|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
12-395 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 787.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00153 116 VESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00153 196 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAM 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00153 276 LAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00153 356 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMP 435
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEWYQNLPPA 395
Cdd:MTH00153 436 RRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPA 499
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
12-388 |
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: 676.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:cd01663 109 VEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:cd01663 189 SLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAM 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:cd01663 269 LSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVV 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:cd01663 349 LANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMP 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLF-PLSMTSSLEW 388
Cdd:cd01663 429 RRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGSTSLEW 486
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
15-356 |
2.29e-151 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 438.41 E-value: 2.29e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 15 GAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLLSLP 94
Cdd:COG0843 123 AADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 95 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAI 174
Cdd:COG0843 203 VLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 175 GLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVVLAN 254
Cdd:COG0843 282 AFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLAS 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 255 SSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMPRRY 334
Cdd:COG0843 362 VPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRY 441
|
330 340
....*....|....*....|....
gi 528749179 335 SDYP--DVYTSWNVLSSIGSTISF 356
Cdd:COG0843 442 ATYPpePGWQPLNLISTIGAFILA 465
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
15-394 |
1.17e-149 |
|
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: 432.80 E-value: 1.17e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 15 GAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLLSLP 94
Cdd:TIGR02891 114 APDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 95 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAI 174
Cdd:TIGR02891 194 VLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 175 GLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVVLAN 254
Cdd:TIGR02891 273 GFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLAS 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 255 SSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMPRRY 334
Cdd:TIGR02891 353 VPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRY 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528749179 335 SDYPD--VYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEWYQNLPP 394
Cdd:TIGR02891 433 YTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPP 494
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
14-354 |
1.89e-103 |
|
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: 312.58 E-value: 1.89e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 14 NGAGTGWTVYPPLSAgiahggasVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLdQTPLFVWSVAITALLLLLSL 93
Cdd:pfam00115 103 GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 94 PVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLA 173
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 174 IGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLT-YSPALLWALGFVFLFTIGGLTGVVL 252
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVML 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 253 ANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMPR 332
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPR 406
|
330 340
....*....|....*....|....*.
gi 528749179 333 RYS----DYPDVYTSWNVLSSIGSTI 354
Cdd:pfam00115 407 RYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
12-395 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 787.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00153 116 VESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00153 196 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAM 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00153 276 LAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00153 356 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMP 435
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEWYQNLPPA 395
Cdd:MTH00153 436 RRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPA 499
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
12-388 |
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: 676.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:cd01663 109 VEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:cd01663 189 SLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAM 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:cd01663 269 LSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVV 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:cd01663 349 LANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMP 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLF-PLSMTSSLEW 388
Cdd:cd01663 429 RRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGSTSLEW 486
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
12-395 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 641.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00142 116 VESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00142 196 SLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAM 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00142 276 LSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00142 356 LANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMP 435
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEWYQNLPPA 395
Cdd:MTH00142 436 RRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLPPD 499
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
12-395 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 638.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00167 118 VEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00167 198 SLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAM 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00167 278 MAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00167 358 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMP 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEWYQNLPPA 395
Cdd:MTH00167 438 RRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPPP 501
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
12-395 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 638.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00223 115 VESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00223 195 SLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAM 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00223 275 LSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGII 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00223 355 LSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMP 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEWYQNLPPA 395
Cdd:MTH00223 435 RRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWDNLLPAD 498
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
12-394 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 637.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00116 118 VEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00116 198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAM 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00116 278 LSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00116 358 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMP 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEWYQNLPP 394
