|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-418 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 838.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00153 91 AFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00153 171 SKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00153 251 MISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00153 331 NYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKI 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLSSSL 400
Cdd:MTH00153 411 QFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSI 490
|
410
....*....|....*...
gi 226441820 401 EWYQSLPPAEHSYSELPI 418
Cdd:MTH00153 491 EWLQNLPPAEHSYSELPL 508
|
|
| 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: 709.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:cd01663 84 AFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:cd01663 164 APGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:cd01663 244 IISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSI 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:cd01663 324 KFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKI 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIF-PFNLSSS 399
Cdd:cd01663 404 HFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGSTS 483
|
...
gi 226441820 400 LEW 402
Cdd:cd01663 484 LEW 486
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-418 |
2.30e-166 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 477.70 E-value: 2.30e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:COG0843 95 AFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:COG0843 175 APGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:COG0843 255 IVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:COG0843 334 RFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRK-SIFPFNlS 397
Cdd:COG0843 414 HFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKaGGNPWG-A 492
|
410 420
....*....|....*....|.
gi 226441820 398 SSLEWYQSLPPAEHSYSELPI 418
Cdd:COG0843 493 RTLEWATPSPPPLYNFASIPV 513
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-413 |
1.47e-160 |
|
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: 461.69 E-value: 1.47e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:TIGR02891 86 AFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:TIGR02891 166 APGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:TIGR02891 246 IISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSI 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:TIGR02891 325 RFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRW 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSifPFNL-- 396
Cdd:TIGR02891 405 HFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA--GANPwg 482
|
410
....*....|....*..
gi 226441820 397 SSSLEWYQSLPPAEHSY 413
Cdd:TIGR02891 483 ATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-368 |
1.03e-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: 324.53 E-value: 1.03e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMaenGAGTGWTVYPPLSAgiahagssVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:pfam00115 79 AFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLdQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:pfam00115 148 APGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:pfam00115 221 IIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 S-YSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLK 319
Cdd:pfam00115 300 RfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 226441820 320 IQFSIMFLGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTSWNILSSLGSTM 368
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-418 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 838.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00153 91 AFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00153 171 SKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00153 251 MISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQI 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00153 331 NYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKI 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLSSSL 400
Cdd:MTH00153 411 QFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSI 490
|
410
....*....|....*...
gi 226441820 401 EWYQSLPPAEHSYSELPI 418
Cdd:MTH00153 491 EWLQNLPPAEHSYSELPL 508
|
|
| 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: 709.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:cd01663 84 AFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:cd01663 164 APGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:cd01663 244 IISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSI 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:cd01663 324 KFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKI 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIF-PFNLSSS 399
Cdd:cd01663 404 HFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGSTS 483
|
...
gi 226441820 400 LEW 402
Cdd:cd01663 484 LEW 486
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-418 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 687.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00167 93 AFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00167 173 PPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00167 253 MISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00167 333 KWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKI 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLSSSL 400
Cdd:MTH00167 413 HFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNV 492
|
410
....*....|....*...
gi 226441820 401 EWYQSLPPAEHSYSELPI 418
Cdd:MTH00167 493 EWLHGCPPPHHTWEEPPF 510
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-417 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 685.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00223 90 AFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00223 170 SPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00223 250 MISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKI 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00223 330 KYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKA 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLSSSL 400
Cdd:MTH00223 410 HFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSL 489
|
410
....*....|....*..
gi 226441820 401 EWYQSLPPAEHSYSELP 417
Cdd:MTH00223 490 EWDNLLPADFHNNSETG 506
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-418 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 678.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00142 91 AFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00142 171 AGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00142 251 MISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00142 331 KYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKA 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLSSSL 400
Cdd:MTH00142 411 HFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSL 490
|
410
....*....|....*...
gi 226441820 401 EWYQSLPPAEHSYSELPI 418
Cdd:MTH00142 491 EWSHRLPPDFHTYDELPI 508
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-417 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 677.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00116 93 AFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00116 173 PPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00116 253 IISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00116 333 KWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKA 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLSSSL 400
Cdd:MTH00116 413 QFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNI 492
|
410
....*....|....*..
gi 226441820 401 EWYQSLPPAEHSYSELP 417
Cdd:MTH00116 493 EWIHGCPPPYHTFEEPA 509
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-418 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 611.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00037 93 AFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00037 173 TPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00037 253 MISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00037 333 RWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKV 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLSSSL 400
Cdd:MTH00037 413 HFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSL 492
|
410
....*....|....*....
