|
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 ... |
1-397 |
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: 750.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:cd01663 49 VTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:cd01663 129 HSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:cd01663 209 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:cd01663 289 DVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHF 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:cd01663 369 HYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISS 446
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 685.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00153 56 VTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00153 136 HSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00153 216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGM 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00153 296 DVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHF 375
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00153 376 HYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 453
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-397 |
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: 537.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLiGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:TIGR02891 52 FTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:TIGR02891 131 SPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLD 240
Cdd:TIGR02891 211 HFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 241 VDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFH 320
Cdd:TIGR02891 291 PLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFH 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 408722335 321 YVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDA--YIGWNLIAS 397
Cdd:TIGR02891 371 YVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLIST 449
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-397 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 531.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 2 TAHAFLMIFFMVMPvLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQSH 81
Cdd:COG0843 62 TMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEAS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 82 SGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTS 161
Cdd:COG0843 141 PGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTH 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 162 FFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDV 241
Cdd:COG0843 221 FFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISP 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 242 DTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHY 321
Cdd:COG0843 301 LVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHY 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 322 VLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYP--DAYIGWNLIAS 397
Cdd:COG0843 381 VLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLIST 458
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-397 |
4.29e-126 |
|
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: 370.36 E-value: 4.29e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVlIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAiveVGAGTGWTVYPPLsaiqs 80
Cdd:pfam00115 45 RTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 hsgGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMyRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNt 160
Cdd:pfam00115 116 ---VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 sffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLD 240
Cdd:pfam00115 191 -----AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 241 VDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHF-KTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:pfam00115 266 PWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHF 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIP----DYPDAYIGWNLI 395
Cdd:pfam00115 346 HYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWI 425
|
..
gi 408722335 396 AS 397
Cdd:pfam00115 426 RT 427
|
|
| |
|
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 ... |
1-397 |
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: 750.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:cd01663 49 VTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:cd01663 129 HSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:cd01663 209 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:cd01663 289 DVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHF 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:cd01663 369 HYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISS 446
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 685.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00153 56 VTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00153 136 HSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00153 216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGM 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00153 296 DVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHF 375
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00153 376 HYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISS 453
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 643.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00167 58 VTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00167 138 HAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00167 218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00167 298 DVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHF 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00167 378 HYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSS 455
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 636.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00223 55 VTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00223 135 HAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRK-PVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00223 215 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00223 295 DVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHF 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00223 375 HYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSS 452
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 617.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00116 58 VTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00116 138 HAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00116 218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGM 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00116 298 DVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHF 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00116 378 HYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISS 455
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 607.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00142 56 VTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00142 136 HSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00142 216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGM 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00142 296 DVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHF 375
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00142 376 HYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSS 453
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 590.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00182 60 VTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00182 140 HSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00182 220 TFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGM 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00182 300 DVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHF 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00182 380 HYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSS 457
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 585.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00184 60 VTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00184 140 HSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00184 220 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGM 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00184 300 DVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHF 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00184 380 HYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISS 457
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 557.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00037 58 VTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00037 138 HAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRK-PVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00037 218 TFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKqEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGM 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00037 298 DVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHF 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00037 378 HYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSS 455
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 549.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00183 58 VTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00183 138 HAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00183 218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00183 298 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHF 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00183 378 HYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSS 455
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 546.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00007 55 VTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00007 135 HAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKP-VFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00007 215 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00007 295 DVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHF 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00007 375 HYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSS 452
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 546.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00103 58 VTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00103 138 HAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00103 218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGM 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00103 298 DVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHF 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00103 378 HYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSS 455
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 545.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00077 58 VTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00077 138 HAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00077 218 TFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00077 298 NVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHF 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00077 378 HYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSS 455
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 538.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAiQS 80
