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Conserved domains on  [gi|1822143186|gb|QIN55173|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Milnesium cf. quadrifidum NO.398]

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 ...
 1-244 1.21e-141

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


The actual alignment was detected with superfamily member cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 405.71  E-value: 1.21e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:cd01663    24 LSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:cd01663   104 LLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:cd01663   184 FLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLG 263


                  ....
gi 1822143186 241 MVYA 244
Cdd:cd01663   264 MVYA 267
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-244 1.21e-141

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: 405.71  E-value: 1.21e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:cd01663    24 LSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:cd01663   104 LLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:cd01663   184 FLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLG 263


                  ....
gi 1822143186 241 MVYA 244
Cdd:cd01663   264 MVYA 267
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-244 1.70e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 393.46  E-value: 1.70e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00153   31 LSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00153  111 LSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITA 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00153  191 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLG 270


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00153  271 MIYA 274
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-244 4.15e-97

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: 292.59  E-value: 4.15e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLiGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:TIGR02891  27 LALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:TIGR02891 106 LASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKgMMFGQIG 240
Cdd:TIGR02891 186 ILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRA 264


                  ....
gi 1822143186 241 MVYA 244
Cdd:TIGR02891 265 MVYA 268
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-244 9.73e-92

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 279.70  E-value: 9.73e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPvLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:COG0843    36 LALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:COG0843   115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIImSTSGKGMMFGQIG 240
Cdd:COG0843   195 ILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEII-PTFSRKPLFGYKA 273


                  ....
gi 1822143186 241 MVYA 244
Cdd:COG0843   274 MVLA 277
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-244 7.36e-56

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: 184.31  E-value: 7.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVlIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:pfam00115  20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMfsdVGVGSGWTLYPPLTNiyghssssVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMdKLPLFVWSIYITA 160
Cdd:pfam00115  99 LASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFstsffdPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGmMFGQIG 240
Cdd:pfam00115 167 ILILLAFPVLAAALLLLLLDRSL------GAGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKL 239


                  ....
gi 1822143186 241 MVYA 244
Cdd:pfam00115 240 SVLA 243
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-244 1.21e-141

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: 405.71  E-value: 1.21e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:cd01663    24 LSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:cd01663   104 LLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:cd01663   184 FLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLG 263


                  ....
gi 1822143186 241 MVYA 244
Cdd:cd01663   264 MVYA 267
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-244 1.70e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 393.46  E-value: 1.70e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00153   31 LSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00153  111 LSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITA 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00153  191 ILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLG 270


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00153  271 MIYA 274
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-244 1.24e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 368.15  E-value: 1.24e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00223   30 LSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00223  110 LSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTA 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00223  190 FLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLG 269


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00223  270 MIYA 273
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-244 1.09e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 365.92  E-value: 1.09e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00167   33 LSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00167  113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTT 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00167  193 ILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMG 272


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00167  273 MVWA 276
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-244 1.73e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 345.15  E-value: 1.73e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00116   33 LSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00116  113 LASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00116  193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMG 272


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00116  273 MVWA 276
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-244 1.81e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 339.78  E-value: 1.81e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00142   31 LSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00142  111 LSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITA 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00142  191 ILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLG 270


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00142  271 MIYA 274
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-244 9.40e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 328.32  E-value: 9.40e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00182   35 FSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00182  115 LGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITA 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00182  195 FLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLG 274


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00182  275 MVYA 278
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-244 2.59e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 324.47  E-value: 2.59e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00184   35 FSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00184  115 LGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTT 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00184  195 FLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLG 274


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00184  275 MVYA 278
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-244 7.99e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 320.62  E-value: 7.99e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00037   33 MSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00037  113 LASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00037  193 FLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLG 272


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00037  273 MVYA 276
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-244 1.32e-106

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 317.01  E-value: 1.32e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00079   34 LSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIyGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00079  114 LDSCFVDMGPGTSWTVYPPLSTL-GHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTV 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00079  193 FLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLG 272


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00079  273 MVYA 276
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-244 7.22e-106

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 315.30  E-value: 7.22e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00007   30 MSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00007  110 VSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITV 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00007  190 VLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLG 269


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00007  270 MIYA 273
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-244 9.44e-104

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 309.93  E-value: 9.44e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00183   33 LSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00183  113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00183  193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMG 272


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00183  273 MVWA 276
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-244 1.09e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 309.95  E-value: 1.09e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00077   33 LSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00077  113 LASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00077  193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMG 272


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00077  273 MVWA 276
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-244 1.44e-103

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 309.51  E-value: 1.44e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00103   33 LSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00103  113 LASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00103  193 VLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMG 272


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00103  273 MVWA 276
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-244 4.15e-97

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: 292.59  E-value: 4.15e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLiGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:TIGR02891  27 LALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:TIGR02891 106 LASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKgMMFGQIG 240
Cdd:TIGR02891 186 ILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRA 264


