|
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 ... |
11-483 |
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: 729.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 11 TSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGpmFLHGNNQVFNVLVTGHAIAMIFLFVMPILIGSFGNYFLPIMI 90
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPG--SQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 91 GAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLGAINFIVT 170
Cdd:cd01663 79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 171 TLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGHPEVYIII 250
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 251 IPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIFSWLATL 329
Cdd:cd01663 239 LPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 330 YGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMFGLKYNK 409
Cdd:cd01663 319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 391224047 410 VLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTNGEN 483
Cdd:cd01663 399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRK 472
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
6-528 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 660.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 6 RWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFlhGNNQVFNVLVTGHAIAMIFLFVMPILIGSFGNYF 85
Cdd:MTH00153 3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLI--GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 86 LPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLGAI 165
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 166 NFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGHPE 245
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 246 VYIIIIPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIFS 324
Cdd:MTH00153 241 VYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 325 WLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMFG 404
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 405 LKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTNgene 484
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMIS---- 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 391224047 485 rEEIQVTPDYLESNntrdvrdsdLELITSRPAQYHTFSELPILI 528
Cdd:MTH00153 477 -KRPVLFSLNLSSS---------IEWLQNLPPAEHSYSELPLLT 510
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
8-482 |
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: 521.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 8 LFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFLhgNNQVFNVLVTGHAIAMIFLFVMPILIGsFGNYFLP 87
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPILAG-FGNYLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 88 IMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLGAINF 167
Cdd:TIGR02891 78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 168 IVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGHPEVY 247
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 248 IIIIPGFGIISHVISTYTKKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIFSWLA 327
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 328 TLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMFGLKY 407
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 391224047 408 NKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDA--FVGWNVVSSWGSIMSVISVLIGLYSVLVQLTNGE 482
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP 474
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
4-527 |
1.22e-180 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 518.53 E-value: 1.22e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 4 VTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFLhgNNQVFNVLVTGHAIAMIFLFVMPILIGsFGN 83
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLL--SPETYNQLFTMHGTIMIFFFATPFLAG-FGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 84 YFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLG 163
Cdd:COG0843 83 YLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 164 AINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGH 243
Cdd:COG0843 163 GVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 244 PEVYIIIIPGFGIISHVISTYTKKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIF 323
Cdd:COG0843 243 PEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 324 SWLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMF 403
Cdd:COG0843 323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 404 GLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYP--DAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTNG 481
Cdd:COG0843 403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKG 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 391224047 482 EnereeiQVTPDYLESNntrdvrdsDLELITSRPAQYHTFSELPIL 527
Cdd:COG0843 483 P------KAGGNPWGAR--------TLEWATPSPPPLYNFASIPVV 514
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
15-462 |
4.73e-127 |
|
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: 378.07 E-value: 4.73e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 15 DIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFLhgNNQVFNVLVTGHAIAMIFLFVMPILIGsFGNYFLPIMIGAVD 94
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 95 MAFARLNNISFWCLPPALVCVIASVlieTGAGTGWTVYPPLssisahsgPSVDLAIFAIHLTSISSLLGAINFIVTTLNM 174
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 175 RSIGIHMiDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGfyevaaGGDPILYEHLFYFFGHPEVYIIIIPGF 254
Cdd:pfam00115 147 RAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 255 GIISHVISTYTKKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIFSWLATLYGGEL 334
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 335 RLA-VPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMFGLKYNKVLAE 413
Cdd:pfam00115 300 RFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 391224047 414 VHYWLLFVSVNIIFLPMHFLGLNGMPRRIP----QYPDAFVGWNVVSSWGSIM 462
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 ... |
