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Conserved domains on  [gi|1196820381|gb|ART30120|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Tigriopus japonicus]

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 ...
 1-369 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 MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 703.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00153   28 GTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00153  108 TLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00153  188 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFG 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00153  268 TLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFT 347

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00153  348 IGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPL 397
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-369 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 703.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00153   28 GTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00153  108 TLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00153  188 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFG 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00153  268 TLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFT 347

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00153  348 IGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPL 397
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-369 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: 644.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:cd01663    21 GTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSAVG-HAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:cd01663   101 LLLLLSALVEGGAGTGWTVYPPLSSILaHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:cd01663   181 ITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFG 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:cd01663   261 YLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFT 340

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:cd01663   341 IGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPK 390
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-368 1.98e-147

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: 426.25  E-value: 1.98e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLiGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:TIGR02891  24 GGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:TIGR02891 103 LLLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGIL 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQeTSKKEVFG 239
Cdd:TIGR02891 183 VTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPT-FARKPIFG 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:TIGR02891 262 YRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFV 341

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFP 368
Cdd:TIGR02891 342 IGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFP 390
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-368 2.73e-142

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 414.14  E-value: 2.73e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPvLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:COG0843    33 GGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:COG0843   112 LLLLISLFVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAAL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQeTSKKEVFG 239
Cdd:COG0843   192 VTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPT-FSRKPLFG 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:COG0843   271 YKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFV 350

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFP 368
Cdd:COG0843   351 IGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFP 399
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-368 1.99e-102

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: 308.73  E-value: 1.99e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVlIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:pfam00115  17 GGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAveaGAGTGWTVYPPLSAVghagssvDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLvPLFVWSVLL 160
Cdd:pfam00115  96 VLLLASFG---GATTGWTEYPPLVGV-------DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRM-PLFVWAILA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 161 TAILLLLSLPVLAGAITMLLTDRNLNScfydvsGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQeTSKKEVFGV 240
Cdd:pfam00115 165 TAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPK-FAGRPLFGY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 241 LGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPS-YSASFSWALGFIFLFT 319
Cdd:pfam00115 238 KLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFI 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFP 368
Cdd:pfam00115 318 IGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLP 366
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-369 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 703.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00153   28 GTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00153  108 TLLLSSSMVESGAGTGWTVYPPLSSnIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00153  188 ITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFG 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00153  268 TLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFT 347

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00153  348 IGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPL 397
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-369 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: 644.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:cd01663    21 GTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSAVG-HAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:cd01663   101 LLLLLSALVEGGAGTGWTVYPPLSSILaHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:cd01663   181 ITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFG 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:cd01663   261 YLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFT 340

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:cd01663   341 IGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPK 390
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-369 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 600.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00223   27 GTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00223  107 YLLLSSSAVESGVGTGWTVYPPLSSnLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVK 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00223  187 VTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFG 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00223  267 TLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFT 346

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00223  347 VGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPL 396
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-369 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 597.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00167   30 GTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00167  110 LLLLASSGVEAGAGTGWTVYPPLAGnLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSIL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00167  190 VTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFG 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00167  270 YMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFT 349

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00167  350 VGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-369 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 592.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00116   30 GTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00116  110 LLLLASSTVEAGAGTGWTVYPPLAGnLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00116  190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFG 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00116  270 YMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFT 349

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00116  350 IGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-369 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 582.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00142   28 GTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPAL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00142  108 LLLLSSAAVESGAGTGWTVYPPLSSnLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVK 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00142  188 ITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFG 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00142  268 TLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFT 347

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00142  348 VGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPL 397
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-369 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 534.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00007   27 GTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPAL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00007  107 ILLVSSAAVEKGVGTGWTVYPPLASnLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVV 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00007  187 ITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFG 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00007  267 TLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFT 346

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00007  347 TGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPL 396
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-369 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 528.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00103   30 GTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00103  110 LLLLASSMVEAGAGTGWTVYPPLAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00103  190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFG 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00103  270 YMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFT 349

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00103  350 VGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPL 399
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-369 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 524.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00037   30 GTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00037  110 LLLLASAGVESGAGTGWTIYPPLSSnIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVF 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00037  190 ITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFG 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00037  270 YLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFT 349

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00037  350 IGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPL 399
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-369 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 523.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00183   30 GTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00183  110 LLLLASSGVEAGAGTGWTVYPPLAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00183  190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFG 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00183  270 YMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFT 349

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00183  350 VGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPL 399
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-369 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 520.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00077   30 GTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00077  110 LLLLASSGVEAGAGTGWTVYPPLAGnLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00077  190 ITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFG 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00077  270 YMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFT 349

