|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-384 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 783.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:MTH00153 115 MVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYA 160
Cdd:MTH00153 195 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:MTH00153 275 MLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00153 355 VLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGM 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078553 321 PRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEWLQNNPP 384
Cdd:MTH00153 435 PRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPP 498
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-380 |
0e+00 |
|
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 683.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:cd01663 108 LVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYA 160
Cdd:cd01663 188 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:cd01663 268 MLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:cd01663 348 VLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGM 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823078553 321 PRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTN-MSSSTEWLQ 380
Cdd:cd01663 428 PRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeGSTSLEWTL 488
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-364 |
6.79e-156 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 449.58 E-value: 6.79e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:COG0843 119 FVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILIL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTIGMIYA 160
Cdd:COG0843 199 LAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:COG0843 278 TVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:COG0843 358 MLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGM 437
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 823078553 321 PRRYSDYP--DAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKR 364
Cdd:COG0843 438 PRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-384 |
8.93e-152 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 437.81 E-value: 8.93e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:TIGR02891 110 FTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILIL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTIGMIYA 160
Cdd:TIGR02891 190 LAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:TIGR02891 269 TVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGV 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:TIGR02891 349 MLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGM 428
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 823078553 321 PRRYSDYPDA--YTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEWLQNNPP 384
Cdd:TIGR02891 429 PRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPP 494
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
4-344 |
5.64e-104 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 313.36 E-value: 5.64e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 4 NGAGTGWTVYPPLASViahsgasvDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLeQTPLFVWSVVITALLLLLSL 83
Cdd:pfam00115 103 GGATTGWTEYPPLVGV--------DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 84 PVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTIGMIYAMLS 163
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 164 IGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFN-PPLLWALGFIFLFTMGGLTGLVL 242
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVML 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 243 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGMPR 322
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPR 406
|
330 340
....*....|....*....|....*.
gi 823078553 323 RYS----DYPDAYTSWNVMSSIGSTI 344
Cdd:pfam00115 407 RYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-384 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 783.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:MTH00153 115 MVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYA 160
Cdd:MTH00153 195 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:MTH00153 275 MLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00153 355 VLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGM 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078553 321 PRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEWLQNNPP 384
Cdd:MTH00153 435 PRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPP 498
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-380 |
0e+00 |
|
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 683.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:cd01663 108 LVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYA 160
Cdd:cd01663 188 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:cd01663 268 MLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:cd01663 348 VLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGM 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823078553 321 PRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTN-MSSSTEWLQ 380
Cdd:cd01663 428 PRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeGSTSLEWTL 488
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
2-384 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 649.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 2 VENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLLL 81
Cdd:MTH00116 118 VEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYAM 161
Cdd:MTH00116 198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAM 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGLV 241
Cdd:MTH00116 278 LSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 242 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:MTH00116 358 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMP 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823078553 322 RRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEWLQNNPP 384
Cdd:MTH00116 438 RRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPP 500
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-378 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 647.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:MTH00223 114 AVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYA 160
Cdd:MTH00223 194 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:MTH00223 274 MLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGI 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00223 354 ILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGM 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 823078553 321 PRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEW 378
Cdd:MTH00223 434 PRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEW 491
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-384 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 645.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:MTH00167 117 GVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYA 160
Cdd:MTH00167 197 LSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:MTH00167 277 MMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00167 357 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGM 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078553 321 PRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEWLQNNPP 384
Cdd:MTH00167 437 PRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPP 500
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-384 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 638.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:MTH00142 115 AVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYA 160
Cdd:MTH00142 195 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:MTH00142 275 MLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGI 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00142 355 VLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGM 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078553 321 PRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEWLQNNPP 384
