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Conserved domains on  [gi|410935671|gb|AFV94461|]
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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

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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 ...
 1-266 2.48e-170

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: 480.13  E-value: 2.48e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00153  98 MSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLD 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00153 178 RMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIS 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00153 258 QESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLL 337

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00153 338 WALGFVFLFTIGGLTGVVLANSSIDII 364
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-266 2.48e-170

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 480.13  E-value: 2.48e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00153  98 MSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLD 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00153 178 RMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIS 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00153 258 QESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLL 337

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00153 338 WALGFVFLFTIGGLTGVVLANSSIDII 364
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-266 1.70e-155

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: 441.92  E-value: 1.70e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVG-HAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:cd01663   91 LSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILaHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLE 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:cd01663  171 KMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIIS 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:cd01663  251 TFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPML 330

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:cd01663  331 WALGFIFLFTIGGLTGVVLANSSLDIA 357
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-265 8.99e-98

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 294.90  E-value: 8.99e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671    1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:TIGR02891  93 FSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLM 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:TIGR02891 173 RMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILP 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  160 QeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:TIGR02891 253 T-FARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPML 331

                         250       260
                  ....*....|....*....|....*.
gi 410935671  240 WALGFIFLFTLGGLTGIVLSNSSLDI 265
Cdd:TIGR02891 332 FALGFIFLFVIGGLTGVMLASVPLDW 357
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-266 1.21e-93

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 285.48  E-value: 1.21e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:COG0843  102 LSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLM 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:COG0843  182 RMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIP 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:COG0843  262 T-FSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPML 340

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:COG0843  341 FALGFIILFVIGGLTGVMLASVPLDYQ 367
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-266 1.53e-63

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: 205.11  E-value: 1.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671    1 LSFWFLVPSLLMLLLSGAveaGAGTGWTVYPPLSAVghagssvDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLDL 80
Cdd:pfam00115  86 LSFWLVVLGAVLLLASFG---GATTGWTEYPPLVGV-------DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRM 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   81 vPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNScfydvsGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQ 160
Cdd:pfam00115 156 -PLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPK 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  161 eTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPS-YSASFS 239
Cdd:pfam00115 229 -FAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPML 307

                         250       260
                  ....*....|....*....|....*..
gi 410935671  240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:pfam00115 308 FFLGFAFLFIIGGLTGVMLALPPVNYY 334
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-266 2.48e-170

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 480.13  E-value: 2.48e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00153  98 MSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLD 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00153 178 RMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIS 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00153 258 QESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLL 337

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00153 338 WALGFVFLFTIGGLTGVVLANSSIDII 364
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-266 1.70e-155

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: 441.92  E-value: 1.70e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVG-HAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:cd01663   91 LSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILaHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLE 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:cd01663  171 KMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIIS 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:cd01663  251 TFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPML 330

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:cd01663  331 WALGFIFLFTIGGLTGVVLANSSLDIA 357
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-266 4.98e-142

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 408.60  E-value: 4.98e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00223  97 MSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSnLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLE 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00223 177 RLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVS 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00223 257 HYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPML 336

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00223 337 WALGFIFLFTVGGLTGIILSNSSLDIM 363
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-266 1.76e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 402.13  E-value: 1.76e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00167 100 MSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGnLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQY 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00167 180 QTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVV 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00167 260 YYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPML 339

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00167 340 WALGFIFLFTVGGLTGIVLANSSLDIV 366
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-266 1.26e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 394.86  E-value: 1.26e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00142  98 MSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSnLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00142 178 RVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIN 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00142 258 HYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPML 337

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00142 338 WALGFIFLFTVGGLTGIVLANSSLDVV 364
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-266 8.70e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 392.53  E-value: 8.70e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00116 100 MSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGnLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQY 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00116 180 QTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVT 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00116 260 YYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPML 339

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00116 340 WALGFIFLFTIGGLTGIVLANSSLDIV 366
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-266 1.07e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 364.00  E-value: 1.07e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLDL 80
Cdd:MTH00079 101 LSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEH 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  81 VPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQ 160
Cdd:MTH00079 181 MSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLY 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 161 ETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSW 240
Cdd:MTH00079 261 LTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLW 340

                        250       260
                 ....*....|....*....|....*.
gi 410935671 241 ALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00079 341 VLGFIFLFTIGGLTGVILSNSSLDII 366
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-266 2.07e-123

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 361.14  E-value: 2.07e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00007  97 MSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASnLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLE 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00007 177 RIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVT 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00007 257 HYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPML 336

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00007 337 WALGFIFLFTTGGLTGIVLSNSSLDII 363
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-266 3.92e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 352.98  E-value: 3.92e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00037 100 MSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSnIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFD 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00037 180 RLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIA 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00037 260 HYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLL 339

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00037 340 WALGFVFLFTIGGLTGIVLANSSIDVV 366
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-266 2.01e-119

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 351.11  E-value: 2.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00103 100 MSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQY 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00103 180 QTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVT 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00103 260 YYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAML 339

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00103 340 WALGFIFLFTVGGLTGIVLANSSLDIV 366
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-266 7.30e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 349.61  E-value: 7.30e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00183 100 MSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQY 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00183 180 QTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVA 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00183 260 YYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLL 339

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00183 340 WALGFIFLFTVGGLTGIVLANSSLDIV 366
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-266 3.11e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 345.39  E-value: 3.11e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00077 100 MSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQY 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00077 180 QTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVT 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00077 260 YYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAML 339