11-483 |
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: 729.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 11 TSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGpmFLHGNNQVFNVLVTGHAIAMIFLFVMPILIGSFGNYFLPIMI 90
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPG--SQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 91 GAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLGAINFIVT 170
Cdd:cd01663 79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 171 TLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGHPEVYIII 250
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 251 IPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIFSWLATL 329
Cdd:cd01663 239 LPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 330 YGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMFGLKYNK 409
Cdd:cd01663 319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 391224047 410 VLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTNGEN 483
Cdd:cd01663 399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRK 472
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
6-528 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 660.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 6 RWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFlhGNNQVFNVLVTGHAIAMIFLFVMPILIGSFGNYF 85
Cdd:MTH00153 3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLI--GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 86 LPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLGAI 165
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 166 NFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGHPE 245
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 246 VYIIIIPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIFS 324
Cdd:MTH00153 241 VYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 325 WLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMFG 404
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 405 LKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTNgene 484
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMIS---- 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 391224047 485 rEEIQVTPDYLESNntrdvrdsdLELITSRPAQYHTFSELPILI 528
Cdd:MTH00153 477 -KRPVLFSLNLSSS---------IEWLQNLPPAEHSYSELPLLT 510
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
3-527 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 639.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 3 YVTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPmfLHGNNQVFNVLVTGHAIAMIFLFVMPILIGSFG 82
Cdd:MTH00167 2 WINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 83 NYFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLL 162
Cdd:MTH00167 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 163 GAINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFG 242
Cdd:MTH00167 160 GSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 243 HPEVYIIIIPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIK 321
Cdd:MTH00167 240 HPEVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 322 IFSWLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPA 401
Cdd:MTH00167 320 VFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 402 MFGLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTNg 481
Cdd:MTH00167 400 FTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSS- 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 391224047 482 enereeiQVTPDYLESNNTrdvrdsDLELITSRPAQYHTFSELPIL 527
Cdd:MTH00167 479 -------KRKLLPVELTST------NVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
6-528 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 625.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 6 RWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGpMFLhGNNQVFNVLVTGHAIAMIFLFVMPILIGSFGNYF 85
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPG-ALL-GDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 86 LPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLGAI 165
Cdd:MTH00223 80 VPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 166 NFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGHPE 245
Cdd:MTH00223 160 NFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 246 VYIIIIPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIFS 324
Cdd:MTH00223 240 VYILILPGFGMISHIVSHYSsKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 325 WLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMFG 404
Cdd:MTH00223 320 WLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 405 LKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTngeNE 484
Cdd:MTH00223 400 VTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFV---SQ 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 391224047 485 REEIQVtpdylesnntrDVRDSDLELITSRPAQYHTFSELPILI 528
Cdd:MTH00223 477 RSVVWS-----------GHLSTSLEWDNLLPADFHNNSETGALV 509
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
2-530 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 609.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 2 SYVTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPmfLHGNNQVFNVLVTGHAIAMIFLFVMPILIGSF 81
Cdd:MTH00116 1 MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 82 GNYFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSL 161
Cdd:MTH00116 79 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 162 LGAINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFF 241
Cdd:MTH00116 159 LGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 242 GHPEVYIIIIPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGI 320
Cdd:MTH00116 239 GHPEVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 321 KIFSWLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGP 400
Cdd:MTH00116 319 KVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 401 AMFGLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTn 480
Cdd:MTH00116 399 LFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFS- 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 391224047 481 geNEREEIQVTPDylesnntrdvrDSDLELITSRPAQYHTFSELPILIQQ 530
