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Conserved domains on  [gi|1734264395|gb|QEL52065|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Trichinella spiralis]

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 ...
 9-378 0e+00

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: 621.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   9 NHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGlisEYYNVIVTAHALAMIFFMVMPMLLSGFGNWLIPIMA 88
Cdd:cd01663     2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGND---QLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  89 GAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITGSINFITT 168
Cdd:cd01663    79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 169 CFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGHPEVYILV 248
Cdd:cd01663   159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 249 LPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKIFSWLATL 328
Cdd:cd01663   239 LPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1734264395 329 YGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:cd01663   319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHF 368
 
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 ...
 9-378 0e+00

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: 621.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   9 NHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGlisEYYNVIVTAHALAMIFFMVMPMLLSGFGNWLIPIMA 88
Cdd:cd01663     2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGND---QLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  89 GAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITGSINFITT 168
Cdd:cd01663    79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 169 CFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGHPEVYILV 248
Cdd:cd01663   159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 249 LPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKIFSWLATL 328
Cdd:cd01663   239 LPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1734264395 329 YGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:cd01663   319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHF 368
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-378 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 594.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   1 MMKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGLIseyYNVIVTAHALAMIFFMVMPMLLSGFG 80
Cdd:MTH00153    1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQI---YNVIVTAHAFIMIFFMVMPIMIGGFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  81 NWLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSIT 160
Cdd:MTH00153   78 NWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 161 GSINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFG 240
Cdd:MTH00153  158 GAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 241 HPEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVK 320
Cdd:MTH00153  238 HPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734264395 321 IFSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00153  318 IFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHF 375
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 5-378 1.38e-143

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: 416.62  E-value: 1.38e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   5 LYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGlisEYYNVIVTAHALAMIFFMVMPMLlSGFGNWLI 84
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDA---ETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  85 PIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITGSIN 164
Cdd:TIGR02891  77 PLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVN 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 165 FITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGHPEV 244
Cdd:TIGR02891 157 FIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 245 YILVLPAFGVVSEALMFMSGKfKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKIFSW 324
Cdd:TIGR02891 237 YIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNW 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1734264395 325 LATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:TIGR02891 316 IATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHF 369
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-378 2.42e-140

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 409.52  E-value: 2.42e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   1 MMKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWtfnvNGLIS-EYYNVIVTAHALAMIFFMVMPMLlSGF 79
Cdd:COG0843     6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPG----LGLLSpETYNQLFTMHGTIMIFFFATPFL-AGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  80 GNWLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSI 159
Cdd:COG0843    81 GNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 160 TGSINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFF 239
Cdd:COG0843   161 LGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 240 GHPEVYILVLPAFGVVSEALMFMSGKfKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGV 319
Cdd:COG0843   241 GHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGV 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1734264395 320 KIFSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:COG0843   320 KVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHF 378
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 12-378 1.27e-91

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: 281.38  E-value: 1.27e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  12 KIGTLYILFGIIGGMLGISLSALIRMILSSPwtfNVNGLISEYYNVIVTAHALAMIFFMVMPMLLsGFGNWLIPIMAGAA 91
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFP---GLNFLSPLTYNQLRTLHGNLMIFWFATPFLF-GFGNYLVPLMIGAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  92 DMSFPRLNNLGFWLLPPALMLLSSSMlinMGAGTGWTIYPPLStwlghpnhSVDLVIFSLHLAGISSITGSINFITTCFL 171
Cdd:pfam00115  77 DMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILK 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 172 SRPIIYTLeRLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTtffetsGGGDPILFQHMFWFFGHPEVYILVLPA 251
Cdd:pfam00115 146 RRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 252 FGVVSEALMFMSGKfKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKIFSWLATLYGT 331
Cdd:pfam00115 219 FGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGG 297

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1734264395 332 HIKM-TPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:pfam00115 298 WIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHF 345
 