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00077 340 WALGFIFLFTVGGLTGIVLANSSLDIV 366
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-266 1.20e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 344.11  E-value: 1.20e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00182 102 ISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIqAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFN 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00182 182 RLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIP 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00182 262 TFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPML 341

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00182 342 WAMGFVFLFTLGGLTGVVLANSSLDIV 368
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-266 1.78e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 343.73  E-value: 1.78e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00184 102 ISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIqAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMD 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00184 182 RMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIP 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:MTH00184 262 TFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPML 341

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00184 342 WAIGFVFLFTMGGLTGIVLANSSLDVV 368
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-266 6.20e-104

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: 309.85  E-value: 6.20e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVG-HAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:cd00919   88 LSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSySSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLD 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:cd00919  168 KMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIP 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QEtAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:cd00919  248 TF-SGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPML 326

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:cd00919  327 FALGFLFLFTIGGLTGVVLANVPLDIV 353
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-266 1.18e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 311.18  E-value: 1.18e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00026 101 ISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIqAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMS 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00026 181 RIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILS 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPS--YSAS 237
Cdd:MTH00026 261 LFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNliFTTP 340

                        250       260
                 ....*....|....*....|....*....
gi 410935671 238 FSWALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00026 341 MAWALGFIFLFTIGGLTGIVLSNSSLDIL 369
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-265 8.99e-98

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 294.90  E-value: 8.99e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671    1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:TIGR02891  93 FSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLM 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:TIGR02891 173 RMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILP 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  160 QeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:TIGR02891 253 T-FARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPML 331

                         250       260
                  ....*....|....*....|....*.
gi 410935671  240 WALGFIFLFTLGGLTGIVLSNSSLDI 265
Cdd:TIGR02891 332 FALGFIFLFVIGGLTGVMLASVPLDW 357
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-266 1.21e-93

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 285.48  E-value: 1.21e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:COG0843  102 LSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLM 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:COG0843  182 RMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIP 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:COG0843  262 T-FSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPML 340

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:COG0843  341 FALGFIILFVIGGLTGVMLASVPLDYQ 367
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-266 1.64e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 274.25  E-value: 1.64e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSgaVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:MTH00048 101 LSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSsLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSR 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 lVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:MTH00048 179 -TSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICL 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QETAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSAS-F 238
Cdd:MTH00048 258 SLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPvV 337

                        250       260
                 ....*....|....*....|....*...
gi 410935671 239 SWALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:MTH00048 338 WWVVSFIVLFTIGGVTGIVLSASVLDNV 365
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-264 2.45e-84

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: 260.59  E-value: 2.45e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVGHA-GSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:cd01662   94 LSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSpGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLM 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:cd01662  174 RMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVP 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:cd01662  254 T-FSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPML 332

                        250       260
                 ....*....|....*....|....*
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLD 264
Cdd:cd01662  333 WAIGFLVTFVIGGLTGVMLASPPAD 357
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-266 1.53e-63

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: 205.11  E-value: 1.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671    1 LSFWFLVPSLLMLLLSGAveaGAGTGWTVYPPLSAVghagssvDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLDL 80
Cdd:pfam00115  86 LSFWLVVLGAVLLLASFG---GATTGWTEYPPLVGV-------DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRM 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   81 vPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNScfydvsGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQ 160
Cdd:pfam00115 156 -PLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPK 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  161 eTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPS-YSASFS 239
Cdd:pfam00115 229 -FAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPML 307

                         250       260
                  ....*....|....*....|....*..
gi 410935671  240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:pfam00115 308 FFLGFAFLFIIGGLTGVMLALPPVNYY 334
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-266 2.24e-56

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 191.30  E-value: 2.24e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVGHA-GSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:PRK15017 144 LSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSpGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMF 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:PRK15017 224 KMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAA 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 160 QeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:PRK15017 304 T-FSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAML 382

                        250       260
                 ....*....|....*....|....*..
gi 410935671 240 WALGFIFLFTLGGLTGIVLSNSSLDIV 266
Cdd:PRK15017 383 WTIGFIVTFSVGGMTGVLLAVPGADFV 409
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-264 4.36e-51

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: 176.58  E-value: 4.36e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671    1 LSFWFLVPSLLMLLLSGAVEAGAGTGWTVYPPLSAVGHA-GSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVFGMYLD 79
Cdd:TIGR02882 137 LSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSpGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLM 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671   80 LVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIS 159
Cdd:TIGR02882 217 QMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIIS 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671  160 QeTAKKEVFGVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFS 239
Cdd:TIGR02882 297 T-FAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPML 375

                         250       260
                  ....*....|....*....|....*
gi 410935671  240 WALGFIFLFTLGGLTGIVLSNSSLD 264
Cdd:TIGR02882 376 FSLAFIPNFLIGGVTGVMLAMASAD 400
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 127-266 6.48e-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: 40.73  E-value: 6.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 127 DPILYQHLFWFFGHPEVYILILPGFGLISHIISQ--------ETAKKEVFgvlgMIYAMASIGVlGFvvwaHHMFT-VGL 197
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKiaggklfsDPLARLAF----ILFLLFSTPV-GF----HHQFAdPGI 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410935671 198 DTDTRAYFTSATMIIAVPT-------------------GIKIFSWVGTLYGSKPSYSASFswaLGFIFlFTLGGLTGIVL 258
Cdd:cd01660  271 GPGWKFIHMVLTFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALF---LAMLM-FIPGGAGGIIN 346


                 ....*...
gi 410935671 259 SNSSLDIV 266
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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