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Conserved domains on  [gi|410935645|gb|AFV94448|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Tigriopus sp. 3 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

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-270 7.01e-173

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: 487.07  E-value: 7.01e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00153 335 SLLWALGFVFLFTIGGLTGVVLANSSIDIIL 365
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-270 7.01e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 487.07  E-value: 7.01e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00153 335 SLLWALGFVFLFTIGGLTGVVLANSSIDIIL 365
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-270 8.27e-159

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: 450.40  E-value: 8.27e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAVG-HAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:cd01663   88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILaHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:cd01663  168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:cd01663  248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:cd01663  328 PMLWALGFIFLFTIGGLTGVVLANSSLDIAL 358
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-268 4.15e-99

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: 298.75  E-value: 4.15e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645    1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:TIGR02891  90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  160 IISQeTSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:TIGR02891 250 ILPT-FARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTT 328

                         250       260
                  ....*....|....*....|....*....
gi 410935645  240 SFCWALGFIFLFTLGGLTGIVLSNSSLDI 268
Cdd:TIGR02891 329 PMLFALGFIFLFVIGGLTGVMLASVPLDW 357
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-270 2.43e-96

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 292.80  E-value: 2.43e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:COG0843   99 LNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGM 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:COG0843  179 TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSE 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQeTSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:COG0843  259 IIPT-FSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTT 337

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:COG0843  338 PMLFALGFIILFVIGGLTGVMLASVPLDYQV 368
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-270 3.49e-65

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: 209.35  E-value: 3.49e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645    1 LNNLSFWFLMPSLLLLLLSGAveaGAGTGWTVYPPLSAVghagssvDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGLY 80
Cdd:pfam00115  83 LNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVGV-------DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   81 LDLvPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNScfydvsGGGDPILYQHLFWFFGHPEVYILILPGFGLISHI 160
Cdd:pfam00115 153 LRM-PLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  161 ISQeTSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSF-SA 239
Cdd:pfam00115 226 LPK-FAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTT 304

                         250       260       270
                  ....*....|....*....|....*....|.
gi 410935645  240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:pfam00115 305 PMLFFLGFAFLFIIGGLTGVMLALPPVNYYV 335
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-270 7.01e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 487.07  E-value: 7.01e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00153 335 SLLWALGFVFLFTIGGLTGVVLANSSIDIIL 365
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-270 8.27e-159

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: 450.40  E-value: 8.27e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAVG-HAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:cd01663   88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILaHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:cd01663  168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:cd01663  248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:cd01663  328 PMLWALGFIFLFTIGGLTGVVLANSSLDIAL 358
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-270 1.00e-144

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 415.53  E-value: 1.00e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00223  94 LNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSnLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGM 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00223 174 QLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00223 254 IVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEA 333

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00223 334 PMLWALGFIFLFTVGGLTGIILSNSSLDIML 364
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-270 3.80e-142

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 409.07  E-value: 3.80e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00167  97 MNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGnLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGI 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00167 177 TQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00167 257 IVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWET 336

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00167 337 PMLWALGFIFLFTVGGLTGIVLANSSLDIVL 367
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-270 3.09e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 401.41  E-value: 3.09e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00142  95 MNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSnLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGM 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00142 175 KFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00142 255 IINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEP 334

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00142 335 PMLWALGFIFLFTVGGLTGIVLANSSLDVVL 365
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-270 2.24e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 399.47  E-value: 2.24e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00116  97 MNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGnLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAM 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00116 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00116 257 IVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDP 336

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00116 337 PMLWALGFIFLFTIGGLTGIVLANSSLDIVL 367
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-270 2.10e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 373.63  E-value: 2.10e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAVGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGLY 80
Cdd:MTH00079  98 LNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSIS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  81 LDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHI 160
Cdd:MTH00079 178 LEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQS 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 161 ISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSAS 240
Cdd:MTH00079 258 TLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPL 337

                        250       260       270
                 ....*....|....*....|....*....|
gi 410935645 241 FCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00079 338 LLWVLGFIFLFTIGGLTGVILSNSSLDIIL 367
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-270 2.70e-126

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 368.46  E-value: 2.70e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00007  94 LNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASnLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00007 174 RLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISH 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00007 254 IVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYET 333

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00007 334 PMLWALGFIFLFTTGGLTGIVLSNSSLDIIL 364
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-270 2.00e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 358.76  E-value: 2.00e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00037  97 MNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSnIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGM 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00037 177 TFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISH 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00037 257 VIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWET 336

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00037 337 PLLWALGFVFLFTIGGLTGIVLANSSIDVVL 367
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-270 5.06e-122

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 357.66  E-value: 5.06e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00103  97 MNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAM 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00103 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00103 257 IVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSP 336

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00103 337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVL 367
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-270 6.99e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 357.70  E-value: 6.99e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00183  97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAI 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00183 177 SQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00183 257 IVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWET 336

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00183 337 PLLWALGFIFLFTVGGLTGIVLANSSLDIVL 367
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-270 8.18e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 352.32  E-value: 8.18e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00077  97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSM 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00077 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00077 257 IVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDA 336

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00077 337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVL 367
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-270 9.95e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 352.20  E-value: 9.95e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00182  99 LNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIqAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGV 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00182 179 TFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQ 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00182 259 IIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDT 338

