|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1005.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTI 480
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|
gi 1812385330 481 LFTMNSNSSIEWLQNFPPAEHSFSELPLMN 510
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLT 510
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
8-494 |
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: 872.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 8 TNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGA 87
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 88 PDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAINFITTTI 167
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 168 NMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPEVYILILP 247
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 248 GFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHG 327
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 328 TKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLSMNKKM 407
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 408 LKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTILF-TMNS 486
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEG 480
|
....*...
gi 1812385330 487 NSSIEWLQ 494
Cdd:cd01663 481 STSLEWTL 488
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
5-503 |
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: 553.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 5 LYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMiGGFGNWLLPLM 84
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 85 IGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAINFIT 164
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 165 TTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPEVYIL 244
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 245 ILPGFGMISHIINQESGKNeSFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLAT 324
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 325 LHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLSMN 404
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 405 KKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD--CYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTILF 482
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 1812385330 483 TMNSNSSIEWLQNFPPAEHSF 503
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-508 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 550.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPiMIGGFGNWL 80
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNeSFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DCYMTWNMISSLGSMISLISVLLFILIMWESMLT-K 477
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKgP 483
|
490 500 510
....*....|....*....|....*....|.
gi 1812385330 478 RTILFTMNSNsSIEWLQNFPPAEHSFSELPL 508
Cdd:COG0843 484 KAGGNPWGAR-TLEWATPSPPPLYNFASIPV 513
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
12-458 |
2.48e-130 |
|
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: 385.77 E-value: 2.48e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 12 DIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPiMIGGFGNWLLPLMIGAPDMA 91
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 92 FPRMNNMSFWLLPPSLTLLISSsilDVGVGTGWTVYPPLAGpiahsgpaVDLAIFSLHLAGASSILGAINFITTTINMKS 171
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLAS---FGGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 172 SDMTMdQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTsffdpvGGGDPILYQHLFWFFGHPEVYILILPGFGM 251
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 252 ISHIINQESGKnESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGTKFK 331
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 332 M-TVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLSMNKKMLKI 410
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1812385330 411 QFFIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDCYMTWNMISSLGSMI 458
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1005.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTI 480
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|
gi 1812385330 481 LFTMNSNSSIEWLQNFPPAEHSFSELPLMN 510
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLT 510
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
8-494 |
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: 872.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 8 TNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPLMIGA 87
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 88 PDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAINFITTTI 167
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 168 NMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPEVYILILP 247
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 248 GFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHG 327
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 328 TKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLSMNKKM 407
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 408 LKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTILF-TMNS 486
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEG 480
|
....*...
gi 1812385330 487 NSSIEWLQ 494
Cdd:cd01663 481 STSLEWTL 488
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 857.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00167 3 INRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:MTH00167 83 VPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00167 163 NFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:MTH00167 243 VYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:MTH00167 323 WLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTI 480
Cdd:MTH00167 403 LTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKL 482
|
490 500 510
....*....|....*....|....*....|
gi 1812385330 481 LFTMNSNSSIEWLQNFPPAEHSFSELPLMN 510
Cdd:MTH00167 483 LPVELTSTNVEWLHGCPPPHHTWEEPPFVQ 512
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 852.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00116 3 ITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:MTH00116 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00116 163 NFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:MTH00116 243 VYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:MTH00116 323 WLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTI 480
Cdd:MTH00116 403 YTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKV 482
|
490 500
....*....|....*....|....*....
