NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2315911266|gb|UYB95288|]
View 

cytochrome c 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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-299 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: 600.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00153   52 YNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLS 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00153  132 SNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDR 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00153  212 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMF 291

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00153  292 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGG 350
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-299 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 600.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00153   52 YNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLS 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00153  132 SNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDR 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00153  212 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMF 291

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00153  292 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGG 350
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-299 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: 560.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:cd01663    45 YNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLS 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:cd01663   125 SILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDR 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:cd01663   205 NFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMF 284

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:cd01663   285 TVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGG 343
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-299 1.00e-124

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 366.37  E-value: 1.00e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:COG0843    57 YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:COG0843   136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDR 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:COG0843   216 SLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMF 294

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:COG0843   295 TPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGG 353
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-299 6.20e-124

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: 363.47  E-value: 6.20e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMiGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:TIGR02891  48 YNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLS 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:TIGR02891 127 STSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDR 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:TIGR02891 207 LFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMF 285

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:TIGR02891 286 TTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGG 344
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-299 2.70e-77

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: 241.71  E-value: 2.70e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSfieKGAGTGWTVYPPLs 80
Cdd:pfam00115  41 YNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 sniahegASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMlSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:pfam00115 116 -------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-TLRMPLFVWAILATAILILLAFPVLAAALLLLLLDR 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:pfam00115 188 SLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLF 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARIT-YSPTSLWSLGFIFLFTIGG 299
Cdd:pfam00115 261 TTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGG 320
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-299 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 600.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00153   52 YNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLS 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00153  132 SNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDR 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00153  212 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMF 291

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00153  292 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGG 350
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-299 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: 560.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:cd01663    45 YNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLS 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:cd01663   125 SILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDR 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:cd01663   205 NFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMF 284

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:cd01663   285 TVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGG 343
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-299 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 522.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00167   54 YNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00167  134 GNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDR 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00167  214 NLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMF 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00167  294 TVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGG 352
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-299 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 521.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00223   51 YNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLS 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00223  131 SNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDR 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00223  211 NFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMF 290

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00223  291 TVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGG 349
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-299 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 514.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00116   54 YNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00116  134 GNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDR 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00116  214 NLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMF 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00116  294 TVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGG 352
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-299 2.18e-180

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 507.34  E-value: 2.18e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00142   52 YNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLS 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00142  132 SNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDR 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00142  212 NFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMF 291

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00142  292 TVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGG 350
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-299 6.18e-165

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 468.23  E-value: 6.18e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00007   51 YNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00007  131 SNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDR 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00007  211 NLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMF 290

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00007  291 TVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGG 349
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-299 3.09e-162

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 461.27  E-value: 3.09e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00103   54 YNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00103  134 GNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDR 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00103  214 NLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMF 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00103  294 TVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGG 352
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-299 3.47e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 458.62  E-value: 3.47e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00183   54 YNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00183  134 GNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDR 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00183  214 NLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMF 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00183  294 TVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGG 352
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-299 2.06e-159

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 453.75  E-value: 2.06e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00079   55 YNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SnIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00079  135 T-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDR 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00079  214 NLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMY 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00079  294 TVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGG 352
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-299 1.46e-158

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 451.98  E-value: 1.46e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00037   54 YNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLS 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00037  134 SNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDR 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00037  214 NINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMF 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00037  294 TVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGG 352
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-299 2.60e-158

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 451.32  E-value: 2.60e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00077   54 YNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00077  134 GNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDR 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00077  214 NLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMF 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00077  294 TVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGG 352
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-299 1.21e-151

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 435.02  E-value: 1.21e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00182   56 YNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLS 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00182  136 SIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDR 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00182  216 NFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMF 295

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00182  296 TVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGG 354
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-299 1.04e-148

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 427.32  E-value: 1.04e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00184   56 YNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLS 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00184  136 SIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDR 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00184  216 NFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMF 295

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00184  296 TVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGG 354
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-299 1.03e-134

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 392.07  E-value: 1.03e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:MTH00026   55 YNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLA 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00026  135 SIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDR 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00026  215 NFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMY 294

