NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|410935663|gb|AFV94457|]
View 

cytochrome oxidase subunit I, partial (mitochondrion) [Tigriopus sp. 2 SL-2012]

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 ...
 1-266 9.79e-172

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 483.99  E-value: 9.79e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00153  91 AFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMR 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00153 171 SKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00153 251 MISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQI 330

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00153 331 NYSPSLLWALGFVFLFTIGGLTGVVLA 357
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-266 9.79e-172

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 483.99  E-value: 9.79e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00153  91 AFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMR 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00153 171 SKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00153 251 MISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQI 330

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00153 331 NYSPSLLWALGFVFLFTIGGLTGVVLA 357
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-266 1.77e-157

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: 446.93  E-value: 1.77e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVG-HAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:cd01663   84 AFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILaHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMR 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:cd01663  164 APGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:cd01663  244 IISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSI 323

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:cd01663  324 KFETPMLWALGFIFLFTIGGLTGVVLA 350
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-266 4.66e-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: 303.38  E-value: 4.66e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663    1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:TIGR02891  86 AFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMR 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:TIGR02891 166 APGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFG 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  160 LISHIISQeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:TIGR02891 246 IISEILPT-FARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSI 324

                         250       260
                  ....*....|....*....|....*..
gi 410935663  240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:TIGR02891 325 RFTTPMLFALGFIFLFVIGGLTGVMLA 351
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-266 7.83e-97

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 293.57  E-value: 7.83e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:COG0843   95 AFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMR 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:COG0843  175 APGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFG 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:COG0843  255 IVSEIIPT-FSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRI 333

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:COG0843  334 RFTTPMLFALGFIILFVIGGLTGVMLA 360
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-266 4.01e-66

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: 211.66  E-value: 4.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663    1 AFPRLNNLSFWFLVPSLLMLLLSGAveaGAGTGWTVYPPLSAVghagssvDFAIFSLHLAGVSSLLGAVNFISTIFNLRV 80
Cdd:pfam00115  79 AFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVGV-------DLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   81 FGMYLDLvPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNScfydvsGGGDPILYQHLFWFFGHPEVYILILPGFGL 160
Cdd:pfam00115 149 PGMTLRM-PLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  161 ISHIISQeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPS 240
Cdd:pfam00115 222 IYYILPK-FAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300

                         250       260
                  ....*....|....*....|....*..
gi 410935663  241 -YSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLA 327
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-266 9.79e-172

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 483.99  E-value: 9.79e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00153  91 AFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMR 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00153 171 SKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00153 251 MISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQI 330

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00153 331 NYSPSLLWALGFVFLFTIGGLTGVVLA 357
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-266 1.77e-157

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: 446.93  E-value: 1.77e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVG-HAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:cd01663   84 AFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILaHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMR 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:cd01663  164 APGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:cd01663  244 IISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSI 323

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:cd01663  324 KFETPMLWALGFIFLFTIGGLTGVVLA 350
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-266 5.16e-143

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 410.91  E-value: 5.16e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00223  90 AFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSnLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMR 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00223 170 SPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00223 250 MISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKI 329

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00223 330 KYEAPMLWALGFIFLFTVGGLTGIILS 356
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-266 1.57e-140

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 404.83  E-value: 1.57e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00167  93 AFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGnLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMK 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00167 173 PPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00167 253 MISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKI 332

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00167 333 KWETPMLWALGFIFLFTVGGLTGIVLA 359
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-266 9.20e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 397.56  E-value: 9.20e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00142  91 AFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSnLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMR 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00142 171 AGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00142 251 MISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKV 330

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00142 331 KYEPPMLWALGFIFLFTVGGLTGIVLA 357
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-266 2.83e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 394.07  E-value: 2.83e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00116  93 AFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGnLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMK 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00116 173 PPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00116 253 IISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTI 332

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00116 333 KWDPPMLWALGFIFLFTIGGLTGIVLA 359
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-266 4.10e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 367.85  E-value: 4.10e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRV 80
Cdd:MTH00079  94 SFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRS 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  81 FGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGL 160
Cdd:MTH00079 174 SSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGI 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 161 ISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPS 240
Cdd:MTH00079 254 ISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMK 333

                        250       260
                 ....*....|....*....|....*.
gi 410935663 241 YSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00079 334 FQPLLLWVLGFIFLFTIGGLTGVILS 359
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-266 8.84e-125

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 364.61  E-value: 8.84e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00007  90 AFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASnLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMR 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00007 170 WKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00007 250 AISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPI 329

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00007 330 KYETPMLWALGFIFLFTTGGLTGIVLS 356
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-266 2.56e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 356.06  E-value: 2.56e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00037  93 AFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSnIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMR 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00037 173 TPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFG 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00037 253 MISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNL 332

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00037 333 RWETPLLWALGFVFLFTIGGLTGIVLA 359
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-266 5.23e-120

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 352.26  E-value: 5.23e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00103  93 AFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMK 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00103 173 PPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00103 253 MISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNI 332

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00103 333 KWSPAMLWALGFIFLFTVGGLTGIVLA 359
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-266 1.86e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 351.15  E-value: 1.86e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00183  93 AFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMK 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00183 173 PPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00183 253 MISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSI 332

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00183 333 KWETPLLWALGFIFLFTVGGLTGIVLA 359
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-266 4.26e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 347.70  E-value: 4.26e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00077  93 AFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMK 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00077 173 PPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFG 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00077 253 MISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAI 332

