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Conserved domains on  [gi|1381394814|ref|YP_009480320|]
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putative cytochrome oxidase I, partial (mitochondrion) [Plasmodium falciparum]

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 ...
 48-511 0e+00

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


The actual alignment was detected with superfamily member cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 534.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  48 CNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIaqeNVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPIL 127
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLG---NDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 128 CGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLStSLMSLSPVAVDVIIFGLLVSGVASIMSSLNFI 207
Cdd:cd01663    78 IGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLS-SILAHSGPSVDLAIFSLHLAGISSILGAINFI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 208 TTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYI 287
Cdd:cd01663   157 TTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 288 LILPAFGVISHVISTNYCRN-LFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWIC 366
Cdd:cd01663   237 LILPGFGIISHIISTFSGKKpVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 367 TYMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKN 446
Cdd:cd01663   317 TMWGGSIKF-ETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLS 395

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1381394814 447 LRENSIVILWsMLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:cd01663   396 YNETLGKIHF-WLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLF 459
 
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 ...
 48-511 0e+00

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 534.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  48 CNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIaqeNVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPIL 127
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLG---NDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 128 CGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLStSLMSLSPVAVDVIIFGLLVSGVASIMSSLNFI 207
Cdd:cd01663    78 IGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLS-SILAHSGPSVDLAIFSLHLAGISSILGAINFI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 208 TTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYI 287
Cdd:cd01663   157 TTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 288 LILPAFGVISHVISTNYCRN-LFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWIC 366
Cdd:cd01663   237 LILPGFGIISHIISTFSGKKpVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 367 TYMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKN 446
Cdd:cd01663   317 TMWGGSIKF-ETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLS 395

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1381394814 447 LRENSIVILWsMLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:cd01663   396 YNETLGKIHF-WLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLF 459
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 48-511 7.94e-163

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 471.38  E-value: 7.94e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  48 CNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIiaqENVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPIL 127
Cdd:MTH00223    7 TNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALL---GDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 128 CGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLStSLMSLSPVAVDVIIFGLLVSGVASIMSSLNFI 207
Cdd:MTH00223   84 LGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLS-SNLAHAGPSVDLAIFSLHLAGVSSILGAINFI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 208 TTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYI 287
Cdd:MTH00223  163 TTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 288 LILPAFGVISHVIStNYC--RNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWI 365
Cdd:MTH00223  243 LILPGFGMISHIVS-HYSskKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 366 CTYMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGK 445
Cdd:MTH00223  322 ATIYGSKIKY-EAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGV 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 446 NLREnsiviLWS----MLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00223  401 TLHR-----RWAkahfFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFF 465
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 49-511 4.92e-142

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: 418.17  E-value: 4.92e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  49 NHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQEnvnLYNMIFTIHGIIMIFFNIMPgLFGGFGNYFLPILC 128
Cdd:TIGR02891   5 DHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAE---TYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 129 GSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSlSPVAVDVIIFGLLVSGVASIMSSLNFIT 208
Cdd:TIGR02891  81 GARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGS-PGVGVDLWLLGLHLLGISSILGAVNFIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 209 TVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYIL 288
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 289 ILPAFGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWICTY 368
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 369 MSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKNLR 448
Cdd:TIGR02891 320 WGGSIRF-TTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1381394814 449 EN-SIVILWsmLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALN--GWNMICSIGSTMTLFGLLIF 511
Cdd:TIGR02891 399 ERlGRWHFW--LTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGfaTLNLISTIGAFILAAGFLVF 462
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
45-511 8.97e-141

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 416.07  E-value: 8.97e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  45 ITNCNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQEnvnLYNMIFTIHGIIMIFFNIMPgLFGGFGNYFL 124
Cdd:COG0843    10 LTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPE---TYNQLFTMHGTIMIFFFATP-FLAGFGNYLV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 125 PILCGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSlSPVAVDVIIFGLLVSGVASIMSSL 204
Cdd:COG0843    86 PLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEAS-PGVGVDLWLLGLALFGVGSILGGV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 205 NFITTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPE 284
Cdd:COG0843   165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 285 VYILILPAFGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNW 364
Cdd:COG0843   245 VYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 365 ICTYMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFG 444
Cdd:COG0843   325 IATMWRGRIRF-TTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 445 KNLREN-SIVILWsmLFFVGVILTFLPMHFLGFNVMPRRIPDYP--DALNGWNMICSIGSTMTLFGLLIF 511
Cdd:COG0843   404 RMLNERlGKIHFW--LWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLF 471
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 53-503 6.83e-101