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGA--RITYSPTSLWSLGFIFLFTIGG 299
Cdd:MTH00026  295 VVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGG 355
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-299 4.38e-129

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: 375.33  E-value: 4.38e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPlMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:cd00919    43 YNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLS 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:cd00919   122 TLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDR 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:cd00919   202 NFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMF 280

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:cd00919   281 TVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGG 339
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-299 1.00e-124

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 366.37  E-value: 1.00e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:COG0843    57 YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLS 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:COG0843   136 GLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDR 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:COG0843   216 SLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMF 294

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:COG0843   295 TPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGG 353
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-299 6.20e-124

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: 363.47  E-value: 6.20e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMiGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:TIGR02891  48 YNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLS 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:TIGR02891 127 STSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDR 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:TIGR02891 207 LFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMF 285

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:TIGR02891 286 TTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGG 344
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-299 2.23e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 352.06  E-value: 2.23e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIekGAGTGWTVYPPLS 80
Cdd:MTH00048   55 YNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLS 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGmLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:MTH00048  133 SSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN-VFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDR 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:MTH00048  212 NFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMF 291

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYS-PTSLWSLGFIFLFTIGG 299
Cdd:MTH00048  292 TVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGG 351
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-299 3.36e-111

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: 330.70  E-value: 3.36e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:cd01662    49 YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLS 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:cd01662   128 GLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDR 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:cd01662   208 YFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMF 286

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:cd01662   287 TTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGG 345
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-299 2.70e-77

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: 241.71  E-value: 2.70e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSfieKGAGTGWTVYPPLs 80
Cdd:pfam00115  41 YNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 sniahegASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMlSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:pfam00115 116 -------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM-TLRMPLFVWAILATAILILLAFPVLAAALLLLLLDR 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:pfam00115 188 SLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLF 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARIT-YSPTSLWSLGFIFLFTIGG 299
Cdd:pfam00115 261 TTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGG 320
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-299 1.51e-75

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 243.30  E-value: 1.51e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESgKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFF 336

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:PRK15017  337 TMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGG 395
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-299 4.47e-73

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: 236.29  E-value: 4.47e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLMSSFIEKGAGTGWTVYPPLS 80
Cdd:TIGR02882  92 YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  81 SNIAHEGASVDLAIFSLHMAGISSILGAINFITTAYNMRPSGMLSERMTLFIWAVSITAILLLFSLPVLAGAITMLLTDR 160
Cdd:TIGR02882 171 GPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDR 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 161 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESgKKETFGVLGMIYAMIAIGLLGFVVWAHHMF 240
Cdd:TIGR02882 251 IFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFF 329

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2315911266 241 TVGLDVDTRAYFTSATMIIAVPTGIKIFSWLATFHGARITYSPTSLWSLGFIFLFTIGG 299
Cdd:TIGR02882 330 TMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGG 388
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-278 3.91e-04

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: 41.89  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266   1 YNTIVTAHAFIM-IFFMVMPIMigGFGNWLIPLMLGAPDMAfPRLNNMSFWLLPPSLTLLLMSSFIEKgAGTGWTVYPPL 79
Cdd:cd01660    44 YYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN-RRLAWAGFWLMVIGTVMAAVPILLGQ-ASVLYTFYPPL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266  80 ssnIAHEGASVDLAIFSLHmagiSSILGAINFITTA-YNMRPSGmlsERMTLFIWAVSITAIL-LLFSLPVlagAITMLL 157
Cdd:cd01660   120 ---QAHPLFYIGAALVVVG----SWISGFAMFVTLWrWKKANPG---KKVPLATFMVVTTMILwLVASLGV---ALEVLF 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315911266 158 tdRNINTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISYESGKKeTFGVLGMIYAMIAIGLLGFVVWAH 237
Cdd:cd01660   187 --QLLPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGK-LFSDPLARLAFILFLLFSTPVGFH 262

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2315911266 238 HMFT-VGLDVDTRAYFTSATMIIAVPTGIKIFSWLATF-HGAR 278
Cdd:cd01660   263 HQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeIAGR 305
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH