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Conserved domains on  [gi|60476514|gb|AAX21399|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Zeuxevania sp. DERV015]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-377 0e+00

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


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 665.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00153  10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00153  90 MAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINM 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00153 170 RSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00153 250 GMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQ 329

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FDiYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00153 330 IN-YSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVF 385
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-377 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 665.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00153  10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00153  90 MAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINM 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00153 170 RSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00153 250 GMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQ 329

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FDiYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00153 330 IN-YSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVF 385
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-377 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: 640.69  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:cd01663   3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:cd01663  83 MAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNM 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:cd01663 163 RAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:cd01663 243 GIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGS 322

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514 321 FDiYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:cd01663 323 IK-FETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVF 378
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-377 4.88e-146

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: 422.79  E-value: 4.88e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514     1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPfMIGGFGNWLIPLMISSPD 80
Cdd:TIGR02891   6 HKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:TIGR02891  85 MAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNM 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:TIGR02891 165 RAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAF 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   241 GIISHIIFNEMNKPsTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:TIGR02891 245 GIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGS 323

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514   321 FDIYNPsLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:TIGR02891 324 IRFTTP-MLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVF 379
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-377 2.08e-143

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 417.22  E-value: 2.08e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNA-FMNNEQiYNSLVTLHAFIMIFFMVMPFmIGGFGNWLIPLMISSP 79
Cdd:COG0843  15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLgLLSPET-YNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGAR 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  80 DLAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMN 159
Cdd:COG0843  93 DMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILK 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 160 MKHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPG 239
Cdd:COG0843 173 MRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPA 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 240 FGIISHIIFNEMNKPsTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGS 319
Cdd:COG0843 253 FGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRG 331

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 60476514 320 KFDIYNPsLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:COG0843 332 RIRFTTP-MLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVF 388
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-377 1.00e-99

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: 302.18  E-value: 1.00e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514     3 DIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFmIGGFGNWLIPLMISSPDLA 82
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    83 FPRMNNASFWLLPPSLILLTIAGMtnsGAGTGWTIYPPLSNnmfhsgysVDLSIFSLHLSGMASILGSINFMASIMNMKH 162
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   163 SIISVnKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTsffdpsGGGDPILFQHLFWFFGHPEVYILILPGFGI 242
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   243 ISHIIFNEMNKPStFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSKFD 322
Cdd:pfam00115 222 IYYILPKFAGRPL-FGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 60476514   323 IYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:pfam00115 301 FRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVF 355
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-377 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 665.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00153  10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00153  90 MAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINM 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00153 170 RSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00153 250 GMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQ 329

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FDiYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00153 330 IN-YSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVF 385
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-377 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: 640.69  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:cd01663   3 HKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:cd01663  83 MAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNM 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:cd01663 163 RAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:cd01663 243 GIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGS 322

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514 321 FDiYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:cd01663 323 IK-FETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVF 378
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-377 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 595.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00223   9 HKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00223  89 MAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINM 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00223 169 RSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00223 249 GMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSK 328

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FDiYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00223 329 IK-YEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVF 384
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-377 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 591.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00167  12 HKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00167  92 MAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINM 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00167 172 KPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00167 252 GMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGK 331

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FdIYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00167 332 I-KWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVF 387
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-377 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 587.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00116  12 HKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00116  92 MAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINM 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00116 172 KPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00116 252 GIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGT 331

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FDiYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00116 332 IK-WDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVF 387
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-377 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 564.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00142  10 HKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00142  90 MAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINM 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00142 170 RAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00142 250 GMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSK 329

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FDiYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00142 330 VK-YEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVF 385
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-377 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 525.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00037  12 HKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00037  92 MAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINM 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00037 172 RTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGF 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00037 252 GMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSN 331

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FdIYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00037 332 L-RWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVF 387
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-377 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 520.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00007   9 HKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00007  89 MAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINM 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00007 169 RWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00007 249 GAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSP 328

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FDiYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00007 329 IK-YETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVF 384
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-377 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 519.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00103  12 HKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00103  92 MAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINM 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00103 172 KPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00103 252 GMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGN 331

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FDiYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00103 332 IK-WSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVF 387
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-377 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 518.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00183  12 HKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00183  92 MAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINM 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00183 172 KPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00183 252 GMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGS 331

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FDIYNPsLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00183 332 IKWETP-LLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVF 387
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-377 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 516.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00079  13 HKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNnMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00079  93 MSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00079 172 RSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAF 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00079 252 GIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMK 331

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FDIyNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00079 332 MKF-QPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVF 387
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-377 3.27e-180

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 510.25  E-value: 3.27e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00077  12 HKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00077  92 MAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINM 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00077 172 KPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGF 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00077 252 GMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGA 331

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FDiYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00077 332 IK-WDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVF 387
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-377 7.41e-175

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 497.04  E-value: 7.41e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00182  14 HKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00182  94 MAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNM 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00182 174 RAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGF 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00182 254 GMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGT 333

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FDIYNPsLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00182 334 LRLDTP-MLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVF 389
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-377 4.69e-172

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 489.72  E-value: 4.69e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00184  14 HKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00184  94 MAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNM 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00184 174 RAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00184 254 GIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGS 333

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514  321 FDIYNPsLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00184 334 LRLDTP-MLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVF 389
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-377 6.72e-157

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: 449.29  E-value: 6.72e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPlMISSPD 80
Cdd:cd00919   1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:cd00919  80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 241 GIISHIIFNEMNKPsTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:cd00919 240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514 321 fDIYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:cd00919 319 -IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVF 374
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-377 5.65e-154

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 444.46  E-value: 5.65e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00026  13 HKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00026  93 MAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNM 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00026 173 RTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00026 253 GIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSG 332

