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Conserved domains on  [gi|1100876467|gb|APB87563|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Sitophilus oryzae]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-269 0e+00

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.


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 551.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00153   56 VTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00153  136 HSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNT 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00153  216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGM 295

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00153  296 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 324
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-269 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 551.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00153   56 VTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00153  136 HSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNT 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00153  216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGM 295

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00153  296 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 324
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-269 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: 518.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:cd01663    49 VTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:cd01663   129 HSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNT 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:cd01663   209 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGL 288

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:cd01663   289 DVDTRAYFTAATMIIAVPTGIKVFSWLAT 317
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-269 2.53e-113

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: 334.96  E-value: 2.53e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMiGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:TIGR02891  52 FTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:TIGR02891 131 SPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGT 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:TIGR02891 211 HFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGM 289

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:TIGR02891 290 PPLALAFFSAATMLIAVPTGVKVFNWIAT 318
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-269 1.13e-112

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 334.40  E-value: 1.13e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:COG0843    61 FTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:COG0843   140 SPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGT 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:COG0843   220 HFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGI 298

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:COG0843   299 SPLVKAFFSIATMLIAVPTGVKVFNWIAT 327
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-269 7.60e-70

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: 221.29  E-value: 7.60e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSfieKGAGTGWTVYPPLssnia 80
Cdd:pfam00115  45 RTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL----- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 hegASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMlSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINt 160
Cdd:pfam00115 116 ---VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-TLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG- 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 sffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:pfam00115 191 -----AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGL 264

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:pfam00115 265 PPWLQALFSVFSMLIAVPSGVKVFNWLAT 293
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-269 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 551.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00153   56 VTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00153  136 HSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNT 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00153  216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGM 295

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00153  296 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 324
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-269 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: 518.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:cd01663    49 VTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:cd01663   129 HSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNT 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:cd01663   209 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGL 288

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:cd01663   289 DVDTRAYFTAATMIIAVPTGIKVFSWLAT 317
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-269 3.74e-172

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 484.95  E-value: 3.74e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00167   58 VTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00167  138 HAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNT 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00167  218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 297

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00167  298 DVDTRAYFTSATMIIAVPTGIKVFSWLAT 326
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-269 2.27e-171

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 482.94  E-value: 2.27e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00223   55 VTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLA 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00223  135 HAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNT 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00223  215 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGM 294

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00223  295 DVDTRAYFTAATMIIAVPTGIKVFSWLAT 323
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-269 1.11e-168

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 476.51  E-value: 1.11e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00116   58 VTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00116  138 HAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00116  218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGM 297

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00116  298 DVDTRAYFTSATMIIAIPTGIKVFSWLAT 326
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-269 2.17e-166

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 470.36  E-value: 2.17e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00142   56 VTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00142  136 HSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNT 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00142  216 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGM 295

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00142  296 DVDTRAYFTAATMVIAVPTGIKVFSWLAT 324
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-269 1.47e-150

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 430.48  E-value: 1.47e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00007   55 VTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLA 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00007  135 HAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNT 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00007  215 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGM 294

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00007  295 DVDTRAYFTAATMIIAVPTGIKVFSWLAT 323
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-269 3.93e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 427.03  E-value: 3.93e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00183   58 VTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00183  138 HAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00183  218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGM 297

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00183  298 DVDTRAYFTSATMIIAIPTGVKVFSWLAT 326
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-269 1.41e-147

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 422.75  E-value: 1.41e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00103   58 VTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00103  138 HAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00103  218 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGM 297

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00103  298 DVDTRAYFTSATMIIAIPTGVKVFSWLAT 326
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-269 7.12e-147

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 421.16  E-value: 7.12e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00037   58 VTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00037  138 HAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINT 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00037  218 TFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGM 297

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00037  298 DVDTRAYFTAATMIIAVPTGIKVFSWMAT 326
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-269 2.68e-145

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 416.77  E-value: 2.68e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSnIA 80
Cdd:MTH00079   59 ITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LG 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00079  138 HPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNT 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00079  218 SFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGM 297

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00079  298 DLDSRAYFTAATMVIAVPTGVKVFSWLAT 326
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-269 4.95e-145

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 416.26  E-value: 4.95e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00077   58 VTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00077  138 HAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00077  218 TFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDL 297

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00077  298 NVDTRAYFTSATMIIAIPTGVKVFSWLAT 326
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-269 3.93e-142