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 ...
 9-378 0e+00

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: 621.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   9 NHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGlisEYYNVIVTAHALAMIFFMVMPMLLSGFGNWLIPIMA 88
Cdd:cd01663     2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGND---QLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  89 GAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITGSINFITT 168
Cdd:cd01663    79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 169 CFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGHPEVYILV 248
Cdd:cd01663   159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 249 LPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKIFSWLATL 328
Cdd:cd01663   239 LPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1734264395 329 YGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:cd01663   319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHF 368
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-378 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 594.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   1 MMKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGLIseyYNVIVTAHALAMIFFMVMPMLLSGFG 80
Cdd:MTH00153    1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQI---YNVIVTAHAFIMIFFMVMPIMIGGFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  81 NWLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSIT 160
Cdd:MTH00153   78 NWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 161 GSINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFG 240
Cdd:MTH00153  158 GAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 241 HPEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVK 320
Cdd:MTH00153  238 HPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734264395 321 IFSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00153  318 IFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHF 375
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-378 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 568.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   2 MKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNgliSEYYNVIVTAHALAMIFFMVMPMLLSGFGN 81
Cdd:MTH00223    1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGD---DQLYNVIVTAHAFVMIFFLVMPMMIGGFGN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  82 WLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITG 161
Cdd:MTH00223   78 WLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 162 SINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGH 241
Cdd:MTH00223  158 AINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 242 PEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKI 321
Cdd:MTH00223  238 PEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734264395 322 FSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00223  318 FSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHF 374
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-378 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 535.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   1 MMKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGLIseyYNVIVTAHALAMIFFMVMPMLLSGFG 80
Cdd:MTH00167    3 INRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQI---YNVIVTAHAFVMIFFMVMPIMIGGFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  81 NWLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSIT 160
Cdd:MTH00167   80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 161 GSINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFG 240
Cdd:MTH00167  160 GSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 241 HPEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVK 320
Cdd:MTH00167  240 HPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734264395 321 IFSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00167  320 VFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHF 377
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-378 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 522.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   1 MMKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGLIseyYNVIVTAHALAMIFFMVMPMLLSGFG 80
Cdd:MTH00116    3 ITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQI---YNVIVTAHAFVMIFFMVMPIMIGGFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  81 NWLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSIT 160
Cdd:MTH00116   80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 161 GSINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFG 240
Cdd:MTH00116  160 GAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 241 HPEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVK 320
Cdd:MTH00116  240 HPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIK 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734264395 321 IFSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00116  320 VFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHF 377
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-378 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 520.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   1 MMKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGlisEYYNVIVTAHALAMIFFMVMPMLLSGFG 80
Cdd:MTH00079    4 LSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNG---QLYNSVITAHAILMIFFMVMPSMIGGFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  81 NWLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTwLGHPNHSVDLVIFSLHLAGISSIT 160
Cdd:MTH00079   81 NWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSIL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 161 GSINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFG 240
Cdd:MTH00079  160 GGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 241 HPEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVK 320
Cdd:MTH00079  240 HPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVK 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734264395 321 IFSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00079  320 VFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHF 377
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-378 2.72e-180

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 510.42  E-value: 2.72e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   1 MMKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNgliSEYYNVIVTAHALAMIFFMVMPMLLSGFG 80
Cdd:MTH00142    1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGD---DQLYNVIVTAHAFVMIFFMVMPVMIGGFG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  81 NWLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSIT 160
Cdd:MTH00142   78 NWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 161 GSINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFG 240
Cdd:MTH00142  158 GAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 241 HPEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVK 320
Cdd:MTH00142  238 HPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIK 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734264395 321 IFSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00142  318 VFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHF 375
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-378 7.97e-166

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 473.62  E-value: 7.97e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   2 MKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNgliSEYYNVIVTAHALAMIFFMVMPMLLSGFGN 81
Cdd:MTH00007    1 MRWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGS---DQLYNTIVTAHAFLMIFFLVMPVFIGGFGN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  82 WLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITG 161
Cdd:MTH00007   78 WLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 162 SINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGH 241
Cdd:MTH00007  158 AINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 242 PEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKI 321
Cdd:MTH00007  238 PEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734264395 322 FSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00007  318 FSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHF 374
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-378 1.56e-165

