|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
9-488 |
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: 832.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 9 TNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVlsGNHQLFNVLVVGHAVLIIFFLVMPALIGGFGNYMLPLLI 88
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 89 GASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAINFIVT 168
Cdd:cd01663 79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 169 TLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPEVYILI 248
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 249 IPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLATI 327
Cdd:cd01663 239 LPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 328 YGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGLYYNE 407
Cdd:cd01663 319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 408 KLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLVNGLENKVNNK 487
Cdd:cd01663 399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVG 478
|
.
gi 50812101 488 S 488
Cdd:cd01663 479 E 479
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
4-528 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 755.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 4 RWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNqvLSGNHQLFNVLVVGHAVLIIFFLVMPALIGGFGNYM 83
Cdd:MTH00153 3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 84 LPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAI 163
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 164 NFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPE 243
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 244 VYILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFS 322
Cdd:MTH00153 241 VYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 323 WLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILG 402
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 403 LYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLVnglen 482
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMI----- 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 50812101 483 kvnnksviynkgpdfveSNQIFATNKIKSSSIEFLLTSPPAVHTFN 528
Cdd:MTH00153 476 -----------------SKRPVLFSLNLSSSIEWLQNLPPAEHSYS 504
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
4-479 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 589.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 4 RWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVLSGNHqlFNVLVVGHAVLIIFFLVMPaLIGGFGNYM 83
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 84 LPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAI 163
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 164 NFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPE 243
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 244 VYILIIPGFGIISHIVSTYSKKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSW 323
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 324 LATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGL 403
Cdd:COG0843 325 IATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGR 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50812101 404 YYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYP--DAFAGWNYVASIGSIIAVFSLFLFIYILYDQLVNG 479
Cdd:COG0843 405 MLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKG 482
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
6-527 |
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: 586.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 6 LYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVLSGnhQLFNVLVVGHAVLIIFFLVMPaLIGGFGNYMLP 85
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDA--ETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 86 LLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAINF 165
Cdd:TIGR02891 78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 166 IVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPEVY 245
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 246 ILIIPGFGIISHIVSTYSKKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLA 325
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 326 TIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGLYY 405
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 406 NEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDA--FAGWNYVASIGSIIAVFSLFLFIYILYDQLVNGlenk 483
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKG---- 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 50812101 484 vnnksviynkgpdfvesnQIFATNKIKSSSIEFLLTSPPAVHTF 527
Cdd:TIGR02891 474 ------------------PKAGANPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
13-460 |
5.39e-143 |
|
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: 418.90 E-value: 5.39e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 13 DIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVLSGnhQLFNVLVVGHAVLIIFFLVMPAlIGGFGNYMLPLLIGASD 92
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSP--LTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 93 MSFARLNNISFWCLPPALVCLVTSTlveSGAGTGWTVYPPLssiqahsgPSVDLAIFALHLTSISSLLGAINFIVTTLNM 172
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 173 RTNGMTMhRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNtsffevAGGGDPVLYQHLFWFFGHPEVYILIIPGF 252
Cdd:pfam00115 147 RAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 253 GIISHIVSTYSKKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLATIYGGSI 332
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 333 RLA-VPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGLYYNEKLAQ 411
Cdd:pfam00115 300 RFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 50812101 412 IQFWLIFVGANVIFLPMHFLGVNGMPRRIP----DYPDAFAGWNYVASIGSII 460
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
9-488 |
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: 832.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 9 TNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVlsGNHQLFNVLVVGHAVLIIFFLVMPALIGGFGNYMLPLLI 88
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 89 GASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAINFIVT 168
Cdd:cd01663 79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 169 TLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPEVYILI 248
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 249 IPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLATI 327
Cdd:cd01663 239 LPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 328 YGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGLYYNE 407
Cdd:cd01663 319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 408 KLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLVNGLENKVNNK 487
Cdd:cd01663 399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVG 478
|
.
