|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
11-453 |
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: 651.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 11 TSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYlyGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGNYFLPMLM 90
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 91 GAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAMNFMVT 169
Cdd:cd01663 79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGwTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 170 FINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPEVYMMI 249
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 250 MPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMATM 328
Cdd:cd01663 239 LPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 329 YGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNYNK 408
Cdd:cd01663 319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1904806543 409 VWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWNY 453
Cdd:cd01663 399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNM 443
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
4-452 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 587.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 4 MTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSgpNPQYLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGN 83
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELG--QPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 84 YFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLG 162
Cdd:MTH00153 79 WLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGwTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 163 AMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGH 242
Cdd:MTH00153 159 AINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 243 PEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKM 321
Cdd:MTH00153 239 PEVYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 322 FSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSM 401
Cdd:MTH00153 319 FSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLF 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1904806543 402 FGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00153 399 TGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWN 449
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
8-453 |
6.81e-161 |
|
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: 466.70 E-value: 6.81e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 8 LYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPvLMGAFGNYFLP 87
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 88 MLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAMNF 166
Cdd:TIGR02891 78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGwTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 167 MVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPEVY 246
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 247 MMIMPGFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMA 326
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 327 TMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNY 406
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1904806543 407 NKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDA--FIGWNY 453
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNL 446
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-452 |
8.86e-157 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 457.67 E-value: 8.86e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 2 SYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPvLMGAF 81
Cdd:COG0843 4 SGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLL--SPETYNQLFTMHGTIMIFFFATP-FLAGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 82 GNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSL 160
Cdd:COG0843 81 GNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGwTFYPPLSGLEASPGVGVDLWLLGLALFGVGSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 161 LGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFF 240
Cdd:COG0843 161 LGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 241 GHPEVYMMIMPGFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMK 320
Cdd:COG0843 241 GHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 321 MFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPS 400
Cdd:COG0843 321 VFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1904806543 401 MFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYP--DAFIGWN 452
Cdd:COG0843 401 MTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLN 454
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
15-452 |
1.11e-113 |
|
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: 343.79 E-value: 1.11e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 15 DMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPVLMGaFGNYFLPMLMGAVD 94
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 95 MAFARLNNMSFWCLPPALVCMMASVLMEQGAGTGncYPPLssinahsgPSVDLAMFALHLTSMSSLLGAMNFMVTFINMR 174
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASFGGATTGWTE--YPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 175 TMGLHMvNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGfyevaaGGDPVTYEHLFWFFGHPEVYMMIMPGFG 254
Cdd:pfam00115 148 APGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAFG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 255 MMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMATMYGGEVR 334
Cdd:pfam00115 221 IIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 335 LA-VPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNYNKVWAEI 413
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1904806543 414 HFWLLFMSVNLIFLPMHFLGTNGMPRRIP----QYPDAFIGWN 452
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLN 423
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
11-453 |
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: 651.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 11 TSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYlyGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGNYFLPMLM 90
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 91 GAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAMNFMVT 169
Cdd:cd01663 79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGwTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 170 FINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPEVYMMI 249
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 250 MPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMATM 328
Cdd:cd01663 239 LPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 329 YGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNYNK 408
Cdd:cd01663 319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1904806543 409 VWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWNY 453
Cdd:cd01663 399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNM 443
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
4-452 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 587.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 4 MTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSgpNPQYLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGN 83
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELG--QPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 84 YFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLG 162
Cdd:MTH00153 79 WLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGwTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 163 AMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGH 242
Cdd:MTH00153 159 AINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 243 PEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKM 321
Cdd:MTH00153 239 PEVYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 322 FSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSM 401
Cdd:MTH00153 319 FSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLF 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1904806543 402 FGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00153 399 TGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWN 449
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
3-452 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 572.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 3 YMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFG 82
