|
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: 1022.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00153 11 KDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00153 91 AFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00153 171 SKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00153 251 MISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00153 331 NYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSI 480
Cdd:MTH00153 411 QFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSI 490
|
490 500
....*....|....*....|.
gi 255098918 481 EWLQNTPPAEHSYSELPLLTN 501
Cdd:MTH00153 491 EWLQNLPPAEHSYSELPLLTN 511
|
|
| 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: 871.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:cd01663 4 KDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:cd01663 84 AFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:cd01663 164 APGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:cd01663 244 IISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:cd01663 324 KFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPV-QLNSS 479
Cdd:cd01663 404 HFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEGSTS 483
|
....*
gi 255098918 480 IEWLQ 484
Cdd:cd01663 484 LEWTL 488
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-500 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 547.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPIMLGAPDM 80
Cdd:COG0843 16 KRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:COG0843 95 AFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:COG0843 175 APGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:COG0843 255 IVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:COG0843 334 RFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQV-MFPVQLN 477
Cdd:COG0843 414 HFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAgGNPWGAR 493
|
490 500
....*....|....*....|...
gi 255098918 478 sSIEWLQNTPPAEHSYSELPLLT 500
Cdd:COG0843 494 -TLEWATPSPPPLYNFASIPVVR 515
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-493 |
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: 545.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMiGGFGNWLVPIMLGAPDM 80
Cdd:TIGR02891 7 KRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:TIGR02891 86 AFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:TIGR02891 166 APGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:TIGR02891 246 IISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:TIGR02891 325 RFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNS 478
Cdd:TIGR02891 405 HFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGAT 484
|
490
....*....|....*
gi 255098918 479 SIEWLQNTPPAEHSY 493
Cdd:TIGR02891 485 TLEWTTSSPPPAHNF 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-448 |
7.03e-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: 381.54 E-value: 7.03e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 2 DIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPIMLGAPDMA 81
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 82 FPRMNNMSFWLLPPALTLLLVSSMvenGAGTGWTVYPPLssniahggASVDLAIFSLHLAGISSILGAVNFITTVINMRS 161
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 162 TGITFdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 241
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 242 ISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLN 321
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 322 -YSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTAWNVISTIGSTI 448
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
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: 1022.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00153 11 KDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00153 91 AFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00153 171 SKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00153 251 MISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00153 331 NYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSI 480
Cdd:MTH00153 411 QFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSI 490
|
490 500
....*....|....*....|.
gi 255098918 481 EWLQNTPPAEHSYSELPLLTN 501
Cdd:MTH00153 491 EWLQNLPPAEHSYSELPLLTN 511
|
|
| 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: 871.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:cd01663 4 KDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:cd01663 84 AFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:cd01663 164 APGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:cd01663 244 IISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:cd01663 324 KFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPV-QLNSS 479
Cdd:cd01663 404 HFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEGSTS 483
|
....*
gi 255098918 480 IEWLQ 484
Cdd:cd01663 484 LEWTL 488
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-499 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 842.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00167 13 KDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00167 93 AFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00167 173 PPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00167 253 MISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00167 333 KWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSI 480
Cdd:MTH00167 413 HFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNV 492
|
490
....*....|....*....
gi 255098918 481 EWLQNTPPAEHSYSELPLL 499
Cdd:MTH00167 493 EWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 833.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00116 13 KDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00116 93 AFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00116 173 PPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00116 253 IISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00116 333 KWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSI 480
Cdd:MTH00116 413 QFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNI 492
|
490 500
....*....|....*....|.
gi 255098918 481 EWLQNTPPAEHSYSELPLLTN 501
Cdd:MTH00116 493 EWIHGCPPPYHTFEEPAFVQV 513
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-497 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 833.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00223 10 KDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00223 90 AFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00223 170 SPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00223 250 MISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00223 330 KYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSI 480
Cdd:MTH00223 410 HFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSL 489
|
490
....*....|....*..
gi 255098918 481 EWLQNTPPAEHSYSELP 497
Cdd:MTH00223 490 EWDNLLPADFHNNSETG 506
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 832.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00142 11 KDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00142 91 AFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00142 171 AGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00142 251 MISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00142 331 KYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSI 480
Cdd:MTH00142 411 HFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSL 490
|
490 500
....*....|....*....|.
gi 255098918 481 EWLQNTPPAEHSYSELPLLTN 501
Cdd:MTH00142 491 EWSHRLPPDFHTYDELPILVV 511
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-495 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 749.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00103 13 KDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00103 93 AFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00103 173 PPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00103 253 MISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00103 333 KWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSI 480
Cdd:MTH00103 413 HFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNL 492
|
490
....*....|....*
gi 255098918 481 EWLQNTPPAEHSYSE 495
Cdd:MTH00103 493 EWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-498 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 747.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00037 13 KDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00037 93 AFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00037 173 TPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00037 253 MISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00037 333 RWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKV 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSI 480
Cdd:MTH00037 413 HFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSL 492
|
490
....*....|....*....
