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Conserved domains on  [gi|1109595619|gb|APG55920|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Chondrocladia grandis]

Protein Classification

cytochrome c oxidase subunit 1( domain architecture ID 10108859)

cytochrome c oxidase subunit 1 is the catalytic subunit of cytochrome c oxidase, which is the component of the respiratory chain that catalyzes the reduction of oxygen to water

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-405 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: 743.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:cd01663    88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:cd01663   168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:cd01663   248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:cd01663   328 PMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWL 407


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:cd01663   408 MFIGV 412
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-405 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: 743.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:cd01663    88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:cd01663   168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:cd01663   248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:cd01663   328 PMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWL 407


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:cd01663   408 MFIGV 412
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-405 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 709.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00153   95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00153  175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00153  255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00153  335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFI 414


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00153  415 MFIGV 419
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-405 0e+00

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: 513.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPvMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:TIGR02891  11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:TIGR02891  90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFaAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:TIGR02891 250 ILPTF-ARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTT 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:TIGR02891 329 PMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWL 408


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:TIGR02891 409 TFVGF 413
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-405 3.59e-180

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 511.98  E-value: 3.59e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   2 LYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPvMIGGFGNWFVPLYIGAPDMAFPRL 81
Cdd:COG0843    21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  82 NNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGIT 161
Cdd:COG0843   100 NALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 162 IDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQI 241
Cdd:COG0843   180 LMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 242 IPTFAAKKqIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTP 321
Cdd:COG0843   260 IPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTP 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 322 MLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWLM 401
Cdd:COG0843   339 MLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLW 418


                  ....
gi 1109595619 402 FIGV 405
Cdd:COG0843   419 FIGF 422
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-405 7.28e-121

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: 357.27  E-value: 7.28e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   2 LYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPvMIGGFGNWFVPLYIGAPDMAFPRL 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  82 NNISFWLLPPALTLLLVSAfveQGAGTGWTVYPPLSGitahsggsVDLVIFSLHLAGISSILGAMNFITTIINMRAPGIT 161
Cdd:pfam00115  84 NALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 162 IdRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNtaffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQI 241
Cdd:pfam00115 153 L-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 242 IPTFAaKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRL-DT 320
Cdd:pfam00115 226 LPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTT 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:pfam00115 305 PMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWL 384


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:pfam00115 385 LFIGF 389
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-405 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: 743.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:cd01663    88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:cd01663   168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:cd01663   248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:cd01663   328 PMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWL 407


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:cd01663   408 MFIGV 412
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-405 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 709.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00153   95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00153  175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00153  255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00153  335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFI 414


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00153  415 MFIGV 419
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-405 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 677.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00184   19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00184   99 LNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGI 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00184  179 TMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00184  259 IIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDT 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00184  339 PMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWL 418


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00184  419 MFIGV 423
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-405 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 666.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00182   19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00182   99 LNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00182  179 TFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQ 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00182  259 IIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDT 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00182  339 PMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWL 418


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00182  419 MFIGV 423
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-405 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 664.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00167   17 TLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00167   97 MNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGI 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00167  177 TQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00167  257 IVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWET 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00167  337 PMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFV 416


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00167  417 MFIGV 421
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-405 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 660.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00223   14 TLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00223   94 LNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGM 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00223  174 QLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00223  254 IVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEA 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00223  334 PMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFL 413


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00223  414 MFLGV 418
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-405 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 649.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00116   17 TLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00116   97 MNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAM 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00116  177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00116  257 IVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDP 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00116  337 PMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGV 416


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00116  417 MFTGV 421
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-405 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 630.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00142   15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00142   95 MNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGM 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00142  175 KFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00142  255 IINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEP 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00142  335 PMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYT 414


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00142  415 MFIGV 419
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-405 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 582.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00037   17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00037   97 MNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGM 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00037  177 TFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISH 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00037  257 VIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWET 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00037  337 PLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFL 416


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00037  417 MFIGV 421
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-405 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 582.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00183   17 TLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00183   97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAI 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00183  177 SQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00183  257 IVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWET 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00183  337 PLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGV 416


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00183  417 MFVGV 421
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-405 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 579.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00103   17 TLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00103   97 MNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAM 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00103  177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00103  257 IVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSP 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00103  337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTI 416


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00103  417 MFVGV 421
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-405 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 574.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00077   17 TLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00077   97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSM 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00077  177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00077  257 IVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDA 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00077  337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGV 416