                  ....
gi 1822143186 241 MVYA 244
Cdd:TIGR02891 265 MVYA 268
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-244 5.25e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 288.07  E-value: 5.25e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00026   34 FSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:MTH00026  114 LGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITA 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00026  194 ILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLG 273


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00026  274 MVYA 277
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-244 9.73e-92

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 279.70  E-value: 9.73e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPvLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:COG0843    36 LALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:COG0843   115 LISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTS 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIImSTSGKGMMFGQIG 240
Cdd:COG0843   195 ILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEII-PTFSRKPLFGYKA 273


                  ....
gi 1822143186 241 MVYA 244
Cdd:COG0843   274 MVLA 277
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-244 5.56e-91

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: 275.56  E-value: 5.56e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPlMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:cd00919    22 LALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:cd00919   101 LSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKgMMFGQIG 240
Cdd:cd00919   181 ILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKL 259


                  ....
gi 1822143186 241 MVYA 244
Cdd:cd00919   260 MVYA 263
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-244 1.58e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 275.79  E-value: 1.58e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:MTH00048   34 LSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFsdVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVrMDKLPLFVWSIYITA 160
Cdd:MTH00048  114 LLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV-FSRTSIILWSYLFTS 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGMMFGQIG 240
Cdd:MTH00048  191 ILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYG 270


                  ....
gi 1822143186 241 MVYA 244
Cdd:MTH00048  271 LVFA 274
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-244 3.76e-78

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: 243.64  E-value: 3.76e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGgFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:cd01662    28 DALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITA 160
Cdd:cd01662   107 NASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTS 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKgMMFGQIG 240
Cdd:cd01662   187 ILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRS 265


                  ....
gi 1822143186 241 MVYA 244
Cdd:cd01662   266 MVYA 269
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-244 7.36e-56

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: 184.31  E-value: 7.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   1 LSVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVlIGGFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILL 80
Cdd:pfam00115  20 LGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  81 VFSMfsdVGVGSGWTLYPPLTNiyghssssVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMdKLPLFVWSIYITA 160
Cdd:pfam00115  99 LASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 161 ILLILALPVLAGAITMLIFDRNFstsffdPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIIMSTSGKGmMFGQIG 240
Cdd:pfam00115 167 ILILLAFPVLAAALLLLLLDRSL------GAGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKL 239


                  ....
gi 1822143186 241 MVYA 244
Cdd:pfam00115 240 SVLA 243
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-244 7.09e-52

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: 178.12  E-value: 7.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186   2 SVLIRLELSQPNTMLMTEDIYNSFITSHALVMIFFFVMPVLIGgFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILLV 81
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  82 FSMFSDVGVGSGWTLYPPLTNIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITAI 161
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 162 LLILALPVLAGAITMLIFDRNFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIImSTSGKGMMFGQIGM 241
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEII-STFAQKRLFGYKSM 309


                  ...
gi 1822143186 242 VYA 244
Cdd:TIGR02882 310 VWS 312
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 22-244 1.46e-46

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 163.95  E-value: 1.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  22 YNSFITSHALVMIFFFVMPVLIGgFGNWLVPLMISSPDMAFPRVNNMSFWMLIASFILLVFSMFSDVGVGSGWTLYPPLT 101
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 102 NIYGHSSSSVDYVILSLHLAGVSSIFGGMNFVVTIRNMHYCGVRMDKLPLFVWSIYITAILLILALPVLAGAITMLIFDR 181
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822143186 182 NFSTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGLISQIImSTSGKGMMFGQIGMVYA 244
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIA-ATFSRKRLFGYTSLVWA 319
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 22-217 1.09e-03

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


Pssm-ID: 238830  Cd Length: 473  Bit Score: 39.58  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186  22 YNSFITSHALVMIFFFVMpVLIGGFGNWLVPLMISSPDMAfPRVNNMSFWMLIASFILLVFSMFSdvGVGSG-WTLYPPL 100
Cdd:cd01660    44 YYQGLTLHGVLLAIVFTT-FFIMGFFYAIVARALLRSLFN-RRLAWAGFWLMVIGTVMAAVPILL--GQASVlYTFYPPL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822143186 101 tniyghSSSSVDYVILSLHLAGvSSIFGGMNFVvtirnmHYCGVRMD----KLPLFVWSIYITAIL-LILALPVlagAIT 175
Cdd:cd01660   120 ------QAHPLFYIGAALVVVG-SWISGFAMFV------TLWRWKKAnpgkKVPLATFMVVTTMILwLVASLGV---ALE 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1822143186 176 MLIFDRNFSTSFFDPAgggDPILFQHLFWFFGHPEVYILILP 217
Cdd:cd01660   184 VLFQLLPWSLGLVDTV---DVLLSRTLFWWFGHPLVYFWLLP 222
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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