Cdd:MTH00167 2 WINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 83 NYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLL 161
Cdd:MTH00167 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGwTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 162 GAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFG 241
Cdd:MTH00167 160 GSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 242 HPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMK 320
Cdd:MTH00167 240 HPEVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 321 MFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPS 400
Cdd:MTH00167 320 VFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1904806543 401 MFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00167 400 FTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWN 451
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
6-452 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 566.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 6 RWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSgpNPQYLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGNYF 85
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELG--QPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 86 LPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAM 164
Cdd:MTH00223 80 VPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGwTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 165 NFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPE 244
Cdd:MTH00223 160 NFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 245 VYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFS 323
Cdd:MTH00223 240 VYILILPGFGMISHIVSHYSsKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 324 WMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFG 403
Cdd:MTH00223 320 WLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTG 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1904806543 404 LNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00223 400 VTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWN 448
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
2-452 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 558.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 2 SYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAF 81
Cdd:MTH00116 1 MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 82 GNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSL 160
Cdd:MTH00116 79 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGwTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 161 LGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFF 240
Cdd:MTH00116 159 LGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 241 GHPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGM 319
Cdd:MTH00116 239 GHPEVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 320 KMFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGP 399
Cdd:MTH00116 319 KVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFP 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1904806543 400 SMFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00116 399 LFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWN 451
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
4-452 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 548.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 4 MTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGN 83
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 84 YFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLG 162
Cdd:MTH00142 79 WLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGwTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 163 AMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGH 242
Cdd:MTH00142 159 AINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 243 PEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKM 321
Cdd:MTH00142 239 PEVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 322 FSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSM 401
Cdd:MTH00142 319 FSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLF 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1904806543 402 FGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00142 399 TGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWN 449
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-452 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 524.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 1 MSYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGA 80
Cdd:MTH00184 2 SLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 81 FGNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSS 159
Cdd:MTH00184 80 FGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGwTVYPPLSSIQAHSGGSVDMAIFSLHLAGISS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 160 LLGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWF 239
Cdd:MTH00184 160 ILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 240 FGHPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTG 318
Cdd:MTH00184 240 FGHPEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 319 MKMFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWG 398
Cdd:MTH00184 320 IKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWF 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1904806543 399 PSMFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00184 400 GKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWN 453
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
2-452 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 520.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 2 SYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAF 81
Cdd:MTH00182 3 LYLTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 82 GNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSL 160
Cdd:MTH00182 81 GNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGwTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 161 LGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFF 240
Cdd:MTH00182 161 LGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 241 GHPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGM 319
Cdd:MTH00182 241 GHPEVYILILPGFGMISQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 320 KMFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGP 399
Cdd:MTH00182 321 KVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1904806543 400 SMFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00182 401 KITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWN 453
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
6-452 |
1.14e-177 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 510.21 E-value: 1.14e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 6 RWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGNYF 85
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 86 LPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAM 164
Cdd:MTH00007 80 VPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGwTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 165 NFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPE 244
Cdd:MTH00007 160 NFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 245 VYMMIMPGFGMMSHIVSTYSKKPM-FGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFS 323
Cdd:MTH00007 240 VYILILPGFGAISHIVTHYAGKLEpFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 324 WMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFG 403
Cdd:MTH00007 320 WLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTG 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1904806543 404 LNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00007 400 LTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWN 448
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
4-452 |
2.46e-177 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 509.46 E-value: 2.46e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 4 MTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGN 83
Cdd:MTH00183 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 84 YFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLG 162
Cdd:MTH00183 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGwTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 163 AMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGH 242
Cdd:MTH00183 161 AINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 243 PEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKM 321
