|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 798.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00153 94 RMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00153 174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00153 254 HIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYS 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00153 334 PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFF 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLEWY 400
Cdd:MTH00153 414 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWL 493
|
....*...
gi 195971001 401 QNSPPAEH 408
Cdd:MTH00153 494 QNLPPAEH 501
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-399 |
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: 684.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:cd01663 87 RLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:cd01663 167 MTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:cd01663 247 HIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFE 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:cd01663 327 TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFW 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALF-PLNMMSSLEW 399
Cdd:cd01663 407 LMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGSTSLEW 486
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-408 |
5.09e-153 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 443.03 E-value: 5.09e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:COG0843 98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:COG0843 178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKtESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:COG0843 258 EIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFT 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:COG0843 337 TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFW 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTAL-FPLNmMSSL 397
Cdd:COG0843 417 LWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAGgNPWG-ARTL 495
|
410
....*....|.
gi 195971001 398 EWYQNSPPAEH 408
Cdd:COG0843 496 EWATPSPPPLY 506
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-408 |
7.64e-152 |
|
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: 438.97 E-value: 7.64e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:TIGR02891 89 RLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:TIGR02891 169 MTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIIS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKtESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:TIGR02891 249 EILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFT 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:TIGR02891 328 TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFW 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPD--IYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLE 398
Cdd:TIGR02891 408 LTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLE 487
|
410
....*....|
gi 195971001 399 WYQNSPPAEH 408
Cdd:TIGR02891 488 WTTSSPPPAH 497
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-365 |
2.18e-104 |
|
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: 315.28 E-value: 2.18e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSlveNGAGTGWTVYPPLSAgiahagasVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:pfam00115 82 RLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLdQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKtESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNF- 239
Cdd:pfam00115 224 YILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFr 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 240 SPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQF 319
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 195971001 320 TIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDIYVSWNIMSSLGSTI 365
Cdd:pfam00115 383 WLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 798.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00153 94 RMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00153 174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00153 254 HIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYS 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00153 334 PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFF 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLEWY 400
Cdd:MTH00153 414 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWL 493
|
....*...
gi 195971001 401 QNSPPAEH 408
Cdd:MTH00153 494 QNLPPAEH 501
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-399 |
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: 684.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:cd01663 87 RLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:cd01663 167 MTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:cd01663 247 HIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFE 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:cd01663 327 TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFW 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALF-PLNMMSSLEW 399
Cdd:cd01663 407 LMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEGSTSLEW 486
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 652.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00167 96 RMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00167 176 ITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00167 256 HIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00167 336 TPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFF 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLEWY 400
Cdd:MTH00167 416 VMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWL 495
|
....*...
gi 195971001 401 QNSPPAEH 408
Cdd:MTH00167 496 HGCPPPHH 503
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 652.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00116 96 RMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00116 176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00116 256 HIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWD 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00116 336 PPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFG 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLEWY 400
Cdd:MTH00116 416 VMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWI 495
|
....*...
gi 195971001 401 QNSPPAEH 408
Cdd:MTH00116 496 HGCPPPYH 503
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 649.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00142 94 RMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00142 174 MKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00142 254 HIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYE 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00142 334 PPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFY 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLEWY 400
Cdd:MTH00142 414 TMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWS 493
|
....*...
gi 195971001 401 QNSPPAEH 408
Cdd:MTH00142 494 HRLPPDFH 501
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 646.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00223 93 RLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00223 173 MQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00223 253 HIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00223 333 APMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFF 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLEWY 400
Cdd:MTH00223 413 LMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWD 492
|
....*...
gi 195971001 401 QNSPPAEH 408
Cdd:MTH00223 493 NLLPADFH 500
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 585.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00037 96 RMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00037 176 MTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMIS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00037 256 HVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00037 336 TPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFF 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLEW- 399
Cdd:MTH00037 416 LMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWq 495
|
....*....
gi 195971001 400 YQNSPPAEH 408
Cdd:MTH00037 496 YSSFPPSHH 504
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 581.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00103 96 RMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00103 176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00103 256 HIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00103 336 PAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFT 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLEWY 400
Cdd:MTH00103 416 IMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWL 495
|
....*...
