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Conserved domains on  [gi|451810449|dbj|BAM84224|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Neogoniolithon brassica-florida]

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 ...
 1-246 1.63e-147

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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 420.74  E-value: 1.63e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNQLllGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:cd01663   16 WSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:cd01663   94 WLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMP 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:cd01663  174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFS 253


                 ....*..
gi 451810449 241 -RKPVFG 246
Cdd:cd01663  254 gKKPVFG 260
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-246 1.63e-147

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: 420.74  E-value: 1.63e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNQLllGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:cd01663   16 WSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:cd01663   94 WLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMP 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:cd01663  174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFS 253


                 ....*..
gi 451810449 241 -RKPVFG 246
Cdd:cd01663  254 gKKPVFG 260
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-246 1.78e-140

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 403.48  E-value: 1.78e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00153  23 WSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00153 101 WLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMP 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00153 181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQES 260


                 ....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00153 261 gKKETFG 267
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-246 1.86e-98

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: 296.06  E-value: 1.86e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449    1 FSGVLGACISMLIRMELAQPGNQLLlgNHQVYNVLITAHAILMIFFLVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:TIGR02891  19 AFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:TIGR02891  96 WLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMP 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:TIGR02891 176 LFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA 255


                  ....*.
gi 451810449  241 RKPVFG 246
Cdd:TIGR02891 256 RKPIFG 261
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-246 7.47e-95

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 287.79  E-value: 7.47e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNQLLLGNHqvYNVLITAHAILMIFFLVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:COG0843   28 VFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSF 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:COG0843  105 WLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMP 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:COG0843  185 LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS 264


                 ....*.
gi 451810449 241 RKPVFG 246
Cdd:COG0843  265 RKPLFG 270
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-246 2.34e-61

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: 198.57  E-value: 2.34e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449    1 FSGVLGACISMLIRMELAQPGNQLLlgNHQVYNVLITAHAILMIFFLVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:pfam00115  12 VWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   81 WLLPPSLCLLLASSLvevGAGTGWTVYPPLssiqshsgAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMyRIP 160
Cdd:pfam00115  89 WLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:pfam00115 157 LFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFA 230


                  ....*.
gi 451810449  241 RKPVFG 246
Cdd:pfam00115 231 GRPLFG 236
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-246 1.63e-147

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: 420.74  E-value: 1.63e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNQLllGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:cd01663   16 WSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:cd01663   94 WLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMP 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:cd01663  174 LFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFS 253


                 ....*..
gi 451810449 241 -RKPVFG 246
Cdd:cd01663  254 gKKPVFG 260
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-246 1.78e-140

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 403.48  E-value: 1.78e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00153  23 WSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00153 101 WLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMP 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00153 181 LFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQES 260


                 ....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00153 261 gKKETFG 267
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-246 5.64e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 371.62  E-value: 5.64e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   2 SGVLGACISMLIRMELAQPGnqLLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFW 81
Cdd:MTH00223  23 SGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  82 LLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIPL 161
Cdd:MTH00223 101 LLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPL 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 162 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFSR 241
Cdd:MTH00223 181 FVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSS 260


                 ....*.
gi 451810449 242 K-PVFG 246
Cdd:MTH00223 261 KkEVFG 266
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-246 6.62e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 371.70  E-value: 6.62e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00167  25 WAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00167 103 WLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTP 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00167 183 LFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYS 262


                 ....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00167 263 gKKEPFG 269
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-242 1.27e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 365.95  E-value: 1.27e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00116  25 WAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00116 103 WLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTP 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00116 183 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYA 262


                 ..
gi 451810449 241 RK 242
Cdd:MTH00116 263 GK 264
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-246 2.18e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 357.50  E-value: 2.18e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00142  23 WAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSF 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00142 101 WLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVP 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00142 181 LFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYS 260


                 ....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00142 261 gKKEVFG 267
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-246 7.01e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 336.41  E-value: 7.01e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00182  27 GAGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISF 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00182 105 WLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLP 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00182 185 LFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFV 264


                 ....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00182 265 aKKQIFG 271
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-246 1.45e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 332.95  E-value: 1.45e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00184  27 FAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISF 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00184 105 WLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMP 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00184 185 LFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFA 264


                 ....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00184 265 aKKQIFG 271
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-242 1.58e-110

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 327.22  E-value: 1.58e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00103  25 WAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00103 103 WLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTP 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00103 183 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYS 262


                 ..
gi 451810449 241 RK 242
Cdd:MTH00103 263 GK 264
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-242 2.03e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 327.17  E-value: 2.03e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00037  25 WAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00037 103 WLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLP 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00037 183 LFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYS 262


                 ..
gi 451810449 241 RK 242
Cdd:MTH00037 263 GK 264
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-242 3.31e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 326.51  E-value: 3.31e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00077  25 WAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00077 103 WLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTP 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00077 183 LFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYS 262


                 ..
gi 451810449 241 RK 242
Cdd:MTH00077 263 AK 264
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-242 9.84e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 325.34  E-value: 9.84e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00183  25 WAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00183 103 WLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTP 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00183 183 LFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYS 262


                 ..
gi 451810449 241 RK 242
Cdd:MTH00183 263 GK 264
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-243 1.09e-107

