|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1007.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00153 9 NHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00153 89 DMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIIN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00153 169 MRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00153 249 FGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00153 329 QINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSSS 480
Cdd:MTH00153 409 KIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSS 488
|
490 500
....*....|....*....|...
gi 6019192 481 SIEWYQNLPPAEHSYNELPILSN 503
Cdd:MTH00153 489 SIEWLQNLPPAEHSYSELPLLTN 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: 862.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:cd01663 82 DMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:cd01663 162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:cd01663 242 FGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:cd01663 322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIF-PLNSS 479
Cdd:cd01663 402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGS 481
|
....*
gi 6019192 480 SSIEW 484
Cdd:cd01663 482 TSLEW 486
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-501 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 549.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAP 80
Cdd:COG0843 14 DHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:COG0843 93 DMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:COG0843 173 MRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKeTFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:COG0843 253 FGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:COG0843 332 RIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQ-LTIFPLN 477
Cdd:COG0843 412 KIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPkAGGNPWG 491
|
490 500
....*....|....*....|....
gi 6019192 478 sSSSIEWYQNLPPAEHSYNELPIL 501
Cdd:COG0843 492 -ARTLEWATPSPPPLYNFASIPVV 514
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-495 |
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 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMiGGFGNWLVPLMLGAP 80
Cdd:TIGR02891 5 DHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:TIGR02891 84 DMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:TIGR02891 164 MRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKeTFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:TIGR02891 244 FGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:TIGR02891 323 SIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQltIFPLN- 477
Cdd:TIGR02891 403 RWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP--KAGANp 480
|
490
....*....|....*....
gi 6019192 478 -SSSSIEWYQNLPPAEHSY 495
Cdd:TIGR02891 481 wGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
4-450 |
3.21e-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: 3.21e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 4 DIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMA 83
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 84 FPWLNNMSFWLLPPSLTLLISSSlveNGAGTGWTVYPPLSSniahagssVDLAIFSLHLAGISSILGAVNFITTVINMRS 163
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 164 YGMSFdQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 243
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 244 ISHIISQESGKKeTFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQIN 323
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 324 -YSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLLKI 402
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 6019192 403 QFLTMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYISWNIVSSLGSYI 450
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1007.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00153 9 NHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00153 89 DMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIIN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00153 169 MRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00153 249 FGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00153 329 QINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSSS 480
Cdd:MTH00153 409 KIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSS 488
|
490 500
....*....|....*....|...
gi 6019192 481 SIEWYQNLPPAEHSYNELPILSN 503
Cdd:MTH00153 489 SIEWLQNLPPAEHSYSELPLLTN 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: 862.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:cd01663 82 DMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:cd01663 162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:cd01663 242 FGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:cd01663 322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIF-PLNSS 479
Cdd:cd01663 402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGS 481
|
....*
gi 6019192 480 SSIEW 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: 835.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00167 11 NHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00167 91 DMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIIN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00167 171 MKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00167 251 FGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00167 331 KIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWT 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSSS 480
Cdd:MTH00167 411 KIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTST 490
|
490 500
....*....|....*....|.
gi 6019192 481 SIEWYQNLPPAEHSYNELPIL 501
Cdd:MTH00167 491 NVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 827.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00116 11 NHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00116 91 DMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCIN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00116 171 MKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00116 251 FGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00116 331 TIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWT 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSSS 480
Cdd:MTH00116 411 KAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTT 490
|
490 500
....*....|....*....|...
gi 6019192 481 SIEWYQNLPPAEHSYNELPILSN 503
Cdd:MTH00116 491 NIEWIHGCPPPYHTFEEPAFVQV 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: 827.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00142 9 NHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00142 89 DMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVIN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00142 169 MRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00142 249 FGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00142 329 KVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSSS 480
Cdd:MTH00142 409 KAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLST 488
|
490 500
....*....|....*....|...
gi 6019192 481 SIEWYQNLPPAEHSYNELPILSN 503
Cdd:MTH00142 489 SLEWSHRLPPDFHTYDELPILVV 511
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-499 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 817.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00223 8 NHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00223 88 DMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIIN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00223 168 MRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00223 248 FGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00223 328 KIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSSS 480
Cdd:MTH00223 408 KAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLST 487
|
490
....*....|....*....