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: 310.27  E-value: 6.83e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  53 LGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQEnvnLYNMIFTIHGIIMIFFNIMPGLFGgFGNYFLPILCGSPE 132
Cdd:pfam00115   2 IGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPL---TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 133 LAYPRINSISLLLQPIAFVLVILSTAaefGGGTGWTLYPPLstslmslspVAVDVIIFGLLVSGVASIMSSLNFITTVMH 212
Cdd:pfam00115  78 MAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL---------VGVDLWYIGLLLAGVSSLLGAINFIVTILK 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 213 LRAKGLTLgILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLffdptfAGDPILYQHLFWFFGHPEVYILILPA 292
Cdd:pfam00115 146 RRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 293 FGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWICTYMSSN 372
Cdd:pfam00115 219 FGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGW 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 373 FGMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKNLRENSI 452
Cdd:pfam00115 299 IRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLG 378

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1381394814 453 VI-LWsmLFFVGVILTFLPMHFLGFNVMPRRIP----DYPDALNGWNMICSIGSTM 503
Cdd:pfam00115 379 KLhFW--LLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
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 ...
 48-511 0e+00

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 534.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  48 CNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIaqeNVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPIL 127
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLG---NDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 128 CGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLStSLMSLSPVAVDVIIFGLLVSGVASIMSSLNFI 207
Cdd:cd01663    78 IGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLS-SILAHSGPSVDLAIFSLHLAGISSILGAINFI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 208 TTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYI 287
Cdd:cd01663   157 TTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 288 LILPAFGVISHVISTNYCRN-LFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWIC 366
Cdd:cd01663   237 LILPGFGIISHIISTFSGKKpVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 367 TYMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKN 446
Cdd:cd01663   317 TMWGGSIKF-ETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLS 395

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1381394814 447 LRENSIVILWsMLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:cd01663   396 YNETLGKIHF-WLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLF 459
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 48-511 7.94e-163

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 471.38  E-value: 7.94e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  48 CNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIiaqENVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPIL 127
Cdd:MTH00223    7 TNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALL---GDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 128 CGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLStSLMSLSPVAVDVIIFGLLVSGVASIMSSLNFI 207
Cdd:MTH00223   84 LGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLS-SNLAHAGPSVDLAIFSLHLAGVSSILGAINFI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 208 TTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYI 287
Cdd:MTH00223  163 TTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 288 LILPAFGVISHVIStNYC--RNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWI 365
Cdd:MTH00223  243 LILPGFGMISHIVS-HYSskKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 366 CTYMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGK 445
Cdd:MTH00223  322 ATIYGSKIKY-EAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGV 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 446 NLREnsiviLWS----MLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00223  401 TLHR-----RWAkahfFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFF 465
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 49-511 1.27e-162

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 470.89  E-value: 1.27e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  49 NHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIiaqENVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILC 128
Cdd:MTH00153    9 NHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLI---GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLML 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 129 GSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLStSLMSLSPVAVDVIIFGLLVSGVASIMSSLNFIT 208
Cdd:MTH00153   86 GAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLS-SNIAHSGASVDLAIFSLHLAGISSILGAINFIT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 209 TVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYIL 288
Cdd:MTH00153  165 TIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 289 ILPAFGVISHVISTNYCRN-LFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWICT 367
Cdd:MTH00153  245 ILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 368 YMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKNL 447
Cdd:MTH00153  325 LHGSQINY-SPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTM 403

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1381394814 448 RENSIVI-LWSMlfFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00153  404 NPKWLKIqFFIM--FIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFF 466
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 49-511 2.36e-156

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 454.91  E-value: 2.36e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  49 NHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIiaqENVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILC 128
Cdd:MTH00167   11 NHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 129 GSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSLSPvAVDVIIFGLLVSGVASIMSSLNFIT 208
Cdd:MTH00167   88 GAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGA-SVDLAIFSLHLAGVSSILGSINFIT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 209 TVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYIL 288
Cdd:MTH00167  167 TIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 289 ILPAFGVISHVIsTNYC--RNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWIC 366
Cdd:MTH00167  247 ILPGFGMISHIV-VYYSgkKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 367 TYMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKN 446
Cdd:MTH00167  326 TLHGGKIKW-ETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLT 404