Cdd:MTH00183 241 PEVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 322 FSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSM 401
Cdd:MTH00183 321 FSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLF 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1904806543 402 FGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00183 401 SGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWN 451
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
4-522 |
3.01e-177 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 509.10 E-value: 3.01e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 4 MTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGN 83
Cdd:MTH00077 3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 84 YFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLG 162
Cdd:MTH00077 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGwTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 163 AMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGH 242
Cdd:MTH00077 161 AINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 243 PEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKM 321
Cdd:MTH00077 241 PEVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 322 FSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSM 401
Cdd:MTH00077 321 FSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 402 FGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWNYISSIGSTISIISVLVGLKSV-EIQLNNG 480
Cdd:MTH00077 401 SGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIwEAFSSKR 480
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1904806543 481 LNHNTELQMTpdylesnltrltrdsDIELILSRPAEYHTFSE 522
Cdd:MTH00077 481 EVLTTELTST---------------NIEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
3-452 |
4.79e-175 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 503.65 E-value: 4.79e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 3 YMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFG 82
Cdd:MTH00103 2 FINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 83 NYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLL 161
Cdd:MTH00103 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGwTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 162 GAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFG 241
Cdd:MTH00103 160 GAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 242 HPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMK 320
Cdd:MTH00103 240 HPEVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 321 MFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPS 400
Cdd:MTH00103 320 VFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1904806543 401 MFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00103 400 FSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWN 451
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
3-531 |
2.55e-172 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 496.66 E-value: 2.55e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 3 YMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFG 82
Cdd:MTH00037 2 QLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 83 NYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLL 161
Cdd:MTH00037 80 NWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGwTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 162 GAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFG 241
Cdd:MTH00037 160 ASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 242 HPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMK 320
Cdd:MTH00037 240 HPEVYILILPGFGMISHVIAHYSgKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 321 MFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPS 400
Cdd:MTH00037 320 VFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 401 MFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWNYISSIGSTISIISVLVGLKSVEIQLNng 480
Cdd:MTH00037 400 FSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFA-- 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1904806543 481 lnhNTELQMTPDYLESNLTRLTRdsdielilSRPAEYHTFSELPVLVSPNK 531
Cdd:MTH00037 478 ---SQREVISPEFSSSSLEWQYS--------SFPPSHHTFDETPSTVILIK 517
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
13-452 |
2.88e-166 |
|
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: 479.33 E-value: 2.88e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 13 HKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGNYFLPMLmGA 92
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFL--DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLI-GA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 93 VDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAMNFMVTFI 171
Cdd:cd00919 78 RDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGwTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 172 NMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPEVYMMIMP 251
Cdd:cd00919 158 NMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 252 GFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMATMYGG 331
Cdd:cd00919 238 AFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 332 EVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNYNKVWA 411
Cdd:cd00919 318 RIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1904806543 412 EIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:cd00919 398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWN 438
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-531 |
4.93e-161 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 468.72 E-value: 4.93e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 1 MSYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGA 80
Cdd:MTH00026 1 MTSFVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 81 FGNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSS 159
Cdd:MTH00026 79 FGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGwTVYPPLASIQAHSGGSVDMAIFSLHLAGLSS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 160 LLGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWF 239
Cdd:MTH00026 159 ILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 240 FGHPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTG 318
Cdd:MTH00026 239 FGHPEVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 319 MKMFSWMATMYGGEVRL--AVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYY 396
Cdd:MTH00026 319 IKIFSWLATVSGSGRNLifTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 397 WGPSMFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWNYISSIGSTISIISVLVGLKSVEIQ 476
Cdd:MTH00026 399 WFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDA 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1904806543 477 LNNGLNHNTELQMTPDYLESNLTRLTRDSdIELILSRPAEYHTFSELPVLVSPNK 531
Cdd:MTH00026 479 YYREEPFDINIMAKGPLIPFSCQPAHFDT-LEWSLTSPPEHHTYNELPYIVGGPK 532
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
8-453 |
6.81e-161 |
|
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: 466.70 E-value: 6.81e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 8 LYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPvLMGAFGNYFLP 87
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 88 MLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAMNF 166
Cdd:TIGR02891 78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGwTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 167 MVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPEVY 246
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 247 MMIMPGFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMA 326
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 327 TMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNY 406
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1904806543 407 NKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDA--FIGWNY 453
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNL 446
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-452 |
1.88e-159 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 463.38 E-value: 1.88e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 1 MSYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNpqYLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGA 80
Cdd:MTH00079 1 QGGLSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 81 FGNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSInAHSGPSVDLAMFALHLTSMSS 159
Cdd:MTH00079 79 FGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSwTVYPPLSTL-GHPGSSVDLAIFSLHCAGISS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 160 LLGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWF 239