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 409.21  E-value: 3.93e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00182   60 VTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00182  140 HSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNT 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00182  220 TFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGM 299

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00182  300 DVDTRAYFTAATMIIAVPTGIKVFSWLAT 328
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-269 8.10e-140

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 403.05  E-value: 8.10e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00184   60 VTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00184  140 HSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNT 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00184  220 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGM 299

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00184  300 DVDTRAYFTAATMIIAVPTGIKIFSWIAT 328
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-269 5.35e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 371.27  E-value: 5.35e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:MTH00026   59 VTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00026  139 HSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNT 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00026  219 TFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGM 298

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:MTH00026  299 DVDTRAYFTAATMIIAVPTGIKIFSWLAT 327
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-269 7.55e-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: 342.59  E-value: 7.55e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPlMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:cd00919    47 VTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSY 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:cd00919   126 SSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGT 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:cd00919   206 SFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGL 284

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:cd00919   285 PVDTRAYFTAATMIIAVPTGIKVFNWLAT 313
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-269 2.53e-113

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: 334.96  E-value: 2.53e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMiGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:TIGR02891  52 FTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:TIGR02891 131 SPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGT 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:TIGR02891 211 HFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGM 289

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:TIGR02891 290 PPLALAFFSAATMLIAVPTGVKVFNWIAT 318
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-269 1.13e-112

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 334.40  E-value: 1.13e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIA 80
Cdd:COG0843    61 FTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:COG0843   140 SPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGT 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:COG0843   220 HFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGI 298

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:COG0843   299 SPLVKAFFSIATMLIAVPTGVKVFNWIAT 327
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-267 6.46e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 331.64  E-value: 6.46e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIekGAGTGWTVYPPLSSNIA 80
Cdd:MTH00048   59 ITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLF 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 HEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGmLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINT 160
Cdd:MTH00048  137 SSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN-VFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGS 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 SFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:MTH00048  216 AFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGL 295

                         250       260
                  ....*....|....*....|....*..
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWL 267
Cdd:MTH00048  296 DVKTAVFFSSVTMIIGVPTGIKVFSWL 322
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-269 1.56e-99

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: 299.88  E-value: 1.56e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   2 TAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIAH 81
Cdd:cd01662    54 TMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYS 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  82 EGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINTS 161
Cdd:cd01662   133 PGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTH 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 162 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGMD 241
Cdd:cd01662   213 FFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAG 291

                         250       260
                  ....*....|....*....|....*...
gi 1100876467 242 VDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:cd01662   292 ALVNAFFSIATMIIAVPTGVKIFNWLFT 319
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-269 7.60e-70

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: 221.29  E-value: 7.60e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   1 VTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSfieKGAGTGWTVYPPLssnia 80
Cdd:pfam00115  45 RTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL----- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  81 hegASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMlSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINt 160
Cdd:pfam00115 116 ---VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-TLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG- 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 161 sffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMFTVGM 240
Cdd:pfam00115 191 -----AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGL 264

                         250       260
                  ....*....|....*....|....*....
gi 1100876467 241 DVDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:pfam00115 265 PPWLQALFSVFSMLIAVPSGVKVFNWLAT 293
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-269 1.22e-66

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 218.65  E-value: 1.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   2 TAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIAH 81
Cdd:PRK15017  104 TAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYS 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  82 EGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINTS 161
Cdd:PRK15017  183 PGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTH 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 162 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESgKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGMD 241
Cdd:PRK15017  263 FFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAG 341

                         250       260
                  ....*....|....*....|....*...
gi 1100876467 242 VDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:PRK15017  342 ANVNAFFGITTMIIAIPTGVKIFNWLFT 369
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-269 6.27e-64

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: 211.25  E-value: 6.27e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467   2 TAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLSSNIAH 81
Cdd:TIGR02882  97 TTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFS 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467  82 EGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDRNINTS 161
Cdd:TIGR02882 176 PGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTA 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100876467 162 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESgKKETFGVLGMIYAMIAIGLLGFVVWAHHMFTVGMD 241
Cdd:TIGR02882 256 FFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNG 334

                         250       260
                  ....*....|....*....|....*...
gi 1100876467 242 VDTRAYFTSATMIIAVPTGIKIFSWLAT 269
Cdd:TIGR02882 335 ALINSFFSITTMAIAIPTGVKIFNWLLT 362
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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