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Conserved domains on  [gi|1783492450|ref|YP_009716207|]
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cytochrome c oxidase subunit I (mitochondrion) [Beroe cucumis]

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 ...
 11-472 6.10e-179

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: 511.26  E-value: 6.10e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  11 HYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLLIPLCFHVAD 90
Cdd:cd01663     3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  91 MCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSINFVSTIFFL 170
Cdd:cd01663    83 MAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 171 PlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHPEVYVLILPA 250
Cdd:cd01663   163 R-APGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 251 FAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWIFTFISE 330
Cdd:cd01663   242 FGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 331 TYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFNLSGSFFYQ 410
Cdd:cd01663   322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1783492450 411 SLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVFSFSSLYSIILIAVSMFLLIFTL 472
Cdd:cd01663   402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIV 463
 
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 ...
 11-472 6.10e-179

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: 511.26  E-value: 6.10e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  11 HYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLLIPLCFHVAD 90
Cdd:cd01663     3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  91 MCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSINFVSTIFFL 170
Cdd:cd01663    83 MAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 171 PlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHPEVYVLILPA 250
Cdd:cd01663   163 R-APGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 251 FAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWIFTFISE 330
Cdd:cd01663   242 FGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 331 TYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFNLSGSFFYQ 410
Cdd:cd01663   322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1783492450 411 SLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVFSFSSLYSIILIAVSMFLLIFTL 472
Cdd:cd01663   402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIV 463
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 5-470 1.18e-169

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 488.61  E-value: 1.18e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   5 WLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLLIPL 84
Cdd:MTH00153    4 WLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  85 CFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSINFV 164
Cdd:MTH00153   84 MLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 165 STIFFLPlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHPEVY 244
Cdd:MTH00153  164 TTIINMR-SKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 245 VLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWI 324
Cdd:MTH00153  243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 325 FTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFNLS 404
Cdd:MTH00153  323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1783492450 405 GSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVFSF-SSLYSII-LIAVSMFLLIF 470
Cdd:MTH00153  403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNViSSIGSTIsLISILFFIFII 470
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-472 3.62e-125

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 376.00  E-value: 3.62e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   2 LTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFsIGGLSNLL 81
Cdd:COG0843     6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  82 IPLCFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSI 161
Cdd:COG0843    85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 162 NFVSTIFFLPLSYKfSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHP 241
Cdd:COG0843   165 NFIVTILKMRAPGM-TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 242 EVYVLILPAFAIISHVISYIInRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIF 321
Cdd:COG0843   244 EVYILILPAFGIVSEIIPTFS-RKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 322 SWIFTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSF 401
Cdd:COG0843   323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1783492450 402 NLSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIY--DLNFYVFSFSSLYSIILIAVSMFLLIFTL 472
Cdd:COG0843   403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFLINL 475
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 6-472 1.02e-123

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: 370.79  E-value: 1.02e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   6 LGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFsIGGLSNLLIPLC 85
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPI-LAGFGNYLLPLM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  86 FHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSINFVS 165
Cdd:TIGR02891  80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 166 TIFFLPLSyKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHPEVYV 245
Cdd:TIGR02891 160 TILNMRAP-GMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 246 LILPAFAIISHVISyIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWIF 325
Cdd:TIGR02891 239 IFLPAFGIISEILP-TFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 326 TFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFNLSG 405
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1783492450 406 SFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIY--DLNFYVFSFSSLYSIILIAVSMFLLIFTL 472
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYppQMGFATLNLISTIGAFILAAGFLVFLWNL 466
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 13-441 2.45e-85

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: 269.83  E-value: 2.45e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  13 DISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFsIGGLSNLLIPLCFHVADMC 92
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  93 LPRINNLSFWMLFFSFIFsILSSMMsfGAASGWTLYPPYssfpaapsISTDFIIFSLHLAGASSILSSINFVSTIffLPL 172
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVL-LLASFG--GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTI--LKR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 173 SYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFstsffsNFLGGDALLYQHLFWFFGHPEVYVLILPAFA 252
Cdd:pfam00115 147 RAPGMTLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSL------GAGGGDPLLDQHLFWWFGHPEVYILILPAFG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 253 IISHVISYIINRStPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWIFTFI--SE 330
Cdd:pfam00115 221 IIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWggWI 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 331 TYIYNPLFnWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFNLSGSFFYQ 410
Cdd:pfam00115 300 RFRTTPML-FFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLG 378