gi 50812101 488 S 488
Cdd:cd01663 479 E 479
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
4-528 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 755.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 4 RWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNqvLSGNHQLFNVLVVGHAVLIIFFLVMPALIGGFGNYM 83
Cdd:MTH00153 3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 84 LPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAI 163
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 164 NFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPE 243
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 244 VYILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFS 322
Cdd:MTH00153 241 VYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 323 WLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILG 402
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 403 LYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLVnglen 482
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMI----- 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 50812101 483 kvnnksviynkgpdfveSNQIFATNKIKSSSIEFLLTSPPAVHTFN 528
Cdd:MTH00153 476 -----------------SKRPVLFSLNLSSSIEWLQNLPPAEHSYS 504
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-532 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 703.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 1 MIERWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNqvLSGNHQLFNVLVVGHAVLIIFFLVMPALIGGFG 80
Cdd:MTH00167 2 WINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 81 NYMLPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLL 160
Cdd:MTH00167 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 161 GAINFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFG 240
Cdd:MTH00167 160 GSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 241 HPEVYILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIK 319
Cdd:MTH00167 240 HPEVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 320 IFSWLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQ 399
Cdd:MTH00167 320 VFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 400 ILGLYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDqlvng 479
Cdd:MTH00167 400 FTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWE----- 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 50812101 480 lenkvnnkSVIYNKGPDFVESNqifatnkikSSSIEFLLTSPPAVHTFNTPAV 532
Cdd:MTH00167 475 --------AFSSKRKLLPVELT---------STNVEWLHGCPPPHHTWEEPPF 510
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
4-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 702.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 4 RWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGnqVLSGNHQLFNVLVVGHAVLIIFFLVMPALIGGFGNYM 83
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 84 LPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAI 163
Cdd:MTH00223 80 VPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 164 NFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPE 243
Cdd:MTH00223 160 NFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 244 VYILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFS 322
Cdd:MTH00223 240 VYILILPGFGMISHIVSHYSsKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 323 WLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILG 402
Cdd:MTH00223 320 WLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTG 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50812101 403 LYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLV 477
Cdd:MTH00223 400 VTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFV 474
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-531 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 684.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 1 MIERWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNqvLSGNHQLFNVLVVGHAVLIIFFLVMPALIGGFG 80
Cdd:MTH00116 2 FITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 81 NYMLPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLL 160
Cdd:MTH00116 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 161 GAINFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFG 240
Cdd:MTH00116 160 GAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 241 HPEVYILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIK 319
Cdd:MTH00116 240 HPEVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 320 IFSWLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQ 399
Cdd:MTH00116 320 VFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 400 ILGLYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLvng 479
Cdd:MTH00116 400 FTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAF--- 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 50812101 480 lenkvnnksviynkgpdfvESNQIFATNKIKSSSIEFLLTSPPAVHTFNTPA 531
Cdd:MTH00116 477 -------------------SSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPA 509
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
2-477 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 667.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 2 IERWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNqvLSGNHQLFNVLVVGHAVLIIFFLVMPALIGGFGN 81
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 82 YMLPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLG 161
Cdd:MTH00142 79 WLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 162 AINFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGH 241
Cdd:MTH00142 159 AINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 242 PEVYILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKI 320
Cdd:MTH00142 239 PEVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 321 FSWLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQI 400
Cdd:MTH00142 319 FSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLF 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50812101 401 LGLYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLV 477
Cdd:MTH00142 399 TGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFV 475
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
2-529 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 635.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 2 IERWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVlsGNHQLFNVLVVGHAVLIIFFLVMPALIGGFGN 81
Cdd:MTH00182 5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAML--GDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 82 YMLPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLG 161
Cdd:MTH00182 83 WLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 162 AINFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGH 241
Cdd:MTH00182 163 AINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 242 PEVYILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKI 320
Cdd:MTH00182 243 PEVYILILPGFGMISQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 321 FSWLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQI 400
Cdd:MTH00182 323 FSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 401 LGLYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLVNgl 480
Cdd:MTH00182 403 TGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVR-- 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 50812101 481 enkvNNKSVIYNKGPDfvesnqifatnkIKSSSIEFLLTSPPAVHTFNT 529
Cdd:MTH00182 481 ----EEKFIGWKEGTG------------ESWASLEWVHSSPPLFHTYNE 513
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
2-528 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 633.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 2 IERWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVlsGNHQLFNVLVVGHAVLIIFFLVMPALIGGFGN 81
Cdd:MTH00184 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSML--GDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 82 YMLPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLG 161
Cdd:MTH00184 83 WFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 162 AINFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGH 241
Cdd:MTH00184 163 AMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 242 PEVYILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKI 320
