NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|343887810|gb|AEM65397|]
View 

cytochrome oxidase subunit 1, partial (mitochondrion) [Porphyra purpurea]

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 ...
 1-250 4.32e-154

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: 437.30  E-value: 4.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNQLllGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:cd01663   19 LVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:cd01663   97 PPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RK 239
Cdd:cd01663  177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKK 256

                        250
                 ....*....|.
gi 343887810 240 PVFGYIGMIYA 250
Cdd:cd01663  257 PVFGYLGMVYA 267
 
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 ...
 1-250 4.32e-154

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: 437.30  E-value: 4.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNQLllGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:cd01663   19 LVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:cd01663   97 PPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RK 239
Cdd:cd01663  177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKK 256

                        250
                 ....*....|.
gi 343887810 240 PVFGYIGMIYA 250
Cdd:cd01663  257 PVFGYLGMVYA 267
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-250 1.83e-143

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 411.18  E-value: 1.83e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   2 LGACASILIRMELAQPGNqlLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLLP 81
Cdd:MTH00153  27 VGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  82 PSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFVW 161
Cdd:MTH00153 105 PSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVW 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 162 SILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RKP 240
Cdd:MTH00153 185 SVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKE 264

                        250
                 ....*....|
gi 343887810 241 VFGYIGMIYA 250
Cdd:MTH00153 265 TFGTLGMIYA 274
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-250 1.74e-101

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: 303.76  E-value: 1.74e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810    2 LGACASILIRMELAQPGNQLLlgNHQVYNVLVTEHAFLMIFFMVMPVLiGGFGNWFVPIMIGAPDMAFPRLNNISFWLLP 81
Cdd:TIGR02891  23 VGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   82 PSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFVW 161
Cdd:TIGR02891 100 FGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVW 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  162 SILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFSRKPV 241
Cdd:TIGR02891 180 GILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPI 259


                  ....*....
gi 343887810  242 FGYIGMIYA 250
Cdd:TIGR02891 260 FGYRAMVYA 268
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-250 1.02e-98

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 297.81  E-value: 1.02e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNQLLLGNHqvYNVLVTEHAFLMIFFMVMPvLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:COG0843   31 LIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:COG0843  108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFSRKP 240
Cdd:COG0843  188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP 267

                        250
                 ....*....|
gi 343887810 241 VFGYIGMIYA 250
Cdd:COG0843  268 LFGYKAMVLA 277
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-250 3.33e-64

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: 206.27  E-value: 3.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810    1 VLGACASILIRMELAQPGNQLLlgNHQVYNVLVTEHAFLMIFFMVMPVlIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:pfam00115  15 LVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   81 PPSLCLLLGSAMvevGAGTGWTLYPPLssiqshsgGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMyRIPLFV 160
Cdd:pfam00115  92 VLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTtffdpsGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFSRKP 240
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP 233

                         250
                  ....*....|
gi 343887810  241 VFGYIGMIYA 250
Cdd:pfam00115 234 LFGYKLSVLA 243
 
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 ...
 1-250 4.32e-154

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: 437.30  E-value: 4.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNQLllGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:cd01663   19 LVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:cd01663   97 PPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFV 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RK 239
Cdd:cd01663  177 WSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKK 256

                        250
                 ....*....|.
gi 343887810 240 PVFGYIGMIYA 250
Cdd:cd01663  257 PVFGYLGMVYA 267
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-250 1.83e-143

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 411.18  E-value: 1.83e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   2 LGACASILIRMELAQPGNqlLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLLP 81
Cdd:MTH00153  27 VGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  82 PSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFVW 161
Cdd:MTH00153 105 PSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVW 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 162 SILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RKP 240
Cdd:MTH00153 185 SVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKE 264

                        250
                 ....*....|
gi 343887810 241 VFGYIGMIYA 250
Cdd:MTH00153 265 TFGTLGMIYA 274
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-250 4.15e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 382.40  E-value: 4.15e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGnqLLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:MTH00223  25 LVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:MTH00223 103 PPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFSRK- 239
Cdd:MTH00223 183 WSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKk 262

                        250
                 ....*....|.
gi 343887810 240 PVFGYIGMIYA 250
Cdd:MTH00223 263 EVFGTLGMIYA 273
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-250 2.84e-131

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 380.56  E-value: 2.84e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNqlLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:MTH00167  28 MVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:MTH00167 106 PPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RK 239
Cdd:MTH00167 186 WSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSgKK 265

                        250
                 ....*....|.
gi 343887810 240 PVFGYIGMIYA 250
Cdd:MTH00167 266 EPFGYMGMVWA 276
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-250 1.67e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 375.97  E-value: 1.67e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNqlLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:MTH00116  28 MVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:MTH00116 106 PPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RK 239
Cdd:MTH00116 186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAgKK 265