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1783492450 411 SLIFFSFFIGSNLLFFPFHFLGLWGLPRHYF 441
Cdd:pfam00115 379 KLHFWLLFIGFNLTFFPMHILGLLGMPRRYA 409
 
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 ...
 11-472 6.10e-179

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: 511.26  E-value: 6.10e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  11 HYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLLIPLCFHVAD 90
Cdd:cd01663     3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  91 MCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSINFVSTIFFL 170
Cdd:cd01663    83 MAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNM 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 171 PlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHPEVYVLILPA 250
Cdd:cd01663   163 R-APGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 251 FAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWIFTFISE 330
Cdd:cd01663   242 FGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 331 TYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFNLSGSFFYQ 410
Cdd:cd01663   322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1783492450 411 SLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVFSFSSLYSIILIAVSMFLLIFTL 472
Cdd:cd01663   402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIV 463
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 5-470 1.18e-169

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 488.61  E-value: 1.18e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   5 WLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLLIPL 84
Cdd:MTH00153    4 WLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  85 CFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSINFV 164
Cdd:MTH00153   84 MLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 165 STIFFLPlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHPEVY 244
Cdd:MTH00153  164 TTIINMR-SKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 245 VLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWI 324
Cdd:MTH00153  243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 325 FTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFNLS 404
Cdd:MTH00153  323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1783492450 405 GSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVFSF-SSLYSII-LIAVSMFLLIF 470
Cdd:MTH00153  403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNViSSIGSTIsLISILFFIFII 470
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-489 8.95e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 466.08  E-value: 8.95e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   1 MLTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNL 80
Cdd:MTH00167    2 WINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  81 LIPLCFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSS 160
Cdd:MTH00167   82 LVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 161 INFVSTIFFLPlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGH 240
Cdd:MTH00167  162 INFITTIINMK-PPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 241 PEVYVLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKI 320
Cdd:MTH00167  241 PEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 321 FSWIFTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKS 400
Cdd:MTH00167  321 FSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 401 FNLSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVFS-FSSLYSII-LIAVSMFLLIFTLRFSSEE 478
Cdd:MTH00167  401 TGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNvVSSIGSLIsLVAVILFLFIIWEAFSSKR 480

                         490
                  ....*....|.
gi 1783492450 479 YYNSYNCDLFN 489
Cdd:MTH00167  481 KLLPVELTSTN 491
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 5-469 5.48e-159

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 461.37  E-value: 5.48e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   5 WLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLLIPL 84
Cdd:MTH00223    3 WLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  85 CFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSINFV 164
Cdd:MTH00223   83 MLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 165 STIFFLPlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHPEVY 244
Cdd:MTH00223  163 TTIINMR-SPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 245 VLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWI 324
Cdd:MTH00223  242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 325 FTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNksfNLS 404
Cdd:MTH00223  322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFP---LFT 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1783492450 405 GSFFYQSLI---FFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFY----VFSFSSLYSiiLIAVSMFLLI 469
Cdd:MTH00223  399 GVTLHRRWAkahFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTkwnqVSSFGSMIS--FVSVLFFMFI 468
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-476 5.84e-153

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 446.46  E-value: 5.84e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   1 MLTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNL 80
Cdd:MTH00116    2 FITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  81 LIPLCFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSS 160
Cdd:MTH00116   82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 161 INFVSTIFFLPlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGH 240
Cdd:MTH00116  162 INFITTCINMK-PPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 241 PEVYVLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKI 320
Cdd:MTH00116  241 PEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 321 FSWIFTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKs 400
Cdd:MTH00116  321 FSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL- 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 401 fnLSGSFFYQSLI---FFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVF-SFSSLYSII-LIAVSMFLLIFTLRFS 475
Cdd:MTH00116  400 --FTGYTLHQTWTkaqFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWnTISSIGSLIsMTAVIMLMFIIWEAFS 477


