMLGAPDMAF 80
Cdd:MTH00048 16 IGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSsmVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:MTH00048 96 PRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTpERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00048 174 NVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGII 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQESSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:MTH00048 253 SHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 S-PSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQ 399
Cdd:MTH00048 333 SdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCH 412
|
...
gi 326417834 400 FLV 402
Cdd:MTH00048 413 CII 415
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-400 |
5.29e-135 |
|
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: 395.80 E-value: 5.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGgFGNWLVPLMLGAPDMAF 80
Cdd:cd01662 10 IGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:cd01662 89 PRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:cd01662 169 GMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQeSSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:cd01662 249 SEIVPT-FSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:cd01662 328 ETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSF 407
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-400 |
5.55e-107 |
|
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: 321.83 E-value: 5.55e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMmIGGFGNWLVPLMLGAPDMAF 80
Cdd:pfam00115 2 IGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMvnkGAGTGWTVYPPLSAniahegasVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:pfam00115 81 PRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTpERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:pfam00115 150 GMT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGII 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQeSSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:pfam00115 223 YYILPK-FAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSS-LWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQ 399
Cdd:pfam00115 302 RTTPmLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLH 381
|
.
gi 326417834 400 F 400
Cdd:pfam00115 382 F 382
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
1-400 |
1.58e-106 |
|
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: 327.40 E-value: 1.58e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAEL-----GNPGSLIGDDqiYNVIVTAHAFIMIFFMVMPMMIGGFgNWLVPLMLGA 75
Cdd:TIGR02843 56 IGIMYIIVALVMLLRGFADAIMMRTQQalasgGSAGYLPPHH--YDQIFTAHGVIMIFFVAMPFVFGLM-NLVVPLQIGA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 76 PDMAFPRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMC 155
Cdd:TIGR02843 133 RDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTII 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 156 NMRTTGMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 235
Cdd:TIGR02843 213 KMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 236 GFGMISHIISQESSKKeSFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHG 315
Cdd:TIGR02843 293 AFGIFSEVVATFSRKR-LFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYK 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 316 ALISFSPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKY 395
Cdd:TIGR02843 372 GRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKL 451
|
....*
gi 326417834 396 LKTQF 400
Cdd:TIGR02843 452 GKRSF 456
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-400 |
3.59e-93 |
|
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: 292.91 E-value: 3.59e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIRAELGNPGSLIGDDQIYNVIVTAHAFIMIFFMVMPMMIGgFGNWLVPLMLGAPDMAF 80
Cdd:TIGR02882 53 IGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 81 PRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMCNMRTT 160
Cdd:TIGR02882 132 PVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 161 GMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:TIGR02882 212 GMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIY 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 241 SHIISQeSSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISF 320
Cdd:TIGR02882 292 SEIIST-FAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRF 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 321 SPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKYLKTQF 400
Cdd:TIGR02882 371 TTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCF 450
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-400 |
1.54e-91 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 289.14 E-value: 1.54e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 1 IGTLYFIFGAWSGMVGTSLSIMIR-----AELGNPGSLigDDQIYNVIVTAHAFIMIFFMVMPMMIGgFGNWLVPLMLGA 75
Cdd:PRK15017 57 LGIMYIIVAIVMLLRGFADAIMMRsqqalASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 76 PDMAFPRLNNMSFWLLPPSLTLLLMSSMVNKGAGTGWTVYPPLSANIAHEGASVDLAIFSLHMAGISSILGAINFISTMC 155
Cdd:PRK15017 134 RDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTIL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 156 NMRTTGMTPERMPLFAWAVAITAVLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 235
Cdd:PRK15017 214 KMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 236 GFGMISHIISQeSSKKESFGVLGMIYAMMAIGILGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHG 315
Cdd:PRK15017 294 VFGVFSEIAAT-FSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQ 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 316 ALISFSPSSLWSLGFIFLFTMGGLTGVVLANSSIDVILHDTYYVVAHFHYVLSMGAVFAILAGMVQWFPLFTGLTLNNKY 395
Cdd:PRK15017 373 GRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETW 452
|
....*
gi 326417834 396 LKTQF 400
Cdd:PRK15017 453 GKRAF 457
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
33-396 |
3.84e-06 |
|
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: 48.82 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 33 LIGDDQIYNVIVTAHAFIMIFFMVMpMMIGGFGNWLVPLMLGAPDMAfPRLNNMSFWLLPPSLTLLlMSSMVNKGAGTGW 112
Cdd:cd01660 37 LPSSGILYYQGLTLHGVLLAIVFTT-FFIMGFFYAIVARALLRSLFN-RRLAWAGFWLMVIGTVMA-AVPILLGQASVLY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 113 TVYPPLsanIAHEGASVDLAIFSLHmagiSSILGAINFISTMCNMRTTgmTPERMPLFAWAVAITAVLLLLSLPVLAGAI 192
Cdd:cd01660 114 TFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLWRWKKAN--PGKKVPLATFMVVTTMILWLVASLGVALEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 193 TMLLtdrnINTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESSKKESFGVLGMIyAMMAIGILGFV 272
Cdd:cd01660 185 LFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326417834 273 VWAHHMFT-VGMDVDTRAYFTSATMIIAVPTGIKIFSWLATYHGALISFSPSSLWS----------------LGFIFlFT 335
Cdd:cd01660 259 VGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLEIAGRLRGGKGLFGwiralpwgdpmflalfLAMLM-FI 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 326417834 336 MGGLTGVVLANSSIDVILHDTYYVVAHFHyvLSMGAVFAILA-GMVQWF-PLFTGLTLNNKYL 396
Cdd:cd01660 338 PGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRL 398
|
|
| |
