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Conserved domains on  [gi|223403378|gb|ACM89206|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Mexitlia trivittata]

Protein Classification

cytochrome-c oxidase subunit 1( domain architecture ID 10009591)

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
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


:

Pssm-ID: 177210  Cd Length: 511  Bit Score: 816.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00153 335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFI 414

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00153 415 MFIGVNLTFFPQHFLGLAGM 434
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 816.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00153 335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFI 414

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00153 415 MFIGVNLTFFPQHFLGLAGM 434
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-420 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: 757.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:cd01663    8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:cd01663   88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:cd01663  168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:cd01663  248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:cd01663  328 PMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWL 407

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:cd01663  408 MFIGVNLTFFPQHFLGLAGM 427
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-420 2.59e-170

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: 486.35  E-value: 2.59e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378    1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILiGGFGNWLVPLMLGAPDMAFPR 80
Cdd:TIGR02891  11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:TIGR02891  90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  241 VISySVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:TIGR02891 250 ILP-TFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTT 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:TIGR02891 329 PMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWL 408

                         410       420
                  ....*....|....*....|
gi 223403378  401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:TIGR02891 409 TFVGFNLTFFPMHLLGLLGM 428
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-420 7.13e-169

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 483.86  E-value: 7.13e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   2 LYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPIlIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:COG0843   21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  82 NNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGMT 161
Cdd:COG0843  100 NALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMT 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 162 MEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHV 241
Cdd:COG0843  180 LMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 242 ISYSVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLESP 321
Cdd:COG0843  260 IPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTP 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 322 LLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMIM 401
Cdd:COG0843  339 MLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLW 418

                        410
                 ....*....|....*....
gi 223403378 402 FLGVNLTFFPQHFLGLNGM 420
Cdd:COG0843  419 FIGFNLTFFPMHILGLLGM 437
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-420 1.66e-114

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: 341.86  E-value: 1.66e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378    2 LYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPIlIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   82 NNLSFWLLPPSLFLLIISSMvevGVGAGWTVYPPLASlvghpgssVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGMT 161
Cdd:pfam00115  84 NALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  162 MeKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNtsffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHV 241
Cdd:pfam00115 153 L-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  242 ISYSVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKL-ES 320
Cdd:pfam00115 226 LPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTT 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:pfam00115 305 PMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWL 384

                         410       420
                  ....*....|....*....|
gi 223403378  401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:pfam00115 385 LFIGFNLTFFPMHILGLLGM 404
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 816.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00153 335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFI 414

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00153 415 MFIGVNLTFFPQHFLGLAGM 434
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-420 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: 757.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:cd01663    8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:cd01663   88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:cd01663  168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:cd01663  248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:cd01663  328 PMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWL 407

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:cd01663  408 MFIGVNLTFFPQHFLGLAGM 427
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 709.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00167  17 TLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00167  97 MNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGI 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00167 177 TQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00167 257 IVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWET 336

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00167 337 PMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFV 416

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00167 417 MFIGVNLTFFPQHFLGLAGM 436
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 705.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00223  14 TLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00223  94 LNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGM 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00223 174 QLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00223 254 IVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEA 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00223 334 PMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFL 413

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00223 414 MFLGVNLTFFPQHFLGLAGM 433
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 693.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00116  17 TLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00116  97 MNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAM 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00116 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00116 257 IVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDP 336

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00116 337 PMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGV 416

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00116 417 MFTGVNLTFFPQHFLGLAGM 436
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 677.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00142  15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00142  95 MNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGM 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00142 175 KFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00142 255 IINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEP 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00142 335 PMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYT 414

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00142 415 MFIGVNLTFFPQHFLGLAGM 434
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 629.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00037  17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00037  97 MNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGM 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00037 177 TFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISH 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00037 257 VIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWET 336

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00037 337 PLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFL 416

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00037 417 MFIGVNLTFFPQHFLGLAGM 436
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-420 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 623.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00007  14 TLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00007  94 LNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00007 174 RLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISH 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00007 254 IVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYET 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00007 334 PMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFL 413

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00007 414 MFLGVNLTFFPQHFLGLSGM 433
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-420 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 619.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00103  17 TLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00103  97 MNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAM 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00103 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00103 257 IVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSP 336

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00103 337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTI 416

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00103 417 MFVGVNMTFFPQHFLGLSGM 436
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 613.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00183  17 TLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00183  97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAI 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00183 177 SQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00183 257 IVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWET 336

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00183 337 PLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGV 416