Cdd:MTH00142 435 PRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLPP 498
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-383 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 578.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:MTH00007 114 AVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYA 160
Cdd:MTH00007 194 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:MTH00007 274 MLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGI 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00007 354 VLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGM 433
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823078553 321 PRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEWLQNNP 383
Cdd:MTH00007 434 PRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLP 496
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-384 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 574.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:MTH00103 117 MVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYA 160
Cdd:MTH00103 197 LSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:MTH00103 277 MMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00103 357 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGM 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078553 321 PRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEWLQNNPP 384
Cdd:MTH00103 437 PRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPP 500
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
2-384 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 572.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 2 VENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLLL 81
Cdd:MTH00183 118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYAM 161
Cdd:MTH00183 198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAM 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGLV 241
Cdd:MTH00183 278 MAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 242 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:MTH00183 358 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMP 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823078553 322 RRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEWLQNNPP 384
Cdd:MTH00183 438 RRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPP 500
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
2-384 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 564.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 2 VENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLLL 81
Cdd:MTH00077 118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYAM 161
Cdd:MTH00077 198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAM 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGLV 241
Cdd:MTH00077 278 MSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 242 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:MTH00077 358 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMP 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823078553 322 RRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEWLQNNPP 384
Cdd:MTH00077 438 RRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPP 500
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
2-384 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 560.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 2 VENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLLL 81
Cdd:MTH00037 118 VESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYAM 161
Cdd:MTH00037 198 SLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAM 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGLV 241
Cdd:MTH00037 278 IAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 242 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:MTH00037 358 LANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMP 437
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823078553 322 RRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEWLQNNPP 384
Cdd:MTH00037 438 RRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWQYSSFP 500
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-384 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 531.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLaSVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:MTH00079 118 FVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYA 160
Cdd:MTH00079 197 LSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:MTH00079 277 ILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGV 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00079 357 ILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGM 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078553 321 PRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEWLQNNPP 384
Cdd:MTH00079 437 PRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSYV 500
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-384 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 520.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:MTH00182 119 FVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYA 160
Cdd:MTH00182 199 LSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:MTH00182 279 MLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00182 359 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGF 438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823078553 321 PRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMS----SSTEWLQNNPP 384
Cdd:MTH00182 439 PRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEGTgeswASLEWVHSSPP 506
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-384 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 517.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:MTH00184 119 FVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYA 160
Cdd:MTH00184 199 LSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:MTH00184 279 MVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGI 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00184 359 VLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGL 438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 823078553 321 PRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKK---RTVMFSTNMSSSTEWLQNNPP 384
Cdd:MTH00184 439 PRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREikfVGWVEDSGHYPSLEWAQTSPP 505
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-360 |
5.18e-168 |
|
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: 477.79 E-value: 5.18e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:cd00919 105 LVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTIGMIYA 160
Cdd:cd00919 185 LALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:cd00919 264 FLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGV 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:cd00919 344 VLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGM 423
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 823078553 321 PRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESM 360
Cdd:cd00919 424 PRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-363 |
2.13e-157 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 453.32 E-value: 2.13e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:MTH00026 118 LVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYA 160
Cdd:MTH00026 198 LSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGT--KFKFNPPLLWALGFIFLFTMGGLT 238
Cdd:MTH00026 278 MLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLT 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 239 GLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLA 318
Cdd:MTH00026 358 GIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLA 437
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 823078553 319 GMPRRYSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKK 363
Cdd:MTH00026 438 GLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYRE 482