gi 1812385330 481 LFTMNSNSSIEWLQNFPPAEHSFSELPLM 509
Cdd:MTH00116 483 LQPELTTTNIEWIHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
3-507 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 837.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 3 KWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLP 82
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAINF 162
Cdd:MTH00223 82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 163 ITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 243 ILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWL 322
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 323 ATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLS 402
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 403 MNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTILF 482
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
|
490 500
....*....|....*....|....*
gi 1812385330 483 TMNSNSSIEWLQNFPPAEHSFSELP 507
Cdd:MTH00223 482 SGHLSTSLEWDNLLPADFHNNSETG 506
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 831.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:MTH00142 81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00142 161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:MTH00142 241 VYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:MTH00142 321 WLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTI 480
Cdd:MTH00142 401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLV 480
|
490 500 510
....*....|....*....|....*....|
gi 1812385330 481 LFTMNSNSSIEWLQNFPPAEHSFSELPLMN 510
Cdd:MTH00142 481 MWSSHLSTSLEWSHRLPPDFHTYDELPILV 510
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 752.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00103 3 INRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:MTH00103 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00103 163 NFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:MTH00103 243 VYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:MTH00103 323 WLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTI 480
Cdd:MTH00103 403 YTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREV 482
|
490 500 510
....*....|....*....|....*....|
gi 1812385330 481 LFTMNSNSSIEWLQNFPPAEHSFSELPLMN 510
Cdd:MTH00103 483 LTVELTTTNLEWLHGCPPPYHTFEEPTYVK 512
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 751.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00037 3 LSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:MTH00037 83 IPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00037 163 NFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:MTH00037 243 VYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:MTH00037 323 WMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTI 480
Cdd:MTH00037 403 VSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREV 482
|
490 500
....*....|....*....|....*....
gi 1812385330 481 LFTMNSNSSIEW-LQNFPPAEHSFSELPL 508
Cdd:MTH00037 483 ISPEFSSSSLEWqYSSFPPSHHTFDETPS 511
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 751.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00183 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:MTH00183 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00183 163 NFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:MTH00183 243 VYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:MTH00183 323 WLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTI 480
Cdd:MTH00183 403 YTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREV 482
|
490 500 510
....*....|....*....|....*....|.
gi 1812385330 481 LFTMNSNSSIEWLQNFPPAEHSFSELPLMNL 511
Cdd:MTH00183 483 LSVELTSTNVEWLHGCPPPYHTFEEPAFVQV 513
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 747.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00077 3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:MTH00077 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00077 163 NFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:MTH00077 243 VYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:MTH00077 323 WLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTI 480
Cdd:MTH00077 403 YTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREV 482
|
490 500
....*....|....*....|....*
gi 1812385330 481 LFTMNSNSSIEWLQNFPPAEHSFSE 505
Cdd:MTH00077 483 LTTELTSTNIEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
3-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 739.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 3 KWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLP 82
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAINF 162
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 163 ITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 243 ILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWL 322
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 323 ATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLS 402
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 403 MNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTILF 482
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|...
gi 1812385330 483 TMNSNSSIEWLQNFPPAEHSFSE 505
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPE 504
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 704.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00182 5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:MTH00182 85 VPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00182 165 NFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:MTH00182 245 VYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:MTH00182 325 WLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTI 480
Cdd:MTH00182 405 YCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKF 484
|
490 500 510
....*....|....*....|....*....|....
gi 1812385330 481 L----FTMNSNSSIEWLQNFPPAEHSFSELPLMN 510
Cdd:MTH00182 485 IgwkeGTGESWASLEWVHSSPPLFHTYNELPFVY 518
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 690.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00184 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:MTH00184 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00184 165 NFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:MTH00184 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:MTH00184 325 WIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMltKRTI 480
Cdd:MTH00184 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAY--VREI 482
|
490 500 510
....*....|....*....|....*....|....