                  .
gi 1783492450 476 S 476
Cdd:MTH00116  478 S 478
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-504 1.23e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 437.57  E-value: 1.23e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   2 LTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLL 81
Cdd:MTH00079    4 LSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  82 IPLCFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFpAAPSISTDFIIFSLHLAGASSILSSI 161
Cdd:MTH00079   84 LPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTL-GHPGSSVDLAIFSLHCAGISSILGGI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 162 NFVSTIFFLPlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHP 241
Cdd:MTH00079  163 NFMVTTKNLR-SSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 242 EVYVLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIF 321
Cdd:MTH00079  242 EVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVF 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 322 SWIFTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSF 401
Cdd:MTH00079  322 SWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMT 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 402 NLSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVFSFSSLYSIILIAVSMFLLIFTLRfsseEYYN 481
Cdd:MTH00079  402 GIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLL----ESFF 477

                         490       500
                  ....*....|....*....|...
gi 1783492450 482 SYNCDLFNKYFNFSQLGHISSSI 504
Cdd:MTH00079  478 SYRLVLHDNYINSSPEYSLSSYV 500
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-469 6.33e-144

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 422.98  E-value: 6.33e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   2 LTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLL 81
Cdd:MTH00142    1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  82 IPLCFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSI 161
Cdd:MTH00142   81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 162 NFVSTIFFLPlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHP 241
Cdd:MTH00142  161 NFITTVINMR-AGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 242 EVYVLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIF 321
Cdd:MTH00142  240 EVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVF 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 322 SWIFTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSF 401
Cdd:MTH00142  320 SWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFT 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 402 NLSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVFS-FSSLYSII-LIAVSMFLLI 469
Cdd:MTH00142  400 GLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNvVSSLGSMIsFIAVLMFVFI 469
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-477 2.87e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 408.93  E-value: 2.87e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   1 MLTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNL 80
Cdd:MTH00183    2 AITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  81 LIPLCFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSS 160
Cdd:MTH00183   82 LIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 161 INFVSTIFFLPLSyKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGH 240
Cdd:MTH00183  162 INFITTIINMKPP-AISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 241 PEVYVLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKI 320
Cdd:MTH00183  241 PEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 321 FSWIFTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKS 400
Cdd:MTH00183  321 FSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLF 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1783492450 401 FNLSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVF-SFSSLYSII-LIAVSMFLLIFTLRFSSE 477
Cdd:MTH00183  401 SGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWnTVSSIGSLIsLVAVIMFLFILWEAFAAK 479
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-477 3.18e-137

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 406.19  E-value: 3.18e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   1 MLTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNL 80
Cdd:MTH00103    2 FINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  81 LIPLCFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSS 160
Cdd:MTH00103   82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 161 INFVSTIFFLPLSyKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGH 240
Cdd:MTH00103  162 INFITTIINMKPP-AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 241 PEVYVLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKI 320
Cdd:MTH00103  241 PEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 321 FSWIFTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKS 400
Cdd:MTH00103  321 FSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1783492450 401 FNLSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVF-SFSSLYSII-LIAVSMFLLIFTLRFSSE 477
Cdd:MTH00103  401 SGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWnTVSSMGSFIsLTAVMLMIFMIWEAFASK 479
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-482 1.97e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 403.94  E-value: 1.97e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   1 MLTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNL 80
Cdd:MTH00077    2 MITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  81 LIPLCFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSS 160
Cdd:MTH00077   82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 161 INFVSTIFFLPLSyKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGH 240
Cdd:MTH00077  162 INFITTSINMKPP-SMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 241 PEVYVLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKI 320
Cdd:MTH00077  241 PEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 321 FSWIFTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKS 400
Cdd:MTH00077  321 FSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 401 FNLSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVF-SFSSLYSII-LIAVSMFLLIFTLRFSSEE 478
Cdd:MTH00077  401 SGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWnTVSSIGSLIsLVAVIMMMFIIWEAFSSKR 480


                  ....
gi 1783492450 479 YYNS 482
Cdd:MTH00077  481 EVLT 484
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-477 2.24e-134

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 398.82  E-value: 2.24e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   2 LTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLL 81
Cdd:MTH00037    3 LSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  82 IPLCFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSI 161
Cdd:MTH00037   83 IPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 162 NFVSTIFFLPlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHP 241
Cdd:MTH00037  163 NFITTIINMR-TPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHP 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 242 EVYVLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIF 321
Cdd:MTH00037  242 EVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 322 SWIFTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSF 401
Cdd:MTH00037  322 SWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFS 401