Cdd:MTH00116 478 --SKRKVLQPELT-----------TTNIEWIHGCPPPYHTFEEPAFVQVQ 514
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
4-529 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 604.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 4 VTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFlhGNNQVFNVLVTGHAIAMIFLFVMPILIGSFGN 83
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLL--GDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 84 YFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLG 163
Cdd:MTH00142 79 WLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 164 AINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGH 243
Cdd:MTH00142 159 AINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 244 PEVYIIIIPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKI 322
Cdd:MTH00142 239 PEVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 323 FSWLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAM 402
Cdd:MTH00142 319 FSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 403 FGLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTNge 482
Cdd:MTH00142 399 TGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVS-- 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 391224047 483 nerEEIQVTPDYLESNntrdvrdsdLELITSRPAQYHTFSELPILIQ 529
Cdd:MTH00142 477 ---QRLVMWSSHLSTS---------LEWSHRLPPDFHTYDELPILVV 511
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-525 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 563.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 1 MSYVTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFlhGNNQVFNVLVTGHAIAMIFLFVMPILIGS 80
Cdd:MTH00184 2 SLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSML--GDDHLYNVIVTAHAFVMIFFLVMPVMIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 81 FGNYFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISS 160
Cdd:MTH00184 80 FGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 161 LLGAINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYF 240
Cdd:MTH00184 160 ILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 241 FGHPEVYIIIIPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTG 319
Cdd:MTH00184 240 FGHPEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 320 IKIFSWLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWG 399
Cdd:MTH00184 320 IKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 400 PAMFGLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLT 479
Cdd:MTH00184 400 GKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYV 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 391224047 480 NGENEREEIQVTPDYlesnntrdvrdSDLELITSRPAQYHTFSELP 525
Cdd:MTH00184 480 REIKFVGWVEDSGHY-----------PSLEWAQTSPPAHHTYNELP 514
|
|
| 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: 561.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 2 SYVTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFlhGNNQVFNVLVTGHAIAMIFLFVMPILIGSF 81
Cdd:MTH00182 3 LYLTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAML--GDDHLYNVIVTAHAFIMIFFLVMPVMIGGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 82 GNYFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSL 161
Cdd:MTH00182 81 GNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 162 LGAINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFF 241
Cdd:MTH00182 161 LGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 242 GHPEVYIIIIPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGI 320
Cdd:MTH00182 241 GHPEVYILILPGFGMISQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 321 KIFSWLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGP 400
Cdd:MTH00182 321 KVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 401 AMFGLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTn 480
Cdd:MTH00182 401 KITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYV- 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 391224047 481 geneREEiqvtpDYLESNNTRDVRDSDLELITSRPAQYHTFSELPILIQ 529
Cdd:MTH00182 480 ----REE-----KFIGWKEGTGESWASLEWVHSSPPLFHTYNELPFVYK 519
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
4-529 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 548.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 4 VTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFlhGNNQVFNVLVTGHAIAMIFLFVMPILIGSFGN 83
Cdd:MTH00183 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 84 YFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLG 163
Cdd:MTH00183 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 164 AINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGH 243
Cdd:MTH00183 161 AINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 244 PEVYIIIIPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKI 322
Cdd:MTH00183 241 PEVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 323 FSWLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAM 402
Cdd:MTH00183 321 FSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 403 FGLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTnge 482
Cdd:MTH00183 401 SGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFA--- 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 391224047 483 NEREEIQVtpdylesnntrDVRDSDLELITSRPAQYHTFSElPILIQ 529
Cdd:MTH00183 478 AKREVLSV-----------ELTSTNVEWLHGCPPPYHTFEE-PAFVQ 512
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
6-472 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 544.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 6 RWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFlhGNNQVFNVLVTGHAIAMIFLFVMPILIGSFGNYF 85
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFL--GSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 86 LPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLGAI 165
Cdd:MTH00007 80 VPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 166 NFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGHPE 245
Cdd:MTH00007 160 NFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 246 VYIIIIPGFGIISHVISTYTKKP-IFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIFS 324
