|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1027.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 1 SRQWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAV 160
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 161 NFITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 241 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 321 WLATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTG 400
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 401 LILNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQV 480
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|.
gi 2044005529 481 IYPMQLNSSIEWLQNTPPTEHSYSELPILTN 511
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| 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: 869.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 8 TNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGA 87
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 88 PDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVI 167
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 168 NMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 247
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 248 GFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 327
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 328 TQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLILNSKW 407
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 408 LKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVIY-PMQL 486
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEG 480
|
....*...
gi 2044005529 487 NSSIEWLQ 494
Cdd:cd01663 481 STSLEWTL 488
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-510 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 560.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 2 RQWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLV 81
Cdd:COG0843 7 RRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVN 161
Cdd:COG0843 86 PLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 162 FITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:COG0843 166 FIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 242 YILILPGFGMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321
Cdd:COG0843 246 YILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 322 LATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGL 401
Cdd:COG0843 325 IATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 402 ILNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQ 479
Cdd:COG0843 405 MLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPK 484
|
490 500 510
....*....|....*....|....*....|..
gi 2044005529 480 V-IYPMQLNsSIEWLQNTPPTEHSYSELPILT 510
Cdd:COG0843 485 AgGNPWGAR-TLEWATPSPPPLYNFASIPVVR 515
|
|
| 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: 554.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 5 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMiGGFGNWLVPLM 84
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 85 LGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFIT 164
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 165 TVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 244
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 245 ILPGFGMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 324
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 325 LHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLILN 404
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 405 SKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVIY 482
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 2044005529 483 PMQLNSSIEWLQNTPPTEHSY 503
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
12-458 |
1.69e-129 |
|
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: 383.46 E-value: 1.69e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 12 DIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMA 91
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 92 FPRMNNMSFWLLPPSLTLLLVSSMvenGAGTGWTVYPPLssviahggASVDLAIFSLHLAGISSILGAVNFITTVINMRS 171
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 172 VGISFdRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 251
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 252 ISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLN 331
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 332 -YSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLILNSKWLKT 410
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2044005529 411 QFLIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTTWNVVSTIGSSI 458
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1027.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 1 SRQWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAV 160
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 161 NFITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 241 VYILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 321 WLATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTG 400
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 401 LILNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQV 480
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|.
gi 2044005529 481 IYPMQLNSSIEWLQNTPPTEHSYSELPILTN 511
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| 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: 869.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 8 TNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGA 87
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 88 PDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVI 167
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 168 NMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 247
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 248 GFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 327
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 328 TQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLILNSKW 407
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 408 LKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVIY-PMQL 486
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEG 480
|
....*...
gi 2044005529 487 NSSIEWLQ 494
Cdd:cd01663 481 STSLEWTL 488
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
4-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 859.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 4 WLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 83
Cdd:MTH00167 6 WLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 84 MLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFI 163
Cdd:MTH00167 86 MIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 164 TTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:MTH00167 166 TTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 244 LILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 323
Cdd:MTH00167 246 LILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 324 TLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLIL 403
Cdd:MTH00167 326 TLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 404 NSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVIYP 483
Cdd:MTH00167 406 NETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPV 485
|
490 500
....*....|....*....|....*.
gi 2044005529 484 MQLNSSIEWLQNTPPTEHSYSELPIL 509
Cdd:MTH00167 486 ELTSTNVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
2-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 844.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 2 RQWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 81
Cdd:MTH00223 1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVN 161
Cdd:MTH00223 81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 162 FITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:MTH00223 161 FITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 242 YILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321
Cdd:MTH00223 241 YILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 322 LATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGL 401
Cdd:MTH00223 321 LATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 402 ILNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVI 481
Cdd:MTH00223 401 TLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVV 480
|
490 500
....*....|....*....|....*...