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 473.22  E-value: 1.56e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   1 MMKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGLIseyYNVIVTAHALAMIFFMVMPMLLSGFG 80
Cdd:MTH00103    3 INRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQI---YNVIVTAHAFVMIFFMVMPIMIGGFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  81 NWLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSIT 160
Cdd:MTH00103   80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 161 GSINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFG 240
Cdd:MTH00103  160 GAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 241 HPEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVK 320
Cdd:MTH00103  240 HPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVK 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734264395 321 IFSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00103  320 VFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHF 377
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-378 1.16e-164

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 471.23  E-value: 1.16e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   1 MMKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNgliSEYYNVIVTAHALAMIFFMVMPMLLSGFG 80
Cdd:MTH00182    5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGD---DHLYNVIVTAHAFIMIFFLVMPVMIGGFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  81 NWLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSIT 160
Cdd:MTH00182   82 NWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSIL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 161 GSINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFG 240
Cdd:MTH00182  162 GAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 241 HPEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVK 320
Cdd:MTH00182  242 HPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734264395 321 IFSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00182  322 VFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHF 379
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 3-378 4.49e-163

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 467.00  E-value: 4.49e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   3 KWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGLIseyYNVIVTAHALAMIFFMVMPMLLSGFGNW 82
Cdd:MTH00037    5 RWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQI---YNVIVTAHALVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  83 LIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITGS 162
Cdd:MTH00037   82 LIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILAS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 163 INFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGHP 242
Cdd:MTH00037  162 INFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHP 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 243 EVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKIF 322
Cdd:MTH00037  242 EVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734264395 323 SWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00037  322 SWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHF 377
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-378 1.27e-162

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 465.84  E-value: 1.27e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   1 MMKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNgliSEYYNVIVTAHALAMIFFMVMPMLLSGFG 80
Cdd:MTH00184    5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGD---DHLYNVIVTAHAFVMIFFLVMPVMIGGFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  81 NWLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSIT 160
Cdd:MTH00184   82 NWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSIL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 161 GSINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFG 240
Cdd:MTH00184  162 GAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 241 HPEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVK 320
Cdd:MTH00184  242 HPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734264395 321 IFSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00184  322 IFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHF 379
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 3-378 5.51e-162

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 464.01  E-value: 5.51e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   3 KWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGLIseyYNVIVTAHALAMIFFMVMPMLLSGFGNW 82
Cdd:MTH00183    5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQI---YNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  83 LIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITGS 162
Cdd:MTH00183   82 LIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 163 INFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGHP 242
Cdd:MTH00183  162 INFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 243 EVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKIF 322
Cdd:MTH00183  242 EVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734264395 323 SWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00183  322 SWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHF 377
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-378 9.47e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 460.95  E-value: 9.47e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   1 MMKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGLIseyYNVIVTAHALAMIFFMVMPMLLSGFG 80
Cdd:MTH00077    3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQI---YNVIVTAHAFVMIFFMVMPIMIGGFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  81 NWLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSIT 160
Cdd:MTH00077   80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 161 GSINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFG 240
Cdd:MTH00077  160 GAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 241 HPEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVK 320
Cdd:MTH00077  240 HPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVK 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1734264395 321 IFSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00077  320 VFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHF 377
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 10-378 5.46e-148

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: 426.56  E-value: 5.46e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  10 HKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGlisEYYNVIVTAHALAMIFFMVMPMLLSGFGNWLIPiMAG 89
Cdd:cd00919     1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDP---QLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  90 AADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITGSINFITTC 169
Cdd:cd00919    77 ARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 170 FLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGHPEVYILVL 249
Cdd:cd00919   157 LNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILIL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 250 PAFGVVSEALMFMSGKfKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKIFSWLATLY 329
Cdd:cd00919   237 PAFGAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLW 315

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1734264395 330 GTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:cd00919   316 GGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHF 364
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-378 3.60e-144