Cdd:MTH00007 240 VYILILPGFGAISHIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 325 WLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMFG 404
Cdd:MTH00007 320 WLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 391224047 405 LKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLY 472
Cdd:MTH00007 400 LTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIF 467
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
4-530 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 542.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 4 VTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFlhGNNQVFNVLVTGHAIAMIFLFVMPILIGSFGN 83
Cdd:MTH00077 3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 84 YFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLG 163
Cdd:MTH00077 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 164 AINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGH 243
Cdd:MTH00077 161 AINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 244 PEVYIIIIPGFGIISHVISTY-TKKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKI 322
Cdd:MTH00077 241 PEVYILILPGFGMISHIVTYYsAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 323 FSWLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAM 402
Cdd:MTH00077 321 FSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 403 FGLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYsVLVQLTNGE 482
Cdd:MTH00077 401 SGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMF-IIWEAFSSK 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 391224047 483 NEREEIQVTPdylesnntrdvrdSDLELITSRPAQYHTFSELPILIQQ 530
Cdd:MTH00077 480 REVLTTELTS-------------TNIEWLHGCPPPYHTFEEPSFVQTR 514
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
3-528 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 539.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 3 YVTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFlhGNNQVFNVLVTGHAIAMIFLFVMPILIGSFG 82
Cdd:MTH00037 2 QLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLL--QDDQIYNVIVTAHALVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 83 NYFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLL 162
Cdd:MTH00037 80 NWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 163 GAINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFG 242
Cdd:MTH00037 160 ASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 243 HPEVYIIIIPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIK 321
Cdd:MTH00037 240 HPEVYILILPGFGMISHVIAHYSgKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 322 IFSWLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPA 401
Cdd:MTH00037 320 VFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 402 MFGLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTNG 481
Cdd:MTH00037 400 FSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQ 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 391224047 482 ENereeiQVTPDYLESNntrdvrdsdLEL-ITSRPAQYHTFSELPILI 528
Cdd:MTH00037 480 RE-----VISPEFSSSS---------LEWqYSSFPPSHHTFDETPSTV 513
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
3-523 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 537.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 3 YVTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFlhGNNQVFNVLVTGHAIAMIFLFVMPILIGSFG 82
Cdd:MTH00103 2 FINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 83 NYFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLL 162
Cdd:MTH00103 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 163 GAINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFG 242
Cdd:MTH00103 160 GAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 243 HPEVYIIIIPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIK 321
Cdd:MTH00103 240 HPEVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 322 IFSWLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPA 401
Cdd:MTH00103 320 VFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 402 MFGLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTng 481
Cdd:MTH00103 400 FSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFA-- 477
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 391224047 482 eNEREEIQVtpdylesnntrDVRDSDLELITSRPAQYHTFSE 523
Cdd:MTH00103 478 -SKREVLTV-----------ELTTTNLEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-475 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 536.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 1 MSYVTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGpmFLHGNNQVFNVLVTGHAIAMIFLFVMPILIGS 80
Cdd:MTH00079 1 QGGLSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 81 FGNYFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSiSAHSGPSVDLAIFAIHLTSISS 160
Cdd:MTH00079 79 FGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 161 LLGAINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYF 240
Cdd:MTH00079 158 ILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 241 FGHPEVYIIIIPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTG 319
Cdd:MTH00079 238 FGHPEVYILILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 320 IKIFSWLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWG 399
Cdd:MTH00079 318 VKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWW 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 391224047 400 PAMFGLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVL 475
Cdd:MTH00079 398 PFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLL 473
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
13-478 |
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: 529.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 13 HKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFLhgNNQVFNVLVTGHAIAMIFLFVMPILIGSFGNYFLPiMIGA 92
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFL--DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 93 VDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLGAINFIVTTL 172