gi 6019192 481 SIEWYQNLPPAEHSYNELP 499
Cdd:MTH00223 488 SLEWDNLLPADFHNNSETG 506
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-500 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 740.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00037 11 NHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00037 91 DMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIIN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00037 171 MRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00037 251 FGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00037 331 NLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSSS 480
Cdd:MTH00037 411 KVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSS 490
|
490 500
....*....|....*....|.
gi 6019192 481 SIEW-YQNLPPAEHSYNELPI 500
Cdd:MTH00037 491 SLEWqYSSFPPSHHTFDETPS 511
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-497 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 732.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00103 11 NHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00103 91 DMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIIN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00103 171 MKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00103 251 FGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00103 331 NIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSSS 480
Cdd:MTH00103 411 KIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTT 490
|
490
....*....|....*..
gi 6019192 481 SIEWYQNLPPAEHSYNE 497
Cdd:MTH00103 491 NLEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-497 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 727.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00183 11 NHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00183 91 DMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIIN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00183 171 MKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00183 251 FGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00183 331 SIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWT 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSSS 480
Cdd:MTH00183 411 KIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTST 490
|
490
....*....|....*..
gi 6019192 481 SIEWYQNLPPAEHSYNE 497
Cdd:MTH00183 491 NVEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-502 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 724.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00007 8 NHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00007 88 DMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVIN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00007 168 MRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00007 248 FGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00007 328 PIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSSS 480
Cdd:MTH00007 408 KAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSS 487
|
490 500
....*....|....*....|..
gi 6019192 481 SIEWYQNLPPAEHSYNELPILS 502
Cdd:MTH00007 488 SLEWQDTLPLDFHNLPETGIIT 509
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 723.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00077 11 NHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00077 91 DMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSIN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00077 171 MKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00077 251 FGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00077 331 AIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSSS 480
Cdd:MTH00077 411 KIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTST 490
|
490 500
....*....|....*....|...
gi 6019192 481 SIEWYQNLPPAEHSYNELPILSN 503
Cdd:MTH00077 491 NIEWLHGCPPPYHTFEEPSFVQT 513
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-504 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 675.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00182 13 NHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00182 93 DMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00182 173 MRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00182 253 FGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00182 333 TLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTI----FPL 476
Cdd:MTH00182 413 KIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIgwkeGTG 492
|
490 500
....*....|....*....|....*...
gi 6019192 477 NSSSSIEWYQNLPPAEHSYNELPILSNF 504
Cdd:MTH00182 493 ESWASLEWVHSSPPLFHTYNELPFVYKS 520
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-497 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 664.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00079 12 NHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSnIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00079 92 DMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00079 171 LRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00079 251 FGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00079 331 KMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSSS 480
Cdd:MTH00079 411 SAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINS 490
|
490
....*....|....*..
gi 6019192 481 SIEWYQNLPPAEHSYNE 497
Cdd:MTH00079 491 SPEYSLSSYVFGHSYQS 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: 662.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00184 13 NHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00184 93 DMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00184 173 MRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00184 253 FGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:MTH00184 333 SLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSS- 479
Cdd:MTH00184 413 KIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVGWVEDSg 492
|
490 500
....*....|....*....|..
gi 6019192 480 --SSIEWYQNLPPAEHSYNELP 499
Cdd:MTH00184 493 hyPSLEWAQTSPPAHHTYNELP 514
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
2-466 |
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: 583.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 2 HKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPlMLGAPD 81
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 82 MAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVINM 161
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 162 RSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 241
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 242 GMISHIISQESGKKeTFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQ 321
Cdd:cd00919 240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 322 INYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLLK 401
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6019192 402 IQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSM 466
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-501 |
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 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00026 12 NHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00026 92 DMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00026 172 MRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00026 252 FGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QIN--YSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPF 398
Cdd:MTH00026 332 GRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 399 LLKIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSM---------IIQ 469
Cdd:MTH00026 412 YGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYyreepfdinIMA 491
|
490 500 510
....*....|....*....|....*....|....*.