gi 2044005529 482 YPMQLNSSIEWLQNTPPTEHSYSELPIL 509
Cdd:MTH00223 481 WSGHLSTSLEWDNLLPADFHNNSETGAL 508
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
2-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 842.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 2 RQWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 81
Cdd:MTH00142 2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVN 161
Cdd:MTH00142 82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 162 FITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 242 YILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321
Cdd:MTH00142 242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 322 LATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGL 401
Cdd:MTH00142 322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 402 ILNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVI 481
Cdd:MTH00142 402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVM 481
|
490 500 510
....*....|....*....|....*....|
gi 2044005529 482 YPMQLNSSIEWLQNTPPTEHSYSELPILTN 511
Cdd:MTH00142 482 WSSHLSTSLEWSHRLPPDFHTYDELPILVV 511
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
3-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 840.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 3 QWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00116 5 RWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNF 162
Cdd:MTH00116 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 163 ITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00116 165 ITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 243 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
Cdd:MTH00116 245 ILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 323 ATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLI 402
Cdd:MTH00116 325 ATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 403 LNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVIY 482
Cdd:MTH00116 405 LHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQ 484
|
490 500
....*....|....*....|....*....
gi 2044005529 483 PMQLNSSIEWLQNTPPTEHSYSELPILTN 511
Cdd:MTH00116 485 PELTTTNIEWIHGCPPPYHTFEEPAFVQV 513
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
3-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 761.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 3 QWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00103 5 RWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNF 162
Cdd:MTH00103 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 163 ITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00103 165 ITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 243 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
Cdd:MTH00103 245 ILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 323 ATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLI 402
Cdd:MTH00103 325 ATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 403 LNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVIY 482
Cdd:MTH00103 405 LNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLT 484
|
490 500
....*....|....*....|...
gi 2044005529 483 PMQLNSSIEWLQNTPPTEHSYSE 505
Cdd:MTH00103 485 VELTTTNLEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
3-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 760.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 3 QWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00037 5 RWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNF 162
Cdd:MTH00037 85 LMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 163 ITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00037 165 ITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 243 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
Cdd:MTH00037 245 ILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 323 ATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLI 402
Cdd:MTH00037 325 ATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 403 LNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVIY 482
Cdd:MTH00037 405 LHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVIS 484
|
490 500
....*....|....*....|....*..
gi 2044005529 483 PMQLNSSIEWLQNT-PPTEHSYSELPI 508
Cdd:MTH00037 485 PEFSSSSLEWQYSSfPPSHHTFDETPS 511
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
3-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 754.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 3 QWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00183 5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNF 162
Cdd:MTH00183 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 163 ITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00183 165 ITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 243 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
Cdd:MTH00183 245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 323 ATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLI 402
Cdd:MTH00183 325 ATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 403 LNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVIY 482
Cdd:MTH00183 405 LHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
|
490 500
....*....|....*....|...
gi 2044005529 483 PMQLNSSIEWLQNTPPTEHSYSE 505
Cdd:MTH00183 485 VELTSTNVEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
3-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 746.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 3 QWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNF 162
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 163 ITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 243 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 323 ATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLI 402
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 403 LNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVIY 482
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|....*...
gi 2044005529 483 PMQLNSSIEWLQNTPPTEHSYSELPILT 510
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPETGIIT 509
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
3-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 744.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 3 QWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00077 5 RWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNF 162
Cdd:MTH00077 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 163 ITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00077 165 ITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 243 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
Cdd:MTH00077 245 ILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 323 ATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLI 402
Cdd:MTH00077 325 ATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 403 LNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVIY 482
Cdd:MTH00077 405 LHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLT 484
|
490 500
....*....|....*....|...
gi 2044005529 483 PMQLNSSIEWLQNTPPTEHSYSE 505
Cdd:MTH00077 485 TELTSTNIEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
3-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 689.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 3 QWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00182 7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNF 162
Cdd:MTH00182 87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 163 ITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00182 167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 243 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
Cdd:MTH00182 247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 323 ATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLI 402
Cdd:MTH00182 327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 403 LNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVI- 481
Cdd:MTH00182 407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIg 486
|
490 500 510
....*....|....*....|....*....|.