gi 1812385330 481 LFT-----MNSNSSIEWLQNFPPAEHSFSELPLM 509
Cdd:MTH00184 483 KFVgwvedSGHYPSLEWAQTSPPAHHTYNELPYV 516
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 686.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00079 4 LSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGpIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:MTH00079 84 LPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00079 163 NFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:MTH00079 243 VYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:MTH00079 323 WLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTI 480
Cdd:MTH00079 403 IVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLV 482
|
490 500
....*....|....*....|....*
gi 1812385330 481 LFTMNSNSSIEWLQNFPPAEHSFSE 505
Cdd:MTH00079 483 LHDNYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
3-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 604.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 3 KWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLP 82
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAINF 162
Cdd:MTH00026 86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 163 ITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 243 ILILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWL 322
Cdd:MTH00026 246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 323 ATLHGT--KFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:MTH00026 326 ATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTI 480
Cdd:MTH00026 406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREEPF 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1812385330 481 LFTMNSN-------------SSIEWLQNFPPAEHSFSELPLM 509
Cdd:MTH00026 486 DINIMAKgplipfscqpahfDTLEWSLTSPPEHHTYNELPYI 527
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
10-474 |
0e+00 |
|
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: 592.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 10 HKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWLlPLMIGAPD 89
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLL-PPLIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 90 MAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAINFITTTINM 169
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 170 KSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPEVYILILPGF 249
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 250 GMISHIINQESGKnESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGTK 329
Cdd:cd00919 240 GAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 330 FKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLSMNKKMLK 409
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812385330 410 IQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESM 474
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
5-503 |
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: 553.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 5 LYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMiGGFGNWLLPLM 84
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 85 IGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAINFIT 164
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 165 TTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPEVYIL 244
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 245 ILPGFGMISHIINQESGKNeSFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLAT 324
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 325 LHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLSMN 404
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 405 KKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD--CYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTILF 482
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 1812385330 483 TMNSNSSIEWLQNFPPAEHSF 503
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-508 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 550.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 1 MTKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPiMIGGFGNWL 80
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 81 LPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAI 160
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 161 NFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPE 240
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 241 VYILILPGFGMISHIINQESGKNeSFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFS 320
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 321 WLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 400
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 401 LSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DCYMTWNMISSLGSMISLISVLLFILIMWESMLT-K 477
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKgP 483
|
490 500 510
....*....|....*....|....*....|.
gi 1812385330 478 RTILFTMNSNsSIEWLQNFPPAEHSFSELPL 508
Cdd:COG0843 484 KAGGNPWGAR-TLEWATPSPPPLYNFASIPV 513
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
4-502 |
4.48e-180 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 515.38 E-value: 4.48e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 4 WLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGGFGNWLLPL 83
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 84 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILdvGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAINFI 163
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 164 TTtINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPEVYI 243
Cdd:MTH00048 165 CT-IYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 244 LILPGFGMISHIINQESGKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLA 323
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 324 TLHGTKFKMTVE-LCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLS 402
Cdd:MTH00048 324 MLLNSRVRKSDPvVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 403 MNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDCYMTWNMISSLGSMISLISVLLFILIMWESMLTKRTILF 482
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLG 483
|
490 500
....*....|....*....|
gi 1812385330 483 TMNSNSSIEWLQNFPPAEHS 502
Cdd:MTH00048 484 LWGSSSCVVNVLMSPVPYHN 503
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
4-503 |
2.67e-162 |
|
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: 469.75 E-value: 2.67e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 4 WLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGgFGNWLLPL 83
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 84 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAINFI 163
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 164 TTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPEVYI 243
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 244 LILPGFGMISHIINQESGKnESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLA 323
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 324 TLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLSM 403
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 404 NKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DCYMTWNMISSLGSMISLISVLLFILIMWESMLtKRTIL 481
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIR-KGKRD 477
|
490 500
....*....|....*....|....
gi 1812385330 482 FTMNS--NSSIEWLQNFPPAEHSF 503
Cdd:cd01662 478 ATGDPwgARTLEWATSSPPPAYNF 501
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
12-458 |
2.48e-130 |
|
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: 385.77 E-value: 2.48e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 12 DIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPiMIGGFGNWLLPLMIGAPDMA 91
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 92 FPRMNNMSFWLLPPSLTLLISSsilDVGVGTGWTVYPPLAGpiahsgpaVDLAIFSLHLAGASSILGAINFITTTINMKS 171
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLAS---FGGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 172 SDMTMdQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTsffdpvGGGDPILYQHLFWFFGHPEVYILILPGFGM 251
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 252 ISHIINQESGKnESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGTKFK 331
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 332 M-TVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLSMNKKMLKI 410
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1812385330 411 QFFIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDCYMTWNMISSLGSMI 458
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
3-510 |
1.34e-110 |
|
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131928 Cd Length: 643 Bit Score: 342.22 E-value: 1.34e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 3 KWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRMELSSPGHLINDDQMYNVIVTSHAFIMIFFMVMPIMIGgFGNWLLP 82
Cdd:TIGR02882 43 EWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSILDVGVGTGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGASSILGAINF 162
Cdd:TIGR02882 122 LQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINF 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 163 ITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFWFFGHPEVY 242
Cdd:TIGR02882 202 FVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVY 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 243 ILILPGFGMISHIINQESGKNeSFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWL 322
Cdd:TIGR02882 282 IVILPAFGIYSEIISTFAQKR-LFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 323 ATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLS 402
Cdd:TIGR02882 361 LTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYK 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 403 MNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDCYMTWNMISSLGSMISLISVLLFIL-IMWESMLTKRT 479
Cdd:TIGR02882 441 LNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKSPRE 520
|
490 500 510
....*....|....*....|....*....|.