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00077  350 VGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPL 399
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-369 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 518.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00079   31 GTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSAVGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVLL 160
Cdd:MTH00079  111 FLILDSCFVDMGPGTSWTVYPPLSTLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFV 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 161 TAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFGV 240
Cdd:MTH00079  191 TVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGS 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 241 LGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFTL 320
Cdd:MTH00079  271 LGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTI 350

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1196820381 321 GGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00079  351 GGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPF 399
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-367 2.38e-176

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 500.50  E-value: 2.38e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00182   32 GTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPAL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00182  112 ILLLGSAFVEQGAGTGWTVYPPLSSIqAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSIL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00182  192 ITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFG 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00182  272 YLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFT 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWF 367
Cdd:MTH00182  352 LGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWF 399
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-367 7.49e-176

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 498.97  E-value: 7.49e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00184   32 GTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPAL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00184  112 TLLLGSAFVEQGAGTGWTVYPPLSSIqAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSIL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00184  192 VTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFG 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:MTH00184  272 YLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFT 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWF 367
Cdd:MTH00184  352 MGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWF 399
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-367 2.29e-158

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 455.24  E-value: 2.29e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00026   31 GTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPAL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:MTH00026  111 FLLLGSSLVEQGAGTGWTVYPPLASIqAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVF 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00026  191 ITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFG 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPS--YSASFSWALGFIFL 317
Cdd:MTH00026  271 YLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNliFTTPMAWALGFIFL 350

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 318 FTLGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWF 367
Cdd:MTH00026  351 FTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWF 400
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-369 4.31e-155

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: 444.28  E-value: 4.31e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPlMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:cd00919    19 GGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSAVG-HAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:cd00919    98 LLLLSSVLVGGGAGTGWTFYPPLSTLSySSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQEtSKKEVFG 239
Cdd:cd00919   178 VTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTF-SGKPLFG 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:cd00919   257 YKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFT 336

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:cd00919   337 IGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPK 386
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-368 1.98e-147

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: 426.25  E-value: 1.98e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLiGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:TIGR02891  24 GGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:TIGR02891 103 LLLLASFFTGGAPDTGWTMYPPLSSTsGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGIL 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQeTSKKEVFG 239
Cdd:TIGR02891 183 VTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPT-FARKPIFG 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:TIGR02891 262 YRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFV 341

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFP 368
Cdd:TIGR02891 342 IGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFP 390
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-368 2.73e-142

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 414.14  E-value: 2.73e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPvLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:COG0843    33 GGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSAV-GHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:COG0843   112 LLLLISLFVGGAADVGWTFYPPLSGLeASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAAL 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQeTSKKEVFG 239
Cdd:COG0843   192 VTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPT-FSRKPLFG 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:COG0843   271 YKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFV 350

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFP 368
Cdd:COG0843   351 IGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFP 399
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-369 6.56e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 381.72  E-value: 6.56e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:MTH00048   31 GLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSgaVEAGAGTGWTVYPPLSA-VGHAGSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDlVPLFVWSVL 159
Cdd:MTH00048  111 VFLLLS--MCLGAGVGWTFYPPLSSsLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSR-TSIILWSYL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQETSKKEVFG 239
Cdd:MTH00048  188 FTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFG 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSAS-FSWALGFIFLF 318
Cdd:MTH00048  268 YYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPvVWWVVSFIVLF 347

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1196820381 319 TLGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFPL 369
Cdd:MTH00048  348 TIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPL 398
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-368 1.10e-127

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: 375.77  E-value: 1.10e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQC-GSFLGNDQlYNVLVTAHAFVMIFFMVMPVLIGgFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPS 79
Cdd:cd01662    25 GGVDALLMRTQLALPgNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  80 LLLLLLSGAVEAGAGTGWTVYPPLSAVGHA-GSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSV 158
Cdd:cd01662   103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSpGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 159 LLTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQeTSKKEVF 238
Cdd:cd01662   183 LVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPT-FSRKPLF 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 239 GVLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLF 318
Cdd:cd01662   262 GYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTF 341

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196820381 319 TLGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFP 368
Cdd:cd01662   342 VIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFP 391
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-368 1.99e-102