                        250
                 ....*....|.
gi 343887810 240 PVFGYIGMIYA 250
Cdd:MTH00116 266 EPFGYMGMVWA 276
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-250 1.99e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 367.90  E-value: 1.99e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   2 LGACASILIRMELAQPGNqlLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLLP 81
Cdd:MTH00142  27 VGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  82 PSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFVW 161
Cdd:MTH00142 105 PALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVW 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 162 SILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RKP 240
Cdd:MTH00142 185 SVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSgKKE 264

                        250
                 ....*....|
gi 343887810 241 VFGYIGMIYA 250
Cdd:MTH00142 265 VFGTLGMIYA 274
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-250 2.72e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 352.97  E-value: 2.72e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNqlLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:MTH00182  30 MIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:MTH00182 108 PPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFV 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RK 239
Cdd:MTH00182 188 WSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVaKK 267

                        250
                 ....*....|.
gi 343887810 240 PVFGYIGMIYA 250
Cdd:MTH00182 268 QIFGYLGMVYA 278
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-250 7.74e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 346.43  E-value: 7.74e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNqlLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:MTH00184  30 MIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:MTH00184 108 PPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFV 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RK 239
Cdd:MTH00184 188 WSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAaKK 267

                        250
                 ....*....|.
gi 343887810 240 PVFGYIGMIYA 250
Cdd:MTH00184 268 QIFGYLGMVYA 278
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-250 5.06e-115

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 339.17  E-value: 5.06e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNqlLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:MTH00103  28 MVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:MTH00103 106 PPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RK 239
Cdd:MTH00103 186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSgKK 265

                        250
                 ....*....|.
gi 343887810 240 PVFGYIGMIYA 250
Cdd:MTH00103 266 EPFGYMGMVWA 276
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-250 2.14e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 337.30  E-value: 2.14e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNqlLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:MTH00077  28 MVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:MTH00077 106 PPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RK 239
Cdd:MTH00077 186 WSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSaKK 265

                        250
                 ....*....|.
gi 343887810 240 PVFGYIGMIYA 250
Cdd:MTH00077 266 EPFGYMGMVWA 276
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-250 2.45e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 337.57  E-value: 2.45e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   2 LGACASILIRMELAQPGNqlLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLLP 81
Cdd:MTH00037  29 VGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIP 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  82 PSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFVW 161
Cdd:MTH00037 107 PSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVW 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 162 SILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFSRK-P 240
Cdd:MTH00037 187 SVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKqE 266

                        250
                 ....*....|
gi 343887810 241 VFGYIGMIYA 250
Cdd:MTH00037 267 PFGYLGMVYA 276
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-250 9.22e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 333.43  E-value: 9.22e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNqlLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:MTH00183  28 MVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:MTH00183 106 PPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RK 239
Cdd:MTH00183 186 WAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSgKK 265

                        250
                 ....*....|.
gi 343887810 240 PVFGYIGMIYA 250
Cdd:MTH00183 266 EPFGYMGMVWA 276
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-250 6.91e-111

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 328.40  E-value: 6.91e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNqlLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:MTH00007  25 LLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:MTH00007 103 PPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFSRKP 240
Cdd:MTH00007 183 WAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKL 262

                        250
                 ....*....|.
gi 343887810 241 -VFGYIGMIYA 250
Cdd:MTH00007 263 ePFGTLGMIYA 273
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-250 3.77e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 321.24  E-value: 3.77e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGnqLLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:MTH00079  29 MVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSiQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:MTH00079 107 PTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RK 239
Cdd:MTH00079 186 WTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTgKK 265

                        250
                 ....*....|.
gi 343887810 240 PVFGYIGMIYA 250
Cdd:MTH00079 266 EVFGSLGMVYA 276
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-250 4.15e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 321.96  E-value: 4.15e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   2 LGACASILIRMELAQPGNqlLLGNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLLP 81
Cdd:MTH00026  30 IGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  82 PSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFVW 161
Cdd:MTH00026 108 PALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVW 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 162 SILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFS-RKP 240
Cdd:MTH00026 188 SVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSyKKQ 267

                        250
                 ....*....|
gi 343887810 241 VFGYIGMIYA 250
Cdd:MTH00026 268 IFGYLGMVYA 277
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-250 2.16e-102

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: 305.22  E-value: 2.16e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNQLLlgNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPiMIGAPDMAFPRLNNISFWLL 80
Cdd:cd00919   17 LLGGLLALLIRLELATPGSLFL--DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:cd00919   94 PPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFV 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFSRKP 240
Cdd:cd00919  174 WSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP 253

                        250
                 ....*....|
gi 343887810 241 VFGYIGMIYA 250
Cdd:cd00919  254 LFGYKLMVYA 263
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-250 1.74e-101

