|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-277 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 513.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00153 58 AHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00153 138 GASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00153 218 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDV 297
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:MTH00153 298 DTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-277 |
3.47e-178 |
|
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: 499.70 E-value: 3.47e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:cd01663 51 AHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:cd01663 131 GPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:cd01663 211 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDV 290
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:cd01663 291 DTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-275 |
2.30e-115 |
|
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: 340.35 E-value: 2.30e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILiGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:TIGR02891 54 MHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:TIGR02891 133 GVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHF 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKiETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:TIGR02891 213 FDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPP 291
|
250 260 270
....*....|....*....|....*....|....*
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYM 275
Cdd:TIGR02891 292 LALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRF 326
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-277 |
6.87e-111 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 330.17 E-value: 6.87e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPIlIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:COG0843 63 MHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:COG0843 142 GVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKiETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:COG0843 222 FDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISP 300
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:COG0843 301 LVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTT 337
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-276 |
5.23e-73 |
|
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: 229.77 E-value: 5.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPIlIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMvesGAGTGWTIYPPLadnmghs 80
Cdd:pfam00115 47 LHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 gMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLdRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTsf 160
Cdd:pfam00115 116 -VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 fdpiGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKiETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:pfam00115 192 ----GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPP 266
|
250 260 270
....*....|....*....|....*....|....*.
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMN 276
Cdd:pfam00115 267 WLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFR 302
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-277 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 513.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00153 58 AHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00153 138 GASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00153 218 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDV 297
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:MTH00153 298 DTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-277 |
3.47e-178 |
|
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: 499.70 E-value: 3.47e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:cd01663 51 AHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:cd01663 131 GPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:cd01663 211 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDV 290
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:cd01663 291 DTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-277 |
5.45e-168 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 474.85 E-value: 5.45e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00223 57 AHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00223 137 GPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00223 217 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDV 296
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:MTH00223 297 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEA 333
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-276 |
1.02e-162 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 461.45 E-value: 1.02e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00167 60 AHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00167 140 GASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00167 220 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDV 299
|
250 260 270
....*....|....*....|....*....|....*.
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMN 276
Cdd:MTH00167 300 DTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWE 335
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-277 |
2.67e-159 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 453.01 E-value: 2.67e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00116 60 AHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00116 140 GASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00116 220 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDV 299
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:MTH00116 300 DTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDP 336
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-277 |
5.19e-158 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 449.56 E-value: 5.19e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00142 58 AHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00142 138 GGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00142 218 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDV 297
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:MTH00142 298 DTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEP 334
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-273 |
6.12e-150 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 428.94 E-value: 6.12e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00007 57 AHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00007 137 GPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00007 217 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDV 296
|
250 260 270
....*....|....*....|....*....|...
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKV 273
Cdd:MTH00007 297 DTRAYFTAATMIIAVPTGIKVFSWLATIHGSPI 329
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-277 |
2.08e-144 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 415.38 E-value: 2.08e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00037 60 AHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00037 140 GGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00037 220 FDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDV 299
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:MTH00037 300 DTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWET 336
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
1.16e-140 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 406.13 E-value: 1.16e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00182 62 AHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00182 142 GGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00182 222 FDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDV 301
|
250 260 270
....*....|....*....|....*....|...
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKV 273
Cdd:MTH00182 302 DTRAYFTAATMIIAVPTGIKVFSWLATIYGGTL 334
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-277 |
1.10e-138 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 400.41 E-value: 1.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00103 60 AHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00103 140 GASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00103 220 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDV 299
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:MTH00103 300 DTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSP 336
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-270 |
2.75e-138 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 399.59 E-value: 2.75e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00184 62 AHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00184 142 GGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00184 222 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDV 301
|
250 260 270
....*....|....*....|....*....|
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYG 270
Cdd:MTH00184 302 DTRAYFTAATMIIAVPTGIKIFSWIATIFG 331
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-273 |
3.27e-137 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 396.99 E-value: 3.27e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00183 60 AHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00183 140 GASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00183 220 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDV 299
|
250 260 270
....*....|....*....|....*....|...
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKV 273
Cdd:MTH00183 300 DTRAYFTSATMIIAIPTGVKVFSWLATLHGGSI 332
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-270 |
4.98e-136 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 393.92 E-value: 4.98e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00077 60 AHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00077 140 GASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00077 220 FDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNV 299
|
250 260 270
....*....|....*....|....*....|
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYG 270
Cdd:MTH00077 300 DTRAYFTSATMIIAIPTGVKVFSWLATMHG 329
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-277 |
2.26e-135 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 391.74 E-value: 2.26e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLAdNMGHS 80
Cdd:MTH00079 61 AHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00079 140 GSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00079 220 FDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDL 299
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:MTH00079 300 DSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQP 336
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-271 |
1.20e-122 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 360.48 E-value: 1.20e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:MTH00026 61 AHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:MTH00026 141 GGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:MTH00026 221 FDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDV 300
|
250 260 270
....*....|....*....|....*....|.