gi 226441820 401 EW-YQSLPPAEHSYSELPI 418
Cdd:MTH00037 493 EWqYSSFPPSHHTFDETPS 511
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-415 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 611.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00103 93 AFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00103 173 PPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00103 253 MISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00103 333 KWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKI 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLSSSL 400
Cdd:MTH00103 413 HFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNL 492
|
410
....*....|....*
gi 226441820 401 EWYQSLPPAEHSYSE 415
Cdd:MTH00103 493 EWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-415 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 604.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00183 93 AFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00183 173 PPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00183 253 MISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00183 333 KWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKI 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLSSSL 400
Cdd:MTH00183 413 HFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNV 492
|
410
....*....|....*
gi 226441820 401 EWYQSLPPAEHSYSE 415
Cdd:MTH00183 493 EWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-415 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 603.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00007 90 AFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00007 170 WKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00007 250 AISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPI 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00007 330 KYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKA 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLSSSL 400
Cdd:MTH00007 410 HFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSL 489
|
410
....*....|....*
gi 226441820 401 EWYQSLPPAEHSYSE 415
Cdd:MTH00007 490 EWQDTLPLDFHNLPE 504
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-415 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 597.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00077 93 AFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00077 173 PPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00077 253 MISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00077 333 KWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKI 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLSSSL 400
Cdd:MTH00077 413 HFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNI 492
|
410
....*....|....*
gi 226441820 401 EWYQSLPPAEHSYSE 415
Cdd:MTH00077 493 EWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-417 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 550.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00182 95 AFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00182 175 APGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00182 255 MISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00182 335 RLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLS--- 397
Cdd:MTH00182 415 HFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEGTges 494
|
410 420
....*....|....*....|.
gi 226441820 398 -SSLEWYQSLPPAEHSYSELP 417
Cdd:MTH00182 495 wASLEWVHSSPPLFHTYNELP 515
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-415 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 548.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAgIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00079 94 SFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00079 173 SSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00079 253 IISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKM 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00079 333 KFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSA 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLSSSL 400
Cdd:MTH00079 413 VFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSP 492
|
410
....*....|....*
gi 226441820 401 EWYQSLPPAEHSYSE 415
Cdd:MTH00079 493 EYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-417 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 542.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00184 95 AFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00184 175 APGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00184 255 IISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:MTH00184 335 RLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLS--- 397
Cdd:MTH00184 415 HFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVGWVEDSghy 494
|
410 420
....*....|....*....|
gi 226441820 398 SSLEWYQSLPPAEHSYSELP 417
Cdd:MTH00184 495 PSLEWAQTSPPAHHTYNELP 514
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-384 |
2.49e-174 |
|
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: 495.13 E-value: 2.49e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:cd00919 81 AFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:cd00919 161 APGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:cd00919 241 AISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRI 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:cd00919 320 RFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKI 399
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESM 384
Cdd:cd00919 400 HFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-417 |
3.98e-167 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 479.51 E-value: 3.98e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00026 94 AFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00026 174 TPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT-- 238
Cdd:MTH00026 254 IISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgr 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 239 HISYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWL 318
Cdd:MTH00026 334 NLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYG 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 319 KIQFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESM---------ISQRK 389
Cdd:MTH00026 414 LIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYyreepfdinIMAKG 493
|
410 420 430
....*....|....*....|....*....|..
gi 226441820 390 SIFPFNLS----SSLEWYQSLPPAEHSYSELP 417
Cdd:MTH00026 494 PLIPFSCQpahfDTLEWSLTSPPEHHTYNELP 525
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-418 |
2.30e-166 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 477.70 E-value: 2.30e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:COG0843 95 AFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:COG0843 175 APGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFG 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:COG0843 255 IVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:COG0843 334 RFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRK-SIFPFNlS 397
Cdd:COG0843 414 HFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKaGGNPWG-A 492
|
410 420
....*....|....*....|.
gi 226441820 398 SSLEWYQSLPPAEHSYSELPI 418
Cdd:COG0843 493 RTLEWATPSPPPLYNFASIPV 513
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-413 |
1.47e-160 |
|
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: 461.69 E-value: 1.47e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:TIGR02891 86 AFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:TIGR02891 166 APGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:TIGR02891 246 IISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSI 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:TIGR02891 325 RFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRW 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSifPFNL-- 396
Cdd:TIGR02891 405 HFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA--GANPwg 482
|
410
....*....|....*..