Cdd:MTH00116 438 RRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPP 500
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
12-395 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 574.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00037 118 VESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00037 198 SLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAM 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00037 278 IAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00037 358 LANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMP 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEW-YQNLPPA 395
Cdd:MTH00037 438 RRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWqYSSFPPS 502
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
12-394 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 568.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00103 118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00103 198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAM 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00103 278 MSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00103 358 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMP 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEWYQNLPP 394
Cdd:MTH00103 438 RRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPP 500
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
12-393 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 560.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00007 115 VEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00007 195 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAM 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00007 275 LGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00007 355 LSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMP 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEWYQNLP 393
Cdd:MTH00007 435 RRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLP 496
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
12-394 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 559.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00183 118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00183 198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAM 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00183 278 MAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00183 358 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMP 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEWYQNLPP 394
Cdd:MTH00183 438 RRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPP 500
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
12-394 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 552.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00077 118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00077 198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAM 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00077 278 MSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00077 358 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMP 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEWYQNLPP 394
Cdd:MTH00077 438 RRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPP 500
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
12-394 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 526.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAgIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00079 119 VDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00079 198 SLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAI 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00079 278 LSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVI 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00079 358 LSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMP 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEWYQNLPP 394
Cdd:MTH00079 438 RKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSYV 500
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
12-395 |
2.55e-179 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 509.36 E-value: 2.55e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00182 120 VEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00182 200 SLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAM 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00182 280 LSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVV 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00182 360 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFP 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVL----FPLSMTSSLEWYQNLPPA 395
Cdd:MTH00182 440 RRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIgwkeGTGESWASLEWVHSSPPL 507
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
12-395 |
1.96e-175 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 498.97 E-value: 1.96e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00184 120 VEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00184 200 SLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAM 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:MTH00184 280 VSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIV 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:MTH00184 360 LANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLP 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMIsnRTVLF-----PLSMTSSLEWYQNLPPA 395
Cdd:MTH00184 440 RRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYV--REIKFvgwveDSGHYPSLEWAQTSPPA 506
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
12-370 |
3.99e-164 |
|
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: 468.16 E-value: 3.99e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:cd00919 106 VGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAM 171
Cdd:cd00919 186 ALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAF 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:cd00919 265 LAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:cd00919 345 LANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMP 424
|
330 340 350
....*....|....*....|....*....|....*....
gi 528749179 332 RRYSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESM 370
Cdd:cd00919 425 RRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
12-355 |
1.10e-153 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 444.46 E-value: 1.10e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:MTH00026 119 VEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAM 171
Cdd:MTH00026 199 SLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAM 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT--QLTYSPALLWALGFVFLFTIGGLTG 249
Cdd:MTH00026 279 LAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 250 VVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAG 329
Cdd:MTH00026 359 IVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAG 438
|
330 340
....*....|....*....|....*.
gi 528749179 330 MPRRYSDYPDVYTSWNVLSSIGSTIS 355
Cdd:MTH00026 439 LPRRYADYPDNFEDFNQISSFGSIIS 464
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
15-356 |
2.29e-151 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 438.41 E-value: 2.29e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 15 GAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLLSLP 94
Cdd:COG0843 123 AADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 95 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAI 174
Cdd:COG0843 203 VLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAI 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 175 GLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVVLAN 254
Cdd:COG0843 282 AFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLAS 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 255 SSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMPRRY 334
Cdd:COG0843 362 VPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRY 441
|
330 340
....*....|....*....|....