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1381394814 447 LRE-NSIVILWSMlfFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00167  405 LNEtWTKIHFFVM--FIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILF 468
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 43-511 9.07e-148

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 432.95  E-value: 9.07e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  43 SLITNCNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIaqeNVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNY 122
Cdd:MTH00079    6 VWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLG---NGQLYNSVITAHAILMIFFMVMPSMIGGFGNW 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 123 FLPILCGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTslMSLSPVAVDVIIFGLLVSGVASIMS 202
Cdd:MTH00079   83 MLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST--LGHPGSSVDLAIFSLHCAGISSILG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 203 SLNFITTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGH 282
Cdd:MTH00079  161 GINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 283 PEVYILILPAFGVISHVIST-NYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKV 361
Cdd:MTH00079  241 PEVYILILPAFGIISQSTLYlTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 362 FNWICTYMSSNFgMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDN 441
Cdd:MTH00079  321 FSWLATLFGMKM-KFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPF 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1381394814 442 FFGKNLREN-SIVILWsmLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00079  400 MTGIVYDKLmMSAVFF--LMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLF 468
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 50-511 1.58e-146

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: 428.10  E-value: 1.58e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  50 HKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIaqeNVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILcG 129
Cdd:cd00919     1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFL---DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLI-G 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 130 SPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSlSPVAVDVIIFGLLVSGVASIMSSLNFITT 209
Cdd:cd00919    77 ARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYS-SGVGVDLAILGLHLAGVSSILGAINFITT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 210 VMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYILI 289
Cdd:cd00919   156 ILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 290 LPAFGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWICTyM 369
Cdd:cd00919   236 LPAFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLAT-L 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 370 SSNFGMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKNLRE 449
Cdd:cd00919   315 WGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSE 394

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1381394814 450 NSIVILWsMLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:cd00919   395 KLGKIHF-WLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLF 455
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 49-511 4.63e-146

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 428.76  E-value: 4.63e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  49 NHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIiaqENVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILC 128
Cdd:MTH00142    9 NHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLL---GDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLML 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 129 GSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLStSLMSLSPVAVDVIIFGLLVSGVASIMSSLNFIT 208
Cdd:MTH00142   86 GAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLS-SNLAHSGGSVDLAIFSLHLAGVSSILGAINFIT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 209 TVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYIL 288
Cdd:MTH00142  165 TVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 289 ILPAFGVISHVIsTNYC--RNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWIC 366
Cdd:MTH00142  245 ILPGFGMISHII-NHYSgkKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLA 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 367 TYMSSNFgMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKN 446
Cdd:MTH00142  324 TLHGSKV-KYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLT 402

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1381394814 447 LRENSIVI-LWSMlfFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00142  403 LNPRWLKAhFYTM--FIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMF 466
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 39-511 1.43e-145

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 427.59  E-value: 1.43e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  39 LNRYSLITNcnHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIiaqENVNLYNMIFTIHGIIMIFFNIMPGLFGG 118
Cdd:MTH00116    3 ITRWLFSTN--HKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 119 FGNYFLPILCGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSLSPvAVDVIIFGLLVSGVA 198
Cdd:MTH00116   78 FGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGA-SVDLAIFSLHLAGVS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 199 SIMSSLNFITTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFW 278
Cdd:MTH00116  157 SILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFW 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 279 FFGHPEVYILILPAFGVISHVISTNYC-RNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPT 357
Cdd:MTH00116  237 FFGHPEVYILILPGFGIISHIVTYYAGkKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPT 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 358 GTKVFNWICTYMSsnfGMIH--SSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTV 435
Cdd:MTH00116  317 GIKVFSWLATLHG---GTIKwdPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGF 393

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1381394814 436 SAFQDNFFGKNLRENSIVI-LWSMlfFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00116  394 THWFPLFTGYTLHQTWTKAqFGVM--FTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIML 468
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 49-511 4.92e-142