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGS 271
Cdd:MTH00026 301 DTRAYFTAATMIIAVPTGIKIFSWLATVSGS 331
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-277 |
3.98e-117 |
|
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: 343.74 E-value: 3.98e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGGFGNWLIPlMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:cd00919 49 AHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:cd00919 128 GVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKiETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:cd00919 208 FDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPV 286
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:cd00919 287 DTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDP 323
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-275 |
2.30e-115 |
|
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: 340.35 E-value: 2.30e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILiGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:TIGR02891 54 MHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:TIGR02891 133 GVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHF 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKiETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:TIGR02891 213 FDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPP 291
|
250 260 270
....*....|....*....|....*....|....*
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYM 275
Cdd:TIGR02891 292 LALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRF 326
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-277 |
6.87e-111 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 330.17 E-value: 6.87e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPIlIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:COG0843 63 MHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:COG0843 142 GVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKiETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:COG0843 222 FDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISP 300
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:COG0843 301 LVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTT 337
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-274 |
2.77e-105 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 315.08 E-value: 2.77e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 2 HGLIMIFFVVMPILIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVesGAGTGWTIYPPLADNMGHSG 81
Cdd:MTH00048 62 HGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 82 MSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLdRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSFF 161
Cdd:MTH00048 140 WGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFF 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 162 DPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKIETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDVD 241
Cdd:MTH00048 219 DPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVK 298
|
250 260 270
....*....|....*....|....*....|...
gi 1409212053 242 TRAYFTAATMIIAVPTGIKVFSWLATIYGSKVY 274
Cdd:MTH00048 299 TAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVR 331
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-277 |
1.04e-96 |
|
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: 292.95 E-value: 1.04e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGgFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:cd01662 55 MHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:cd01662 134 GVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHF 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKiETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:cd01662 214 FTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGA 292
|
250 260 270
....*....|....*....|....*....|....*..
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMNP 277
Cdd:cd01662 293 LVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFET 329
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-276 |
5.23e-73 |
|
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: 229.77 E-value: 5.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPIlIGGFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMvesGAGTGWTIYPPLadnmghs 80
Cdd:pfam00115 47 LHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 gMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLdRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTsf 160
Cdd:pfam00115 116 -VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 fdpiGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKiETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:pfam00115 192 ----GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPP 266
|
250 260 270
....*....|....*....|....*....|....*.
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMN 276
Cdd:pfam00115 267 WLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFR 302
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-276 |
2.09e-66 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 218.27 E-value: 2.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 1 AHGLIMIFFVVMPILIGgFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHS 80
Cdd:PRK15017 105 AHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSP 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 81 GMSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSF 160
Cdd:PRK15017 184 GVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHF 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 161 FDPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKiETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDV 240
Cdd:PRK15017 264 FTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGA 342
|
250 260 270
....*....|....*....|....*....|....*.
gi 1409212053 241 DTRAYFTAATMIIAVPTGIKVFSWLATIYGSKVYMN 276
Cdd:PRK15017 343 NVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFH 378
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-273 |
1.75e-63 |
|
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: 210.10 E-value: 1.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 2 HGLIMIFFVVMPILIGgFGNWLIPLMIGSPDMAFPRLNNLSFWLLPPSMTMLLSSSMVESGAGTGWTIYPPLADNMGHSG 81
Cdd:TIGR02882 99 HGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 82 MSVDMAIFSLHLAGASSILGSLNFITTIFNMRWPGMSLDRIPLFIWSVAITTVLLLLSLPVLAAAITMLLTDRNINTSFF 161
Cdd:TIGR02882 178 VGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFF 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409212053 162 DPIGGGDPILFQHLFWFFGHPEVYILILPGFGAISHIITSHSKKiETFGTLGMIYAMVGIAILGFIVWAHHMFTVGLDVD 241
Cdd:TIGR02882 258 TVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGAL 336
|
250 260 270
....*....|....*....|....*....|..
gi 1409212053 242 TRAYFTAATMIIAVPTGIKVFSWLATIYGSKV 273
Cdd:TIGR02882 337 INSFFSITTMAIAIPTGVKIFNWLLTLYKGKI 368
|
|
|