gi 1812385330 480 ILFTMNSNSSIEWLQNFPPAEHSFSELPLMN 510
Cdd:TIGR02882 521 ATGDPWNGRTLEWATASPPPKYNFAVTPDVN 551
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
2-507 |
1.01e-98 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 311.87 E-value: 1.01e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 2 TKWLYSTNHKDIGTLYFIFGAWAGLTGTALSMLIRME--LSSPGHL-INDDQMYNVIVTSHAFIMIFFMVMPIMIGgFGN 78
Cdd:PRK15017 46 KEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAgFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 79 WLLPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIsssiLDVGVG----TGWTVYPPLAGPIAHSGPAVDLAIFSLHLAGAS 154
Cdd:PRK15017 125 LVVPLQIGARDVAFPFLNNLSFWFTVVGVILVN----VSLGVGefaqTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 155 SILGAINFITTTINMKSSDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPVGGGDPILYQHLFW 234
Cdd:PRK15017 201 TTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 235 FFGHPEVYILILPGFGMISHIINQESgKNESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPT 314
Cdd:PRK15017 281 AWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 315 GIKVFSWLATLHGTKFKMTVELCWAMGFIFLFTMGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQW 394
Cdd:PRK15017 360 GVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYW 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 395 YPLITGLSMNKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-CYMTWNMISSLGSMISLISVLLFILIMWES 473
Cdd:PRK15017 440 WPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVS 519
|
490 500 510
....*....|....*....|....*....|....*..
gi 1812385330 474 MLTK---RTILFTMNSNSSIEWLQNFPPAEHSFSELP 507
Cdd:PRK15017 520 IRDRdqnRDLTGDPWGGRTLEWATSSPPPFYNFAVVP 556
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
13-475 |
8.43e-20 |
|
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: 91.96 E-value: 8.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 13 IGTLYFIFGAWAGLtgtaLSMLIRmelSSPGHLINDDQMYNVIVTSHAFIM-IFFMVMPIMigGFGNWLLPLMIGAPDMA 91
Cdd:cd01660 12 VAFLALLLGGLFGL----LQVLVR---TGVFPLPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 92 fPRMNNMSFWLLPPSlTLLISSSILDVGVGTGWTVYPPLagpIAHSGPAVDLAIFSLhlagASSILGAINFITTTINMKs 171
Cdd:cd01660 83 -RRLAWAGFWLMVIG-TVMAAVPILLGQASVLYTFYPPL---QAHPLFYIGAALVVV----GSWISGFAMFVTLWRWKK- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 172 sDMTMDQLPLFVWSVMITAILLLLSLPVLAGAITMLLtdrnLNTSFF--DPVgggDPILYQHLFWFFGHPEVYILILPGF 249
Cdd:cd01660 153 -ANPGKKVPLATFMVVTTMILWLVASLGVALEVLFQL----LPWSLGlvDTV---DVLLSRTLFWWFGHPLVYFWLLPAY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 250 GMISHIINQESGKNESFGTLGMIYAMLSIgLMGFIVWAHHMFT-VGMDVDTRAYFTSATMIIAIPTGIKVFSWLATL--- 325
Cdd:cd01660 225 IAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeia 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 326 ----HGTK-FKMTVELCW--------AMGFIFlFTMGGLTGLILANSSIDIILHDTYYVVAHFHyvLSMGAVFAIMG-GI 391
Cdd:cd01660 304 grlrGGKGlFGWIRALPWgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812385330 392 IQWY-PLITGLSM-NKKMLKIQFFIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDCYMT-----WNMISSLGSMISLIS 462
Cdd:cd01660 381 AYWLvPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPAAgewapYQQLMAIGGTILFVS 460
|
490
....*....|...
gi 1812385330 463 VLLFILIMWESML 475
Cdd:cd01660 461 GALFLYILFRTLL 473
|
|
| |
