|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-404 |
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: 724.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:cd01663 14 GLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:cd01663 92 SFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:cd01663 172 MPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIIST 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:cd01663 252 FSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLW 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:cd01663 332 ALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIG 411
|
....*
gi 780959588 400 VNITF 404
Cdd:cd01663 412 VNLTF 416
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 664.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00153 21 GAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00153 99 SFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00153 179 MPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00153 259 ESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLW 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00153 339 ALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIG 418
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00153 419 VNLTF 423
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-404 |
0e+00 |
|
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: 514.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNYLLlgNHQLYNVLVTAHGFIMVFFMVMPVLiGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:TIGR02891 17 AFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:TIGR02891 94 SYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:TIGR02891 174 MPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FSRKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLFA 320
Cdd:TIGR02891 254 FARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 321 VGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIGV 400
Cdd:TIGR02891 334 LGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGF 413
|
....
gi 780959588 401 NITF 404
Cdd:TIGR02891 414 NLTF 417
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
3-404 |
2.54e-179 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 510.05 E-value: 2.54e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 3 FSGILGGCMSILIRMELSQPGNYLLLGNHqlYNVLVTAHGFIMVFFMVMPvLIGGFGNWLVPIMIGSPDMAFPRLNNISF 82
Cdd:COG0843 28 VFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 83 WLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYRMP 162
Cdd:COG0843 105 WLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 163 LFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIISTFS 242
Cdd:COG0843 185 LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 243 RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLFAVG 322
Cdd:COG0843 265 RKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 323 FVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIGVNI 402
Cdd:COG0843 345 FIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNL 424
|
..
gi 780959588 403 TF 404
Cdd:COG0843 425 TF 426
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-404 |
1.29e-121 |
|
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: 359.19 E-value: 1.29e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNYLLlgNHQLYNVLVTAHGFIMVFFMVMPVlIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:pfam00115 10 ALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLveiGAGTGWTVYPPLssiqshsgGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMyR 160
Cdd:pfam00115 87 SFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-R 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTtffdssGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:pfam00115 155 MPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FSRKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICF-KVPMLF 319
Cdd:pfam00115 229 FAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:pfam00115 309 FLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIG 388
|
....*
gi 780959588 400 VNITF 404
Cdd:pfam00115 389 FNLTF 393
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-404 |
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: 724.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:cd01663 14 GLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:cd01663 92 SFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:cd01663 172 MPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIIST 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:cd01663 252 FSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLW 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:cd01663 332 ALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIG 411
|
....*
gi 780959588 400 VNITF 404
Cdd:cd01663 412 VNLTF 416
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 664.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00153 21 GAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00153 99 SFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00153 179 MPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00153 259 ESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLW 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00153 339 ALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIG 418
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00153 419 VNLTF 423
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 625.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00167 23 GAWAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00167 101 SFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00167 181 TPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00167 261 YSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLW 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00167 341 ALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIG 420
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00167 421 VNLTF 425
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 612.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00116 23 GAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00116 101 SFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00116 181 TPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00116 261 YAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLW 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00116 341 ALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTG 420
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00116 421 VNLTF 425
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 608.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGnyLLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00223 20 GMWSGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00223 98 SFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLER 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00223 178 LPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSH 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FSRKF-VFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00223 258 YSSKKeVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLW 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00223 338 ALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLG 417
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00223 418 VNLTF 422
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 589.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00142 21 GAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00142 99 SFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFER 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00142 179 VPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINH 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00142 259 YSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLW 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00142 339 ALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIG 418
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00142 419 VNLTF 423
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 574.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00184 25 GAFAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00184 103 SFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00184 183 MPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00184 263 FAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLW 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00184 343 AIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIG 422
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00184 423 VNLTF 427
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 567.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00182 25 GAGAGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00182 103 SFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00182 183 LPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00182 263 FVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLW 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00182 343 AMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIG 422
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00182 423 VNLTF 427
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 536.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00037 23 GAWAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00037 101 SFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00037 181 LPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAH 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FSRKF-VFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00037 261 YSGKQePFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLW 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00037 341 ALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIG 420
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00037 421 VNLTF 425
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 536.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00183 23 GAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00183 101 SFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00183 181 TPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00183 261 YSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLW 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00183 341 ALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVG 420
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00183 421 VNLTF 425
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 534.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00103 23 GAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00103 101 SFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00103 181 TPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00103 261 YSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLW 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00103 341 ALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVG 420
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00103 421 VNMTF 425
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 534.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00077 23 GAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00077 101 SFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00077 181 TPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00077 261 YSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLW 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00077 341 ALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIG 420
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00077 421 VNLTF 425
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 530.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNYLllGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00007 20 GVWGGLLGTSMSLLIRIELGQPGAFL--GSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00007 98 SFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLER 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00007 178 IPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTH 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FSRKF-VFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00007 258 YAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLW 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00007 338 ALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLG 417
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00007 418 VNLTF 422
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 522.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGnyLLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00079 24 GLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSiQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00079 102 SFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00079 181 MSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLY 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLF 319
Cdd:MTH00079 261 LTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLW 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:MTH00079 341 VLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVG 420
|
....*
gi 780959588 400 VNITF 404
Cdd:MTH00079 421 VNLTF 425
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-404 |
0e+00 |
|
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: 514.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNYLLlgNHQLYNVLVTAHGFIMVFFMVMPVLiGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:TIGR02891 17 AFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:TIGR02891 94 SYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:TIGR02891 174 MPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FSRKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLFA 320
Cdd:TIGR02891 254 FARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 321 VGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIGV 400
Cdd:TIGR02891 334 LGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGF 413
|
....