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00077 333 KWDAAMLWALGFIFLFTVGGLTGIVLA 359
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-266 7.49e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 347.20  E-value: 7.49e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00184  95 AFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIqAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMR 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00184 175 APGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00184 255 IISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSL 334

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00184 335 RLDTPMLWAIGFVFLFTMGGLTGIVLA 361
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-266 1.09e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 346.81  E-value: 1.09e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00182  95 AFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIqAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMR 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00182 175 APGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFG 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00182 255 MISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTL 334

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00182 335 RLDTPMLWAMGFVFLFTLGGLTGVVLA 361
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-266 4.49e-106

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: 315.24  E-value: 4.49e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVG-HAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:cd00919   81 AFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSySSGVGVDLAILGLHLAGVSSILGAINFITTILNMR 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:cd00919  161 APGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFG 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQEtAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:cd00919  241 AISEIIPTF-SGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRI 319

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:cd00919  320 RFDPPMLFALGFLFLFTIGGLTGVVLA 346
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-266 5.46e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 314.64  E-value: 5.46e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00026  94 AFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIqAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMR 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00026 174 TPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFG 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00026 254 IISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGR 333

                        250       260
                 ....*....|....*....|....*....
gi 410935663 240 S--YSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00026 334 NliFTTPMAWALGFIFLFTIGGLTGIVLS 362
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-266 4.66e-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: 303.38  E-value: 4.66e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663    1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:TIGR02891  86 AFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMR 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:TIGR02891 166 APGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFG 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  160 LISHIISQeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:TIGR02891 246 IISEILPT-FARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSI 324

                         250       260
                  ....*....|....*....|....*..
gi 410935663  240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:TIGR02891 325 RFTTPMLFALGFIFLFVIGGLTGVMLA 351
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-266 7.83e-97

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 293.57  E-value: 7.83e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:COG0843   95 AFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMR 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:COG0843  175 APGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFG 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:COG0843  255 IVSEIIPT-FSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRI 333

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:COG0843  334 RFTTPMLFALGFIILFVIGGLTGVMLA 360
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-266 1.48e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 276.94  E-value: 1.48e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSgaVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:MTH00048  94 NLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSsLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAF 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDlVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:MTH00048 172 MTNVFSR-TSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFG 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:MTH00048 251 IISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRV 330

                        250       260
                 ....*....|....*....|....*...
gi 410935663 240 SYSAS-FSWALGFIFLFTLGGLTGIVLS 266
Cdd:MTH00048 331 RKSDPvVWWVVSFIVLFTIGGVTGIVLS 358
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-266 5.39e-89

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: 272.53  E-value: 5.39e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVGHA-GSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:cd01662   87 AFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSpGVGVDYWILGLQFSGIGTLLGAINFIVTILKMR 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:cd01662  167 APGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFG 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:cd01662  247 IFSEIVPT-FSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRI 325

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:cd01662  326 RFETPMLWAIGFLVTFVIGGLTGVMLA 352
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-266 4.01e-66

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: 211.66  E-value: 4.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663    1 AFPRLNNLSFWFLVPSLLMLLLSGAveaGAGTGWTVYPPLSAVghagssvDFAIFSLHLAGVSSLLGAVNFISTIFNLRV 80
Cdd:pfam00115  79 AFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVGV-------DLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   81 FGMYLDLvPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNScfydvsGGGDPILYQHLFWFFGHPEVYILILPGFGL 160
Cdd:pfam00115 149 PGMTLRM-PLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  161 ISHIISQeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPS 240
Cdd:pfam00115 222 IYYILPK-FAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300

                         250       260
                  ....*....|....*....|....*..
gi 410935663  241 -YSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLA 327
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-266 5.22e-60

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 200.93  E-value: 5.22e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVGHA-GSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:PRK15017 137 AFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSpGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMR 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:PRK15017 217 APGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFG 296

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 160 LISHIISQeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:PRK15017 297 VFSEIAAT-FSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRI 375

                        250       260
                 ....*....|....*....|....*..
gi 410935663 240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:PRK15017 376 VFHSAMLWTIGFIVTFSVGGMTGVLLA 402
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-266 7.91e-55

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: 186.60  E-value: 7.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663    1 AFPRLNNLSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVGHA-GSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLR 79
Cdd:TIGR02882 130 AFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSpGVGVNYYLIALQISGIGTLMTGINFFVTILKMR 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663   80 VFGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFG 159
Cdd:TIGR02882 210 APGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFG 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663  160 LISHIISQeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKP 239
Cdd:TIGR02882 290 IYSEIIST-FAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKI 368

                         250       260
                  ....*....|....*....|....*..
gi 410935663  240 SYSASFSWALGFIFLFTLGGLTGIVLS 266
Cdd:TIGR02882 369 RFTTPMLFSLAFIPNFLIGGVTGVMLA 395
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 134-264 2.39e-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: 38.81  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935663 134 DPILYQHLFWFFGHPEVYILILPGFGLISHIISQ--------ETAKKEVFgvlgMIYAMASIGVlGFvvwaHHMFT-VGL 204
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKiaggklfsDPLARLAF----ILFLLFSTPV-GF----HHQFAdPGI 270

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410935663 205 DTDTRAYFTSATMIIAVPT-------------------GIKIFSWVGTLYGSKPSYSASFswaLGFIFlFTLGGLTGIV 264
Cdd:cd01660  271 GPGWKFIHMVLTFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALF---LAMLM-FIPGGAGGII 345
 
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