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1783492450 402 NLSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVF-SFSSLYSII-LIAVSMFLLIFTLRFSSE 477
Cdd:MTH00037  402 GVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWnTVSSIGSTIsLVATLFFLFLIWEAFASQ 479
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 5-472 2.11e-132

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 393.50  E-value: 2.11e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   5 WLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLLIPL 84
Cdd:MTH00007    3 WLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  85 CFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSINFV 164
Cdd:MTH00007   83 MLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 165 STIFFLPLSyKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHPEVY 244
Cdd:MTH00007  163 TTVINMRWK-GLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 245 VLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWI 324
Cdd:MTH00007  242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 325 FTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFNLS 404
Cdd:MTH00007  322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1783492450 405 GSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVFSFSSLYSIILIAVSMFLLIFTL 472
Cdd:MTH00007  402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFIL 469
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-468 4.12e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 388.03  E-value: 4.12e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   2 LTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLL 81
Cdd:MTH00184    5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  82 IPLCFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSI 161
Cdd:MTH00184   85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAM 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 162 NFVSTIFFLPLSyKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHP 241
Cdd:MTH00184  165 NFITTIFNMRAP-GITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 242 EVYVLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIF 321
Cdd:MTH00184  244 EVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIF 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 322 SWIFTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSF 401
Cdd:MTH00184  324 SWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKIT 403

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1783492450 402 NLSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFY----VFSFSSLYSIILIAVSMFLL 468
Cdd:MTH00184  404 GYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAgwnqISSLGSVISIVGVVWFIYIV 474
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 11-472 1.34e-129

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: 384.58  E-value: 1.34e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  11 HYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLLIPLCfHVAD 90
Cdd:cd00919     1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLI-GARD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  91 MCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSINFVSTIFFL 170
Cdd:cd00919    80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 171 pLSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHPEVYVLILPA 250
Cdd:cd00919   160 -RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 251 FAIISHVISYIINRStPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWIFTFISE 330
Cdd:cd00919   239 FGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 331 TYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFNLSGSFFYQ 410
Cdd:cd00919   318 RIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1783492450 411 SLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVFSFSSLYSIILIAVSMFLLIFTL 472
Cdd:cd00919   398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNL 459
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-484 1.16e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 384.56  E-value: 1.16e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   2 LTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLL 81
Cdd:MTH00182    5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  82 IPLCFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSI 161
Cdd:MTH00182   85 VPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 162 NFVSTIFFLPLSyKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHP 241
Cdd:MTH00182  165 NFITTIFNMRAP-GVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 242 EVYVLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIF 321
Cdd:MTH00182  244 EVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 322 SWIFTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSF 401
Cdd:MTH00182  324 SWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKIT 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 402 NLSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVFSF-SSLYSII-LIAVSMFLLIFTLRFSSEEY 479
Cdd:MTH00182  404 GYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLvSSLGSIIsIVGVVWFIYIIYDAYVREEK 483


                  ....*
gi 1783492450 480 YNSYN 484
Cdd:MTH00182  484 FIGWK 488
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-472 4.16e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 382.49  E-value: 4.16e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   1 MLTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNL 80
Cdd:MTH00048    3 SLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  81 LIPLCFHVADMCLPRINNLSFWMLFFSFIFSILSsmMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSS 160
Cdd:MTH00048   83 LLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 161 INFVSTIFFLplSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGH 240
Cdd:MTH00048  161 INFICTIYSA--FMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 241 PEVYVLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKI 320
Cdd:MTH00048  239 PEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 321 FSWIFTFI-SETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNK 399
Cdd:MTH00048  319 FSWLYMLLnSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPL 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1783492450 400 SFNLSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVFSFSSLYSIILIAVSMFLLIFTL 472
Cdd:MTH00048  399 ITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFIL 471
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-472 3.62e-125