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-364 |
6.79e-156 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 449.58 E-value: 6.79e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:COG0843 119 FVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILIL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTIGMIYA 160
Cdd:COG0843 199 LAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:COG0843 278 TVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:COG0843 358 MLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGM 437
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 823078553 321 PRRYSDYP--DAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKR 364
Cdd:COG0843 438 PRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-384 |
8.93e-152 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 437.81 E-value: 8.93e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:TIGR02891 110 FTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILIL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTIGMIYA 160
Cdd:TIGR02891 190 LAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:TIGR02891 269 TVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGV 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:TIGR02891 349 MLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGM 428
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 823078553 321 PRRYSDYPDA--YTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSSTEWLQNNPP 384
Cdd:TIGR02891 429 PRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPP 494
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
5-375 |
2.45e-139 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 406.37 E-value: 2.45e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 5 GAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEqTPLFVWSVVITALLLLLSLP 84
Cdd:MTH00048 120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSR-TSIILWSYLFTSILLLLSLP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 85 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTIGMIYAMLSI 164
Cdd:MTH00048 199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 165 GLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLL-WALGFIFLFTMGGLTGLVLA 243
Cdd:MTH00048 279 VCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLS 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 244 NSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRR 323
Cdd:MTH00048 359 ASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRR 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 823078553 324 YSDYPDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSS 375
Cdd:MTH00048 439 VCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLGLWGSSSC 490
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-384 |
7.35e-133 |
|
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: 389.63 E-value: 7.35e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 1 LVENGAGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLL 80
Cdd:cd01662 111 LIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILIL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTIGMIYA 160
Cdd:cd01662 191 FAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGL 240
Cdd:cd01662 270 TVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGV 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 241 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:cd01662 350 MLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGM 429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 823078553 321 PRRYSDYP--DAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSST-EWLQNNPP 384
Cdd:cd01662 430 PRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDATGDPWGARTlEWATSSPP 496
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
4-344 |
5.64e-104 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 313.36 E-value: 5.64e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 4 NGAGTGWTVYPPLASViahsgasvDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLeQTPLFVWSVVITALLLLLSL 83
Cdd:pfam00115 103 GGATTGWTEYPPLVGV--------DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 84 PVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTIGMIYAMLS 163
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 164 IGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFN-PPLLWALGFIFLFTMGGLTGLVL 242
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVML 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 243 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGMPR 322
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPR 406
|
330 340
....*....|....*....|....*.
gi 823078553 323 RYS----DYPDAYTSWNVMSSIGSTI 344
Cdd:pfam00115 407 RYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
9-384 |
1.57e-83 |
|
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: 267.10 E-value: 1.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 9 GWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLLLSLPVLAG 88
Cdd:TIGR02882 162 GWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTV 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 89 AITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTIGMIYAMLSIGLMG 168
Cdd:TIGR02882 242 ALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLS 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 169 FIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGLVLANSSLD 248
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 249 IVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDY- 327
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYs 480
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 823078553 328 -PDAYTSWNVMSSIGSTISITGIIMFILIMWESMIKKRTVMFSTNMSSST-EWLQNNPP 384
Cdd:TIGR02882 481 pSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREATGDPWNGRTlEWATASPP 539
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
6-384 |
1.65e-80 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 259.48 E-value: 1.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 6 AGTGWTVYPPLASVIAHSGASVDLAIFSLHLAGISSILGAINFITTAINMRSSNMTLEQTPLFVWSVVITALLLLLSLPV 85
Cdd:PRK15017 166 AQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPI 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 86 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTIGMIYAMLSIG 165
Cdd:PRK15017 246 LTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCIT 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 166 LMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTMGGLTGLVLANS 245
Cdd:PRK15017 325 VLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 246 SLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGMTMNNKWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYS 325
Cdd:PRK15017 405 GADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLS 484
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823078553 326 DYPD-AYTSWNVMSSIGSTISITGIIMFILIMWESMIKK---RTVMFSTNMSSSTEWLQNNPP 384
Cdd:PRK15017 485 QQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRdqnRDLTGDPWGGRTLEWATSSPP 547
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
111-360 |
4.85e-20 |
|
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: 91.19 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 111 DPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGkIESFGTIGMIYAMLSIGLMGFIVWAHHMFT-VGMDVDTRAYF 189
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAG-GKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 190 TSATMIIAVPTGIKVFSWMATL-YGTKFKFNPPLLW---------------ALGFIFlFTMGGLTGLVLANSSLDIVLHD 253
Cdd:cd01660 279 MVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHN 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078553 254 TYYVVAHFHyvLSMGAVFAIMG-GIIQWY-PLFTGMTMNNKWL-KIQFTIMFIGVNLTFFPQHFLGLAGMPRR--YSDYP 328
Cdd:cd01660 358 TAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435
|
250 260 270
....*....|....*....|....*....|....*..
gi 823078553 329 DAY-----TSWNVMSSIGSTISITGIIMFILIMWESM 360
Cdd:cd01660 436 GLPaagewAPYQQLMAIGGTILFVSGALFLYILFRTL 472
|
|
| |