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: 418.17  E-value: 4.92e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  49 NHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQEnvnLYNMIFTIHGIIMIFFNIMPgLFGGFGNYFLPILC 128
Cdd:TIGR02891   5 DHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAE---TYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 129 GSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSlSPVAVDVIIFGLLVSGVASIMSSLNFIT 208
Cdd:TIGR02891  81 GARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGS-PGVGVDLWLLGLHLLGISSILGAVNFIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 209 TVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYIL 288
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 289 ILPAFGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWICTY 368
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 369 MSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKNLR 448
Cdd:TIGR02891 320 WGGSIRF-TTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1381394814 449 EN-SIVILWsmLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALN--GWNMICSIGSTMTLFGLLIF 511
Cdd:TIGR02891 399 ERlGRWHFW--LTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGfaTLNLISTIGAFILAAGFLVF 462
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
45-511 8.97e-141

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 416.07  E-value: 8.97e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  45 ITNCNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQEnvnLYNMIFTIHGIIMIFFNIMPgLFGGFGNYFL 124
Cdd:COG0843    10 LTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPE---TYNQLFTMHGTIMIFFFATP-FLAGFGNYLV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 125 PILCGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSlSPVAVDVIIFGLLVSGVASIMSSL 204
Cdd:COG0843    86 PLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEAS-PGVGVDLWLLGLALFGVGSILGGV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 205 NFITTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPE 284
Cdd:COG0843   165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 285 VYILILPAFGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNW 364
Cdd:COG0843   245 VYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 365 ICTYMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFG 444
Cdd:COG0843   325 IATMWRGRIRF-TTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 445 KNLREN-SIVILWsmLFFVGVILTFLPMHFLGFNVMPRRIPDYP--DALNGWNMICSIGSTMTLFGLLIF 511
Cdd:COG0843   404 RMLNERlGKIHFW--LWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLF 471
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 49-511 1.16e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 412.69  E-value: 1.16e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  49 NHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIiaqENVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILC 128
Cdd:MTH00037   11 NHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLL---QDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 129 GSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLmSLSPVAVDVIIFGLLVSGVASIMSSLNFIT 208
Cdd:MTH00037   88 GAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNI-AHAGGSVDLAIFSLHLAGASSILASINFIT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 209 TVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYIL 288
Cdd:MTH00037  167 TIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYIL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 289 ILPAFGVISHVIsTNYC--RNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWIC 366
Cdd:MTH00037  247 ILPGFGMISHVI-AHYSgkQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMA 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 367 TYMSSNFgMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKN 446
Cdd:MTH00037  326 TLQGSNL-RWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVS 404

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1381394814 447 LRENSIVILWsMLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00037  405 LHPLWSKVHF-FLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFF 468
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 49-511 2.78e-137

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 406.21  E-value: 2.78e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  49 NHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQEnvnLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILC 128
Cdd:MTH00007    8 NHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQ---LYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLML 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 129 GSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSLSPvAVDVIIFGLLVSGVASIMSSLNFIT 208
Cdd:MTH00007   85 GAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGP-SVDLAIFSLHLAGVSSILGAINFIT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 209 TVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYIL 288
Cdd:MTH00007  164 TVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 289 ILPAFGVISHVIsTNYCRNL--FGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWIC 366
Cdd:MTH00007  244 ILPGFGAISHIV-THYAGKLepFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 367 TYMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKN 446
Cdd:MTH00007  323 TIHGSPIKY-ETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1381394814 447 LRENSIVILWsMLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00007  402 LHDRWAKAHF-FLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLF 465
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 49-511 8.98e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 400.07  E-value: 8.98e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  49 NHKTLGLYYLWFSFLFGSYGFLLSVILRTELySSSLRIIAQENVnlYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILC 128
Cdd:MTH00183   11 NHKDIGTLYLVFGAWAGMVGTALSLLIRAEL-SQPGALLGDDQI--YNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 129 GSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSLSPvAVDVIIFGLLVSGVASIMSSLNFIT 208
Cdd:MTH00183   88 GAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGA-SVDLTIFSLHLAGVSSILGAINFIT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 209 TVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYIL 288
Cdd:MTH00183  167 TIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 289 ILPAFGVISHVISTNYCRNL-FGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWICT 367
Cdd:MTH00183  247 ILPGFGMISHIVAYYSGKKEpFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLAT 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 368 YMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKNL 447
Cdd:MTH00183  327 LHGGSIKW-ETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTL 405