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 376.00  E-value: 3.62e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   2 LTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFsIGGLSNLL 81
Cdd:COG0843     6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  82 IPLCFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSI 161
Cdd:COG0843    85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 162 NFVSTIFFLPLSYKfSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHP 241
Cdd:COG0843   165 NFIVTILKMRAPGM-TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 242 EVYVLILPAFAIISHVISYIInRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIF 321
Cdd:COG0843   244 EVYILILPAFGIVSEIIPTFS-RKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 322 SWIFTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSF 401
Cdd:COG0843   323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1783492450 402 NLSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIY--DLNFYVFSFSSLYSIILIAVSMFLLIFTL 472
Cdd:COG0843   403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFLINL 475
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 6-472 1.02e-123

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: 370.79  E-value: 1.02e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   6 LGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFsIGGLSNLLIPLC 85
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPI-LAGFGNYLLPLM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  86 FHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSINFVS 165
Cdd:TIGR02891  80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 166 TIFFLPLSyKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHPEVYV 245
Cdd:TIGR02891 160 TILNMRAP-GMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 246 LILPAFAIISHVISyIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWIF 325
Cdd:TIGR02891 239 IFLPAFGIISEILP-TFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 326 TFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFNLSG 405
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1783492450 406 SFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIY--DLNFYVFSFSSLYSIILIAVSMFLLIFTL 472
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYppQMGFATLNLISTIGAFILAAGFLVFLWNL 466
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 5-481 1.64e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 351.24  E-value: 1.64e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   5 WLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGGLSNLLIPL 84
Cdd:MTH00026    7 WFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  85 CFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSINFV 164
Cdd:MTH00026   87 MIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFI 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 165 STIFFLPlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHPEVY 244
Cdd:MTH00026  167 TTVMNMR-TPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 245 VLILPAFAIISHVISYIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWI 324
Cdd:MTH00026  246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 325 FTF--ISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFN 402
Cdd:MTH00026  326 ATVsgSGRNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 403 LSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLNFYVFS-FSSLYSII-LIAVSMFLLIFTLRFSSEEYY 480
Cdd:MTH00026  406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNqISSFGSIIsIIAVIWFIVVIFDAYYREEPF 485


                  .
gi 1783492450 481 N 481
Cdd:MTH00026  486 D 486
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 5-472 1.04e-107

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: 329.93  E-value: 1.04e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   5 WLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFsIGGLSNLLIPL 84
Cdd:cd01662     1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPL-VFGLMNYLVPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  85 CFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSINFV 164
Cdd:cd01662    80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 165 STIFFLPlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHPEVY 244
Cdd:cd01662   160 VTILKMR-APGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 245 VLILPAFAIISHVISyIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWI 324
Cdd:cd01662   239 ILILPAFGIFSEIVP-TFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 325 FTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFNLS 404
Cdd:cd01662   318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 405 GSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYDLN--FYVFSFSSLYSIILIAVSMFLLIFTL 472
Cdd:cd01662   398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGpgWDPLNLISTIGAFLIAAGVLLFLINV 467
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 13-441 2.45e-85

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: 269.83  E-value: 2.45e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  13 DISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFsIGGLSNLLIPLCFHVADMC 92
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  93 LPRINNLSFWMLFFSFIFsILSSMMsfGAASGWTLYPPYssfpaapsISTDFIIFSLHLAGASSILSSINFVSTIffLPL 172
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVL-LLASFG--GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTI--LKR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 173 SYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFstsffsNFLGGDALLYQHLFWFFGHPEVYVLILPAFA 252
Cdd:pfam00115 147 RAPGMTLRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSL------GAGGGDPLLDQHLFWWFGHPEVYILILPAFG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 253 IISHVISYIINRStPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWIFTFI--SE 330
Cdd:pfam00115 221 IIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWggWI 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 331 TYIYNPLFnWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFNLSGSFFYQ 410
Cdd:pfam00115 300 RFRTTPML-FFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLG 378

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1783492450 411 SLIFFSFFIGSNLLFFPFHFLGLWGLPRHYF 441
Cdd:pfam00115 379 KLHFWLLFIGFNLTFFPMHILGLLGMPRRYA 409
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-438 4.03e-76

