|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 845.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00153 12 DIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00153 92 FPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00153 172 KGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLT 320
Cdd:MTH00153 252 ISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQIN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 INkihPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00153 332 YS---PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEISN 480
Cdd:MTH00153 409 KIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSS 488
|
490 500
....*....|....*....|.
gi 544583314 481 NLEWhYPIFPPQEHTFNETPL 501
Cdd:MTH00153 489 SIEW-LQNLPPAEHSYSELPL 508
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-484 |
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: 799.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:cd01663 5 DIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:cd01663 85 FPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:cd01663 165 PGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLt 320
Cdd:cd01663 245 ISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSI- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:cd01663 324 --KFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNT-NNNYFNNEIS 479
Cdd:cd01663 402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGrKVIFNVGEGS 481
|
....*
gi 544583314 480 NNLEW 484
Cdd:cd01663 482 TSLEW 486
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-496 |
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: 517.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMiGGFGNWLVPLMIGAPDMA 80
Cdd:TIGR02891 8 RIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:TIGR02891 87 FPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:TIGR02891 167 PGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNqPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLT 320
Cdd:TIGR02891 247 ISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inkIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:TIGR02891 326 ---FTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--FTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEI 478
Cdd:TIGR02891 403 RWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWG 482
|
490
....*....|....*...
gi 544583314 479 SNNLEWHYPIfPPQEHTF 496
Cdd:TIGR02891 483 ATTLEWTTSS-PPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-501 |
1.41e-179 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 514.68 E-value: 1.41e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 80
Cdd:COG0843 17 RIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:COG0843 96 FPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:COG0843 176 PGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNqPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLT 320
Cdd:COG0843 256 VSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 INkihPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:COG0843 335 FT---TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEI 478
Cdd:COG0843 412 KIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAGGNPWG 491
|
490 500
....*....|....*....|...
gi 544583314 479 SNNLEWHYPIfPPQEHTFNETPL 501
Cdd:COG0843 492 ARTLEWATPS-PPPLYNFASIPV 513
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-441 |
2.62e-128 |
|
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: 379.99 E-value: 2.62e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 80
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGnesGVGTGWTLYPPLSGptahaggcVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLdRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTtffdptGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKnQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLT 320
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 INKihPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:pfam00115 301 FRT--TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLG 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAFTFWN 441
Cdd:pfam00115 379 KLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLN 423
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 845.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00153 12 DIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00153 92 FPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00153 172 KGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLT 320
Cdd:MTH00153 252 ISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQIN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 INkihPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00153 332 YS---PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEISN 480
Cdd:MTH00153 409 KIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSS 488
|
490 500
....*....|....*....|.
gi 544583314 481 NLEWhYPIFPPQEHTFNETPL 501
Cdd:MTH00153 489 SIEW-LQNLPPAEHSYSELPL 508
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 817.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00037 14 DIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00037 94 FPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00037 174 PGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLT 320
Cdd:MTH00037 254 ISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 INkihPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00037 334 WE---TPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEISN 480
Cdd:MTH00037 411 KVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSS 490
|
490 500
....*....|....*....|...
gi 544583314 481 NLEWHYPIFPPQEHTFNETPLSI 503
Cdd:MTH00037 491 SLEWQYSSFPPSHHTFDETPSTV 513
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-484 |
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: 799.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:cd01663 5 DIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:cd01663 85 FPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:cd01663 165 PGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLt 320
Cdd:cd01663 245 ISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSI- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:cd01663 324 --KFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNT-NNNYFNNEIS 479
Cdd:cd01663 402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGrKVIFNVGEGS 481
|
....*
gi 544583314 480 NNLEW 484
Cdd:cd01663 482 TSLEW 486
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 778.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00167 14 DIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00167 94 FPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00167 174 PGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLt 320
Cdd:MTH00167 254 ISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKI- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00167 333 --KWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWT 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEISN 480
Cdd:MTH00167 411 KIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTST 490
|
490 500
....*....|....*....|.