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00182 339 PMLWAMGFVFLFTLGGLTGVVLANSSLDIVL 369
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-270 1.46e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 351.82  E-value: 1.46e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00184  99 LNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIqAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGI 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00184 179 TMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00184 259 IIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDT 338

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00184 339 PMLWAIGFVFLFTMGGLTGIVLANSSLDVVL 369
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-270 3.07e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 318.11  E-value: 3.07e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00026  98 LNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIqAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGM 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00026 178 TMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPS--F 237
Cdd:MTH00026 258 ILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNliF 337

                        250       260       270
                 ....*....|....*....|....*....|...
gi 410935645 238 SASFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00026 338 TTPMAWALGFIFLFTIGGLTGIVLSNSSLDILL 370
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-270 3.69e-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: 315.62  E-value: 3.69e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAVG-HAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:cd00919   85 LNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSySSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGM 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:cd00919  165 TLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISE 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQEtSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:cd00919  245 IIPTF-SGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDP 323

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:cd00919  324 PMLFALGFLFLFTIGGLTGVVLANVPLDIVL 354
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-268 4.15e-99

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: 298.75  E-value: 4.15e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645    1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:TIGR02891  90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  160 IISQeTSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:TIGR02891 250 ILPT-FARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTT 328

                         250       260
                  ....*....|....*....|....*....
gi 410935645  240 SFCWALGFIFLFTLGGLTGIVLSNSSLDI 268
Cdd:TIGR02891 329 PMLFALGFIFLFVIGGLTGVMLASVPLDW 357
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-270 2.43e-96

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 292.80  E-value: 2.43e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:COG0843   99 LNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGM 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:COG0843  179 TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSE 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQeTSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:COG0843  259 IIPT-FSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTT 337

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:COG0843  338 PMLFALGFIILFVIGGLTGVMLASVPLDYQV 368
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-270 1.56e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 279.64  E-value: 1.56e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSgaVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:MTH00048  98 LNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSsLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDlVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:MTH00048 176 FSR-TSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISH 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQETSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:MTH00048 255 ICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSD 334

                        250       260       270
                 ....*....|....*....|....*....|..
gi 410935645 240 S-FCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:MTH00048 335 PvVWWVVSFIVLFTIGGVTGIVLSASVLDNVL 366
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-270 3.04e-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: 265.60  E-value: 3.04e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAVGHA-GSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:cd01662   91 LNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSpGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGM 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:cd01662  171 TLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSE 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQeTSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:cd01662  251 IVPT-FSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFET 329

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:cd01662  330 PMLWAIGFLVTFVIGGLTGVMLASPPADFQV 360
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-270 3.49e-65

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: 209.35  E-value: 3.49e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645    1 LNNLSFWFLMPSLLLLLLSGAveaGAGTGWTVYPPLSAVghagssvDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGLY 80
Cdd:pfam00115  83 LNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVGV-------DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   81 LDLvPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNScfydvsGGGDPILYQHLFWFFGHPEVYILILPGFGLISHI 160
Cdd:pfam00115 153 LRM-PLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  161 ISQeTSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSF-SA 239
Cdd:pfam00115 226 LPK-FAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTT 304

                         250       260       270
                  ....*....|....*....|....*....|.
gi 410935645  240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:pfam00115 305 PMLFFLGFAFLFIIGGLTGVMLALPPVNYYV 335
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-270 1.87e-59

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 199.78  E-value: 1.87e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAVGHA-GSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:PRK15017 141 LNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSpGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGM 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:PRK15017 221 TMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSE 300

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 160 IISQeTSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:PRK15017 301 IAAT-FSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHS 379

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410935645 240 SFCWALGFIFLFTLGGLTGIVLSNSSLDIVL 270
Cdd:PRK15017 380 AMLWTIGFIVTFSVGGMTGVLLAVPGADFVL 410
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-267 3.69e-53

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: 182.36  E-value: 3.69e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645    1 LNNLSFWFLMPSLLLLLLSGAVEAGAGTGWTVYPPLSAVGHA-GSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGL 79
Cdd:TIGR02882 134 LNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSpGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGM 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645   80 YLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISH 159
Cdd:TIGR02882 214 KLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSE 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645  160 IISQeTSKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSFSA 239
Cdd:TIGR02882 294 IIST-FAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTT 372

                         250       260
                  ....*....|....*....|....*...
gi 410935645  240 SFCWALGFIFLFTLGGLTGIVLSNSSLD 267
Cdd:TIGR02882 373 PMLFSLAFIPNFLIGGVTGVMLAMASAD 400
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 130-269 2.76e-04

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 41.89  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 130 DPILYQHLFWFFGHPEVYILILPGFGLISHIISQ--------ETSKKEVFgvlgMIYAMASIGVlGFvvwaHHMFT-VGL 200
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKiaggklfsDPLARLAF----ILFLLFSTPV-GF----HHQFAdPGI 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935645 201 DTDTRAYFTSATMIIAVPT-------------------GIKIFSWVGTLYGSKPSFSASFcwaLGFIFlFTLGGLTGIVL 261
Cdd:cd01660  271 GPGWKFIHMVLTFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALF---LAMLM-FIPGGAGGIIN 346


                 ....*...
gi 410935645 262 SNSSLDIV 269
Cdd:cd01660  347 ASYQLNYV 354
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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