gi 255098918 481 EWLQNT-PPAEHSYSELPL 498
Cdd:MTH00037 493 EWQYSSfPPSHHTFDETPS 511
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-495 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 743.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00183 13 KDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00183 93 AFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00183 173 PPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00183 253 MISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00183 333 KWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSI 480
Cdd:MTH00183 413 HFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNV 492
|
490
....*....|....*
gi 255098918 481 EWLQNTPPAEHSYSE 495
Cdd:MTH00183 493 EWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-500 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 737.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00007 10 KDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00007 90 AFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00007 170 WKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00007 250 AISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00007 330 KYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSI 480
Cdd:MTH00007 410 HFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSL 489
|
490 500
....*....|....*....|
gi 255098918 481 EWLQNTPPAEHSYSELPLLT 500
Cdd:MTH00007 490 EWQDTLPLDFHNLPETGIIT 509
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 733.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00077 13 KDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00077 93 AFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00077 173 PPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00077 253 MISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00077 333 KWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKI 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSI 480
Cdd:MTH00077 413 HFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNI 492
|
490 500
....*....|....*....|.
gi 255098918 481 EWLQNTPPAEHSYSELPLLTN 501
Cdd:MTH00077 493 EWLHGCPPPYHTFEEPSFVQT 513
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-499 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 681.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00182 15 KDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00182 95 AFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00182 175 APGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00182 255 MISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00182 335 RLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLN--- 477
Cdd:MTH00182 415 HFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEGTges 494
|
490 500
....*....|....*....|...
gi 255098918 478 -SSIEWLQNTPPAEHSYSELPLL 499
Cdd:MTH00182 495 wASLEWVHSSPPLFHTYNELPFV 517
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-495 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 676.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00079 14 KDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSnIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00079 94 SFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00079 173 SSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00079 253 IISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00079 333 KFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSI 480
Cdd:MTH00079 413 VFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSP 492
|
490
....*....|....*
gi 255098918 481 EWLQNTPPAEHSYSE 495
Cdd:MTH00079 493 EYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-499 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 666.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00184 15 KDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00184 95 AFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00184 175 APGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00184 255 IISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:MTH00184 335 RLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQV---MFPVQLN 477
Cdd:MTH00184 415 HFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFvgwVEDSGHY 494
|
490 500
....*....|....*....|..
gi 255098918 478 SSIEWLQNTPPAEHSYSELPLL 499
Cdd:MTH00184 495 PSLEWAQTSPPAHHTYNELPYV 516
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-464 |
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: 590.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPiMLGAPDM 80
Cdd:cd00919 2 KDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:cd00919 81 AFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:cd00919 161 APGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:cd00919 241 AISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:cd00919 320 RFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKI 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESL 464
Cdd:cd00919 400 HFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-499 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 582.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00026 14 KDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00026 94 AFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00026 174 TPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00026 254 IISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 N--YSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKML 398
Cdd:MTH00026 334 NliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 399 KSQFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWEslASQRQVMFPVQLNS 478
Cdd:MTH00026 414 LIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFD--AYYREEPFDINIMA 491
|
490 500 510
....*....|....*....|....*....|....*.
gi 255098918 479 ---------------SIEWLQNTPPAEHSYSELPLL 499
Cdd:MTH00026 492 kgplipfscqpahfdTLEWSLTSPPEHHTYNELPYI 527
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-500 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 547.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPIMLGAPDM 80
Cdd:COG0843 16 KRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:COG0843 95 AFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:COG0843 175 APGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:COG0843 255 IVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:COG0843 334 RFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQV-MFPVQLN 477
Cdd:COG0843 414 HFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAgGNPWGAR 493
|
490 500
....*....|....*....|...
gi 255098918 478 sSIEWLQNTPPAEHSYSELPLLT 500
Cdd:COG0843 494 -TLEWATPSPPPLYNFASIPVVR 515
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-493 |
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: 545.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMiGGFGNWLVPIMLGAPDM 80
Cdd:TIGR02891 7 KRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:TIGR02891 86 AFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:TIGR02891 166 APGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:TIGR02891 246 IISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:TIGR02891 325 RFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNS 478
Cdd:TIGR02891 405 HFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGAT 484
|
490
....*....|....*
gi 255098918 479 SIEWLQNTPPAEHSY 493
Cdd:TIGR02891 485 TLEWTTSSPPPAHNF 499
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-471 |
9.86e-175 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 501.52 E-value: 9.86e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDM 80
Cdd:MTH00048 14 KRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVenGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:MTH00048 94 NLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:MTH00048 172 MTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:MTH00048 251 IISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYS-PATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLK 399
Cdd:MTH00048 331 RKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQ 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255098918 400 SQFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVM 471
Cdd:MTH00048 411 CHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-493 |
2.34e-164 |
|
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: 474.76 E-value: 2.34e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPIMLGAPDM 80
Cdd:cd01662 8 KRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:cd01662 87 AFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:cd01662 167 APGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:cd01662 247 IFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:cd01662 326 RFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKW 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTAWNVISTIGSTISLLGILFFffiIWESLASQRQVMFPVQLN- 477
Cdd:cd01662 406 SFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLF---LINVIVSIRKGKRDATGDp 482
|
490
....*....|....*....