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1381394814 448 RENSIVILWSMLfFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00183  406 HSTWTKIHFGVM-FVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMF 468
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 49-510 1.19e-134

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 399.70  E-value: 1.19e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  49 NHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIiaqENVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILC 128
Cdd:MTH00077   11 NHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 129 GSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSLSPvAVDVIIFGLLVSGVASIMSSLNFIT 208
Cdd:MTH00077   88 GAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGA-SVDLTIFSLHLAGVSSILGAINFIT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 209 TVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYIL 288
Cdd:MTH00077  167 TSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYIL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 289 ILPAFGVISHVIS-TNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWICT 367
Cdd:MTH00077  247 ILPGFGMISHIVTyYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLAT 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 368 yMSSNFGMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKNL 447
Cdd:MTH00077  327 -MHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTL 405

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1381394814 448 RENSIVILWSMLfFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLI 510
Cdd:MTH00077  406 HSTWSKIHFGVM-FIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIM 467
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 49-511 2.56e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 393.81  E-value: 2.56e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  49 NHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIiaqENVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILC 128
Cdd:MTH00184   13 NHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSML---GDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 129 GSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLStSLMSLSPVAVDVIIFGLLVSGVASIMSSLNFIT 208
Cdd:MTH00184   90 GAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLS-SIQAHSGGSVDMAIFSLHLAGISSILGAMNFIT 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 209 TVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYIL 288
Cdd:MTH00184  169 TIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 289 ILPAFGVISHVIST-NYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWICT 367
Cdd:MTH00184  249 ILPGFGIISQIIPTfAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIAT 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 368 YMSSNFgMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKNL 447
Cdd:MTH00184  329 IFGGSL-RLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCY 407

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1381394814 448 RENSIVI-LWSMlfFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00184  408 NEVYGKIhFWLM--FIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWF 470
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 37-510 2.76e-132

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 393.48  E-value: 2.76e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  37 IVLNRYSLITNcnHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIiaqENVNLYNMIFTIHGIIMIFFNIMPGLF 116
Cdd:MTH00103    1 MFINRWLFSTN--HKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 117 GGFGNYFLPILCGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLmSLSPVAVDVIIFGLLVSG 196
Cdd:MTH00103   76 GGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNL-AHAGASVDLTIFSLHLAG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 197 VASIMSSLNFITTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHL 276
Cdd:MTH00103  155 VSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 277 FWFFGHPEVYILILPAFGVISHVIsTNYC--RNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILIS 354
Cdd:MTH00103  235 FWFFGHPEVYILILPGFGMISHIV-TYYSgkKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 355 IPTGTKVFNWICTYMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTT 434
Cdd:MTH00103  314 IPTGVKVFSWLATLHGGNIKW-SPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGG 392

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1381394814 435 VSAFQDNFFGKNLRENSIVILWSMLfFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLI 510
Cdd:MTH00103  393 FVHWFPLFSGYTLNDTWAKIHFTIM-FVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVML 467
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 49-511 4.83e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 393.42  E-value: 4.83e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  49 NHKTLGLYYLWFSFLFGSYGFLLSVILRTELySSSLRIIAQENvnLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPILC 128
Cdd:MTH00182   13 NHKDIGTLYLVFGAGAGMIGTAFSMLIRLEL-SAPGAMLGDDH--LYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 129 GSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLStSLMSLSPVAVDVIIFGLLVSGVASIMSSLNFIT 208
Cdd:MTH00182   90 GAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLS-SIQAHSGGAVDMAIFSLHLAGVSSILGAINFIT 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 209 TVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVYIL 288
Cdd:MTH00182  169 TIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYIL 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 289 ILPAFGVISHVISTNYCRN-LFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWICT 367
Cdd:MTH00182  249 ILPGFGMISQIIPTFVAKKqIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLAT 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 368 YMSSNFgMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFT-------TVSAFQD 440
Cdd:MTH00182  329 IYGGTL-RLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGgfyywfgKITGYCY 407

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1381394814 441 N-FFGKnlrensiVILWSMlfFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00182  408 NeLYGK-------IHFWLM--FIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWF 470
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 45-511 3.65e-126