gi 6019192 470 QLTIFPLNSS----SSIEWYQNLPPAEHSYNELPIL 501
Cdd:MTH00026 492 KGPLIPFSCQpahfDTLEWSLTSPPEHHTYNELPYI 527
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-501 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 549.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAP 80
Cdd:COG0843 14 DHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:COG0843 93 DMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:COG0843 173 MRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKeTFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:COG0843 253 FGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:COG0843 332 RIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQ-LTIFPLN 477
Cdd:COG0843 412 KIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPkAGGNPWG 491
|
490 500
....*....|....*....|....
gi 6019192 478 sSSSIEWYQNLPPAEHSYNELPIL 501
Cdd:COG0843 492 -ARTLEWATPSPPPLYNFASIPVV 514
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-495 |
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 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMiGGFGNWLVPLMLGAP 80
Cdd:TIGR02891 5 DHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:TIGR02891 84 DMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:TIGR02891 164 MRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKeTFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:TIGR02891 244 FGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:TIGR02891 323 SIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQltIFPLN- 477
Cdd:TIGR02891 403 RWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP--KAGANp 480
|
490
....*....|....*....
gi 6019192 478 -SSSSIEWYQNLPPAEHSY 495
Cdd:TIGR02891 481 wGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-494 |
3.48e-172 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 494.97 E-value: 3.48e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAP 80
Cdd:MTH00048 12 DHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVenGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:MTH00048 92 DLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFdQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:MTH00048 170 AFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESGKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:MTH00048 249 FGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYS-PSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFL 399
Cdd:MTH00048 329 RVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 400 LKIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYISWNIVSSLGSYISLISVIMLLVIVWNSMIIQQLTIFPLNSS 479
Cdd:MTH00048 409 LQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLGLWGSS 488
|
490
....*....|....*
gi 6019192 480 SSIEWYQNLPPAEHS 494
Cdd:MTH00048 489 SCVVNVLMSPVPYHN 503
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-495 |
2.84e-166 |
|
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: 479.38 E-value: 2.84e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGM-SGSLIGNDQvYNTIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGA 79
Cdd:cd01662 6 DHKRIGIMYIITAFVFFLRGGVDALLMRTQLALpGNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 80 PDMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVI 159
Cdd:cd01662 84 RDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 160 NMRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 239
Cdd:cd01662 164 KMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 240 GFGMISHIISQESGKKeTFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHG 319
Cdd:cd01662 244 AFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 320 TQINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFL 399
Cdd:cd01662 323 GRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 400 LKIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYISWNIVSSLGSYISLISVIMLLVIVWNSmIIQQLTIFPLN 477
Cdd:cd01662 403 GKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVS-IRKGKRDATGD 481
|
490 500
....*....|....*....|
gi 6019192 478 S--SSSIEWYQNLPPAEHSY 495
Cdd:cd01662 482 PwgARTLEWATSSPPPAYNF 501
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
4-450 |
3.21e-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: 3.21e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 4 DIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPiMIGGFGNWLVPLMLGAPDMA 83
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 84 FPWLNNMSFWLLPPSLTLLISSSlveNGAGTGWTVYPPLSSniahagssVDLAIFSLHLAGISSILGAVNFITTVINMRS 163
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 164 YGMSFdQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 243
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 244 ISHIISQESGKKeTFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQIN 323
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 324 -YSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLLKI 402
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 6019192 403 QFLTMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYISWNIVSSLGSYI 450
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-504 |
4.76e-107 |
|
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: 332.59 E-value: 4.76e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTELGMSGSLIGNDQVYNTIVTAHAFIMIFFMVMPIMIGgFGNWLVPLMLGAP 80
Cdd:TIGR02882 49 DHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGAR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 81 DMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFITTVIN 160
Cdd:TIGR02882 128 DVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 161 MRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 240
Cdd:TIGR02882 208 MRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 241 FGMISHIISQESgKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 320
Cdd:TIGR02882 288 FGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 321 QINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSLNPFLL 400
Cdd:TIGR02882 367 KIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLG 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 401 KIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYISWNIVSSLGSYISLISVIMLLVIVWNSMII--QQLTIFPL 476
Cdd:TIGR02882 447 KWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKspREATGDPW 526
|
490 500
....*....|....*....|....*...