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00077  417 MFIGV 421
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-405 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 567.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00007   14 TLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00007   94 LNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00007  174 RLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISH 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00007  254 IVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYET 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00007  334 PMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFL 413


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00007  414 MFLGV 418
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-405 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 559.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00026   18 SLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00026   98 LNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGM 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00026  178 TMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGA--LRL 318
Cdd:MTH00026  258 ILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGrnLIF 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 319 DTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHF 398
Cdd:MTH00026  338 TTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHF 417


                  ....*..
gi 1109595619 399 WLMFIGV 405
Cdd:MTH00026  418 WLMFIGV 424
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-405 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 548.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:MTH00079   18 TLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSgITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:MTH00079   98 LNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSI 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:MTH00079  177 SLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQ 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:MTH00079  257 STLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQP 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00079  337 LLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFL 416


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:MTH00079  417 MFVGV 421
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-405 0e+00

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: 513.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPvMIGGFGNWFVPLYIGAPDMAFPR 80
Cdd:TIGR02891  11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:TIGR02891  90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFaAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:TIGR02891 250 ILPTF-ARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTT 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:TIGR02891 329 PMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWL 408


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:TIGR02891 409 TFVGF 413
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-405 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.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 511.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   1 TLYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLyIGAPDMAFPR 80
Cdd:cd00919     6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPL-IGARDLAFPR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  81 LNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGI 160
Cdd:cd00919    85 LNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGM 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 161 TIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 240
Cdd:cd00919   165 TLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 241 IIPTFAAKKqIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDT 320
Cdd:cd00919   245 IIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDP 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:cd00919   324 PMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWL 403


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:cd00919   404 WFIGF 408
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-405 3.59e-180

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 511.98  E-value: 3.59e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   2 LYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPvMIGGFGNWFVPLYIGAPDMAFPRL 81
Cdd:COG0843    21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  82 NNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGIT 161
Cdd:COG0843   100 NALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 162 IDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQI 241
Cdd:COG0843   180 LMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 242 IPTFAAKKqIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTP 321
Cdd:COG0843   260 IPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTP 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 322 MLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWLM 401
Cdd:COG0843   339 MLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLW 418


                  ....
gi 1109595619 402 FIGV 405
Cdd:COG0843   419 FIGF 422
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-404 1.19e-159

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: 458.58  E-value: 1.19e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   2 LYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGgFGNWFVPLYIGAPDMAFPRL 81
Cdd:cd01662    13 MYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  82 NNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGIT 161
Cdd:cd01662    92 NALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMT 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 162 IDRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQI 241
Cdd:cd01662   172 LMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEI 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 242 IPTFAaKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTP 321
Cdd:cd01662   252 VPTFS-RKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETP 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 322 MLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWLM 401
Cdd:cd01662   331 MLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLW 410


                  ...
gi 1109595619 402 FIG 404
Cdd:cd01662   411 FIG 413
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-404 4.08e-142

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 414.46  E-value: 4.08e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   2 LYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRL 81
Cdd:MTH00048   19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  82 NNISFWLLPPALTLLLVSAFVeqGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGIT 161
Cdd:MTH00048   99 NALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 162 IdRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQI 241
Cdd:MTH00048  177 S-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHI 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 242 IPTFAAKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTP 321
Cdd:MTH00048  256 CLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDP 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 322 ML-WAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:MTH00048  336 VVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCII 415


                  ....
gi 1109595619 401 MFIG 404
Cdd:MTH00048  416 SMIG 419
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-405 7.28e-121

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: 357.27  E-value: 7.28e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   2 LYLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPvMIGGFGNWFVPLYIGAPDMAFPRL 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  82 NNISFWLLPPALTLLLVSAfveQGAGTGWTVYPPLSGitahsggsVDLVIFSLHLAGISSILGAMNFITTIINMRAPGIT 161
Cdd:pfam00115  84 NALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 162 IdRMPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNtaffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQI 241
Cdd:pfam00115 153 L-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 242 IPTFAaKKQIFGYLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRL-DT 320
Cdd:pfam00115 226 LPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTT 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 321 PMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWL 400
Cdd:pfam00115 305 PMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWL 384


                  ....*
gi 1109595619 401 MFIGV 405
Cdd:pfam00115 385 LFIGF 389
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 36-404 5.22e-119