gi 2044005529 482 ---YPMQLNSSIEWLQNTPPTEHSYSELPIL 509
Cdd:MTH00182 487 wkeGTGESWASLEWVHSSPPLFHTYNELPFV 517
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
4-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 677.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 4 WLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 83
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 84 MLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSvIAHGGASVDLAIFSLHLAGISSILGAVNFI 163
Cdd:MTH00079 87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 164 TTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:MTH00079 166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 244 LILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 323
Cdd:MTH00079 246 LILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 324 TLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLIL 403
Cdd:MTH00079 326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 404 NSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVIYP 483
Cdd:MTH00079 406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHD 485
|
490 500
....*....|....*....|..
gi 2044005529 484 MQLNSSIEWLQNTPPTEHSYSE 505
Cdd:MTH00079 486 NYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
3-507 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 674.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 3 QWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00184 7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNF 162
Cdd:MTH00184 87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 163 ITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00184 167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 243 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 323 ATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLI 402
Cdd:MTH00184 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 403 LNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVIY 482
Cdd:MTH00184 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVG 486
|
490 500
....*....|....*....|....*...
gi 2044005529 483 PMQ---LNSSIEWLQNTPPTEHSYSELP 507
Cdd:MTH00184 487 WVEdsgHYPSLEWAQTSPPAHHTYNELP 514
|
|
| 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: 589.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 10 HKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPlMLGAPD 89
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 90 MAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINM 169
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 170 RSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 250 GMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQ 329
Cdd:cd00919 240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 330 LNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLILNSKWLK 409
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044005529 410 TQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESL 474
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| 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: 588.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 3 QWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNF 162
Cdd:MTH00026 86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 163 ITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 243 ILILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
Cdd:MTH00026 246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 323 ATLHGTQLN--YSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTG 400
Cdd:MTH00026 326 ATVSGSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 401 LILNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESL------ 474
Cdd:MTH00026 406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYyreepf 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2044005529 475 ---ISQRQVIYPMQLN----SSIEWLQNTPPTEHSYSELPIL 509
Cdd:MTH00026 486 dinIMAKGPLIPFSCQpahfDTLEWSLTSPPEHHTYNELPYI 527
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-510 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 560.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 2 RQWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLV 81
Cdd:COG0843 7 RRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVN 161
Cdd:COG0843 86 PLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 162 FITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:COG0843 166 FIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 242 YILILPGFGMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321
Cdd:COG0843 246 YILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 322 LATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGL 401
Cdd:COG0843 325 IATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 402 ILNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQ 479
Cdd:COG0843 405 MLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPK 484
|
490 500 510
....*....|....*....|....*....|..
gi 2044005529 480 V-IYPMQLNsSIEWLQNTPPTEHSYSELPILT 510
Cdd:COG0843 485 AgGNPWGAR-TLEWATPSPPPLYNFASIPVVR 515
|
|
| 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: 554.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 5 LFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMiGGFGNWLVPLM 84
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 85 LGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFIT 164
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 165 TVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 244
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 245 ILPGFGMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 324
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 325 LHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLILN 404
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 405 SKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVIY 482
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 2044005529 483 PMQLNSSIEWLQNTPPTEHSY 503
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
4-481 |
7.69e-176 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 504.60 E-value: 7.69e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 4 WLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 83
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 84 MLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVenGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFI 163
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 164 TTVINMRSVGISFdRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:MTH00048 165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 244 LILPGFGMISHIISQESGKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 323
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 324 TLHGTQLNYS-PAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLI 402
Cdd:MTH00048 324 MLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044005529 403 LNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVI 481
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
4-503 |
4.86e-169 |
|
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: 486.70 E-value: 4.86e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 4 WLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPL 83
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 84 MLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVNFI 163
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 164 TTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 244 LILPGFGMISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 323
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 324 TLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLIL 403
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 404 NSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVVSTIGSSISLLGILFFLFIIWESLISQRQVI 481
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDA 478
|
490 500
....*....|....*....|...