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00183 417 MFVGVNLTFFPQHFLGLAGM 436
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 611.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00077  17 TLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00077  97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSM 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00077 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00077 257 IVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDA 336

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00077 337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGV 416

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00077 417 MFIGVNLTFFPQHFLGLAGM 436
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 593.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00182  19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00182  99 LNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGV 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00182 179 TFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQ 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00182 259 IIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDT 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00182 339 PMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWL 418

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00182 419 MFIGVNLTFFPQHFLGLAGF 438
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 584.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00079  18 TLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLvGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00079  98 LNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTL-GHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSI 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00079 177 SLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQ 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00079 257 STLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQP 336

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00079 337 LLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFL 416

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00079 417 MFVGVNLTFFPLHFAGLHGM 436
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 581.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00184  19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00184  99 LNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGI 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00184 179 TMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:MTH00184 259 IIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDT 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00184 339 PMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWL 418

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00184 419 MFIGVNLTFFPQHFLGLAGL 438
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-420 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 526.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00026  18 SLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:MTH00026  98 LNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGM 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00026 178 TMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKL-- 318
Cdd:MTH00026 258 ILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNLif 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 319 ESPLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQF 398
Cdd:MTH00026 338 TTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHF 417

                        410       420
                 ....*....|....*....|..
gi 223403378 399 MIMFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00026 418 WLMFIGVNITFFPQHFLGLAGL 439
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-420 5.21e-177

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: 502.06  E-value: 5.21e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPlMLGAPDMAFPR 80
Cdd:cd00919    6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:cd00919   85 LNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGM 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:cd00919  165 TLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISE 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 241 VISYSVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:cd00919  245 IIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDP 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:cd00919  324 PMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWL 403

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:cd00919  404 WFIGFNLTFFPMHFLGLLGM 423
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-420 2.59e-170

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: 486.35  E-value: 2.59e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378    1 TLYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILiGGFGNWLVPLMLGAPDMAFPR 80
Cdd:TIGR02891  11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   81 MNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGM 160
Cdd:TIGR02891  90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  161 TMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  241 VISySVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLES 320
Cdd:TIGR02891 250 ILP-TFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTT 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:TIGR02891 329 PMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWL 408

                         410       420
                  ....*....|....*....|
gi 223403378  401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:TIGR02891 409 TFVGFNLTFFPMHLLGLLGM 428
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-420 7.13e-169

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 483.86  E-value: 7.13e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   2 LYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPIlIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:COG0843   21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  82 NNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGMT 161
Cdd:COG0843  100 NALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMT 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 162 MEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHV 241
Cdd:COG0843  180 LMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 242 ISYSVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLESP 321
Cdd:COG0843  260 IPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTP 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 322 LLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMIM 401
Cdd:COG0843  339 MLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLW 418

                        410
                 ....*....|....*....
gi 223403378 402 FLGVNLTFFPQHFLGLNGM 420
Cdd:COG0843  419 FIGFNLTFFPMHILGLLGM 437
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-420 5.25e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 432.56  E-value: 5.25e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   2 LYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00048  19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  82 NNLSFWLLPPSLFLLIISsmVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGMT 161
Cdd:MTH00048  99 NALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 162 mEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHV 241
Cdd:MTH00048 177 -SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHI 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 242 ISYSVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLESP 321
Cdd:MTH00048 256 CLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDP 335

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 322 LL-WSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:MTH00048 336 VVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCII 415

                        410       420
                 ....*....|....*....|
gi 223403378 401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:MTH00048 416 SMIGFNLCFFPMHYFGLCGL 435
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-420 1.14e-145

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: 423.92  E-value: 1.14e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   2 LYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGgFGNWLVPLMLGAPDMAFPRM 81
Cdd:cd01662   13 MYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  82 NNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGMT 161
Cdd:cd01662   92 NALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMT 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 162 MEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHV 241
Cdd:cd01662  172 LMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEI 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 242 ISYSVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLESP 321
Cdd:cd01662  252 VPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETP 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 322 LLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMIM 401
Cdd:cd01662  331 MLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLW 410

                        410
                 ....*....|....*....
gi 223403378 402 FLGVNLTFFPQHFLGLNGM 420
Cdd:cd01662  411 FIGFNLTFFPMHILGLMGM 429
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-420 1.66e-114

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: 341.86  E-value: 1.66e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378    2 LYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPIlIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   82 NNLSFWLLPPSLFLLIISSMvevGVGAGWTVYPPLASlvghpgssVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGMT 161
Cdd:pfam00115  84 NALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  162 MeKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNtsffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHV 241
Cdd:pfam00115 153 L-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  242 ISYSVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKL-ES 320
Cdd:pfam00115 226 LPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTT 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  321 PLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMI 400
Cdd:pfam00115 305 PMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWL 384