gi 226441820 397 SSSLEWYQSLPPAEHSY 413
Cdd:TIGR02891 483 ATTLEWTTSSPPPAHNF 499
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-413 |
4.33e-142 |
|
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: 414.67 E-value: 4.33e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:cd01662 87 AFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:cd01662 167 APGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:cd01662 247 IFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRI 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:cd01662 326 RFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKW 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNILSSLGSTMSLIGILMLIFIMWESmISQRKSIFPFNL-- 396
Cdd:cd01662 406 SFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVS-IRKGKRDATGDPwg 484
|
410
....*....|....*..
gi 226441820 397 SSSLEWYQSLPPAEHSY 413
Cdd:cd01662 485 ARTLEWATSSPPPAYNF 501
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-412 |
4.77e-140 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 409.84 E-value: 4.77e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAenGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:MTH00048 94 NLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAF 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLdQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:MTH00048 172 MTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:MTH00048 251 IISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYS-PALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLK 319
Cdd:MTH00048 331 RKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 320 IQFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNILSSLGSTMSLIGILMLIFIMWESMISQRKSIFPFNLSSS 399
Cdd:MTH00048 411 CHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLGLWGSSSC 490
|
410
....*....|...
gi 226441820 400 LEWYQSLPPAEHS 412
Cdd:MTH00048 491 VVNVLMSPVPYHN 503
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-368 |
1.03e-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: 324.53 E-value: 1.03e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMaenGAGTGWTVYPPLSAgiahagssVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:pfam00115 79 AFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLdQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:pfam00115 148 APGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:pfam00115 221 IIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 S-YSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLK 319
Cdd:pfam00115 300 RfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 226441820 320 IQFSIMFLGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTSWNILSSLGSTM 368
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
1-420 |
3.54e-105 |
|
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: 324.70 E-value: 3.54e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:TIGR02843 136 AFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMR 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:TIGR02843 216 APGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFG 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:TIGR02843 296 IFSEVVATFSRKR-LFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRI 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:TIGR02843 375 RFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKR 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTSWNILSSLGSTMSLIGILMLIFIMWESmISQRKSIF-----PF 394
Cdd:TIGR02843 455 SFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVS-IRDRDQNRdttgdPW 533
|
410 420
....*....|....*....|....*.
gi 226441820 395 NlSSSLEWYQSLPPAEHSYSELPIKH 420
Cdd:TIGR02843 534 G-GRTLEWSTSSPPPFYNFAVIPKVQ 558
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-420 |
1.57e-89 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 284.52 E-value: 1.57e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 1 AFPRMNNMSFWLLPPSLTLLLASSMAENGAGTGWTVYPPLSAGIAHAGSSVDLAIFSLHLAGISSILGAANFITTMINMR 80
Cdd:PRK15017 137 AFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 81 SPGMSLDQTPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 160
Cdd:PRK15017 217 APGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFG 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 161 MISHIISQESgKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTHI 240
Cdd:PRK15017 297 VFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRI 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 241 SYSPALLWSLGFVFLFTIGGLTGIVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWFPLLTGVTMNSKWLKI 320
Cdd:PRK15017 376 VFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKR 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 321 QFSIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDA-YTSWNILSSLGSTMSLIGILMLIFIMWESMISQRK----SIFPFN 395
Cdd:PRK15017 456 AFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPqFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQnrdlTGDPWG 535
|
410 420
....*....|....*....|....*
gi 226441820 396 lSSSLEWYQSLPPAEHSYSELPIKH 420
Cdd:PRK15017 536 -GRTLEWATSSPPPFYNFAVVPHVH 559
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
135-384 |
1.67e-21 |
|
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: 96.20 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 135 DPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIyAMLAIGLLGFVVWAHHMFT-VGMDVDTRAYF 213
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 214 TSATMIIAVPTGIKIFSWLATL--------HGTHISYSPALLWS----LGFVF---LFTIGGLTGIVLANSSIDIILHDT 278
Cdd:cd01660 279 MVLTFMVALPSLLTAFTVFASLeiagrlrgGKGLFGWIRALPWGdpmfLALFLamlMFIPGGAGGIINASYQLNYVVHNT 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226441820 279 YYVVAHFHyvLSMGAVFAIMA-GFIHWF-PLLTGVTMNSKWL-KIQFSIMFLGVNLTFFPQHFLGLAGMPRR--YSDYPD 353
Cdd:cd01660 359 AWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGG 436
|
250 260 270
....*....|....*....|....*....|....*.
gi 226441820 354 AY-----TSWNILSSLGSTMSLIGILMLIFIMWESM 384
Cdd:cd01660 437 LPaagewAPYQQLMAIGGTILFVSGALFLYILFRTL 472
|
|
| |