Cdd:cd00919 78 RDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 173 NMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGHPEVYIIIIP 252
Cdd:cd00919 158 NMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 253 GFGIISHVISTYTKKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIFSWLATLYGG 332
Cdd:cd00919 238 AFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 333 ELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMFGLKYNKVLA 412
Cdd:cd00919 318 RIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 391224047 413 EVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQL 478
Cdd:cd00919 398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
8-482 |
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: 521.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 8 LFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFLhgNNQVFNVLVTGHAIAMIFLFVMPILIGsFGNYFLP 87
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPILAG-FGNYLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 88 IMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLGAINF 167
Cdd:TIGR02891 78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 168 IVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGHPEVY 247
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 248 IIIIPGFGIISHVISTYTKKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIFSWLA 327
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 328 TLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMFGLKY 407
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 391224047 408 NKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDA--FVGWNVVSSWGSIMSVISVLIGLYSVLVQLTNGE 482
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP 474
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
4-527 |
1.22e-180 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 518.53 E-value: 1.22e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 4 VTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFLhgNNQVFNVLVTGHAIAMIFLFVMPILIGsFGN 83
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLL--SPETYNQLFTMHGTIMIFFFATPFLAG-FGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 84 YFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLG 163
Cdd:COG0843 83 YLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 164 AINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGH 243
Cdd:COG0843 163 GVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 244 PEVYIIIIPGFGIISHVISTYTKKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIF 323
Cdd:COG0843 243 PEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 324 SWLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMF 403
Cdd:COG0843 323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 404 GLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYP--DAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTNG 481
Cdd:COG0843 403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKG 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 391224047 482 EnereeiQVTPDYLESNntrdvrdsDLELITSRPAQYHTFSELPIL 527
Cdd:COG0843 483 P------KAGGNPWGAR--------TLEWATPSPPPLYNFASIPVV 514
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-528 |
1.90e-172 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 497.61 E-value: 1.90e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 1 MSYVTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFlhGNNQVFNVLVTGHAIAMIFLFVMPILIGS 80
Cdd:MTH00026 1 MTSFVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSML--GDDHLYNVIVTAHAFVMIFFLVMPTMIGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 81 FGNYFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISS 160
Cdd:MTH00026 79 FGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 161 LLGAINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYF 240
Cdd:MTH00026 159 ILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 241 FGHPEVYIIIIPGFGIISHVISTYT-KKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTG 319
Cdd:MTH00026 239 FGHPEVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 320 IKIFSWLATLYGG--ELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYY 397
Cdd:MTH00026 319 IKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 398 WGPAMFGLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVlIGLYSVLVQ 477
Cdd:MTH00026 399 WFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAV-IWFIVVIFD 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 391224047 478 LTNGENEREEIQVTPDYLESNNTRDVRDSDLELITSRPAQYHTFSELPILI 528
Cdd:MTH00026 478 AYYREEPFDINIMAKGPLIPFSCQPAHFDTLEWSLTSPPEHHTYNELPYIV 528
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
7-484 |
1.09e-156 |
|
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: 456.27 E-value: 1.09e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 7 WLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFLHgnNQVFNVLVTGHAIAMIFLFVMPILIGsFGNYFL 86
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLS--PEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 87 PIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISSLLGAIN 166
Cdd:cd01662 78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 167 FIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYFFGHPEV 246
Cdd:cd01662 158 FIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 247 YIIIIPGFGIISHVISTYTKKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIFSWL 326
Cdd:cd01662 238 YILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 327 ATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMFGLK 406
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 407 YNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYP--DAFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTNGENE 484
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRD 477
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-481 |
1.51e-134 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 399.82 E-value: 1.51e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 1 MSYVTRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLELSGPgpMFLHGNNQVFNVLVTGHAIAMIFLFVMPILIGS 80
