|
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 ... |
9-479 |
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: 804.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 9 TNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQQylHGNNQLFNVLVVGHAILMIFFMVMPALIGGFGNYMLPLMI 88
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQ--LGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 89 GATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLGAINFIVT 168
Cdd:cd01663 79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 169 TLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGHPEVYILI 248
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 249 IPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLATI 327
Cdd:cd01663 239 LPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 328 YGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQILGLYYNE 407
Cdd:cd01663 319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21263115 408 KLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLVNG 479
Cdd:cd01663 399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSG 470
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
2-528 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 738.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 2 LQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFGN 81
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 82 YMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLG 161
Cdd:MTH00153 79 WLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 162 AINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGH 241
Cdd:MTH00153 159 AINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 242 PEVYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKI 320
Cdd:MTH00153 239 PEVYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 321 FSWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQI 400
Cdd:MTH00153 319 FSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 401 LGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLvngl 480
Cdd:MTH00153 399 TGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESM---- 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 21263115 481 tnkINNKAVVFYktpdfmeSNMvfntntvkSSSLEFLLTSPPAVHSFN 528
Cdd:MTH00153 475 ---ISKRPVLFS-------LNL--------SSSIEWLQNLPPAEHSYS 504
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-479 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 570.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 2 LQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQQYLhgNNQLFNVLVVGHAILMIFFMVMPaLIGGFGN 81
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLL--SPETYNQLFTMHGTIMIFFFATP-FLAGFGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 82 YMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLG 161
Cdd:COG0843 83 YLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 162 AINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGH 241
Cdd:COG0843 163 GVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 242 PEVYILIIPGFGIISHVVSTYSKKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIF 321
Cdd:COG0843 243 PEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 322 SWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQIL 401
Cdd:COG0843 323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 402 GLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYP--DAFAGWNYISSIGAVVSMISLLLFVYILYDQLVNG 479
Cdd:COG0843 403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKG 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: 569.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 6 LYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQQYLhgNNQLFNVLVVGHAILMIFFMVMPaLIGGFGNYMLP 85
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 86 LMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLGAINF 165
Cdd:TIGR02891 78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 166 IVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGHPEVY 245
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 246 ILIIPGFGIISHVVSTYSKKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLA 325
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 326 TIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQILGLYY 405
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 406 NEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDA--FAGWNYISSIGAVVSMISLLLFVYILYDQLVNGltnk 483
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKG---- 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 21263115 484 innkavvfyktpdfmesnMVFNTNTVKSSSLEFLLTSPPAVHSF 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 |
1.61e-137 |
|
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: 404.65 E-value: 1.61e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 13 DIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQQYLhgNNQLFNVLVVGHAILMIFFMVMPAlIGGFGNYMLPLMIGATD 92
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 93 TAFPRINNIGFWLLPMGLVCLVTSTlveSGAGTGWTVYPPLasiqahsgPSVDLAIFALHMTSISSLLGAINFIVTTLNM 172
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 173 RTNGMTMhKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNtsffevAGGGDPILYEHLFWFFGHPEVYILIIPGF 252
Cdd:pfam00115 147 RAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 253 GIISHVVSTYSKKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLATIYGGSI 332
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 333 RLA-TPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQILGLYYNEKLSQ 411
Cdd:pfam00115 300 RFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 21263115 412 IQFWLIFVGANMVFLPMHFLGINGMPRRIP----DYPDAFAGWNYISSIGAVV 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 ... |
9-479 |
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: 804.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 9 TNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQQylHGNNQLFNVLVVGHAILMIFFMVMPALIGGFGNYMLPLMI 88
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQ--LGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 89 GATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLGAINFIVT 168
Cdd:cd01663 79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 169 TLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGHPEVYILI 248
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 249 IPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLATI 327
Cdd:cd01663 239 LPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 328 YGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQILGLYYNE 407
Cdd:cd01663 319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21263115 408 KLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLVNG 479
Cdd:cd01663 399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSG 470
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
2-528 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 738.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 2 LQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFGN 81
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 82 YMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLG 161
Cdd:MTH00153 79 WLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 162 AINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGH 241
Cdd:MTH00153 159 AINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 242 PEVYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKI 320
Cdd:MTH00153 239 PEVYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 321 FSWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQI 400
Cdd:MTH00153 319 FSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 401 LGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLvngl 480
Cdd:MTH00153 399 TGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESM---- 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 21263115 481 tnkINNKAVVFYktpdfmeSNMvfntntvkSSSLEFLLTSPPAVHSFN 528
Cdd:MTH00153 475 ---ISKRPVLFS-------LNL--------SSSIEWLQNLPPAEHSYS 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: 680.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 1 MLQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFG 80
Cdd:MTH00167 2 WINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 81 NYMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLL 160
Cdd:MTH00167 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 161 GAINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFG 240
Cdd:MTH00167 160 GSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 241 HPEVYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIK 319
Cdd:MTH00167 240 HPEVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 320 IFSWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQ 399
Cdd:MTH00167 320 VFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 400 ILGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLVng 479
Cdd:MTH00167 400 FTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFS-- 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 21263115 480 ltnkinnkavvfyktpdfmeSNMVFNTNTVKSSSLEFLLTSPPAVHSFNTPAV 532
Cdd:MTH00167 478 --------------------SKRKLLPVELTSTNVEWLHGCPPPHHTWEEPPF 510
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
4-527 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 669.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 4 RWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFGNYM 83
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGA--LLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 84 LPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLGAI 163
Cdd:MTH00223 80 VPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 164 NFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGHPE 243
Cdd:MTH00223 160 NFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 244 VYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFS 322
Cdd:MTH00223 240 VYILILPGFGMISHIVSHYSsKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 323 WLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQILG 402
Cdd:MTH00223 320 WLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 403 LYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLvngltn 482
Cdd:MTH00223 400 VTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAF------ 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 21263115 483 kINNKAVVFYKTPdfmesnmvfntntvkSSSLEFLLTSPPAVHSF 527
Cdd:MTH00223 474 -VSQRSVVWSGHL---------------STSLEWDNLLPADFHNN 502
|
|
| 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: 668.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 1 MLQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFG 80
Cdd:MTH00116 2 FITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 81 NYMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLL 160
Cdd:MTH00116 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 161 GAINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFG 240
Cdd:MTH00116 160 GAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 241 HPEVYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIK 319
Cdd:MTH00116 240 HPEVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 320 IFSWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQ 399
Cdd:MTH00116 320 VFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 400 ILGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQlvng 479
Cdd:MTH00116 400 FTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEA---- 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 21263115 480 ltnkinnkavvfyktpdfMESNMVFNTNTVKSSSLEFLLTSPPAVHSFNTPA 531
Cdd:MTH00116 476 ------------------FSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPA 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: 649.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 2 LQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFGN 81
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 82 YMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLG 161
Cdd:MTH00142 79 WLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 162 AINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGH 241
Cdd:MTH00142 159 AINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 242 PEVYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKI 320
Cdd:MTH00142 239 PEVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 321 FSWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQI 400
Cdd:MTH00142 319 FSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLF 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21263115 401 LGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLV 477
Cdd:MTH00142 399 TGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFV 475
|
|
| 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: 617.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 2 LQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFGN 81
Cdd:MTH00184 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 82 YMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLG 161
Cdd:MTH00184 83 WFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 162 AINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGH 241
Cdd:MTH00184 163 AMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 242 PEVYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKI 320
Cdd:MTH00184 243 PEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 321 FSWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQI 400
Cdd:MTH00184 323 FSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 401 LGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLVngl 480
Cdd:MTH00184 403 TGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYV--- 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 21263115 481 tnkinnKAVVFYKTPDfmesnmvfntNTVKSSSLEFLLTSPPAVHSFN 528
Cdd:MTH00184 480 ------REIKFVGWVE----------DSGHYPSLEWAQTSPPAHHTYN 511
|
|
| 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: 613.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 2 LQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFGN 81
Cdd:MTH00182 5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 82 YMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLG 161
Cdd:MTH00182 83 WLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 162 AINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGH 241
Cdd:MTH00182 163 AINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 242 PEVYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKI 320
Cdd:MTH00182 243 PEVYILILPGFGMISQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 321 FSWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQI 400
Cdd:MTH00182 323 FSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 401 LGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDqlvngl 480
Cdd:MTH00182 403 TGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYD------ 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 21263115 481 tnkinnkavVFYKTPDFMESNmvfNTNTVKSSSLEFLLTSPPAVHSFNT 529
Cdd:MTH00182 477 ---------AYVREEKFIGWK---EGTGESWASLEWVHSSPPLFHTYNE 513
|
|
| 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: 596.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 4 RWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFGNYM 83
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 84 LPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLGAI 163
Cdd:MTH00007 80 VPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 164 NFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGHPE 243
Cdd:MTH00007 160 NFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 244 VYILIIPGFGIISHVVSTYSKKP-VFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFS 322
Cdd:MTH00007 240 VYILILPGFGAISHIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 323 WLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQILG 402
Cdd:MTH00007 320 WLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTG 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21263115 403 LYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQL 476
Cdd:MTH00007 400 LTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAF 473
|
|
| 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: 594.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 1 MLQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFG 80
Cdd:MTH00077 2 MITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 81 NYMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLL 160
Cdd:MTH00077 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 161 GAINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFG 240
Cdd:MTH00077 160 GAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 241 HPEVYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIK 319
Cdd:MTH00077 240 HPEVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 320 IFSWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQ 399
Cdd:MTH00077 320 VFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 400 ILGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLvng 479
Cdd:MTH00077 400 FSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAF--- 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 21263115 480 ltnkinnkavvfyktpdfmESNMVFNTNTVKSSSLEFLLTSPPAVHSFNTPA 531
Cdd:MTH00077 477 -------------------SSKREVLTTELTSTNIEWLHGCPPPYHTFEEPS 509
|
|
| 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: 592.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 1 MLQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFG 80
Cdd:MTH00183 2 AITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 81 NYMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLL 160
Cdd:MTH00183 80 NWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 161 GAINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFG 240
Cdd:MTH00183 160 GAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 241 HPEVYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIK 319
Cdd:MTH00183 240 HPEVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 320 IFSWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQ 399
Cdd:MTH00183 320 VFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 400 ILGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDqlvng 479
Cdd:MTH00183 400 FSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWE----- 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 21263115 480 ltnkinnkavVFYKTPDFMESNMVfntntvkSSSLEFLLTSPPAVHSFNTPA 531
Cdd:MTH00183 475 ----------AFAAKREVLSVELT-------STNVEWLHGCPPPYHTFEEPA 509
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
2-528 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 591.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 2 LQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGqqYLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFGN 81
Cdd:MTH00079 4 LSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 82 YMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLaSIQAHSGPSVDLAIFALHMTSISSLLG 161
Cdd:MTH00079 82 WMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 162 AINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGH 241
Cdd:MTH00079 161 GINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 242 PEVYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKI 320
Cdd:MTH00079 241 PEVYILILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 321 FSWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQI 400
Cdd:MTH00079 321 FSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 401 LGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQlvngl 480
Cdd:MTH00079 401 TGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLES----- 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 21263115 481 tnkinnkavvfyktpdFMESNMVFNTNTVKSSSlEFLLTSPPAVHSFN 528
Cdd:MTH00079 476 ----------------FFSYRLVLHDNYINSSP-EYSLSSYVFGHSYQ 506
|
|
| 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: 585.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 1 MLQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFG 80
Cdd:MTH00103 2 FINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 81 NYMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLL 160
Cdd:MTH00103 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 161 GAINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFG 240
Cdd:MTH00103 160 GAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 241 HPEVYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIK 319
Cdd:MTH00103 240 HPEVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 320 IFSWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQ 399
Cdd:MTH00103 320 VFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 400 ILGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLVng 479
Cdd:MTH00103 400 FSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFA-- 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 21263115 480 ltnkiNNKAVVFYKTPdfmesnmvfntntvkSSSLEFLLTSPPAVHSFNTPA 531
Cdd:MTH00103 478 -----SKREVLTVELT---------------TTNLEWLHGCPPPYHTFEEPT 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: 576.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 2 LQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFGN 81
Cdd:MTH00037 3 LSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 82 YMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLG 161
Cdd:MTH00037 81 WLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 162 AINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGH 241
Cdd:MTH00037 161 SINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 242 PEVYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKI 320
Cdd:MTH00037 241 PEVYILILPGFGMISHVIAHYSgKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 321 FSWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQI 400
Cdd:MTH00037 321 FSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 401 LGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLVNGL 480
