|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-410 |
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: 731.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGnhFLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:cd01663 8 TLYLIFGLWSGLVGTSLSLLIRLELSQPG--SQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:cd01663 86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:cd01663 166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:cd01663 246 SHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:cd01663 326 ETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHF 405
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:cd01663 406 WLMFIGVNLTF 416
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 679.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNhfLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00153 15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00153 93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00153 173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00153 253 SHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00153 333 SPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQF 412
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00153 413 FIMFIGVNLTF 423
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-410 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 518.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNHFLigNHQLYNVLITAHAFLMIFFMVMPILiGGFGNWLVPIMIGSPDMAF 80
Cdd:TIGR02891 11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:TIGR02891 88 PRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:TIGR02891 168 GMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGII 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFSRKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHLK 320
Cdd:TIGR02891 248 SEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 321 VPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHFW 400
Cdd:TIGR02891 328 TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFW 407
|
410
....*....|
gi 780959610 401 TTFLGVNLTF 410
Cdd:TIGR02891 408 LTFVGFNLTF 417
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-410 |
4.11e-179 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 509.67 E-value: 4.11e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 2 LYLFFGTFSGVLGGCMSLLIRMELMQPGNHFLigNHQLYNVLITAHAFLMIFFMVMPIlIGGFGNWLVPIMIGSPDMAFP 81
Cdd:COG0843 21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLL--SPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 82 RLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSPG 161
Cdd:COG0843 98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 162 QSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 241
Cdd:COG0843 178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 242 HIVSTFSRKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHLKV 321
Cdd:COG0843 258 EIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 322 PMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHFWT 401
Cdd:COG0843 338 PMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWL 417
|
....*....
gi 780959610 402 TFLGVNLTF 410
Cdd:COG0843 418 WFIGFNLTF 426
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-410 |
4.72e-121 |
|
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: 358.04 E-value: 4.72e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 2 LYLFFGTFSGVLGGCMSLLIRMELMQPGNHFLigNHQLYNVLITAHAFLMIFFMVMPIlIGGFGNWLVPIMIGSPDMAFP 81
Cdd:pfam00115 5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 82 RLNNISFWLLPPSLCLLLLSSLvevGAGTGWTVYPPLssiqshsgGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSPG 161
Cdd:pfam00115 82 RLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 162 QSMyRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTaffdpsGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 241
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 242 HIVSTFSRKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL-K 320
Cdd:pfam00115 224 YILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 321 VPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHFW 400
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFW 383
|
410
....*....|
gi 780959610 401 TTFLGVNLTF 410
Cdd:pfam00115 384 LLFIGFNLTF 393
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-410 |
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: 731.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGnhFLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:cd01663 8 TLYLIFGLWSGLVGTSLSLLIRLELSQPG--SQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:cd01663 86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:cd01663 166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:cd01663 246 SHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:cd01663 326 ETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHF 405
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:cd01663 406 WLMFIGVNLTF 416
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 679.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNhfLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00153 15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00153 93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00153 173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00153 253 SHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00153 333 SPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQF 412
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00153 413 FIMFIGVNLTF 423
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 637.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNhfLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00167 17 TLYFIFGAWAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00167 95 PRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00167 175 GITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00167 255 SHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKW 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00167 335 ETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHF 414
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00167 415 FVMFIGVNLTF 425
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 618.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGnhFLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00116 17 TLYLIFGAWAGMVGTALSLLIRAELGQPG--TLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00116 95 PRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00116 175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00116 255 SHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKW 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00116 335 DPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQF 414
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00116 415 GVMFTGVNLTF 425
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 618.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNhfLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00223 14 TLYLIFGMWSGLVGTSLSLLIRAELGQPGA--LLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00223 92 PRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00223 172 GMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFSRK-PVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00223 252 SHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00223 332 EAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHF 411
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00223 412 FLMFLGVNLTF 422
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 597.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNhfLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00142 15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00142 93 PRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00142 173 GMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00142 253 SHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00142 333 EPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHF 412
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00142 413 YTMFIGVNLTF 423
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 578.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNhfLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00182 19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00182 97 PRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00182 177 GVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00182 257 SQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00182 337 DTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHF 416
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00182 417 WLMFIGVNLTF 427
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 575.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNhfLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00184 19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00184 97 PRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00184 177 GITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00184 257 SQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00184 337 DTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHF 416