                         410       420
                  ....*....|....*....|
gi 223403378  401 MFLGVNLTFFPQHFLGLNGM 420
Cdd:pfam00115 385 LFIGFNLTFFPMHILGLLGM 404
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 36-420 6.89e-109

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: 334.33  E-value: 6.89e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   36 HLYNVMVTAHAFVMIFFMVMPILIGGFgNWLVPLMLGAPDMAFPRMNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPP 115
Cdd:TIGR02843  96 HHYDQIFTAHGVIMIFFVAMPFVFGLM-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  116 LASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGMTMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLT 195
Cdd:TIGR02843 175 LSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTL 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  196 DRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHVISYSVGKREpFGSLGMIYAMVGIGGMGFVVWAHH 275
Cdd:TIGR02843 255 DRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRL-FGYTSMVWATIAITVLSFIVWLHH 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  276 MFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLESPLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTY 355
Cdd:TIGR02843 334 FFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSL 413

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223403378  356 YVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMIMFLGVNLTFFPQHFLGLNGM 420
Cdd:TIGR02843 414 FLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGM 478
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-420 1.52e-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: 320.26  E-value: 1.52e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378    2 LYLVFGAWSALLGTAMSVLIRIELGQSGSLLGDDHLYNVMVTAHAFVMIFFMVMPILIGgFGNWLVPLMLGAPDMAFPRM 81
Cdd:TIGR02882  56 MYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   82 NNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMRSFGMT 161
Cdd:TIGR02882 135 NALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMK 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  162 MEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHV 241
Cdd:TIGR02882 215 LMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEI 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  242 ISySVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYFKLESP 321
Cdd:TIGR02882 295 IS-TFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTP 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  322 LLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKLQFMIM 401
Cdd:TIGR02882 374 MLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFF 453

                         410
                  ....*....|....*....
gi 223403378  402 FLGVNLTFFPQHFLGLNGM 420
Cdd:TIGR02882 454 MIGFNVCFFPMYILGLDGM 472
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-420 3.15e-93

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 294.15  E-value: 3.15e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378   2 LYLVFGAWSALLGTAMSVLIRIE-----LGQSGSLlgDDHLYNVMVTAHAFVMIFFMVMPILIGgFGNWLVPLMLGAPDM 76
Cdd:PRK15017  60 MYIIVAIVMLLRGFADAIMMRSQqalasAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378  77 AFPRMNNLSFWLLPPSLFLLIISSMVEVGVGAGWTVYPPLASLVGHPGSSVDFAIFSLHLAGASSIMGAVNFISTILNMR 156
Cdd:PRK15017 137 AFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMR 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 157 SFGMTMEKVSLFVWSVLITAVLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFG 236
Cdd:PRK15017 217 APGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFG 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 237 IVSHVISySVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMIIAVPTGIKIFSWMATLHGSYF 316
Cdd:PRK15017 297 VFSEIAA-TFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRI 375

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 317 KLESPLLWSIGFVFLFTLGGITGVVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAILAGITYWFPLFFGIILNEKKSKL 396
Cdd:PRK15017 376 VFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKR 455

                        410       420
                 ....*....|....*....|....
gi 223403378 397 QFMIMFLGVNLTFFPQHFLGLNGM 420
Cdd:PRK15017 456 AFWFWIIGFFVAFMPLYALGFMGM 479
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 211-420 6.81e-10

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 60.76  E-value: 6.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 211 DPILFQHLFWFFGHPEVYILILPGFGIVSHVISYSVGKR---EPFGSLGMIYAMVGIGGMGFvvwaHHMFS-VGMDVDTR 286
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKlfsDPLARLAFILFLLFSTPVGF----HHQFAdPGIGPGWK 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223403378 287 AYFTAATMIIAVPTGIKIFSWMATLH------------GSYFKLE--SPLLWSIGFVFL-FTLGGITGVVLSNSSLDIIL 351
Cdd:cd01660  276 FIHMVLTFMVALPSLLTAFTVFASLEiagrlrggkglfGWIRALPwgDPMFLALFLAMLmFIPGGAGGIINASYQLNYVV 355

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223403378 352 HDTYYVVAHFHyvLSMGAVFAILA-GITYWF-PLFFGIILNEKK-SKLQFMIMFLGVNLTFFPQHFLGLNGM 420
Cdd:cd01660  356 HNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGA 425
 
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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