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 252.16  E-value: 4.03e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   1 MLTNWLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHY---VTLHAIYMIFFFVMPFSIGgL 77
Cdd:PRK15017   44 LWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYdqiFTAHGVIMIFFVAMPFVIG-L 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  78 SNLLIPLCFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSI 157
Cdd:PRK15017  123 MNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTT 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 158 LSSINFVSTIFFLPlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWF 237
Cdd:PRK15017  203 LTGINFFVTILKMR-APGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWA 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 238 FGHPEVYVLILPAFAIISHVISyIINRSTPFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTG 317
Cdd:PRK15017  282 WGHPEVYILILPVFGVFSEIAA-TFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTG 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 318 IKIFSWIFTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIF 397
Cdd:PRK15017  361 VKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWW 440

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1783492450 398 NKSFNLSGSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPR 438
Cdd:PRK15017  441 PKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTR 481
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 5-475 2.23e-71

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: 239.37  E-value: 2.23e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450   5 WLGSVYHYDISSLYFFFSISMGFCAFFYSFVIRLSLVWPFAFLSTGSIYLHYVTLHAIYMIFFFVMPFSIGgLSNLLIPL 84
Cdd:TIGR02882  44 WLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  85 CFHVADMCLPRINNLSFWMLFFSFIFSILSSMMSFGAASGWTLYPPYSSFPAAPSISTDFIIFSLHLAGASSILSSINFV 164
Cdd:TIGR02882 123 QIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFF 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 165 STIFFLPlSYKFSFFQYPLFIVAQLVVAFLLIISLPVLAAAITMLLFDRNFSTSFFSNFLGGDALLYQHLFWFFGHPEVY 244
Cdd:TIGR02882 203 VTILKMR-APGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVY 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 245 VLILPAFAIISHVISYIINRSTpFSYPGLSVAIIAIGVLGCVVWAHHMFTSGMDLDTRFYFASATLIIAIPTGIKIFSWI 324
Cdd:TIGR02882 282 IVILPAFGIYSEIISTFAQKRL-FGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWL 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 325 FTFISETYIYNPLFNWTLGFIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKSFNLS 404
Cdd:TIGR02882 361 LTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYK 440

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1783492450 405 GSFFYQSLIFFSFFIGSNLLFFPFHFLGLWGLPRHYFIYD--LNFYVFSFSSLYSIILIAVSMFLLIFTLRFS 475
Cdd:TIGR02882 441 LNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYSpsDGWFPLNLISTIGALLMAIGFIFLVYNIYYS 513
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 44-446 9.57e-10

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: 60.76  E-value: 9.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450  44 FAFLSTGSIYLHYVTLHAIYMIF----FFVMPFSIGGLSNLLIPLCFHvadmclPRINNLSFWMLFFSFIFSILSsMMSF 119
Cdd:cd01660    35 FPLPSSGILYYQGLTLHGVLLAIvfttFFIMGFFYAIVARALLRSLFN------RRLAWAGFWLMVIGTVMAAVP-ILLG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 120 GAASGWTLYPPYSSFPAapsistdfiifsLHLAGASSILSSINFVSTIFFLPLSYKFSFFQYPLFIVAQLVVAFLLIISL 199
Cdd:cd01660   108 QASVLYTFYPPLQAHPL------------FYIGAALVVVGSWISGFAMFVTLWRWKKANPGKKVPLATFMVVTTMILWLV 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 200 PVLAAAITMLLFDRNFStsfFSNFLGGDALLYQHLFWFFGHPEVYVLILPAFAIISHVISYIINRSTpFSYPGLSVAIIA 279
Cdd:cd01660   176 ASLGVALEVLFQLLPWS---LGLVDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKL-FSDPLARLAFIL 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 280 IGVLGCVVWAHHMFTS-GMDLDTRFYFASATLIIAIPTGIKIFSWIFTF---------------ISETYIYNPLFNWTLG 343
Cdd:cd01660   252 FLLFSTPVGFHHQFADpGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeiagrlrggkglfgwIRALPWGDPMFLALFL 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783492450 344 FIFLFTFGGLSGIVLSNCHLNLFFHDSYYVIAHFHYVLSLGAVIGVILSTYYIFNKsfnLSGSFFYQ----SLIFFSFFI 419
Cdd:cd01660   332 AMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPH---LTGRELAAkrlaLAQPWLWFV 408

                         410       420
                  ....*....|....*....|....*..
gi 1783492450 420 GSNLLFFPFHFLGLWGLPRHYFIYDLN 446
Cdd:cd01660   409 GMTIMSTAMHVAGLLGAPRRTAEAQYG 435
 
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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