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: 377.31  E-value: 3.65e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  45 ITNCNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQEnvnLYNMIFTIHGIIMIFFNIMPgLFGGFGNYFL 124
Cdd:cd01662     2 LTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPE---HYNQIFTMHGTIMIFLFAMP-LVFGLMNYLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 125 PILCGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSlSPVAVDVIIFGLLVSGVASIMSSL 204
Cdd:cd01662    78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYS-PGVGVDYWILGLQFSGIGTLLGAI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 205 NFITTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPE 284
Cdd:cd01662   157 NFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 285 VYILILPAFGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNW 364
Cdd:cd01662   237 VYILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNW 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 365 ICTYMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFG 444
Cdd:cd01662   317 LFTMWRGRIRF-ETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFG 395

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 445 KNLREN-SIVILWsmLFFVGVILTFLPMHFLGFNVMPRRIPDYP--DALNGWNMICSIGSTMTLFGLLIF 511
Cdd:cd01662   396 RMLNERlGKWSFW--LWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLF 463
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 47-511 4.10e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 375.89  E-value: 4.10e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  47 NCNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIiaqENVNLYNMIFTIHGIIMIFFNIMPGLFGGFGNYFLPI 126
Cdd:MTH00026   10 SCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSML---GDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 127 LCGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLStSLMSLSPVAVDVIIFGLLVSGVASIMSSLNF 206
Cdd:MTH00026   87 MIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLA-SIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 207 ITTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPEVY 286
Cdd:MTH00026  166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 287 ILILPAFGVISHVIST-NYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWI 365
Cdd:MTH00026  246 ILILPGFGIISQILSLfSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 366 CTYMSSNFGMIHSS-SLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFG 444
Cdd:MTH00026  326 ATVSGSGRNLIFTTpMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1381394814 445 KNLRE-NSIVILWsmLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00026  406 YAYKDiYGLIHFW--LMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWF 471
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 38-511 8.67e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 353.60  E-value: 8.67e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  38 VLNRYSLITNCNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQEnvnLYNMIFTIHGIIMIFFNIMPGLFG 117
Cdd:MTH00048    1 MNSLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLD---VYNFLITNHGIIMIFFFLMPVLIG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 118 GFGNYFLPILCGSPELAYPRINSISLLLQPIAFVLVILSTAaeFGGGTGWTLYPPLSTSLMSLSpVAVDVIIFGLLVSGV 197
Cdd:MTH00048   78 GFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSS-WGVDFLMFSLHLAGV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 198 ASIMSSLNFITTVMHLRAKGLTLGIlSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLF 277
Cdd:MTH00048  155 SSLFGSINFICTIYSAFMTNVFSRT-SIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 278 WFFGHPEVYILILPAFGVISHV-ISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIP 356
Cdd:MTH00048  234 WFFGHPEVYVLILPGFGIISHIcLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVP 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 357 TGTKVFNWICTYMSSNFGMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVS 436
Cdd:MTH00048  314 TGIKVFSWLYMLLNSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFI 393

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1381394814 437 AFQDNFFGKNLRENSIVILWsMLFFVGVILTFLPMHFLGFNVMPRRIPDYPDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:MTH00048  394 WWWPLITGLSLNKYLLQCHC-IISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFF 467
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 53-503 6.83e-101

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: 310.27  E-value: 6.83e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  53 LGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQEnvnLYNMIFTIHGIIMIFFNIMPGLFGgFGNYFLPILCGSPE 132
Cdd:pfam00115   2 IGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPL---TYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 133 LAYPRINSISLLLQPIAFVLVILSTAaefGGGTGWTLYPPLstslmslspVAVDVIIFGLLVSGVASIMSSLNFITTVMH 212
Cdd:pfam00115  78 MAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL---------VGVDLWYIGLLLAGVSSLLGAINFIVTILK 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 213 LRAKGLTLgILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLffdptfAGDPILYQHLFWFFGHPEVYILILPA 292
Cdd:pfam00115 146 RRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 293 FGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNWICTYMSSN 372
Cdd:pfam00115 219 FGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGW 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 373 FGMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKNLRENSI 452
Cdd:pfam00115 299 IRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLG 378

