|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 556.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00153 20 FGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00153 100 FWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRM 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00153 180 PLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQE 259
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00153 260 SGKKETFGTLGMIYAMLAIGLLGFIVWAH 288
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-269 |
7.32e-176 |
|
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: 493.54 E-value: 7.32e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:cd01663 13 FGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:cd01663 93 FWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:cd01663 173 PLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTF 252
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:cd01663 253 SGKKPVFGYLGMVYAMLSIGILGFIVWAH 281
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
6-269 |
1.95e-101 |
|
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: 304.53 E-value: 1.95e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 6 GMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMiGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 85
Cdd:TIGR02891 21 FLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 86 PSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQTPLFVW 165
Cdd:TIGR02891 100 FGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 166 SVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiE 245
Cdd:TIGR02891 180 GILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-P 258
|
250 260
....*....|....*....|....
gi 1790787371 246 SFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:TIGR02891 259 IFGYRAMVYATVAIGFLSFGVWAH 282
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
7-269 |
2.94e-97 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 295.11 E-value: 2.94e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 7 MVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 86
Cdd:COG0843 31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 87 SLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQTPLFVWS 166
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 167 VAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiES 246
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PL 268
|
250 260
....*....|....*....|...
gi 1790787371 247 FGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:COG0843 269 FGYKAMVLATVAIAFLSFLVWAH 291
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-269 |
8.65e-65 |
|
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: 208.20 E-value: 8.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:pfam00115 9 TALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMvdsGVGTGWTVYPPLAGaiahggasVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLdQT 160
Cdd:pfam00115 88 FWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:pfam00115 156 PLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKF 229
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKiESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:pfam00115 230 AGR-PLFGYKLSVLAFWLIAFLGFLVWAH 257
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 556.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00153 20 FGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00153 100 FWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRM 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00153 180 PLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQE 259
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00153 260 SGKKETFGTLGMIYAMLAIGLLGFIVWAH 288
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-269 |
7.32e-176 |
|
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: 493.54 E-value: 7.32e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:cd01663 13 FGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:cd01663 93 FWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:cd01663 173 PLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTF 252
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:cd01663 253 SGKKPVFGYLGMVYAMLSIGILGFIVWAH 281
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
2.62e-169 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 478.02 E-value: 2.62e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00167 22 FGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00167 102 FWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00167 182 PLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYY 261
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00167 262 SGKKEPFGYMGMVWAMMAIGLLGFIVWAH 290
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
4.36e-168 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 474.97 E-value: 4.36e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00116 22 FGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00116 102 FWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00116 182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYY 261
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00116 262 AGKKEPFGYMGMVWAMLSIGFLGFIVWAH 290
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
1.85e-164 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 465.61 E-value: 1.85e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00223 19 FGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00223 99 FWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00223 179 PLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHY 258
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00223 259 SSKKEVFGTLGMIYAMLSIGVLGFIVWAH 287
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
5.32e-164 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 464.20 E-value: 5.32e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00142 20 FGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00142 100 FWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00142 180 PLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHY 259
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00142 260 SGKKEVFGTLGMIYAMLSIGLLGFIVWAH 288
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
1.15e-150 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 430.52 E-value: 1.15e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00077 22 FGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00077 102 FWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00077 182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYY 261
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00077 262 SAKKEPFGYMGMVWAMMSIGLLGFIVWAH 290
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-269 |
1.64e-150 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 430.07 E-value: 1.64e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00103 22 FGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00103 102 FWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00103 182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYY 261
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00103 262 SGKKEPFGYMGMVWAMMSIGFLGFIVWAH 290
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
4.87e-148 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 423.95 E-value: 4.87e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00183 22 FGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00183 102 FWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00183 182 PLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYY 261
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00183 262 SGKKEPFGYMGMVWAMMAIGLLGFIVWAH 290
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-269 |
1.90e-147 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 422.39 E-value: 1.90e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00007 19 LGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00007 99 FWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00007 179 PLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHY 258
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00007 259 AGKLEPFGTLGMIYAMLGIGVLGFIVWAH 287
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
2.47e-147 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 422.32 E-value: 2.47e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00037 22 FGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00037 102 FWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00037 182 PLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHY 261
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00037 262 SGKQEPFGYLGMVYAMIAIGILGFLVWAH 290
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
3.20e-134 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 389.18 E-value: 3.20e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00182 24 FGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNIS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00182 104 FWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00182 184 PLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTF 263
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00182 264 VAKKQIFGYLGMVYAMLSIGILGFIVWAH 292
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
1.06e-133 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 387.11 E-value: 1.06e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00079 23 FGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAgAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00079 103 FWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHM 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00079 182 SLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYL 261
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00079 262 TGKKEVFGSLGMVYAILSIGLIGCVVWAH 290
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
1.20e-133 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 387.64 E-value: 1.20e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00184 24 FGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNIS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00184 104 FWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00184 184 PLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTF 263
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00184 264 AAKKQIFGYLGMVYAMVSIGILGFIVWAH 292
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
7.68e-122 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 358.17 E-value: 7.68e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00026 23 FGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNIS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:MTH00026 103 FWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00026 183 PLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLF 262
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00026 263 SYKKQIFGYLGMVYAMLAIGVLGFIVWAH 291
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-269 |
4.87e-109 |
|
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: 322.94 E-value: 4.87e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPlMIGAPDMAFPRMNNMS 80
Cdd:cd00919 11 FAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQT 160
Cdd:cd00919 90 FWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:cd00919 170 PLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTF 249
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKiESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:cd00919 250 SGK-PLFGYKLMVYAFLAIGFLSFLVWAH 277
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
6-269 |
1.95e-101 |
|
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: 304.53 E-value: 1.95e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 6 GMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMiGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLP 85
Cdd:TIGR02891 21 FLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 86 PSLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQTPLFVW 165
Cdd:TIGR02891 100 FGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVW 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 166 SVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiE 245
Cdd:TIGR02891 180 GILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-P 258
|
250 260
....*....|....*....|....