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: 308.73  E-value: 1.99e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVlIGGFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:pfam00115  17 GGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAveaGAGTGWTVYPPLSAVghagssvDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLvPLFVWSVLL 160
Cdd:pfam00115  96 VLLLASFG---GATTGWTEYPPLVGV-------DLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTLRM-PLFVWAILA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 161 TAILLLLSLPVLAGAITMLLTDRNLNScfydvsGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQeTSKKEVFGV 240
Cdd:pfam00115 165 TAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPK-FAGRPLFGY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 241 LGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPS-YSASFSWALGFIFLFT 319
Cdd:pfam00115 238 KLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFI 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFP 368
Cdd:pfam00115 318 IGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLP 366
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 25-368 1.07e-95

cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]


Pssm-ID: 131890  Cd Length: 646  Bit Score: 298.12  E-value: 1.07e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  25 YNVLVTAHAFVMIFFMVMPVLIGGFgNWLVPLMLGAPDMAFPRLNNLSFWFLIPSLLLLLLSGAVEAGAGTGWTVYPPLS 104
Cdd:TIGR02843  98 YDQIFTAHGVIMIFFVAMPFVFGLM-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLS 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 105 AVGHA-GSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDR 183
Cdd:TIGR02843 177 ELQYSpGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDR 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 184 NLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQeTSKKEVFGVLGMIYAMASIGVLGFVVWAHHMF 263
Cdd:TIGR02843 257 YLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVAT-FSRKRLFGYTSMVWATIAITVLSFIVWLHHFF 335

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 264 TVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFTLGGLTGIVLSNSSLDIVLHDTYYV 343
Cdd:TIGR02843 336 TMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFL 415

                         330       340
                  ....*....|....*....|....*
gi 1196820381 344 VAHFHYVLSMGAVFALLGSLIHWFP 368
Cdd:TIGR02843 416 IAHFHNVIIGGVVFGCFAGLTYWFP 440
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 25-368 1.00e-83

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 267.57  E-value: 1.00e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  25 YNVLVTAHAFVMIFFMVMPVLIGgFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSLLLLLLSGAVEAGAGTGWTVYPPLS 104
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 105 AVGHA-GSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVLLTAILLLLSLPVLAGAITMLLTDR 183
Cdd:PRK15017  178 GIEYSpGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 184 NLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQeTSKKEVFGVLGMIYAMASIGVLGFVVWAHHMF 263
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAAT-FSRKRLFGYTSLVWATVCITVLSFIVWLHHFF 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 264 TVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFTLGGLTGIVLSNSSLDIVLHDTYYV 343
Cdd:PRK15017  337 TMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFL 416

                         330       340
                  ....*....|....*....|....*
gi 1196820381 344 VAHFHYVLSMGAVFALLGSLIHWFP 368
Cdd:PRK15017  417 IAHFHNVIIGGVVFGCFAGMTYWWP 441
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-368 6.15e-83

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: 264.79  E-value: 6.15e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381   1 GAAMSVLIRLELGQCGSFLGNDQLYNVLVTAHAFVMIFFMVMPVLIGgFGNWLVPLMLGAPDMAFPRLNNLSFWFLIPSL 80
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381  81 LLLLLSGAVEAGAGTGWTVYPPLSAVGHA-GSSVDFAIFSLHLAGVSSLLGAVNFISTIFNLRVLGMYLDLVPLFVWSVL 159
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSpGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 160 LTAILLLLSLPVLAGAITMLLTDRNLNSCFYDVSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIISQeTSKKEVFG 239
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIIST-FAQKRLFG 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 240 VLGMIYAMASIGVLGFVVWAHHMFTVGLDTDTRAYFTSATMIIAVPTGIKIFSWVGTLYGSKPSYSASFSWALGFIFLFT 319
Cdd:TIGR02882 306 YKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFL 385

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1196820381 320 LGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFALLGSLIHWFP 368
Cdd:TIGR02882 386 IGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYP 434
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 197-359 1.10e-08

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: 56.53  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 197 DPILYQHLFWFFGHPEVYILILPGFGLISHIISQ--------ETSKKEVFgvlgMIYAMASIGVlGFvvwaHHMFT-VGL 267
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKiaggklfsDPLARLAF----ILFLLFSTPV-GF----HHQFAdPGI 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196820381 268 DTDTRAYFTSATMIIAVPT-------------------GIKIFSWVGTLYGSKPSYSASFswaLGFIFlFTLGGLTGIVL 328
Cdd:cd01660   271 GPGWKFIHMVLTFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALF---LAMLM-FIPGGAGGIIN 346

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1196820381 329 SNSSLDIVLHDTYYVVAHFHyvLSMGAVFAL 359
Cdd:cd01660   347 ASYQLNYVVHNTAWVPGHFH--LTVGGAVAL 375
 
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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