Cdd:MTH00184 243 PEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 321 FSWLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQI 400
Cdd:MTH00184 323 FSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 401 LGLYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQlvngl 480
Cdd:MTH00184 403 TGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDA----- 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 50812101 481 enkvnnksviYNKGPDFVEsnqiFATNKIKSSSIEFLLTSPPAVHTFN 528
Cdd:MTH00184 478 ----------YVREIKFVG----WVEDSGHYPSLEWAQTSPPAHHTYN 511
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-531 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 611.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 1 MIERWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNqvLSGNHQLFNVLVVGHAVLIIFFLVMPALIGGFG 80
Cdd:MTH00077 2 MITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 81 NYMLPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLL 160
Cdd:MTH00077 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 161 GAINFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFG 240
Cdd:MTH00077 160 GAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 241 HPEVYILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIK 319
Cdd:MTH00077 240 HPEVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 320 IFSWLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQ 399
Cdd:MTH00077 320 VFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 400 ILGLYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLvng 479
Cdd:MTH00077 400 FSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAF--- 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 50812101 480 lenkvnnksviynkgpdfvESNQIFATNKIKSSSIEFLLTSPPAVHTFNTPA 531
Cdd:MTH00077 477 -------------------SSKREVLTTELTSTNIEWLHGCPPPYHTFEEPS 509
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
4-476 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 607.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 4 RWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNqvLSGNHQLFNVLVVGHAVLIIFFLVMPALIGGFGNYM 83
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 84 LPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAI 163
Cdd:MTH00007 80 VPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 164 NFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPE 243
Cdd:MTH00007 160 NFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 244 VYILIIPGFGIISHIVSTYSKKP-VFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFS 322
Cdd:MTH00007 240 VYILILPGFGAISHIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 323 WLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILG 402
Cdd:MTH00007 320 WLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTG 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50812101 403 LYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQL 476
Cdd:MTH00007 400 LTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAF 473
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
5-504 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 606.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 5 WLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGnqVLSGNHQLFNVLVVGHAVLIIFFLVMPALIGGFGNYML 84
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWML 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 85 PLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSiQAHSGPSVDLAIFALHLTSISSLLGAIN 164
Cdd:MTH00079 85 PLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 165 FIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPEV 244
Cdd:MTH00079 164 FMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 245 YILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSW 323
Cdd:MTH00079 244 YILILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 324 LATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGL 403
Cdd:MTH00079 324 LATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 404 YYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLVNgleNK 483
Cdd:MTH00079 404 VYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFS---YR 480
|
490 500
....*....|....*....|.
gi 50812101 484 VNNKSVIYNKGPDFVESNQIF 504
Cdd:MTH00079 481 LVLHDNYINSSPEYSLSSYVF 501
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-531 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 606.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 1 MIERWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNqvLSGNHQLFNVLVVGHAVLIIFFLVMPALIGGFG 80
Cdd:MTH00183 2 AITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 81 NYMLPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLL 160
Cdd:MTH00183 80 NWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 161 GAINFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFG 240
Cdd:MTH00183 160 GAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 241 HPEVYILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIK 319
Cdd:MTH00183 240 HPEVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 320 IFSWLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQ 399
Cdd:MTH00183 320 VFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 400 ILGLYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLVNG 479
Cdd:MTH00183 400 FSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAK 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 50812101 480 LEnkvnnksviynkgpdfVESNQIFATNkiksssIEFLLTSPPAVHTFNTPA 531
Cdd:MTH00183 480 RE----------------VLSVELTSTN------VEWLHGCPPPYHTFEEPA 509
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-531 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 601.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 1 MIERWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNqvLSGNHQLFNVLVVGHAVLIIFFLVMPALIGGFG 80
Cdd:MTH00103 2 FINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 81 NYMLPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLL 160
Cdd:MTH00103 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 161 GAINFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFG 240
Cdd:MTH00103 160 GAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 241 HPEVYILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIK 319
Cdd:MTH00103 240 HPEVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 320 IFSWLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQ 399
Cdd:MTH00103 320 VFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 400 ILGLYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLVng 479
Cdd:MTH00103 400 FSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFA-- 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 50812101 480 lenkvnnksviynkgpdfveSNQIFATNKIKSSSIEFLLTSPPAVHTFNTPA 531
Cdd:MTH00103 478 --------------------SKREVLTVELTTTNLEWLHGCPPPYHTFEEPT 509
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
2-528 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 596.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 2 IERWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNqvLSGNHQLFNVLVVGHAVLIIFFLVMPALIGGFGN 81
Cdd:MTH00037 3 LSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 82 YMLPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLG 161
Cdd:MTH00037 81 WLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 162 AINFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGH 241
Cdd:MTH00037 161 SINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 242 PEVYILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKI 320
Cdd:MTH00037 241 PEVYILILPGFGMISHVIAHYSgKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 321 FSWLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQI 400
Cdd:MTH00037 321 FSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 401 LGLYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLVNGL 480
Cdd:MTH00037 401 SGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQR 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 50812101 481 ENKVNNKSviynkgpdfvesnqifatnkikSSSIEFLLTS-PPAVHTFN 528
Cdd:MTH00037 481 EVISPEFS----------------------SSSLEWQYSSfPPSHHTFD 507
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
11-476 |
0e+00 |
|
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.