gi 195971001 401 QNSPPAEH 408
Cdd:MTH00103 496 HGCPPPYH 503
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 573.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00183 96 RMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00183 176 ISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00183 256 HIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00183 336 TPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFG 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLEWY 400
Cdd:MTH00183 416 VMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWL 495
|
....*...
gi 195971001 401 QNSPPAEH 408
Cdd:MTH00183 496 HGCPPPYH 503
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 570.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00007 93 RLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00007 173 LRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAIS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00007 253 HIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00007 333 TPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFF 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLEWY 400
Cdd:MTH00007 413 LMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQ 492
|
....*...
gi 195971001 401 QNSPPAEH 408
Cdd:MTH00007 493 DTLPLDFH 500
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 564.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00077 96 RMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00077 176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMIS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00077 256 HIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWD 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00077 336 AAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFG 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLEWY 400
Cdd:MTH00077 416 VMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWL 495
|
....*...
gi 195971001 401 QNSPPAEH 408
Cdd:MTH00077 496 HGCPPPYH 503
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 536.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAgIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00079 97 RLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00079 176 ISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIIS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00079 256 QSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQ 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00079 336 PLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFF 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLEWY 400
Cdd:MTH00079 416 LMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYS 495
|
....*...
gi 195971001 401 QNSPPAEH 408
Cdd:MTH00079 496 LSSYVFGH 503
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 527.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00182 98 RLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00182 178 VTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMIS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00182 258 QIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLD 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00182 338 TPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFW 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTAL----FPLNMMSS 396
Cdd:MTH00182 418 LMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIgwkeGTGESWAS 497
|
410
....*....|..
gi 195971001 397 LEWYQNSPPAEH 408
Cdd:MTH00182 498 LEWVHSSPPLFH 509
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 515.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00184 98 RLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00184 178 ITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:MTH00184 258 QIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLD 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:MTH00184 338 TPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFW 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESM---ISNRTALFPLNMMSSL 397
Cdd:MTH00184 418 LMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYvreIKFVGWVEDSGHYPSL 497
|
410
....*....|.
gi 195971001 398 EWYQNSPPAEH 408
Cdd:MTH00184 498 EWAQTSPPAHH 508
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-381 |
5.40e-167 |
|
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: 476.25 E-value: 5.40e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:cd00919 84 RLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:cd00919 164 MTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAIS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKtESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:cd00919 244 EIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFD 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:cd00919 323 PPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFW 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESM 381
Cdd:cd00919 403 LWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
2.27e-158 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 456.78 E-value: 2.27e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:MTH00026 97 RLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:MTH00026 177 MTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLN-- 238
Cdd:MTH00026 257 QILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNli 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 239 FSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQ 318
Cdd:MTH00026 337 FTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIH 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 319 FTIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMIsnRTALFPLNMMS--- 395
Cdd:MTH00026 417 FWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYY--REEPFDINIMAkgp 494
|
410 420
....*....|....*....|....*
gi 195971001 396 ------------SLEWYQNSPPAEH 408
Cdd:MTH00026 495 lipfscqpahfdTLEWSLTSPPEHH 519
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-408 |
5.09e-153 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 443.03 E-value: 5.09e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:COG0843 98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:COG0843 178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKtESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:COG0843 258 EIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFT 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:COG0843 337 TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFW 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTAL-FPLNmMSSL 397
Cdd:COG0843 417 LWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAGgNPWG-ARTL 495
|
410
....*....|.