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00184 417 WLMFIGVNLTF 427
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 550.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNhfLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00037 17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00037 95 PRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00037 175 GMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFSRK-PVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00037 255 SHVIAHYSGKqEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRW 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00037 335 ETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHF 414
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00037 415 FLMFIGVNLTF 425
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 542.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNhfLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00183 17 TLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00183 95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00183 175 AISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00183 255 SHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKW 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00183 335 ETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHF 414
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00183 415 GVMFVGVNLTF 425
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 540.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNhfLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00103 17 TLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00103 95 PRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00103 175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00103 255 SHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKW 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00103 335 SPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHF 414
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00103 415 TIMFVGVNMTF 425
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 538.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNhfLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00077 17 TLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00077 95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00077 175 SMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00077 255 SHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKW 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00077 335 DAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHF 414
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00077 415 GVMFIGVNLTF 425
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 534.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNhfLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00007 14 TLYFILGVWGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00007 92 PRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00007 172 GLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFSRKP-VFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00007 252 SHIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00007 332 ETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHF 411
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00007 412 FLMFLGVNLTF 422
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 525.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGnhFLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00079 18 TLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSiQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00079 96 PRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00079 175 SISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGII 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00079 255 SQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKF 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00079 335 QPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVF 414
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00079 415 FLMFVGVNLTF 425
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-410 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 518.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNHFLigNHQLYNVLITAHAFLMIFFMVMPILiGGFGNWLVPIMIGSPDMAF 80
Cdd:TIGR02891 11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:TIGR02891 88 PRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:TIGR02891 168 GMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGII 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFSRKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHLK 320
Cdd:TIGR02891 248 SEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 321 VPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHFW 400
Cdd:TIGR02891 328 TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFW 407
|
410
....*....|
gi 780959610 401 TTFLGVNLTF 410
Cdd:TIGR02891 408 LTFVGFNLTF 417
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
7.42e-180 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 511.48 E-value: 7.42e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNhfLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00026 18 SLYLVFGALSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:MTH00026 96 PRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:MTH00026 176 GMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFS-RKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL 319
Cdd:MTH00026 256 SQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 320 --KVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQI 397
Cdd:MTH00026 336 ifTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLI 415
|
410
....*....|...
gi 780959610 398 HFWTTFLGVNLTF 410
Cdd:MTH00026 416 HFWLMFIGVNITF 428
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-410 |
4.11e-179 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 509.67 E-value: 4.11e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 2 LYLFFGTFSGVLGGCMSLLIRMELMQPGNHFLigNHQLYNVLITAHAFLMIFFMVMPIlIGGFGNWLVPIMIGSPDMAFP 81
Cdd:COG0843 21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLL--SPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 82 RLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSPG 161
Cdd:COG0843 98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 162 QSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 241
Cdd:COG0843 178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 242 HIVSTFSRKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHLKV 321
Cdd:COG0843 258 EIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 322 PMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHFWT 401
Cdd:COG0843 338 PMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWL 417
|
....*....
gi 780959610 402 TFLGVNLTF 410
Cdd:COG0843 418 WFIGFNLTF 426
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-410 |
4.11e-178 |
|
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: 504.37 E-value: 4.11e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 1 TLYLFFGTFSGVLGGCMSLLIRMELMQPGNHFLigNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPiMIGSPDMAF 80
Cdd:cd00919 6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFL--DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 81 PRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSP 160
Cdd:cd00919 83 PRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 161 GQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMI 240
Cdd:cd00919 163 GMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 241 SHIVSTFSRKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHLK 320
Cdd:cd00919 243 SEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 321 VPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHFW 400
Cdd:cd00919 323 PPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFW 402
|
410
....*....|
gi 780959610 401 TTFLGVNLTF 410
Cdd:cd00919 403 LWFIGFNLTF 412
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-410 |
9.88e-160 |
|
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: 458.97 E-value: 9.88e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 2 LYLFFGTFSGVLGGCMSLLIRMELMQPGNHFLIGNHqlYNVLITAHAFLMIFFMVMPILIGgFGNWLVPIMIGSPDMAFP 81
Cdd:cd01662 13 MYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 82 RLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSPG 161
Cdd:cd01662 90 RLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 162 QSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 241
Cdd:cd01662 170 MTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 242 HIVSTFSRKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHLKV 321
Cdd:cd01662 250 EIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFET 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 322 PMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHFWT 401
Cdd:cd01662 330 PMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWL 409
|
....*....