gi 528749179 335 SDYP--DVYTSWNVLSSIGSTISF 356
Cdd:COG0843 442 ATYPpePGWQPLNLISTIGAFILA 465
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
15-394 |
1.17e-149 |
|
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: 432.80 E-value: 1.17e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 15 GAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLLSLP 94
Cdd:TIGR02891 114 APDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 95 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAI 174
Cdd:TIGR02891 194 VLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 175 GLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVVLAN 254
Cdd:TIGR02891 273 GFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLAS 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 255 SSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMPRRY 334
Cdd:TIGR02891 353 VPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRY 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528749179 335 SDYPD--VYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVLFPLSMTSSLEWYQNLPP 394
Cdd:TIGR02891 433 YTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPP 494
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
15-377 |
2.83e-137 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 401.75 E-value: 2.83e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 15 GAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLdQTPLFVWSVAITALLLLLSLP 94
Cdd:MTH00048 120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 95 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAI 174
Cdd:MTH00048 199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 175 GLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYS-PALLWALGFVFLFTIGGLTGVVLA 253
Cdd:MTH00048 279 VCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLS 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 254 NSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMPRR 333
Cdd:MTH00048 359 ASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRR 438
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 528749179 334 YSDYPDVYTSWNVLSSIGSTISFIGIIMLIFIIWESMISNRTVL 377
Cdd:MTH00048 439 VCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
12-354 |
6.29e-132 |
|
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: 387.71 E-value: 6.29e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 12 VENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLL 91
Cdd:cd01662 112 IGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILF 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 92 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAM 171
Cdd:cd01662 192 AFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYAT 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 172 LAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVV 251
Cdd:cd01662 271 VAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVM 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 252 LANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMP 331
Cdd:cd01662 351 LASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMP 430
|
330 340
....*....|....*....|....*
gi 528749179 332 RRYSDYPDV--YTSWNVLSSIGSTI 354
Cdd:cd01662 431 RRVYTYLPGpgWDPLNLISTIGAFL 455
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
14-354 |
1.89e-103 |
|
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: 312.58 E-value: 1.89e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 14 NGAGTGWTVYPPLSAgiahggasVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLdQTPLFVWSVAITALLLLLSL 93
Cdd:pfam00115 103 GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 94 PVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLA 173
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 174 IGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLT-YSPALLWALGFVFLFTIGGLTGVVL 252
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVML 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 253 ANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMPR 332
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPR 406
|
330 340
....*....|....*....|....*.
gi 528749179 333 RYS----DYPDVYTSWNVLSSIGSTI 354
Cdd:pfam00115 407 RYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
19-354 |
1.22e-82 |
|
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: 265.18 E-value: 1.22e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 19 GWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLLSLPVLAG 98
Cdd:TIGR02882 162 GWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTV 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 99 AITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKEAFGTLGMIYAMLAIGLLG 178
Cdd:TIGR02882 242 ALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLS 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 179 FVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVVLANSSID 258
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 259 IILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMPRRYSDY- 337
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYs 480
|
330
....*....|....*...
gi 528749179 338 -PDVYTSWNVLSSIGSTI 354
Cdd:TIGR02882 481 pSDGWFPLNLISTIGALL 498
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
16-339 |
3.54e-79 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 256.40 E-value: 3.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 16 AGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTTINMRTPGMSLDQTPLFVWSVAITALLLLLSLPV 95
Cdd:PRK15017 166 AQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPI 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 96 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKEAFGTLGMIYAMLAIG 175
Cdd:PRK15017 246 LTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCIT 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 176 LLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWALGFVFLFTIGGLTGVVLANS 255
Cdd:PRK15017 325 VLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 256 SIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLTIQFTIMFVGVNLTFFPQHFLGLAGMPRRYS 335
Cdd:PRK15017 405 GADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLS 484
|
....
gi 528749179 336 DYPD 339
Cdd:PRK15017 485 QQID 488
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
121-356 |
2.18e-19 |
|
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: 89.65 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 121 DPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMIyAMLAIGLLGFVVWAHHMFT-VGMDVDTRAYF 199
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 200 TSATMIIAVPTGIKIFSWLATL-HGTQLTYSPALLW---------------ALGFVFlFTIGGLTGVVLANSSIDIILHD 263
Cdd:cd01660 279 MVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHN 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528749179 264 TYYVVAHFHyvLSMGAVFAIMAGFIQWY--PLFTGLSLNPKWLTI-QFTIMFVGVNLTFFPQHFLGLAGMPRR--YSDYP 338
Cdd:cd01660 358 TAWVPGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435
|
250 260
....*....|....*....|...
gi 528749179 339 DVY-----TSWNVLSSIGSTISF 356
Cdd:cd01660 436 GLPaagewAPYQQLMAIGGTILF 458
|
|
| |