Cdd:MTH00079 158 ILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 240 FGHPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTG 318
Cdd:MTH00079 238 FGHPEVYILILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 319 MKMFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWG 398
Cdd:MTH00079 318 VKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWW 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1904806543 399 PSMFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00079 398 PFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWN 451
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-452 |
8.86e-157 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 457.67 E-value: 8.86e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 2 SYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPvLMGAF 81
Cdd:COG0843 4 SGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLL--SPETYNQLFTMHGTIMIFFFATP-FLAGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 82 GNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSL 160
Cdd:COG0843 81 GNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGwTFYPPLSGLEASPGVGVDLWLLGLALFGVGSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 161 LGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFF 240
Cdd:COG0843 161 LGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 241 GHPEVYMMIMPGFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMK 320
Cdd:COG0843 241 GHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 321 MFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPS 400
Cdd:COG0843 321 VFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1904806543 401 MFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYP--DAFIGWN 452
Cdd:COG0843 401 MTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLN 454
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
7-452 |
4.89e-134 |
|
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: 398.49 E-value: 4.89e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 7 WLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPVLMGaFGNYFL 86
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFL--SPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 87 PMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAMN 165
Cdd:cd01662 78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGwFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 166 FMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPEV 245
Cdd:cd01662 158 FIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 246 YMMIMPGFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWM 325
Cdd:cd01662 238 YILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 326 ATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLN 405
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1904806543 406 YNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAfIGWN 452
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPG-PGWD 443
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-448 |
2.84e-122 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 368.62 E-value: 2.84e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 1 MSYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSgpNPQYLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGA 80
Cdd:MTH00048 1 MNSLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFL--DPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 81 FGNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASvlMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSS 159
Cdd:MTH00048 79 FGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGwTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 160 LLGAMNFMVTfINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWF 239
Cdd:MTH00048 157 LFGSINFICT-IYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 240 FGHPEVYMMIMPGFGMMSHIVSTYSKKP-MFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTG 318
Cdd:MTH00048 236 FGHPEVYVLILPGFGIISHICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 319 MKMFSWMATMYGGEVRLAVP-MLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYW 397
Cdd:MTH00048 316 IKVFSWLYMLLNSRVRKSDPvVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWW 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1904806543 398 GPSMFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAF 448
Cdd:MTH00048 396 WPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSY 446
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
15-452 |
1.11e-113 |
|
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: 343.79 E-value: 1.11e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 15 DMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPVLMGaFGNYFLPMLMGAVD 94
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 95 MAFARLNNMSFWCLPPALVCMMASVLMEQGAGTGncYPPLssinahsgPSVDLAMFALHLTSMSSLLGAMNFMVTFINMR 174
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASFGGATTGWTE--YPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 175 TMGLHMvNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGfyevaaGGDPVTYEHLFWFFGHPEVYMMIMPGFG 254
Cdd:pfam00115 148 APGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAFG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 255 MMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMATMYGGEVR 334
Cdd:pfam00115 221 IIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 335 LA-VPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNYNKVWAEI 413
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1904806543 414 HFWLLFMSVNLIFLPMHFLGTNGMPRRIP----QYPDAFIGWN 452
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLN 423
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
5-446 |
3.04e-82 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 269.11 E-value: 3.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 5 TRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRME---LSGPNPQYLYGNNqvYNVLVTGHAMAMMFLFVMPVLMGAF 81
Cdd:PRK15017 46 KEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqalASAGEAGFLPPHH--YDQIFTAHGVIMIFFVAMPFVIGLM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 82 gNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSL 160
Cdd:PRK15017 124 -NLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGwLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 161 LGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFF 240
Cdd:PRK15017 203 LTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAW 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 241 GHPEVYMMIMPGFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMK 320
Cdd:PRK15017 283 GHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 321 MFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPS 400
Cdd:PRK15017 363 IFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPK 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1904806543 401 MFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPD 446
Cdd:PRK15017 443 AFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
236-446 |
7.94e-11 |
|
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: 64.23 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 236 LFWFFGHPEVYMMIMPGFGMMSHIVSTYSKKPMFGEmgmlyAMGSMGLLGFLVWS-----HHMYV-VGLDIDSRAYFTSA 309
Cdd:cd01660 207 LFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSD-----PLARLAFILFLLFStpvgfHHQFAdPGIGPGWKFIHMVL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 310 TMVMAVPT-------------------GMKMFSWMATMYGGEVRLAVPMLFALGFLFlftmGGLTGVMLSNASMDVAFHD 370
Cdd:cd01660 282 TFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHN 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 371 TYYVVGHFHyvLSMGALFSLV--GGYYYWGPSMFGLNYNKVW-AEIHFWLLFMSVNLIFLPMHFLGTNGMPRR--IPQYP 445
Cdd:cd01660 358 TAWVPGHFH--LTVGGAVALTfmAVAYWLVPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435
|
.
gi 1904806543 446 D 446
Cdd:cd01660 436 G 436
|
|
| PRK14485 |
PRK14485 |
putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional |
351-433 |
8.26e-03 |
|
putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional
Pssm-ID: 184703 [Multi-domain] Cd Length: 712 Bit Score: 38.91 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 351 MGGLTGVMLSNASMDVAFHDTYYVVGHFHyvlsMGAL----FSLVGGYYYWGPSMFGLN-YNKVWAEIHFWLLFMSVNLI 425
Cdd:PRK14485 318 MATFEGPMLSLKNVNAIAHYTDWIIAHVH----VGALgwngFLTFGMLYWLLPRLFKTKlYSTKLANFHFWIGTLGIILY 393
|
....*...
gi 1904806543 426 FLPMHFLG 433
Cdd:PRK14485 394 ALPMYVAG 401
|
|
|