gi 544583314 481 NLEWhYPIFPPQEHTFNETPL 501
Cdd:MTH00167 491 NVEW-LHGCPPPHHTWEEPPF 510
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-504 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 759.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00223 11 DIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00223 91 FPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00223 171 PGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLt 320
Cdd:MTH00223 251 ISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKI- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00223 330 --KYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEISN 480
Cdd:MTH00223 408 KAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLST 487
|
490 500
....*....|....*....|....
gi 544583314 481 NLEWHYpIFPPQEHTFNETPLSIT 504
Cdd:MTH00223 488 SLEWDN-LLPADFHNNSETGALVI 510
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-504 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 755.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00116 14 DIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00116 94 FPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00116 174 PAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLt 320
Cdd:MTH00116 254 ISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTI- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00116 333 --KWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWT 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEISN 480
Cdd:MTH00116 411 KAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTT 490
|
490 500
....*....|....*....|....
gi 544583314 481 NLEWHYPIfPPQEHTFNETPLSIT 504
Cdd:MTH00116 491 NIEWIHGC-PPPYHTFEEPAFVQV 513
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 733.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00142 12 DIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00142 92 FPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00142 172 GGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLt 320
Cdd:MTH00142 252 ISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKV- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00142 331 --KYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEISN 480
Cdd:MTH00142 409 KAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLST 488
|
490 500
....*....|....*....|...
gi 544583314 481 NLEWHYpIFPPQEHTFNETPLSI 503
Cdd:MTH00142 489 SLEWSH-RLPPDFHTYDELPILV 510
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 683.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00183 14 DIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00183 94 FPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00183 174 PAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLt 320
Cdd:MTH00183 254 ISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSI- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00183 333 --KWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWT 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEISN 480
Cdd:MTH00183 411 KIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTST 490
|
490 500
....*....|....*....|.
gi 544583314 481 NLEWHYPIfPPQEHTFNETPL 501
Cdd:MTH00183 491 NVEWLHGC-PPPYHTFEEPAF 510
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-500 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 683.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00103 14 DIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00103 94 FPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00103 174 PAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLt 320
Cdd:MTH00103 254 ISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNI- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00103 333 --KWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEISN 480
Cdd:MTH00103 411 KIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTT 490
|
490 500
....*....|....*....|
gi 544583314 481 NLEWHYPIfPPQEHTFNETP 500
Cdd:MTH00103 491 NLEWLHGC-PPPYHTFEEPT 509
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-504 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 679.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00077 14 DIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00077 94 FPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00077 174 PSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGtslT 320
Cdd:MTH00077 254 ISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHG---G 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 INKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00077 331 AIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEISN 480
Cdd:MTH00077 411 KIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTST 490
|
490 500
....*....|....*....|....
gi 544583314 481 NLEWHYPiFPPQEHTFNETPLSIT 504
Cdd:MTH00077 491 NIEWLHG-CPPPYHTFEEPSFVQT 513
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-499 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 666.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00007 11 DIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00007 91 FPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00007 171 KGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLt 320
Cdd:MTH00007 251 ISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPI- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00007 330 --KYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEISN 480
Cdd:MTH00007 408 KAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSS 487
|
490
....*....|....*....
gi 544583314 481 NLEWHYPiFPPQEHTFNET 499
Cdd:MTH00007 488 SLEWQDT-LPLDFHNLPET 505
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 636.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00182 16 DIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00182 96 FPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00182 176 PGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGM 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLt 320
Cdd:MTH00182 256 ISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTL- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00182 335 --RLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEIS- 479
Cdd:MTH00182 413 KIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEGTg 492
|
490 500
....*....|....*....|....*
gi 544583314 480 ---NNLEWHYPIfPPQEHTFNETPL 501
Cdd:MTH00182 493 eswASLEWVHSS-PPLFHTYNELPF 516
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 628.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00184 16 DIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00184 96 FPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00184 176 PGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLt 320
Cdd:MTH00184 256 ISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSL- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00184 335 --RLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEISN 480
Cdd:MTH00184 413 KIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVGWVEDSG 492
|
490 500
....*....|....*....|....