gi 780959588 401 NITF 404
Cdd:TIGR02891 414 NLTF 417
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-404 |
1.32e-179 |
|
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: 507.84 E-value: 1.32e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNYLLlgNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPiMIGSPDMAFPRLNNI 80
Cdd:cd00919 12 AFVALLLGGLLALLIRLELATPGSLFL--DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:cd00919 89 SFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:cd00919 169 MPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FSRKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLFA 320
Cdd:cd00919 249 FSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 321 VGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIGV 400
Cdd:cd00919 329 LGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGF 408
|
....
gi 780959588 401 NITF 404
Cdd:cd00919 409 NLTF 412
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
3-404 |
2.54e-179 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 510.05 E-value: 2.54e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 3 FSGILGGCMSILIRMELSQPGNYLLLGNHqlYNVLVTAHGFIMVFFMVMPvLIGGFGNWLVPIMIGSPDMAFPRLNNISF 82
Cdd:COG0843 28 VFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 83 WLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYRMP 162
Cdd:COG0843 105 WLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 163 LFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIISTFS 242
Cdd:COG0843 185 LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 243 RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLFAVG 322
Cdd:COG0843 265 RKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 323 FVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIGVNI 402
Cdd:COG0843 345 FIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNL 424
|
..
gi 780959588 403 TF 404
Cdd:COG0843 425 TF 426
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
4.03e-179 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 509.55 E-value: 4.03e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNylLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00026 24 GALSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYR 160
Cdd:MTH00026 102 SFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00026 182 IPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FS-RKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEG--SICFKVPM 317
Cdd:MTH00026 262 FSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 318 LFAVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTF 397
Cdd:MTH00026 342 AWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMF 421
|
....*..
gi 780959588 398 IGVNITF 404
Cdd:MTH00026 422 IGVNITF 428
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
6-404 |
1.24e-160 |
|
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: 461.28 E-value: 1.24e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 6 ILGGCMSILIRMELSQPGNYLLLGNHqlYNVLVTAHGFIMVFFMVMPVLIGgFGNWLVPIMIGSPDMAFPRLNNISFWLL 85
Cdd:cd01662 23 LRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 86 PPSLCLLLASSLVEIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYRMPLFV 165
Cdd:cd01662 100 LFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 166 WAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIISTFSRKF 245
Cdd:cd01662 180 WTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 246 VFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLFAVGFVF 325
Cdd:cd01662 260 LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLV 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780959588 326 LFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIGVNITF 404
Cdd:cd01662 340 TFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTF 418
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-404 |
1.44e-129 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 382.49 E-value: 1.44e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPgnYLLLGNHQLYNVLVTAHGFIMVFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:MTH00048 24 GVWSGFVGLSLSLLIRLNFLDP--YYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLveIGAGTGWTVYPPLSSIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSmYR 160
Cdd:MTH00048 102 SAWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:MTH00048 179 TSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FSRKF-VFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPML- 318
Cdd:MTH00048 259 LSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVw 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 319 FAVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFI 398
Cdd:MTH00048 339 WVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMI 418
|
....*.