gi 195971001 398 EWYQNSPPAEH 408
Cdd:COG0843 496 EWATPSPPPLY 506
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-408 |
7.64e-152 |
|
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: 438.97 E-value: 7.64e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:TIGR02891 89 RLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:TIGR02891 169 MTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIIS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKtESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:TIGR02891 249 EILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFT 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:TIGR02891 328 TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFW 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPD--IYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLE 398
Cdd:TIGR02891 408 LTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLE 487
|
410
....*....|
gi 195971001 399 WYQNSPPAEH 408
Cdd:TIGR02891 488 WTTSSPPPAH 497
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
26-408 |
4.49e-138 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 404.44 E-value: 4.49e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 26 GAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPGMSLdQTPLFVWAVAITALLLLLSLP 105
Cdd:MTH00048 120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 106 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKTESFGALGMIYAMLAI 185
Cdd:MTH00048 199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 186 GLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS-PALLWALGFVFLFTIGGLTGVVLA 264
Cdd:MTH00048 279 VCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLS 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 265 NSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRR 344
Cdd:MTH00048 359 ASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRR 438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195971001 345 YSDYPDIYVSWNIMSSLGSTISFIGILLLIFIIWESMISNRTALFPLNMMSSLEWYQNSPPAEH 408
Cdd:MTH00048 439 VCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLGLWGSSSCVVNVLMSPVPYH 502
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-408 |
1.95e-134 |
|
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.
Pssm-ID: 238832 Cd Length: 501 Bit Score: 394.64 E-value: 1.95e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:cd01662 90 RLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:cd01662 170 MTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKtESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:cd01662 250 EIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:cd01662 329 TPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFW 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DIYVSWNIMSSLGSTISFIGILLLIFIIWESMIS--NRTALFPLNmMSS 396
Cdd:cd01662 409 LWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKgkRDATGDPWG-ART 487
|
410
....*....|..
gi 195971001 397 LEWYQNSPPAEH 408
Cdd:cd01662 488 LEWATSSPPPAY 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-365 |
2.18e-104 |
|
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: 315.28 E-value: 2.18e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSlveNGAGTGWTVYPPLSAgiahagasVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:pfam00115 82 RLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLdQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKtESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNF- 239
Cdd:pfam00115 224 YILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFr 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 240 SPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQF 319
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 195971001 320 TIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDIYVSWNIMSSLGSTI 365
Cdd:pfam00115 383 WLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-348 |
9.24e-84 |
|
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: 268.65 E-value: 9.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 1 RMNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPG 80
Cdd:TIGR02882 133 VLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 81 MSLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 160
Cdd:TIGR02882 213 MKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 161 HIISQESGKtESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFS 240
Cdd:TIGR02882 293 EIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 241 PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFT 320
Cdd:TIGR02882 372 TPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFW 451
|
330 340
....*....|....*....|....*...
gi 195971001 321 IMFIGVNLTFFPQHFLGLAGMPRRYSDY 348
Cdd:TIGR02882 452 FFMIGFNVCFFPMYILGLDGMPRRMYTY 479
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
2-350 |
4.87e-83 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 267.19 E-value: 4.87e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 2 MNNMSFWLLPPSLTLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGVSSILGAVNFITTTINMRSPGM 81
Cdd:PRK15017 141 LNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGM 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 82 SLDQTPLFVWAVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 161
Cdd:PRK15017 221 TMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 162 IISQESgKTESFGALGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNFSP 241
Cdd:PRK15017 301 IAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHS 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 242 ALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLSLNPKWLKIQFTI 321
Cdd:PRK15017 380 AMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWF 459
|
330 340
....*....|....*....|....*....
gi 195971001 322 MFIGVNLTFFPQHFLGLAGMPRRYSDYPD 350
Cdd:PRK15017 460 WIIGFFVAFMPLYALGFMGMTRRLSQQID 488
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
132-365 |
8.38e-18 |
|
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: 85.03 E-value: 8.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 132 DPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGkTESFGALGMIYAMLAIGLLGFVVWAHHMFT-VGMDVDTRAYF 210
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAG-GKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 211 TSATMIIAVPTGIKIFSWLATL-HGTQLNFSPALLW---------------ALGFVFlFTIGGLTGVVLANSSLDIILHD 274
Cdd:cd01660 279 MVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHN 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195971001 275 TYYVVAHFHyvLSMGAVFAIMAGFIQWY--PLFTGLSLNPKWL-KIQFTIMFIGVNLTFFPQHFLGLAGMPRR--YSDYP 349
Cdd:cd01660 358 TAWVPGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435
|
250 260
....*....|....*....|.
gi 195971001 350 DIYV-----SWNIMSSLGSTI 365
Cdd:cd01660 436 GLPAagewaPYQQLMAIGGTI 456
|
|
| |