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 419.42  E-value: 3.60e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   2 MKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNgliSEYYNVIVTAHALAMIFFMVMPMLLSGFGN 81
Cdd:MTH00026    5 VRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGD---DHLYNVIVTAHAFVMIFFLVMPTMIGGFGN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  82 WLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITG 161
Cdd:MTH00026   82 WFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 162 SINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGH 241
Cdd:MTH00026  162 AMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGH 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 242 PEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKI 321
Cdd:MTH00026  242 PEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKI 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1734264395 322 FSWLATLYGT--HIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00026  322 FSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHF 380
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 5-378 1.38e-143

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: 416.62  E-value: 1.38e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   5 LYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGlisEYYNVIVTAHALAMIFFMVMPMLlSGFGNWLI 84
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDA---ETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  85 PIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITGSIN 164
Cdd:TIGR02891  77 PLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVN 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 165 FITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGHPEV 244
Cdd:TIGR02891 157 FIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 245 YILVLPAFGVVSEALMFMSGKfKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKIFSW 324
Cdd:TIGR02891 237 YIIFLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNW 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1734264395 325 LATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:TIGR02891 316 IATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHF 369
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-378 2.42e-140

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 409.52  E-value: 2.42e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   1 MMKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWtfnvNGLIS-EYYNVIVTAHALAMIFFMVMPMLlSGF 79
Cdd:COG0843     6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPG----LGLLSpETYNQLFTMHGTIMIFFFATPFL-AGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  80 GNWLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSI 159
Cdd:COG0843    81 GNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 160 TGSINFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFF 239
Cdd:COG0843   161 LGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 240 GHPEVYILVLPAFGVVSEALMFMSGKfKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGV 319
Cdd:COG0843   241 GHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGV 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1734264395 320 KIFSWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:COG0843   320 KVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHF 378
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-378 2.53e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 403.67  E-value: 2.53e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   1 MMKWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWtFNVngLISEYYNVIVTAHALAMIFFMVMPMLLSGFG 80
Cdd:MTH00048    4 LLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPY-YNV--ISLDVYNFLITNHGIIMIFFFLMPVLIGGFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  81 NWLIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLinMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSIT 160
Cdd:MTH00048   81 NYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 161 GSINFITTCFlSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFG 240
Cdd:MTH00048  159 GSINFICTIY-SAFMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 241 HPEVYILVLPAFGVVSEALMFMSGKFKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVK 320
Cdd:MTH00048  238 HPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIK 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1734264395 321 IFSWLATLYGTHIKMT-PAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:MTH00048  318 VFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHF 376
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 4-378 1.07e-123

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: 366.14  E-value: 1.07e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   4 WLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPwtfNVNGLISEYYNVIVTAHALAMIFFMVMPMLlSGFGNWL 83
Cdd:cd01662     1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALP---GNDFLSPEHYNQIFTMHGTIMIFLFAMPLV-FGLMNYL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  84 IPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITGSI 163
Cdd:cd01662    77 VPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 164 NFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGHPE 243
Cdd:cd01662   157 NFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 244 VYILVLPAFGVVSEALMFMSGKfKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKIFS 323
Cdd:cd01662   237 VYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFN 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1734264395 324 WLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:cd01662   316 WLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHF 370
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 12-378 1.27e-91

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: 281.38  E-value: 1.27e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  12 KIGTLYILFGIIGGMLGISLSALIRMILSSPwtfNVNGLISEYYNVIVTAHALAMIFFMVMPMLLsGFGNWLIPIMAGAA 91
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFP---GLNFLSPLTYNQLRTLHGNLMIFWFATPFLF-GFGNYLVPLMIGAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  92 DMSFPRLNNLGFWLLPPALMLLSSSMlinMGAGTGWTIYPPLStwlghpnhSVDLVIFSLHLAGISSITGSINFITTCFL 171
Cdd:pfam00115  77 DMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILK 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 172 SRPIIYTLeRLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTtffetsGGGDPILFQHMFWFFGHPEVYILVLPA 251
Cdd:pfam00115 146 RRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 252 FGVVSEALMFMSGKfKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKIFSWLATLYGT 331
Cdd:pfam00115 219 FGIIYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGG 297