gi 780959610 402 TFLGVNLTF 410
Cdd:cd01662 410 WFIGFNLTF 418
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-410 |
6.13e-133 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 391.35 E-value: 6.13e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 2 LYLFFGTFSGVLGGCMSLLIRMELMQPgnHFLIGNHQLYNVLITAHAFLMIFFMVMPILIGGFGNWLVPIMIGSPDMAFP 81
Cdd:MTH00048 19 IYTLLGVWSGFVGLSLSLLIRLNFLDP--YYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 82 RLNNISFWLLPPSLCLLLLSSLVevGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSPG 161
Cdd:MTH00048 97 RLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 162 QSmYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 241
Cdd:MTH00048 175 VF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIIS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 242 HIVSTFSRKP-VFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHLK 320
Cdd:MTH00048 254 HICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 321 VPML-FAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHF 399
Cdd:MTH00048 334 DPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHC 413
|
410
....*....|.
gi 780959610 400 WTTFLGVNLTF 410
Cdd:MTH00048 414 IISMIGFNLCF 424
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
2-410 |
4.72e-121 |
|
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: 358.04 E-value: 4.72e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 2 LYLFFGTFSGVLGGCMSLLIRMELMQPGNHFLigNHQLYNVLITAHAFLMIFFMVMPIlIGGFGNWLVPIMIGSPDMAFP 81
Cdd:pfam00115 5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 82 RLNNISFWLLPPSLCLLLLSSLvevGAGTGWTVYPPLssiqshsgGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSPG 161
Cdd:pfam00115 82 RLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 162 QSMyRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTaffdpsGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 241
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 242 HIVSTFSRKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHL-K 320
Cdd:pfam00115 224 YILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 321 VPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHFW 400
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFW 383
|
410
....*....|
gi 780959610 401 TTFLGVNLTF 410
Cdd:pfam00115 384 LLFIGFNLTF 393
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-410 |
5.60e-103 |
|
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: 318.72 E-value: 5.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 2 LYLFFGTFSGVLGGCMSLLIRMELMQPGNHFLIGNHqlYNVLITAHAFLMIFFMVMPILIGgFGNWLVPIMIGSPDMAFP 81
Cdd:TIGR02882 56 MYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 82 RLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLSSIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSPG 161
Cdd:TIGR02882 133 VLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 162 QSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDRNFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 241
Cdd:TIGR02882 213 MKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 242 HIVSTFSRKPVFGYIGMVYAMVSIGLLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHLKV 321
Cdd:TIGR02882 293 EIISTFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTT 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 322 PMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHFWT 401
Cdd:TIGR02882 373 PMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWF 452
|
....*....
gi 780959610 402 TFLGVNLTF 410
Cdd:TIGR02882 453 FMIGFNVCF 461
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
40-410 |
3.60e-97 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 304.17 E-value: 3.60e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 40 YNVLITAHAFLMIFFMVMPILIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLCLLLLSSLVEVGAGTGWTVYPPLS 119
Cdd:PRK15017 99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 120 SIQSHSGGAVDLAIFSLHLSGAASILGAVNFISTIMNMRSPGQSMYRIPLFVWSIFITAFLLLLSLPVLAGAITMLLTDR 199
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 200 NFNTAFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSTFSRKPVFGYIGMVYAMVSIGLLGFIVWAHHMYT 279
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFT 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 280 VGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSLHLKVPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVV 359
Cdd:PRK15017 338 MGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLI 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 780959610 360 AHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEVLGQIHFWTTFLGVNLTF 410
Cdd:PRK15017 418 AHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAF 468
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
213-405 |
2.59e-10 |
|
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: 61.92 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 213 DPILYQHLFWFFGHPEVYILILPGFGMISHIVSTFSRKPVFGYIGMVYAMVSIGLLGFIVWAHHMYT-VGLDVDTRAYFT 291
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHM 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780959610 292 AATMIIAVPTGIKIFSWIATM--------------WEGSLHLKVPMLFAIGF-IFLFTIGGLTGIVLANSGLDISLHDTY 356
Cdd:cd01660 280 VLTFMVALPSLLTAFTVFASLeiagrlrggkglfgWIRALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTA 359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 780959610 357 YVVAHFHYVLSMGAVFAIFAGFYFWFGKISGLQYPEV-LGQIHFWTTFLG 405
Cdd:cd01660 360 WVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELAAKrLALAQPWLWFVG 409
|
|
| |