gi 2044005529 482 YPMQLN-SSIEWLQNTPPTEHSY 503
Cdd:cd01662 479 TGDPWGaRTLEWATSSPPPAYNF 501
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
12-458 |
1.69e-129 |
|
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: 383.46 E-value: 1.69e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 12 DIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMA 91
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 92 FPRMNNMSFWLLPPSLTLLLVSSMvenGAGTGWTVYPPLssviahggASVDLAIFSLHLAGISSILGAVNFITTVINMRS 171
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 172 VGISFdRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 251
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 252 ISHIISQESGKKeTFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLN 331
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 332 -YSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLILNSKWLKT 410
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2044005529 411 QFLIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTTWNVVSTIGSSI 458
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-508 |
4.03e-112 |
|
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: 346.07 E-value: 4.03e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 2 RQWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLV 81
Cdd:TIGR02882 42 NEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSILGAVN 161
Cdd:TIGR02882 121 PLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGIN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 162 FITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:TIGR02882 201 FFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 242 YILILPGFGMISHIISQESgKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321
Cdd:TIGR02882 281 YIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNW 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 322 LATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGL 401
Cdd:TIGR02882 360 LLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 402 ILNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTTWNVVSTIGSSISLLGILFFLF-IIWESLISQR 478
Cdd:TIGR02882 440 KLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKSPR 519
|
490 500 510
....*....|....*....|....*....|
gi 2044005529 479 QVIYPMQLNSSIEWLQNTPPTEHSYSELPI 508
Cdd:TIGR02882 520 EATGDPWNGRTLEWATASPPPKYNFAVTPD 549
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
3-507 |
7.00e-107 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 333.06 E-value: 7.00e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 3 QWLFSTNHKDIGTLYFIFGAWAGMVGTSLSILIR-----AELGHPGALigDDQIYNVIVTAHAFVMIFFMVMPIMIGgFG 77
Cdd:PRK15017 47 EWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRsqqalASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 78 NWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSVIAHGGASVDLAIFSLHLAGISSIL 157
Cdd:PRK15017 124 NLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 158 GAVNFITTVINMRSVGISFDRMPLFVWAVVLTALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237
Cdd:PRK15017 204 TGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 238 HPEVYILILPGFGMISHIISQESgKKETFGSLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 317
Cdd:PRK15017 284 HPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 318 IFSWLATLHGTQLNYSPAMLWTLGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPL 397
Cdd:PRK15017 363 IFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPK 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 398 FTGLILNSKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTTWNVVSTIGSSISLLGILFFLFIIWESLIS 476
Cdd:PRK15017 443 AFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRD 522
|
490 500 510
....*....|....*....|....*....|....
gi 2044005529 477 Q---RQVIYPMQLNSSIEWLQNTPPTEHSYSELP 507
Cdd:PRK15017 523 RdqnRDLTGDPWGGRTLEWATSSPPPFYNFAVVP 556
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
225-474 |
8.91e-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: 8.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 225 DPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMIyAMMAIGLLGFIVWAHHMFT-VGMDVDTRAYF 303
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 304 TSATMIIAVPTGIKIFSWLATL-------HG-------TQLNYSPAMLWTLGFVFL-FTVGGLTGVVLANSSVDIILHDT 368
Cdd:cd01660 279 MVLTFMVALPSLLTAFTVFASLeiagrlrGGkglfgwiRALPWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNT 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044005529 369 YYVVAHFHyvLSMGAVFAIMA-GFVHWY-PLFTGLILNSKWL-KTQFLIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPD 443
Cdd:cd01660 359 AWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGG 436
|
250 260 270
....*....|....*....|....*....|....*.
gi 2044005529 444 AY-----TTWNVVSTIGSSISLLGILFFLFIIWESL 474
Cdd:cd01660 437 LPaagewAPYQQLMAIGGTILFVSGALFLYILFRTL 472
|
|
| |