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


Pssm-ID: 131890  Cd Length: 646  Bit Score: 359.76  E-value: 5.22e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  36 HLYNVIVTGHAFVMIFFLVMPVMIGGFgNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPP 115
Cdd:TIGR02843  96 HHYDQIFTAHGVIMIFFVAMPFVFGLM-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 116 LSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGITIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLT 195
Cdd:TIGR02843 175 LSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTL 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 196 DRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGVLGFIVWAHH 275
Cdd:TIGR02843 255 DRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFS-RKRLFGYTSMVWATIAITVLSFIVWLHH 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 276 MFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTY 355
Cdd:TIGR02843 334 FFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSL 413

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1109595619 356 YVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWLMFIG 404
Cdd:TIGR02843 414 FLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIG 462
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 36-404 2.26e-103

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 319.96  E-value: 2.26e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  36 HLYNVIVTGHAFVMIFFLVMPVMIGgFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLVSAFVEQGAGTGWTVYPP 115
Cdd:PRK15017   97 HHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 116 LSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGITIDRMPLFVWSILVTAILLLLSLPVLAGGITMLLT 195
Cdd:PRK15017  176 LSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTL 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 196 DRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFaAKKQIFGYLGMVYAMVSIGVLGFIVWAHH 275
Cdd:PRK15017  256 DRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATF-SRKRLFGYTSLVWATVCITVLSFIVWLHH 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 276 MFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFTMGGLTGIVLANSALDVVLHDTY 355
Cdd:PRK15017  335 FFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSL 414

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1109595619 356 YVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWLMFIG 404
Cdd:PRK15017  415 FLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIG 463
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 14-404 3.90e-103

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: 318.72  E-value: 3.90e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  14 GTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMPVMIGgFGNWFVPLYIGAPDMAFPRLNNISFWLLPPAL 93
Cdd:TIGR02882  68 GGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  94 TLLLVSAFVEQGAGTGWTVYPPLSGITAHSGGSVDLVIFSLHLAGISSILGAMNFITTIINMRAPGITIDRMPLFVWSIL 173
Cdd:TIGR02882 147 MLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTL 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 174 VTAILLLLSLPVLAGGITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFaAKKQIFG 253
Cdd:TIGR02882 227 ITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTF-AQKRLFG 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 254 YLGMVYAMVSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMFGGALRLDTPMLWAIGFVFLFT 333
Cdd:TIGR02882 306 YKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFL 385

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109595619 334 MGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKITGYCYNEAYGKIHFWLMFIG 404
Cdd:TIGR02882 386 IGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIG 456
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 3-386 7.67e-13

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: 69.62  E-value: 7.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619   3 YLLFGCFAGMIGTAFSVLIRLELSGPGSTLGSDHLYNVIVTGHAFVMIFFLVMpVMIGGFGNWFVPLYIGAPDMAfPRLN 82
Cdd:cd01660     9 HFVVAFLALLLGGLFGLLQVLVRTGVFPLPSSGILYYQGLTLHGVLLAIVFTT-FFIMGFFYAIVARALLRSLFN-RRLA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619  83 NISFWLLPPALTLLLVSAFVEQgAGTGWTVYPPLSGITAHSGGSVDLVIFSLhlagissILGAMNFITTIINMRA-PGIT 161
Cdd:cd01660    87 WAGFWLMVIGTVMAAVPILLGQ-ASVLYTFYPPLQAHPLFYIGAALVVVGSW-------ISGFAMFVTLWRWKKAnPGKK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 162 IdrmPLFVWSILVTAILLLLSLPVLAGGITMLLTDRNFNTAffdpaGGGDPILYQHLFWFFGHPEVYILILPGFGIISQI 241
Cdd:cd01660   159 V---PLATFMVVTTMILWLVASLGVALEVLFQLLPWSLGLV-----DTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 242 IPTFAAKKQIFGYLGMVyAMVSIGVLGFIVWAHHMFT-VGMDVDTRAYFTAATMIIAVPTGIKIFSWIATM--------- 311
Cdd:cd01660   231 LPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeiagrlrgg 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109595619 312 ---FG--GALRLDTPMLWAIGFVFL-FTMGGLTGIVLANSALDVVLHDTYYVVAHFHYVLSMGAIFSIFGGFYYWFGKIT 385
Cdd:cd01660   310 kglFGwiRALPWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLT 389


                  .
gi 1109595619 386 G 386
Cdd:cd01660   390 G 390
 
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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