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 319.93  E-value: 1.09e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00007  22 WGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00007 100 WLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIP 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00007 180 LFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYA 259


                 ...
gi 451810449 241 RKP 243
Cdd:MTH00007 260 GKL 262
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-246 1.01e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 315.08  E-value: 1.01e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   2 SGVLGACISMLIRMELAQPGnqLLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFW 81
Cdd:MTH00079  27 SGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  82 LLPPSLCLLLASSLVEVGAGTGWTVYPPLSSiQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIPL 161
Cdd:MTH00079 105 LLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 162 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS- 240
Cdd:MTH00079 184 FVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTg 263


                 ....*.
gi 451810449 241 RKPVFG 246
Cdd:MTH00079 264 KKEVFG 269
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-246 3.32e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 306.94  E-value: 3.32e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNqlLLGNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:MTH00026  26 LSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:MTH00026 104 WLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIP 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00026 184 LFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFS 263


                 ....*..
gi 451810449 241 -RKPVFG 246
Cdd:MTH00026 264 yKKQIFG 270
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-246 1.86e-98

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: 296.06  E-value: 1.86e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449    1 FSGVLGACISMLIRMELAQPGNQLLlgNHQVYNVLITAHAILMIFFLVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:TIGR02891  19 AFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:TIGR02891  96 WLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMP 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:TIGR02891 176 LFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA 255


                  ....*.
gi 451810449  241 RKPVFG 246
Cdd:TIGR02891 256 RKPIFG 261
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-246 5.66e-98

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: 293.67  E-value: 5.66e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNQLLlgNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPiMIGSPDMAFPRLNNISF 80
Cdd:cd00919   14 VALLLGGLLALLIRLELATPGSLFL--DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:cd00919   91 WLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:cd00919  171 LFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFS 250


                 ....*.
gi 451810449 241 RKPVFG 246
Cdd:cd00919  251 GKPLFG 256
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-246 7.47e-95

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 287.79  E-value: 7.47e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   1 FSGVLGACISMLIRMELAQPGNQLLLGNHqvYNVLITAHAILMIFFLVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:COG0843   28 VFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSF 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  81 WLLPPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIP 160
Cdd:COG0843  105 WLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMP 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:COG0843  185 LFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS 264


                 ....*.
gi 451810449 241 RKPVFG 246
Cdd:COG0843  265 RKPLFG 270
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 4-246 4.88e-82

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: 254.04  E-value: 4.88e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   4 VLGACISMLIRMELAQPGNQLLLGNHqvYNVLITAHAILMIFFLVMPVMIGgFGNWLVPIMIGSPDMAFPRLNNISFWLL 83
Cdd:cd01662   23 LRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  84 PPSLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIPLFV 163
Cdd:cd01662  100 LFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFT 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449 164 WSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFSRKP 243
Cdd:cd01662  180 WTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP 259


                 ...
gi 451810449 244 VFG 246
Cdd:cd01662  260 LFG 262
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-240 1.12e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 240.35  E-value: 1.12e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   2 SGVLGACISMLIRMELAQPGNQLLlgNHQVYNVLITAHAILMIFFLVMPVMIGGFGNWLVPIMIGSPDMAFPRLNNISFW 81
Cdd:MTH00048  27 SGFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  82 LLPPSLCLLLASSLVevGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSmYRIPL 161
Cdd:MTH00048 105 LLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSI 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 451810449 162 FVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:MTH00048 182 ILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLS 260
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-246 2.34e-61

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: 198.57  E-value: 2.34e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449    1 FSGVLGACISMLIRMELAQPGNQLLlgNHQVYNVLITAHAILMIFFLVMPvMIGGFGNWLVPIMIGSPDMAFPRLNNISF 80
Cdd:pfam00115  12 VWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   81 WLLPPSLCLLLASSLvevGAGTGWTVYPPLssiqshsgAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMyRIP 160
Cdd:pfam00115  89 WLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  161 LFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFS 240
Cdd:pfam00115 157 LFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFA 230


                  ....*.
gi 451810449  241 RKPVFG 246
Cdd:pfam00115 231 GRPLFG 236
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 9-246 6.04e-51

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 175.89  E-value: 6.04e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   9 ISMLIRMELAQPGNQLLLGNHQvYNVLITAHAILMIFFLVMPVMIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 88
Cdd:PRK15017  77 IMMRSQQALASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVI 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  89 LLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIPLFVWSIFV 168
Cdd:PRK15017 155 LVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLC 234

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 451810449 169 TAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFSRKPVFG 246
Cdd:PRK15017 235 ANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFG 312
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 6-246 2.99e-50

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: 173.50  E-value: 2.99e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449    6 GACISMLIRMELAQPGNQLLLGNHqvYNVLITAHAILMIFFLVMPVMIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 85
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFA 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449   86 SLCLLLASSLVEVGAGTGWTVYPPLSSIQSHSGAAIDLAIFSLHLAGASSILGAVNFISTILNMRNPGQSMYRIPLFVWS 165
Cdd:TIGR02882 145 GAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWT 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451810449  166 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHVVSTFSRKPVF 245
Cdd:TIGR02882 225 TLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLF 304


                  .
gi 451810449  246 G 246
Cdd:TIGR02882 305 G 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.
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