Cdd:MTH00037 401 SGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQR 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 21263115 481 TNkinnkavvfyKTPDFMesnmvfntntvkSSSLEFLLTS-PPAVHSFN 528
Cdd:MTH00037 481 EV----------ISPEFS------------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: 572.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 11 AKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQQYLhgNNQLFNVLVVGHAILMIFFMVMPALIGGFGNYMlPLMIGA 90
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFL--DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLL-PPLIGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 91 TDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLGAINFIVTTL 170
Cdd:cd00919 78 RDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 171 NMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGHPEVYILIIP 250
Cdd:cd00919 158 NMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 251 GFGIISHVVSTYSKKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLATIYGG 330
Cdd:cd00919 238 AFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 331 SIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQILGLYYNEKLS 410
Cdd:cd00919 318 RIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21263115 411 QIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQL 476
Cdd:cd00919 398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-479 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 570.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 2 LQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQQYLhgNNQLFNVLVVGHAILMIFFMVMPaLIGGFGN 81
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLL--SPETYNQLFTMHGTIMIFFFATP-FLAGFGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 82 YMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLG 161
Cdd:COG0843 83 YLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 162 AINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGH 241
Cdd:COG0843 163 GVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 242 PEVYILIIPGFGIISHVVSTYSKKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIF 321
Cdd:COG0843 243 PEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 322 SWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQIL 401
Cdd:COG0843 323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 402 GLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYP--DAFAGWNYISSIGAVVSMISLLLFVYILYDQLVNG 479
Cdd:COG0843 403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKG 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: 569.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 6 LYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQQYLhgNNQLFNVLVVGHAILMIFFMVMPaLIGGFGNYMLP 85
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 86 LMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLGAINF 165
Cdd:TIGR02891 78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 166 IVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGHPEVY 245
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 246 ILIIPGFGIISHVVSTYSKKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLA 325
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 326 TIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQILGLYY 405
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 406 NEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDA--FAGWNYISSIGAVVSMISLLLFVYILYDQLVNGltnk 483
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKG---- 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 21263115 484 innkavvfyktpdfmesnMVFNTNTVKSSSLEFLLTSPPAVHSF 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: 536.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 4 RWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQqyLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFGNYM 83
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 84 LPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLGAI 163
Cdd:MTH00026 84 VPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 164 NFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGHPE 243
Cdd:MTH00026 164 NFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 244 VYILIIPGFGIISHVVSTYS-KKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFS 322
Cdd:MTH00026 244 VYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 323 WLATIYGGSIRL--ATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQI 400
Cdd:MTH00026 324 WLATVSGSGRNLifTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 401 LGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLVNGL 480
Cdd:MTH00026 404 TGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREE 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 21263115 481 TNKINnkavVFYKTPdfmesNMVFNTNTVKSSSLEFLLTSPPAVHSFN 528
Cdd:MTH00026 484 PFDIN----IMAKGP-----LIPFSCQPAHFDTLEWSLTSPPEHHTYN 522
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
5-473 |
5.08e-175 |
|
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: 502.88 E-value: 5.08e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 5 WLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQQYLHgnNQLFNVLVVGHAILMIFFMVMPALIGgFGNYML 84
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLS--PEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 85 PLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLGAIN 164
Cdd:cd01662 78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 165 FIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGHPEV 244
Cdd:cd01662 158 FIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 245 YILIIPGFGIISHVVSTYSKKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWL 324
Cdd:cd01662 238 YILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 325 ATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQILGLY 404
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21263115 405 YNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYP--DAFAGWNYISSIGAVVSMISLLLFVYILY 473
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVI 468
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-479 |
1.64e-147 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 433.33 E-value: 1.64e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 1 MLQRWLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPgqQYLHGNNQLFNVLVVGHAILMIFFMVMPALIGGFG 80
Cdd:MTH00048 3 SLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDP--YYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 81 NYMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVesGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLL 160
Cdd:MTH00048 81 NYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 161 GAINFIvTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFG 240
Cdd:MTH00048 159 GSINFI-CTIYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 241 HPEVYILIIPGFGIISHVVSTYSKKP-VFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIK 319
Cdd:MTH00048 238 HPEVYVLILPGFGIISHICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 320 IFSWLATIYGGSIRLATPML-FAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSP 398
Cdd:MTH00048 318 VFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 399 QILGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLVN 478
Cdd:MTH00048 398 LITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVV 477
|
.