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1734264395 332 HIKM-TPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:pfam00115 298 WIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHF 345
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 3-378 1.63e-81

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 262.18  E-value: 1.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   3 KWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPWTFNVNGLISEYYNVIVTAHALAMIFFMVMPMLLsGFGNW 82
Cdd:PRK15017   47 EWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVI-GLMNL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  83 LIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITGS 162
Cdd:PRK15017  126 VVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTG 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 163 INFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGHP 242
Cdd:PRK15017  206 INFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHP 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 243 EVYILVLPAFGVVSEALMFMSGKfKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKIF 322
Cdd:PRK15017  286 EVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIF 364

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734264395 323 SWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:PRK15017  365 NWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHF 420
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 3-378 2.55e-80

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: 258.63  E-value: 2.55e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395   3 KWLYSGNHKKIGTLYILFGIIGGMLGISLSALIRMILSSPwtfNVNGLISEYYNVIVTAHALAMIFFMVMPMLLsGFGNW 82
Cdd:TIGR02882  43 EWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVP---DNKFLDAQHYNEIFTTHGVIMIIFMAMPFII-GLMNI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  83 LIPIMAGAADMSFPRLNNLGFWLLPPALMLLSSSMLINMGAGTGWTIYPPLSTWLGHPNHSVDLVIFSLHLAGISSITGS 162
Cdd:TIGR02882 119 VVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTG 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 163 INFITTCFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTDRNFGTTFFETSGGGDPILFQHMFWFFGHP 242
Cdd:TIGR02882 199 INFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHP 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 243 EVYILVLPAFGVVSEALMFMSGKfKVFGPLGMIYAMTSIGILGCFVWGHHMYTVGMDIDTRAYFTAATMIIGIPTGVKIF 322
Cdd:TIGR02882 279 EVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIF 357

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1734264395 323 SWLATLYGTHIKMTPAMLWVLGFLLLFTMGGLTGVSLSNASLDLLLHDTYYVVGHF 378
Cdd:TIGR02882 358 NWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHF 413
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 55-378 2.36e-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: 43.04  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395  55 YNVIVTAHALAMIFfmVMPML-LSGFGNWLIPIMAGAADMSfPRLNNLGFWLLPPALMLLSSSMLINMgAGTGWTIYPPL 133
Cdd:cd01660    44 YYQGLTLHGVLLAI--VFTTFfIMGFFYAIVARALLRSLFN-RRLAWAGFWLMVIGTVMAAVPILLGQ-ASVLYTFYPPL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 134 StwlGHPNHSVDLVIFSLHlagiSSITGSINFITtcFLSRPIIYTLERLSMFVWSVLITSFMLIISLPVLAGGITMLLTD 213
Cdd:cd01660   120 Q---AHPLFYIGAALVVVG----SWISGFAMFVT--LWRWKKANPGKKVPLATFMVVTTMILWLVASLGVALEVLFQLLP 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 214 RNFGTTffetsGGGDPILFQHMFWFFGHPEVYILVLPAFGVVSEALMFMSGKfKVFGPLGMIYAMTSIGILGCFVWGHHM 293
Cdd:cd01660   191 WSLGLV-----DTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGG-KLFSDPLARLAFILFLLFSTPVGFHHQ 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734264395 294 YT-VGMDIDTRAYFTAATMIIGIPTGVKIFSWLAT------------LYGTHIKM---TPAMLWVLGFLLLFTMGGLTGV 357
Cdd:cd01660   265 FAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASleiagrlrggkgLFGWIRALpwgDPMFLALFLAMLMFIPGGAGGI 344

                         330       340
                  ....*....|....*....|.
gi 1734264395 358 SLSNASLDLLLHDTYYVVGHF 378
Cdd:cd01660   345 INASYQLNYVVHNTAWVPGHF 365
 
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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