gi 1790787371 246 SFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:TIGR02891 259 IFGYRAMVYATVAIGFLSFGVWAH 282
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
7-269 |
2.94e-97 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 295.11 E-value: 2.94e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 7 MVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 86
Cdd:COG0843 31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 87 SLTLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQTPLFVWS 166
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 167 VAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiES 246
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PL 268
|
250 260
....*....|....*....|...
gi 1790787371 247 FGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:COG0843 269 FGYKAMVLATVAIAFLSFLVWAH 291
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-269 |
1.60e-93 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 284.65 E-value: 1.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:MTH00048 23 LGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMVdsGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLdQT 160
Cdd:MTH00048 103 AWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:MTH00048 180 SIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSL 259
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKIESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:MTH00048 260 SNNDDPFGYYGLVFAMFSIVCLGSVVWAH 288
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
9-269 |
1.02e-80 |
|
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: 251.35 E-value: 1.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 9 GTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 88
Cdd:cd01662 25 GGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 89 TLLIASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQTPLFVWSVA 168
Cdd:cd01662 104 LLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 169 ITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFG 248
Cdd:cd01662 184 VTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFG 262
|
250 260
....*....|....*....|.
gi 1790787371 249 TLGMIYAMLSIGLMGFIVWAH 269
Cdd:cd01662 263 YRSMVYATVAIGFLSFGVWVH 283
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-269 |
8.65e-65 |
|
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: 208.20 E-value: 8.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 1 FGAWSGMVGTSMSMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMAFPRMNNMS 80
Cdd:pfam00115 9 TALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 81 FWLLPPSLTLLIASSMvdsGVGTGWTVYPPLAGaiahggasVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLdQT 160
Cdd:pfam00115 88 FWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 161 PLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQE 240
Cdd:pfam00115 156 PLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKF 229
|
250 260
....*....|....*....|....*....
gi 1790787371 241 SGKiESFGTLGMIYAMLSIGLMGFIVWAH 269
Cdd:pfam00115 230 AGR-PLFGYKLSVLAFWLIAFLGFLVWAH 257
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
13-269 |
3.40e-52 |
|
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: 179.66 E-value: 3.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 13 SMIIRAELGQPGYLIGDDQIYNVIITAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLI 92
Cdd:TIGR02882 72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 93 ASSMVDSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQTPLFVWSVAITAL 172
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 173 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGM 252
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQK-RLFGYKSM 309
|
250
....*....|....*..
gi 1790787371 253 IYAMLSIGLMGFIVWAH 269
Cdd:TIGR02882 310 VWSTVGIAFLSFLVWVH 326
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
18-269 |
1.01e-49 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 173.58 E-value: 1.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 18 AELGQPGYLigDDQIYNVIITAHAFVMIFFMVMPIMIGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLIASSMV 97
Cdd:PRK15017 86 ASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 98 DSGVGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSKSMTLDQTPLFVWSVAITALLLLLS 177
Cdd:PRK15017 163 GEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIAS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 178 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAML 257
Cdd:PRK15017 243 FPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATV 321
|
250
....*....|..
gi 1790787371 258 SIGLMGFIVWAH 269
Cdd:PRK15017 322 CITVLSFIVWLH 333
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
26-242 |
6.47e-03 |
|
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: 37.65 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 26 LIGDDQIYNVIITAHAFVM-IFFMVMPIMigGFGNWLVPLMIGAPDMAfPRMNNMSFWLLppSLTLLIASSMVDSGVGTG 104
Cdd:cd01660 37 LPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN-RRLAWAGFWLM--VIGTVMAAVPILLGQASV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 105 -WTVYPPLagaIAHGGASVDLAIFSLHlagiSSILGAVNFITTAinmRSKSMTLDQ-TPLFVWSVAITALLLLLSLPVLA 182
Cdd:cd01660 112 lYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLW---RWKKANPGKkVPLATFMVVTTMILWLVASLGVA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790787371 183 GAITMLLtdrnLNTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESG 242
Cdd:cd01660 182 LEVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAG 236
|
|
|