gi 21263115 479 G 479
Cdd:MTH00048 478 K 478
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
13-460 |
1.61e-137 |
|
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: 404.65 E-value: 1.61e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 13 DIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQQYLhgNNQLFNVLVVGHAILMIFFMVMPAlIGGFGNYMLPLMIGATD 92
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 93 TAFPRINNIGFWLLPMGLVCLVTSTlveSGAGTGWTVYPPLasiqahsgPSVDLAIFALHMTSISSLLGAINFIVTTLNM 172
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 173 RTNGMTMhKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNtsffevAGGGDPILYEHLFWFFGHPEVYILIIPGF 252
Cdd:pfam00115 147 RAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 253 GIISHVVSTYSKKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWLATIYGGSI 332
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 333 RLA-TPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQILGLYYNEKLSQ 411
Cdd:pfam00115 300 RFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 21263115 412 IQFWLIFVGANMVFLPMHFLGINGMPRRIP----DYPDAFAGWNYISSIGAVV 460
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
5-473 |
5.30e-123 |
|
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131928 Cd Length: 643 Bit Score: 374.96 E-value: 5.30e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 5 WLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLELAAPGQQYLHGNNqlFNVLVVGHAILMIFFMVMPALIGgFGNYML 84
Cdd:TIGR02882 44 WLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 85 PLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSLLGAIN 164
Cdd:TIGR02882 121 PLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGIN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 165 FIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFFGHPEV 244
Cdd:TIGR02882 201 FFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 245 YILIIPGFGIISHVVSTYSKKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIKIFSWL 324
Cdd:TIGR02882 281 YIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 325 ATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQILGLY 404
Cdd:TIGR02882 361 LTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYK 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21263115 405 YNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDAfAGW---NYISSIGAVVSMISLLLFVYILY 473
Cdd:TIGR02882 441 LNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYSPS-DGWfplNLISTIGALLMAIGFIFLVYNIY 511
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
5-473 |
3.99e-105 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 329.20 E-value: 3.99e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 5 WLYSTNAKDIAVLYFLLALFSGMAGTAMSLIIRLE--LAAPGQQYL---HGNNQLFNvlvvGHAILMIFFMVMPALIGgF 79
Cdd:PRK15017 48 WLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAGFlppHHYDQIFT----AHGVIMIFFVAMPFVIG-L 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 80 GNYMLPLMIGATDTAFPRINNIGFWLLPMGLVCLVTSTLVESGAGTGWTVYPPLASIQAHSGPSVDLAIFALHMTSISSL 159
Cdd:PRK15017 123 MNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 160 LGAINFIVTTLNMRTNGMTMHKLPLFVWAILITAVLLLLTLPVLSAGVTMLLLDRNFNTSFFEVAGGGDPILYEHLFWFF 239
Cdd:PRK15017 203 LTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAW 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 240 GHPEVYILIIPGFGIISHVVSTYSKKPVFGEISMVYAMASIGLLGLLVWSHHMYIVGLDADTRAYFTSATMIIAIPTGIK 319
Cdd:PRK15017 283 GHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 320 IFSWLATIYGGSIRLATPMLFAIAFLFLFTMGGLTGVALANASLDVAFHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQ 399
Cdd:PRK15017 363 IFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPK 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21263115 400 ILGLYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRIPDYPDA-FAGWNYISSIGAVVSMISLLLFVYILY 473
Cdd:PRK15017 443 AFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPqFHTMLMIAASGAALIALGILCQVIQMY 517
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|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
228-477 |
3.43e-21 |
|
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: 96.59 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 228 DPILYEHLFWFFGHPEVYILIIPGFGIISHVVSTYSKKPVFGEismvyAMASIGLLGLLVWS-----HHMYI-VGLDADT 301
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSD-----PLARLAFILFLLFStpvgfHHQFAdPGIGPGW 274
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 302 RAYFTSATMIIAIPTGIKIFSWLATI-YGGSIRLAT-------------PMLFAIAF-LFLFTMGGLTGVALANASLDVA 366
Cdd:cd01660 275 KFIHMVLTFMVALPSLLTAFTVFASLeIAGRLRGGKglfgwiralpwgdPMFLALFLaMLMFIPGGAGGIINASYQLNYV 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263115 367 FHDTYYVVGHFHYVLSMGAVFSLLAGYYYWSPQILG-LYYNEKLSQIQFWLIFVGANMVFLPMHFLGINGMPRRI----- 440
Cdd:cd01660 355 VHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGrELAAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTaeaqy 434
|
250 260 270
....*....|....*....|....*....|....*....
gi 21263115 441 --PDYPDAFAGWNYISSIGAVVSMISLLLFVYILYDQLV 477
Cdd:cd01660 435 ggLPAAGEWAPYQQLMAIGGTILFVSGALFLYILFRTLL 473
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