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: 303.76  E-value: 1.74e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810    2 LGACASILIRMELAQPGNQLLlgNHQVYNVLVTEHAFLMIFFMVMPVLiGGFGNWFVPIMIGAPDMAFPRLNNISFWLLP 81
Cdd:TIGR02891  23 VGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   82 PSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFVW 161
Cdd:TIGR02891 100 FGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVW 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  162 SILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFSRKPV 241
Cdd:TIGR02891 180 GILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPI 259


                  ....*....
gi 343887810  242 FGYIGMIYA 250
Cdd:TIGR02891 260 FGYRAMVYA 268
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-250 1.02e-98

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 297.81  E-value: 1.02e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNQLLLGNHqvYNVLVTEHAFLMIFFMVMPvLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:COG0843   31 LIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:COG0843  108 LFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFT 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFSRKP 240
Cdd:COG0843  188 WAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP 267

                        250
                 ....*....|
gi 343887810 241 VFGYIGMIYA 250
Cdd:COG0843  268 LFGYKAMVLA 277
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-250 7.41e-86

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: 264.06  E-value: 7.41e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   1 VLGACASILIRMELAQPGNQLLLGNHqvYNVLVTEHAFLMIFFMVMPVLIGgFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:cd01662   23 LRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:cd01662  100 LFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFT 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFSRKP 240
Cdd:cd01662  180 WTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP 259

                        250
                 ....*....|
gi 343887810 241 VFGYIGMIYA 250
Cdd:cd01662  260 LFGYRSMVYA 269
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-250 3.67e-79

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 246.90  E-value: 3.67e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   2 LGACASILIRMELAQPGNQLLlgNHQVYNVLVTEHAFLMIFFMVMPVLIGGFGNWFVPIMIGAPDMAFPRLNNISFWLLP 81
Cdd:MTH00048  30 VGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  82 PSLCLLLGSamVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSmYRIPLFVW 161
Cdd:MTH00048 108 PSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILW 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 162 SILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFSRKP- 240
Cdd:MTH00048 185 SYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDd 264

                        250
                 ....*....|
gi 343887810 241 VFGYIGMIYA 250
Cdd:MTH00048 265 PFGYYGLVFA 274
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-250 3.33e-64

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: 206.27  E-value: 3.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810    1 VLGACASILIRMELAQPGNQLLlgNHQVYNVLVTEHAFLMIFFMVMPVlIGGFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:pfam00115  15 LVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   81 PPSLCLLLGSAMvevGAGTGWTLYPPLssiqshsgGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMyRIPLFV 160
Cdd:pfam00115  92 VLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTtffdpsGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFSRKP 240
Cdd:pfam00115 160 WAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP 233

                         250
                  ....*....|
gi 343887810  241 VFGYIGMIYA 250
Cdd:pfam00115 234 LFGYKLSVLA 243
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 3-250 8.43e-53

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 180.90  E-value: 8.43e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810   3 GACASILIRME--LAQPGNQLLLGNHQvYNVLVTEHAFLMIFFMVMPVLIGgFGNWFVPIMIGAPDMAFPRLNNISFWLL 80
Cdd:PRK15017  72 GFADAIMMRSQqaLASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFT 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  81 PPSLCLLLGSAMVEVGAGTGWTLYPPLSSIQSHSGGAVDLAIFSLHLSGASSILGAINFITTIFNMRNPGQSMYRIPLFV 160
Cdd:PRK15017 150 VVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFT 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810 161 WSILITAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIVSHIVSTFSRKP 240
Cdd:PRK15017 230 WASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKR 309

                        250
                 ....*....|
gi 343887810 241 VFGYIGMIYA 250
Cdd:PRK15017 310 LFGYTSLVWA 319
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 18-224 4.93e-03

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: 37.65  E-value: 4.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  18 GNQLLLGNHQVYNVLVTEHAFLMIFfmVMPVL-IGGFGNWFVPIMIGAPDMAfPRLNNISFWLLPPslclllGSAMVEVG 96
Cdd:cd01660   33 GVFPLPSSGILYYQGLTLHGVLLAI--VFTTFfIMGFFYAIVARALLRSLFN-RRLAWAGFWLMVI------GTVMAAVP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887810  97 AGTG-----WTLYPPLssiQSHSGGAVDLAIFSLhlsgASSILGAINFITT-IFNMRNPGQsmyRIPLFVWSILITAFLL 170
Cdd:cd01660  104 ILLGqasvlYTFYPPL---QAHPLFYIGAALVVV----GSWISGFAMFVTLwRWKKANPGK---KVPLATFMVVTTMILW 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 343887810 171 LLAVPVLagAITMLLtdrnfnttFFDPSGGG-----DPVLYQHLFWFFGHPEVYILILP 224
Cdd:cd01660  174 LVASLGV--ALEVLF--------QLLPWSLGlvdtvDVLLSRTLFWWFGHPLVYFWLLP 222
 
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