Pssm-ID: 238461 Cd Length: 463 Bit Score: 592.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 11 AKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVLSGnhQLFNVLVVGHAVLIIFFLVMPALIGGFGNYMlPLLIGA 90
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDP--QLYNQLVTAHGVIMIFFFVMPAIFGGFGNLL-PPLIGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 91 SDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAINFIVTTL 170
Cdd:cd00919 78 RDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 171 NMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPEVYILIIP 250
Cdd:cd00919 158 NMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 251 GFGIISHIVSTYSKKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLATIYGG 330
Cdd:cd00919 238 AFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 331 SIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGLYYNEKLA 410
Cdd:cd00919 318 RIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50812101 411 QIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQL 476
Cdd:cd00919 398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
4-479 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 589.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 4 RWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVLSGNHqlFNVLVVGHAVLIIFFLVMPaLIGGFGNYM 83
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 84 LPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAI 163
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 164 NFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPE 243
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 244 VYILIIPGFGIISHIVSTYSKKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSW 323
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 324 LATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGL 403
Cdd:COG0843 325 IATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGR 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50812101 404 YYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYP--DAFAGWNYVASIGSIIAVFSLFLFIYILYDQLVNG 479
Cdd:COG0843 405 MLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKG 482
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
6-527 |
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: 586.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 6 LYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVLSGnhQLFNVLVVGHAVLIIFFLVMPaLIGGFGNYMLP 85
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDA--ETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 86 LLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAINF 165
Cdd:TIGR02891 78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 166 IVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPEVY 245
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 246 ILIIPGFGIISHIVSTYSKKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLA 325
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 326 TIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGLYY 405
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 406 NEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDA--FAGWNYVASIGSIIAVFSLFLFIYILYDQLVNGlenk 483
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKG---- 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 50812101 484 vnnksviynkgpdfvesnQIFATNKIKSSSIEFLLTSPPAVHTF 527
Cdd:TIGR02891 474 ------------------PKAGANPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
4-528 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 552.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 4 RWLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVlsGNHQLFNVLVVGHAVLIIFFLVMPALIGGFGNYM 83
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSML--GDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 84 LPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAI 163
Cdd:MTH00026 84 VPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 164 NFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPE 243
Cdd:MTH00026 164 NFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 244 VYILIIPGFGIISHIVSTYS-KKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFS 322
Cdd:MTH00026 244 VYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 323 WLATIYGGSIRL--AVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQI 400
Cdd:MTH00026 324 WLATVSGSGRNLifTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 401 LGLYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLVNGL 480
Cdd:MTH00026 404 TGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREE 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 50812101 481 ENKVNnksvIYNKGPDFVesnqiFATNKIKSSSIEFLLTSPPAVHTFN 528
Cdd:MTH00026 484 PFDIN----IMAKGPLIP-----FSCQPAHFDTLEWSLTSPPEHHTYN 522
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
5-473 |
1.77e-178 |
|
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: 511.74 E-value: 1.77e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 5 WLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVLSGNHqlFNVLVVGHAVLIIFFLVMPALIGgFGNYML 84
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 85 PLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAIN 164
Cdd:cd01662 78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 165 FIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPEV 244
Cdd:cd01662 158 FIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 245 YILIIPGFGIISHIVSTYSKKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWL 324