gi 544583314 481 ---NLEWHYPIfPPQEHTFNETPL 501
Cdd:MTH00184 493 hypSLEWAQTS-PPAHHTYNELPY 515
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-490 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 617.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00079 15 DIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGpTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00079 95 FPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00079 174 SSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLt 320
Cdd:MTH00079 254 ISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKM- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00079 333 --KFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEISN 480
Cdd:MTH00079 411 SAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINS 490
|
490
....*....|
gi 544583314 481 NLEWHYPIFP 490
Cdd:MTH00079 491 SPEYSLSSYV 500
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-500 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 560.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMA 80
Cdd:MTH00026 15 DIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:MTH00026 95 FPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:MTH00026 175 PGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLT 320
Cdd:MTH00026 255 ISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 INKIHPsLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:MTH00026 335 LIFTTP-MAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIV-------------ILSLN 467
Cdd:MTH00026 414 LIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIfdayyreepfdinIMAKG 493
|
490 500 510
....*....|....*....|....*....|...
gi 544583314 468 NTNNNYFNNEISNNLEWHYpIFPPQEHTFNETP 500
Cdd:MTH00026 494 PLIPFSCQPAHFDTLEWSL-TSPPEHHTYNELP 525
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-466 |
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: 551.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPlMIGAPDMA 80
Cdd:cd00919 3 DIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:cd00919 82 FPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:cd00919 162 PGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNqPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLT 320
Cdd:cd00919 242 ISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 INkihPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:cd00919 321 FD---PPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSL 466
Cdd:cd00919 398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-496 |
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: 517.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMiGGFGNWLVPLMIGAPDMA 80
Cdd:TIGR02891 8 RIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:TIGR02891 87 FPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:TIGR02891 167 PGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNqPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLT 320
Cdd:TIGR02891 247 ISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 inkIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:TIGR02891 326 ---FTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--FTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEI 478
Cdd:TIGR02891 403 RWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWG 482
|
490
....*....|....*...
gi 544583314 479 SNNLEWHYPIfPPQEHTF 496
Cdd:TIGR02891 483 ATTLEWTTSS-PPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-501 |
1.41e-179 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 514.68 E-value: 1.41e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 80
Cdd:COG0843 17 RIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:COG0843 96 FPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:COG0843 176 PGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKNqPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLT 320
Cdd:COG0843 256 VSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 INkihPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:COG0843 335 FT---TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAFTFWNTLSSLGSLLSFIGTIGFLTIVILSLNNTNNNYFNNEI 478
Cdd:COG0843 412 KIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAGGNPWG 491
|
490 500
....*....|....*....|...