gi 6019192 477 NsSSSIEWYQNLPPAEHSYNELPILSNF 504
Cdd:TIGR02882 527 N-GRTLEWATASPPPKYNFAVTPDVNDY 553
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-499 |
9.92e-100 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 314.18 E-value: 9.92e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 1 NHKDIGTLYFIFGIWAGMVGTSLSLLIRTE-----LGMSGSLIGNDqvYNTIVTAHAFIMIFFMVMPIMIGgFGNWLVPL 75
Cdd:PRK15017 53 DHKRLGIMYIIVAIVMLLRGFADAIMMRSQqalasAGEAGFLPPHH--YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 76 MLGAPDMAFPWLNNMSFWLLPPSLTLLISSSLVENGAGTGWTVYPPLSSNIAHAGSSVDLAIFSLHLAGISSILGAVNFI 155
Cdd:PRK15017 130 QIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 156 TTVINMRSYGMSFDQMPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 235
Cdd:PRK15017 210 VTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYI 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 236 LILPGFGMISHIISQESgKKETFGCLGMIYAMMAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWLA 315
Cdd:PRK15017 290 LILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 316 TLHGTQINYSPSMMWSLGFVFLFTVGGLTGVILANSSIDVMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLSL 395
Cdd:PRK15017 369 TMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKL 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 396 NPFLLKIQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYISWNIVSSLGSYI----SLISVIMLLVIVWNSMIIQQ 470
Cdd:PRK15017 449 NETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALialgILCQVIQMYVSIRDRDQNRD 528
|
490 500
....*....|....*....|....*....
gi 6019192 471 LTIFPLnSSSSIEWYQNLPPAEHSYNELP 499
Cdd:PRK15017 529 LTGDPW-GGRTLEWATSSPPPFYNFAVVP 556
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
5-466 |
6.45e-20 |
|
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.
Pssm-ID: 238830 Cd Length: 473 Bit Score: 92.35 E-value: 6.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 5 IGTLYFIFGIWAGMvgtsLSLLIRTELGmsgSLIGNDQVYNTIVTAHAFIM-IFFMVMPIMigGFGNWLVPLMLGAPDMA 83
Cdd:cd01660 12 VAFLALLLGGLFGL----LQVLVRTGVF---PLPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 84 FPWLNnMSFWLLPpSLTLLISSSLVENGAGTGWTVYPPLssnIAHAGSSVDLAIFSLHlagiSSILGAVNFITTVINMRS 163
Cdd:cd01660 83 RRLAW-AGFWLMV-IGTVMAAVPILLGQASVLYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLWRWKKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 164 YGMSfdQMPLFVWAVAITALLLLLSLPVLAGAITMLLtdrnLNTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 243
Cdd:cd01660 154 NPGK--KVPLATFMVVTTMILWLVASLGVALEVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 244 ISHIISQESGKKeTFGCLGMIYAMMAIGLLGFVVWAHHMFT-VGMDIDTRAYFTSATMIIAVPTGIKIFSWLATL----- 317
Cdd:cd01660 227 WYTILPKIAGGK-LFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeiagr 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 318 --HG-------TQINYSPSMMWSLGFVFL-FTVGGLTGVILANSSIDVMLHDTYYVVAHFHyvLSMGAVFAIMA-GFIHW 386
Cdd:cd01660 306 lrGGkglfgwiRALPWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAYW 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6019192 387 Y-PLFTGLSL-NPFLLKIQFLTMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDAY-----ISWNIVSSLGSYISLISVIM 457
Cdd:cd01660 384 LvPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGAL 463
|
....*....
gi 6019192 458 LLVIVWNSM 466
Cdd:cd01660 464 FLYILFRTL 472
|
|
| |