Cdd:cd01662 238 YILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 325 ATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGLY 404
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50812101 405 YNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYP--DAFAGWNYVASIGSIIAVFSLFLFIYILY 473
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVI 468
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
5-479 |
3.17e-155 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 452.98 E-value: 3.17e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 5 WLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVLSgnHQLFNVLVVGHAVLIIFFLVMPALIGGFGNYML 84
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVIS--LDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 85 PLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVesGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAIN 164
Cdd:MTH00048 85 PLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSIN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 165 FIvTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHPEV 244
Cdd:MTH00048 163 FI-CTIYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 245 YILIIPGFGIISHIVSTYSKKP-VFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSW 323
Cdd:MTH00048 242 YVLILPGFGIISHICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 324 LATIYGGSIRLAVPML-YAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILG 402
Cdd:MTH00048 322 LYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITG 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50812101 403 LYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLVNG 479
Cdd:MTH00048 402 LSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVK 478
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
13-460 |
5.39e-143 |
|
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: 418.90 E-value: 5.39e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 13 DIAVLYFIFAIFCGMAGTAMSLIIRLELAAPGNQVLSGnhQLFNVLVVGHAVLIIFFLVMPAlIGGFGNYMLPLLIGASD 92
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSP--LTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 93 MSFARLNNISFWCLPPALVCLVTSTlveSGAGTGWTVYPPLssiqahsgPSVDLAIFALHLTSISSLLGAINFIVTTLNM 172
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 173 RTNGMTMhRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNtsffevAGGGDPVLYQHLFWFFGHPEVYILIIPGF 252
Cdd:pfam00115 147 RAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 253 GIISHIVSTYSKKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLATIYGGSI 332
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 333 RLA-VPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGLYYNEKLAQ 411
Cdd:pfam00115 300 RFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 50812101 412 IQFWLIFVGANVIFLPMHFLGVNGMPRRIP----DYPDAFAGWNYVASIGSII 460
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
5-473 |
1.76e-104 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 327.66 E-value: 1.76e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 5 WLYSTNAKDIAVLYFIFAIFCGMAGTAMSLIIRLE--LAAPGNQVLSGNHQlFNVLVVGHAVLIIFFLVMPALIGgFGNY 82
Cdd:PRK15017 48 WLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 83 MLPLLIGASDMSFARLNNISFWCLPPALVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGA 162
Cdd:PRK15017 126 VVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 163 INFIVTTLNMRTNGMTMHRLPLFVWSIFITAFLLLLSLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPVLYQHLFWFFGHP 242
Cdd:PRK15017 206 INFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 243 EVYILIIPGFGIISHIVSTYSKKPVFGEVSMVYAMASIGLLGFLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFS 322
Cdd:PRK15017 286 EVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFN 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 323 WLATIYGGSIRLAVPMLYAIAFLFLFTIGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILG 402
Cdd:PRK15017 366 WLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFG 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50812101 403 LYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRIPDYPDA-FAGWNYVASIGSIIAVFSLFLFIYILY 473
Cdd:PRK15017 446 FKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPqFHTMLMIAASGAALIALGILCQVIQMY 517
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
228-477 |
7.69e-23 |
|
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: 101.59 E-value: 7.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 228 DPVLYQHLFWFFGHPEVYILIIPGFGIISHIVSTYSKKPVFGEvsmvyAMASIGLLGFLVWS-----HHMYI-VGLDADT 301
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSD-----PLARLAFILFLLFStpvgfHHQFAdPGIGPGW 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 302 RAYFTSATMIIAIPTGIKIFSWLATI-YGGSIRLAV-------------PMLYAIAF-LFLFTIGGLTGVALANASLDVA 366
Cdd:cd01660 275 KFIHMVLTFMVALPSLLTAFTVFASLeIAGRLRGGKglfgwiralpwgdPMFLALFLaMLMFIPGGAGGIINASYQLNYV 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50812101 367 FHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILG-LYYNEKLAQIQFWLIFVGANVIFLPMHFLGVNGMPRRI----- 440
Cdd:cd01660 355 VHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGrELAAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTaeaqy 434
|
250 260 270
....*....|....*....|....*....|....*....
gi 50812101 441 --PDYPDAFAGWNYVASIGSIIAVFSLFLFIYILYDQLV 477
Cdd:cd01660 435 ggLPAAGEWAPYQQLMAIGGTILFVSGALFLYILFRTLL 473
|
|
| |