Cdd:MTH00079 59 ITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00079 138 HPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00079 218 SFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGM 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:MTH00079 298 DLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHF 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00079 378 HYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISS 455
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-397 |
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: 537.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLiGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:TIGR02891 52 FTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:TIGR02891 131 SPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLD 240
Cdd:TIGR02891 211 HFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 241 VDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFH 320
Cdd:TIGR02891 291 PLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFH 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 408722335 321 YVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDA--YIGWNLIAS 397
Cdd:TIGR02891 371 YVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLIST 449
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-397 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 531.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 2 TAHAFLMIFFMVMPvLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQSH 81
Cdd:COG0843 62 TMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEAS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 82 SGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTS 161
Cdd:COG0843 141 PGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTH 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 162 FFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDV 241
Cdd:COG0843 221 FFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISP 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 242 DTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHY 321
Cdd:COG0843 301 LVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHY 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 322 VLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYP--DAYIGWNLIAS 397
Cdd:COG0843 381 VLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLIST 458
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-397 |
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: 530.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPiMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:cd00919 47 VTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:cd00919 126 SSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLD 240
Cdd:cd00919 206 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 241 VDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFH 320
Cdd:cd00919 286 VDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFH 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 408722335 321 YVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:cd00919 366 YVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISS 442
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
1.61e-180 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 512.64 E-value: 1.61e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQS 80
Cdd:MTH00026 59 VTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00026 139 HSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00026 219 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGM 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEG--SIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVA 317
Cdd:MTH00026 299 DVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVA 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 318 HFHYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00026 379 HFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISS 458
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-397 |
3.63e-170 |
|
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: 485.16 E-value: 3.63e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 2 TAHAFLMIFFMVMPVLIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQSH 81
Cdd:cd01662 54 TMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 82 SGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTS 161
Cdd:cd01662 133 PGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 162 FFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDV 241
Cdd:cd01662 213 FFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 242 DTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHY 321
Cdd:cd01662 293 LVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHY 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 408722335 322 VLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYP--DAYIGWNLIAS 397
Cdd:cd01662 373 VLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLIST 450
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-397 |
5.72e-138 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 403.67 E-value: 5.72e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVevGAGTGWTVYPPLSAIQS 80
Cdd:MTH00048 59 ITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 HSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPgQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNT 160
Cdd:MTH00048 137 SSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMT-NVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKP-VFGYIGMVYAMVSIGVLGFIVWAHHMYTVGL 239
Cdd:MTH00048 216 AFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 240 DVDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPML-FTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAH 318
Cdd:MTH00048 296 DVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAH 375
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 408722335 319 FHYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAYIGWNLIAS 397
Cdd:MTH00048 376 FHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCT 454
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
2-388 |
3.94e-128 |
|
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131890 Cd Length: 646 Bit Score: 382.87 E-value: 3.94e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 2 TAHAFLMIFFMVMPVLIGGFgNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQSH 81
Cdd:TIGR02843 103 TAHGVIMIFFVAMPFVFGLM-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 82 SGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTS 161
Cdd:TIGR02843 182 PGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMH 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 162 FFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDV 241
Cdd:TIGR02843 262 FFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 242 DTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHY 321
Cdd:TIGR02843 342 NVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHN 421
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 408722335 322 VLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDA 388
Cdd:TIGR02843 422 VIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNP 488
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-397 |
4.29e-126 |
|
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: 370.36 E-value: 4.29e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 1 ITAHAFLMIFFMVMPVlIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAiveVGAGTGWTVYPPLsaiqs 80
Cdd:pfam00115 45 RTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 81 hsgGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMyRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNt 160
Cdd:pfam00115 116 ---VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 161 sffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLD 240
Cdd:pfam00115 191 -----AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 241 VDTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHF-KTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHF 319
Cdd:pfam00115 266 PWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHF 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 320 HYVLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIP----DYPDAYIGWNLI 395
Cdd:pfam00115 346 HYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWI 425
|
..
gi 408722335 396 AS 397
Cdd:pfam00115 426 RT 427
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-395 |
2.77e-109 |
|
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: 334.51 E-value: 2.77e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 2 TAHAFLMIFFMVMPVLIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQSH 81
Cdd:TIGR02882 97 TTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 82 SGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTS 161
Cdd:TIGR02882 176 PGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 162 FFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDV 241
Cdd:TIGR02882 256 FFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 242 DTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHY 321
Cdd:TIGR02882 336 LINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHY 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 408722335 322 VLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRIPDYPDAyIGWNLI 395
Cdd:TIGR02882 416 VLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYSPS-DGWFPL 488
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
2-382 |
1.44e-107 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 330.74 E-value: 1.44e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 2 TAHAFLMIFFMVMPVLIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLTSAIVEVGAGTGWTVYPPLSAIQSH 81
Cdd:PRK15017 104 TAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 82 SGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTS 161
Cdd:PRK15017 183 PGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTH 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 162 FFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDV 241
Cdd:PRK15017 263 FFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 242 DTRAYFTAATMIIAVPTGIKIFSWVATMWEGSIHFKTPMLFTIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHY 321
Cdd:PRK15017 343 NVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHN 422
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 408722335 322 VLSMGAVFAIFAGFYYWFGKITGLQYPETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRRI 382
Cdd:PRK15017 423 VIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRL 483
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
170-387 |
1.31e-16 |
|
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: 81.18 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 170 DPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYT-VGLDVDTRAYFT 248
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHM 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 408722335 249 AATMIIAVPTGIKIFSWVATM--------------WEGSIHFKTPMLFTIGF-IFLFTIGGLTGIVLANSGLDISLHDTY 313
Cdd:cd01660 280 VLTFMVALPSLLTAFTVFASLeiagrlrggkglfgWIRALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTA 359
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 408722335 314 YVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYP-ETLGQIHFWSTFIGVNLTFMPMHFLGLAGMPRR--IPDYPD 387
Cdd:cd01660 360 WVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELAaKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGG 436
|
|
| |