gi 255098918 478 ---SSIEWLQNTPPAEHSY 493
Cdd:cd01662 483 wgaRTLEWATSSPPPAYNF 501
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-448 |
7.03e-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: 381.54 E-value: 7.03e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 2 DIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPIMLGAPDMA 81
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 82 FPRMNNMSFWLLPPALTLLLVSSMvenGAGTGWTVYPPLssniahggASVDLAIFSLHLAGISSILGAVNFITTVINMRS 161
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 162 TGITFdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 241
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 242 ISHIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLN 321
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 322 -YSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTAWNVISTIGSTI 448
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-497 |
3.87e-110 |
|
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131928 Cd Length: 643 Bit Score: 340.68 E-value: 3.87e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPIMLGAPDM 80
Cdd:TIGR02882 51 KKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 81 AFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMR 160
Cdd:TIGR02882 130 AFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 161 STGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 240
Cdd:TIGR02882 210 APGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 241 MISHIISQESgKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQL 320
Cdd:TIGR02882 290 IYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 321 NYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKS 400
Cdd:TIGR02882 369 RFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKW 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 401 QFTIMFMGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTAWNVISTIGSTISLLGILFFFF-IIWESLASQRQVMFPVQLN 477
Cdd:TIGR02882 449 CFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKSPREATGDPWNG 528
|
490 500
....*....|....*....|
gi 255098918 478 SSIEWLQNTPPAEHSYSELP 497
Cdd:TIGR02882 529 RTLEWATASPPPKYNFAVTP 548
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-497 |
2.60e-100 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 315.72 E-value: 2.60e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 1 KDIGTLYFIFGAWAGMVGTSLSILIR-----AELGHPGALigDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPIML 75
Cdd:PRK15017 55 KRLGIMYIIVAIVMLLRGFADAIMMRsqqalASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 76 GAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITT 155
Cdd:PRK15017 132 GARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVT 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 156 VINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 235
Cdd:PRK15017 212 ILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 236 LPGFGMISHIISQESgKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATL 315
Cdd:PRK15017 292 LPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTM 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 316 YGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNT 395
Cdd:PRK15017 371 YQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 396 KMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTAWNVISTIGSTISLLGILFFFFIIWESLASQ---RQVM 471
Cdd:PRK15017 451 TWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRdqnRDLT 530
|
490 500
....*....|....*....|....*.
gi 255098918 472 FPVQLNSSIEWLQNTPPAEHSYSELP 497
Cdd:PRK15017 531 GDPWGGRTLEWATSSPPPFYNFAVVP 556
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
3-464 |
2.69e-20 |
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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: 93.50 E-value: 2.69e-20
10 20 30 40 50 60 70 80
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gi 255098918 3 IGTLYFIFGAWAGMvgtsLSILIRAELGhpgALIGDDQIYNVIVTAHAFIM-IFFMVMPIMigGFGNWLVPIMLGAPDMA 81
Cdd:cd01660 12 VAFLALLLGGLFGL----LQVLVRTGVF---PLPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN 82
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 82 fPRMNNMSFWLLPPALTLLLVSsMVENGAGTGWTVYPPLssnIAHGGASVDLAIFSLHlagiSSILGAVNFITTVINMRS 161
Cdd:cd01660 83 -RRLAWAGFWLMVIGTVMAAVP-ILLGQASVLYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLWRWKKA 153
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 162 tgITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLtdrnINTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 241
Cdd:cd01660 154 --NPGKKVPLATFMVVTTMILWLVASLGVALEVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIA 226
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 242 ISHIISQESGKKETFGSLGMIyAMLAIGLLGFIVWAHHMFT-VGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT------ 314
Cdd:cd01660 227 WYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASleiagr 305
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330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 315 ------LYG--TQLNYSPATLWALGFVFL-FTVGGLTGVVLANSSVDIILHDTYYVVAHFHyvLSMGAVFAIMA-GFVHW 384
Cdd:cd01660 306 lrggkgLFGwiRALPWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAYW 383
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410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255098918 385 Y-PLFTGLTMNTKMLKS-QFTIMFMGVNLTFFPQHFLGLAGMPRR--YSDYPDAY-----TAWNVISTIGSTISLLGILF 455
Cdd:cd01660 384 LvPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGAL 463
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....*....
gi 255098918 456 FFFIIWESL 464
Cdd:cd01660 464 FLYILFRTL 472
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