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1381394814 453 VI-LWsmLFFVGVILTFLPMHFLGFNVMPRRIP----DYPDALNGWNMICSIGSTM 503
Cdd:pfam00115 379 KLhFW--LLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 45-509 2.99e-82

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 268.73  E-value: 2.99e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  45 ITNCNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIAQENVNLYNMIFTIHGIIMIFFNIMPGLFGgFGNYFL 124
Cdd:PRK15017   49 LTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVV 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 125 PILCGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTslMSLSP-VAVDVIIFGLLVSGVASIMSS 203
Cdd:PRK15017  128 PLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSG--IEYSPgVGVDYWIWSLQLSGIGTTLTG 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 204 LNFITTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHP 283
Cdd:PRK15017  206 INFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHP 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 284 EVYILILPAFGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFN 363
Cdd:PRK15017  286 EVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFN 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 364 WICTYMSSNFGMiHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFF 443
Cdd:PRK15017  366 WLFTMYQGRIVF-HSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAF 444

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1381394814 444 GKNLREN-SIVILWsmLFFVGVILTFLPMHFLGFNVMPRRIPDYPDA-LNGWNMICSIGSTMTLFGLL 509
Cdd:PRK15017  445 GFKLNETwGKRAFW--FWIIGFFVAFMPLYALGFMGMTRRLSQQIDPqFHTMLMIAASGAALIALGIL 510
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 45-511 2.91e-79

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: 260.17  E-value: 2.91e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814  45 ITNCNHKTLGLYYLWFSFLFGSYGFLLSVILRTELYSSSLRIIaqeNVNLYNMIFTIHGIIMIFFNIMPGLFGgFGNYFL 124
Cdd:TIGR02882  45 LTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFL---DAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 125 PILCGSPELAYPRINSISLLLQPIAFVLVILSTAAEFGGGTGWTLYPPLSTSLMSLSPvAVDVIIFGLLVSGVASIMSSL 204
Cdd:TIGR02882 121 PLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGV-GVNYYLIALQISGIGTLMTGI 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 205 NFITTVMHLRAKGLTLGILSVSTWSLIITSGMLLLTLPVLTGGVLMLLSDLHFNTLFFDPTFAGDPILYQHLFWFFGHPE 284
Cdd:TIGR02882 200 NFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPE 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 285 VYILILPAFGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTTGLEVDTRAYFTSTTILISIPTGTKVFNW 364
Cdd:TIGR02882 280 VYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNW 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 365 ICTYMSSNFgMIHSSSLLSLLFICTFTFGGTTGVILGNAAIDVALHDTYYVIAHFHFVLSIGAIIGLFTTVSAFQDNFFG 444
Cdd:TIGR02882 360 LLTLYKGKI-RFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFG 438

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1381394814 445 KNLRENsiVILWSMLFFV-GVILTFLPMHFLGFNVMPRRIPDYPDALnGW---NMICSIGSTMTLFGLLIF 511
Cdd:TIGR02882 439 YKLNER--LGKWCFWFFMiGFNVCFFPMYILGLDGMPRRMYTYSPSD-GWfplNLISTIGALLMAIGFIFL 506
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 269-511 6.17e-11

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: 64.61  E-value: 6.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 269 DPILYQHLFWFFGHPEVYILILPAFGVISHVISTNYCRNLFGNQSMILAMGCIAVLGSLVWVHHMYTT-GLEVDTRAYFT 347
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFADpGIGPGWKFIHM 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 348 STTILISIPTGTKVFNWICTYMSSN--------FGMIHSSSLLSLLF------ICTFTFGGTTGVILGNAAIDVALHDTY 413
Cdd:cd01660   280 VLTFMVALPSLLTAFTVFASLEIAGrlrggkglFGWIRALPWGDPMFlalflaMLMFIPGGAGGIINASYQLNYVVHNTA 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381394814 414 YVIAHFHFVLSIGAIIGLFTTVSAFQDNFFGKNLRENSIVILWSMLFFVGVILTFLPMHFLGFNVMPRRI-------PDY 486
Cdd:cd01660   360 WVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELAAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTaeaqyggLPA 439

                         250       260
                  ....*....|....*....|....*
gi 1381394814 487 PDALNGWNMICSIGSTMTLFGLLIF 511
Cdd:cd01660   440 AGEWAPYQQLMAIGGTILFVSGALF 464
 
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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