Cdd:MTH00048 1 MNSLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDP--YYNVISLDVYNFLITNHGIIMIFFFLMPVLIGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 81 FGNYFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIetGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSISS 160
Cdd:MTH00048 79 FGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 161 LLGAINFIVTTLNMRSIGIhMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFYF 240
Cdd:MTH00048 157 LFGSINFICTIYSAFMTNV-FSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 241 FGHPEVYIIIIPGFGIISHVISTYTKKP-IFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTG 319
Cdd:MTH00048 236 FGHPEVYVLILPGFGIISHICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 320 IKIFSWLATLYGGELRLAVP-MLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYW 398
Cdd:MTH00048 316 IKVFSWLYMLLNSRVRKSDPvVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWW 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 399 GPAMFGLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPDAFVGWNVVSSWGSIMSVISVLIGLYSVLVQL 478
Cdd:MTH00048 396 WPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESL 475
|
...
gi 391224047 479 TNG 481
Cdd:MTH00048 476 VVK 478
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
15-462 |
4.73e-127 |
|
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: 378.07 E-value: 4.73e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 15 DIGILYLIYGMVSAMVATGMSVIIRLELSGPGPMFLhgNNQVFNVLVTGHAIAMIFLFVMPILIGsFGNYFLPIMIGAVD 94
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 95 MAFARLNNISFWCLPPALVCVIASVlieTGAGTGWTVYPPLssisahsgPSVDLAIFAIHLTSISSLLGAINFIVTTLNM 174
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 175 RSIGIHMiDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGfyevaaGGDPILYEHLFYFFGHPEVYIIIIPGF 254
Cdd:pfam00115 147 RAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 255 GIISHVISTYTKKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTGIKIFSWLATLYGGEL 334
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 335 RLA-VPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWGPAMFGLKYNKVLAE 413
Cdd:pfam00115 300 RFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 391224047 414 VHYWLLFVSVNIIFLPMHFLGLNGMPRRIP----QYPDAFVGWNVVSSWGSIM 462
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
5-525 |
1.85e-90 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 290.68 E-value: 1.85e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 5 TRWLFSTSHKDIGILYLIYGMVSAMVATGMSVIIRLE--LSGPGPM-FL--HGNNQVFnvlvTGHAIAMIFLFVMPILIG 79
Cdd:PRK15017 46 KEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAgFLppHHYDQIF----TAHGVIMIFFVAMPFVIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 80 sFGNYFLPIMIGAVDMAFARLNNISFWCLPPALVCVIASVLIETGAGTGWTVYPPLSSISAHSGPSVDLAIFAIHLTSIS 159
Cdd:PRK15017 122 -LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 160 SLLGAINFIVTTLNMRSIGIHMIDMPLFVWAIFFTAILLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPILYEHLFY 239
Cdd:PRK15017 201 TTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 240 FFGHPEVYIIIIPGFGIISHVISTYTKKPIFGQIGMIYAIGSIGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVIAIPTG 319
Cdd:PRK15017 281 AWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 320 IKIFSWLATLYGGELRLAVPMLFALGFLFLFTIGGLTGVMLSNASIDVAFHDTYYVVGHFHYVLSMGALFSLIAGYYYWG 399
Cdd:PRK15017 361 VKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWW 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 400 PAMFGLKYNKVLAEVHYWLLFVSVNIIFLPMHFLGLNGMPRRIPQYPD-AFVGWNVVSSWGSIMSVISVLIGLYSVLVQL 478
Cdd:PRK15017 441 PKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSI 520
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 391224047 479 TNGENEREeiqVTPDYLESNNtrdvrdsdLELITSRPAQYHTFSELP 525
Cdd:PRK15017 521 RDRDQNRD---LTGDPWGGRT--------LEWATSSPPPFYNFAVVP 556
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
230-474 |
1.18e-09 |
|
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: 60.38 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 230 DPILYEHLFYFFGHPEVYIIIIPGfgiishVISTYTKKP-IFGqiGMIY--AIGSIGLLGFLVWS-----HHMYV-VGLD 300
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPA------YIAWYTILPkIAG--GKLFsdPLARLAFILFLLFStpvgfHHQFAdPGIG 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 301 IDSRAYFTSATMVIAIPT-------------------GIKIFSWLATLYGGELRLAVPMLFALGFLflftIGGLTGVMLS 361
Cdd:cd01660 272 PGWKFIHMVLTFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALFLAMLMFI----PGGAGGIINA 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 362 NASIDVAFHDTYYVVGHFHyvLSMGALFSL--IAGYYYWGPAMFGLKY-NKVLAEVHYWLLFVSVNIIFLPMHFLGLNGM 438
Cdd:cd01660 348 SYQLNYVVHNTAWVPGHFH--LTVGGAVALtfMAVAYWLVPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGA 425
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 391224047 439 PRR--IPQYPDAFV-----GWNVVSSWGSIMSVISVLIGLYSV 474
Cdd:cd01660 426 PRRtaEAQYGGLPAagewaPYQQLMAIGGTILFVSGALFLYIL 468
|
|
| PRK14485 |
PRK14485 |
putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional |
357-528 |
3.44e-03 |
|
putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional
Pssm-ID: 184703 [Multi-domain] Cd Length: 712 Bit Score: 40.06 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 357 GVMLSNASIDVAFHDTYYVVGHFHyvlsMGAL----FsLIAGYYYW-GPAMFGLK-YNKVLAEVHYWLLFVSVNIIFLPM 430
Cdd:PRK14485 323 GPMLSLKNVNAIAHYTDWIIAHVH----VGALgwngF-LTFGMLYWlLPRLFKTKlYSTKLANFHFWIGTLGIILYALPM 397
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391224047 431 HFLGL-NGM------PRRIPQYPD------AFVGWNVVSSWGSIMSVISVLIGLYSVLVQLTNGENEREEIQVTPDYLES 497
Cdd:PRK14485 398 YVAGFtQGLmwkeftPDGTLAYPNfletvlAIRPMYWMRAIGGSLYLVGMIVMAYNIIKTVRAGSAVENELAEAAPLTKV 477
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170 180 190
....*....|....*....|....*....|.
gi 391224047 498 NNTRDVRDSDLELITSRPAQYHTFSELPILI 528
Cdd:PRK14485 478 YHPRASGEKWHRWLERKPIQLTVLTTIAILI 508
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