gi 544583314 479 SNNLEWHYPIfPPQEHTFNETPL 501
Cdd:COG0843 492 ARTLEWATPS-PPPLYNFASIPV 513
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-442 |
3.12e-161 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 467.23 E-value: 3.12e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 2 IGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 81
Cdd:MTH00048 16 IGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 82 PRMNNMSFWLIPPSFLLLLASAgnESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRAP 161
Cdd:MTH00048 96 PRLNALSAWLLVPSIVFLLLSM--CLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 162 GMSLdRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGII 241
Cdd:MTH00048 174 NVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGII 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 242 SHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLti 321
Cdd:MTH00048 253 SHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRV-- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 322 NKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGAT 401
Cdd:MTH00048 331 RKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQ 410
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 544583314 402 AHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTFWNT 442
Cdd:MTH00048 411 CHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINV 451
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-463 |
1.72e-149 |
|
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: 436.63 E-value: 1.72e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 2 IGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAF 81
Cdd:cd01662 10 IGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 82 PRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLSGPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRAP 161
Cdd:cd01662 89 PRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 162 GMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGII 241
Cdd:cd01662 169 GMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 242 SHVVTNRTGKNQpFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLTi 321
Cdd:cd01662 249 SEIVPTFSRKPL-FGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIR- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 322 nkIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGAT 401
Cdd:cd01662 327 --FETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGK 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544583314 402 AHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAfTFWNTLSSLGSLLSFIGTIGFLTIVI 463
Cdd:cd01662 405 WSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPG-PGWDPLNLISTIGAFLIAAGVLLFLI 465
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-441 |
2.62e-128 |
|
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: 379.99 E-value: 2.62e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 1 DIGTLYLIFGAWAGTVGTAMSNIIRVELSQPGSLIQNDQIYNVMVTSHALIMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 80
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 81 FPRMNNMSFWLIPPSFLLLLASAGnesGVGTGWTLYPPLSGptahaggcVDLAIFSLHLAGASSIMASINFISTIINMRA 160
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 161 PGMSLdRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDRNINTtffdptGGGDPILFQHLFWFFGHPEVYILILPGFGI 240
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 241 ISHVVTNRTGKnQPFGFLGMMYAMIAIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLT 320
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 321 INKihPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDTYYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGA 400
Cdd:pfam00115 301 FRT--TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLG 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 544583314 401 TAHFILMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAFTFWN 441
Cdd:pfam00115 379 KLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLN 423
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
41-435 |
6.72e-92 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 293.77 E-value: 6.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 41 YNVMVTSHALIMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGNESGVGTGWTLYPPLS 120
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 121 GPTAHAGGCVDLAIFSLHLAGASSIMASINFISTIINMRAPGMSLDRTPLFVWSILITTFLLLLSLPVLAGAITMLLTDR 200
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 201 NINTTFFDPTGGGDPILFQHLFWFFGHPEVYILILPGFGIISHVVTNRTgKNQPFGFLGMMYAMIAIGILGFIVWAHHMF 280
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFF 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 281 TVGLDVDTRAYFTAATMIIAIPTGVKVFSWLATLQGTSLtinKIHPSLMWALGFIFLFTIGGLTGIILSNSSLNIALHDT 360
Cdd:PRK15017 337 TMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRI---VFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNS 413
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544583314 361 YYVTAHFHYVLSMGAVFAIFSGFNHWFSLFTGCHLDESGATAHFILMFIGVNLTFFPQHFLGLAGMPRRYSDYPD 435
Cdd:PRK15017 414 LFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
214-466 |
2.74e-14 |
|
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: 75.02 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 214 DPILFQHLFWFFGHPEVYILILPGFgIISHVVTNRTGKNQPFGFLGMMYAMIAIGILGFIVWAHHMFT-VGLDVDTRAYF 292
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAY-IAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 293 TAATMIIAIPTGVKVFSWLATL------QGTSLTINKIHpSLMW--------ALGFIFlFTIGGLTGIILSNSSLNIALH 358
Cdd:cd01660 279 MVLTFMVALPSLLTAFTVFASLeiagrlRGGKGLFGWIR-ALPWgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVH 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544583314 359 DTYYVTAHFHyvLSMGAVFAI-FSGFNHWF-SLFTGCHLDESG-ATAHFILMFIGVNLTFFPQHFLGLAGMPRR------ 429
Cdd:cd01660 357 NTAWVPGHFH--LTVGGAVALtFMAVAYWLvPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaeaqy 434
|
250 260 270
....*....|....*....|....*....|....*...
gi 544583314 430 -YSDYPDAFTFWNTLSSLGSLLSFIGTIGFLTIVILSL 466
Cdd:cd01660 435 gGLPAAGEWAPYQQLMAIGGTILFVSGALFLYILFRTL 472
|
|
|