gi 780959588 399 GVNITF 404
Cdd:MTH00048 419 GFNLCF 424
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-404 |
1.29e-121 |
|
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: 359.19 E-value: 1.29e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 1 GAFSGILGGCMSILIRMELSQPGNYLLlgNHQLYNVLVTAHGFIMVFFMVMPVlIGGFGNWLVPIMIGSPDMAFPRLNNI 80
Cdd:pfam00115 10 ALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 81 SFWLLPPSLCLLLASSLveiGAGTGWTVYPPLssiqshsgGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMyR 160
Cdd:pfam00115 87 SFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-R 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 161 MPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTtffdssGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIST 240
Cdd:pfam00115 155 MPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 241 FSRKFVFGYIGMVYAMVSIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICF-KVPMLF 319
Cdd:pfam00115 229 FAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 320 AVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIG 399
Cdd:pfam00115 309 FLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIG 388
|
....*
gi 780959588 400 VNITF 404
Cdd:pfam00115 389 FNLTF 393
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
34-404 |
6.13e-118 |
|
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: 357.06 E-value: 6.13e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 34 YNVLVTAHGFIMVFFMVMPVLIGGFgNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLS 113
Cdd:TIGR02843 98 YDQIFTAHGVIMIFFVAMPFVFGLM-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 114 SIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYRMPLFVWAIFITAILLLLAVPVLAGAITMLLTDR 193
Cdd:TIGR02843 177 ELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 194 NFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIISTFSRKFVFGYIGMVYAMVSIGILGFIVWAHHMYT 273
Cdd:TIGR02843 257 YLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATIAITVLSFIVWLHHFFT 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 274 VGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLFAVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVV 353
Cdd:TIGR02843 337 MGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLI 416
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 780959588 354 AHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIGVNITF 404
Cdd:TIGR02843 417 AHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAF 467
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
34-404 |
1.92e-102 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 317.65 E-value: 1.92e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 34 YNVLVTAHGFIMVFFMVMPVLIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLASSLVEIGAGTGWTVYPPLS 113
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 114 SIQSHSGGSVDLAIFSLHLAGISSILGAINFISTILNMRNPGQSMYRMPLFVWAIFITAILLLLAVPVLAGAITMLLTDR 193
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 194 NFNTTFFDSSGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIISTFSRKFVFGYIGMVYAMVSIGILGFIVWAHHMYT 273
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFT 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 274 VGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSICFKVPMLFAVGFVFLFTIGGLTGIVLANSGLDISLHDTYYVV 353
Cdd:PRK15017 338 MGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLI 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 780959588 354 AHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEILGQIHFWGTFIGVNITF 404
Cdd:PRK15017 418 AHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAF 468
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
5-399 |
6.60e-13 |
|
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: 70.01 E-value: 6.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 5 GILGGCMSILIRMelsqpGNYLLLGNHQLYNVLVTAHGFIMVFfmVMPVL-IGGFGNWLVPIMIGSPDMAfPRLNNISFW 83
Cdd:cd01660 20 GGLFGLLQVLVRT-----GVFPLPSSGILYYQGLTLHGVLLAI--VFTTFfIMGFFYAIVARALLRSLFN-RRLAWAGFW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 84 LLPPSLCLLLasslVEIGAGTG---WTVYPPLssiQSHSGGSVDLAIFSLHlagiSSILGAINFI-STILNMRNPGQsmy 159
Cdd:cd01660 92 LMVIGTVMAA----VPILLGQAsvlYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVtLWRWKKANPGK--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 160 RMPLFVWAIFITAILLLLAVPVLAGAITMLLTDRNFNTTffdssGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIIS 239
Cdd:cd01660 158 KVPLATFMVVTTMILWLVASLGVALEVLFQLLPWSLGLV-----DTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 240 TFSRKFVFGYIGMVYAMVSIGILGFIVWAHHMYT-VGLDVDTRAYFTAATMIIAVPTGIKIFSWIATM------------ 306
Cdd:cd01660 233 KIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeiagrlrggkgl 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959588 307 --WEGSICFKVPMLFAVGFVFL-FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQ 383
Cdd:cd01660 313 fgWIRALPWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRE 392
|
410
....*....|....*..
gi 780959588 384 YPEI-LGQIHFWGTFIG 399
Cdd:cd01660 393 LAAKrLALAQPWLWFVG 409
|
|
| |