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 60476514  321 FD-IYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:MTH00026 333 RNlIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVF 390
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-377 4.88e-146

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: 422.79  E-value: 4.88e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514     1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPfMIGGFGNWLIPLMISSPD 80
Cdd:TIGR02891   6 HKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:TIGR02891  85 MAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNM 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:TIGR02891 165 RAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAF 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   241 GIISHIIFNEMNKPsTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:TIGR02891 245 GIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGS 323

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514   321 FDIYNPsLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:TIGR02891 324 IRFTTP-MLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVF 379
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-375 1.10e-143

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 417.16  E-value: 1.10e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGGFGNWLIPLMISSPD 80
Cdd:MTH00048  13 HKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   81 LAFPRMNNASFWLLPPSLILLTIAgmTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:MTH00048  93 LNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  161 KHSIISvNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:MTH00048 171 FMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGF 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  241 GIISHIIFNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:MTH00048 250 GIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSR 329

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 60476514  321 FDIYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGA 375
Cdd:MTH00048 330 VRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGS 384
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-377 2.08e-143

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 417.22  E-value: 2.08e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNA-FMNNEQiYNSLVTLHAFIMIFFMVMPFmIGGFGNWLIPLMISSP 79
Cdd:COG0843  15 HKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLgLLSPET-YNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGAR 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  80 DLAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMN 159
Cdd:COG0843  93 DMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILK 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 160 MKHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPG 239
Cdd:COG0843 173 MRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPA 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 240 FGIISHIIFNEMNKPsTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGS 319
Cdd:COG0843 253 FGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRG 331

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 60476514 320 KFDIYNPsLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:COG0843 332 RIRFTTP-MLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVF 388
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-377 1.57e-122

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: 363.05  E-value: 1.57e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTP-NAFMNNEQiYNSLVTLHAFIMIFFMVMPFMIGgFGNWLIPLMISSP 79
Cdd:cd01662   7 HKRIGIMYIITAFVFFLRGGVDALLMRTQLALPgNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGAR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  80 DLAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMN 159
Cdd:cd01662  85 DVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILK 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 160 MKHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPG 239
Cdd:cd01662 165 MRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPA 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 240 FGIISHIIFNEMNKPsTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGS 319
Cdd:cd01662 245 FGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRG 323

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 60476514 320 KFdIYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:cd01662 324 RI-RFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVF 380
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 3-377 1.00e-99

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: 302.18  E-value: 1.00e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514     3 DIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFmIGGFGNWLIPLMISSPDLA 82
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    83 FPRMNNASFWLLPPSLILLTIAGMtnsGAGTGWTIYPPLSNnmfhsgysVDLSIFSLHLSGMASILGSINFMASIMNMKH 162
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   163 SIISVnKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTsffdpsGGGDPILFQHLFWFFGHPEVYILILPGFGI 242
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   243 ISHIIFNEMNKPStFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSKFD 322
Cdd:pfam00115 222 IYYILPKFAGRPL-FGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 60476514   323 IYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:pfam00115 301 FRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVF 355
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-377 2.14e-89

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: 282.13  E-value: 2.14e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514     1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGgFGNWLIPLMISSPD 80
Cdd:TIGR02882  50 HKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARD 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    81 LAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASIMNM 160
Cdd:TIGR02882 129 VAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKM 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   161 KHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILILPGF 240
Cdd:TIGR02882 209 RAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAF 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   241 GIISHIIfNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSK 320
Cdd:TIGR02882 289 GIYSEII-STFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGK 367

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 60476514   321 FDIYNPsLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:TIGR02882 368 IRFTTP-MLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVF 423
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-377 1.86e-84

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 269.88  E-value: 1.86e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514    1 HKDIGMLYFIFAMWSGMMGSSLSLIIRIE---LSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMPFMIGgFGNWLIPLMIS 77
Cdd:PRK15017  54 HKRLGIMYIIVAIVMLLRGFADAIMMRSQqalASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIG 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   78 SPDLAFPRMNNASFWLLPPSLILLTIAGMTNSGAGTGWTIYPPLSNNMFHSGYSVDLSIFSLHLSGMASILGSINFMASI 157
Cdd:PRK15017 133 ARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTI 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  158 MNMKHSIISVNKLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDRNMNTSFFDPSGGGDPILFQHLFWFFGHPEVYILIL 237
Cdd:PRK15017 213 LKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILIL 292

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  238 PGFGIISHIIfNEMNKPSTFGPISMIYALISISFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFY 317
Cdd:PRK15017 293 PVFGVFSEIA-ATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMY 371

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  318 GSKFdIYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFHYVLSMGAVF 377
Cdd:PRK15017 372 QGRI-VFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVF 430
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 8-368 1.61e-09

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: 59.22  E-value: 1.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514   8 YFIFAMWSGMMGSSLSLIIRIELSTPNAFMNNEQIYNSLVTLHAFIMIFFMVMpFMIGGFGNWLIPLMISSPDLAfPRMN 87
Cdd:cd01660   9 HFVVAFLALLLGGLFGLLQVLVRTGVFPLPSSGILYYQGLTLHGVLLAIVFTT-FFIMGFFYAIVARALLRSLFN-RRLA 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514  88 NASFWLLPPSLILLTIAGMTNSgAGTGWTIYPPLSNNMFhsgYSVDLSIFslhlsgmasILGSINFMASIMNMKHSIISV 167
Cdd:cd01660  87 WAGFWLMVIGTVMAAVPILLGQ-ASVLYTFYPPLQAHPL---FYIGAALV---------VVGSWISGFAMFVTLWRWKKA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 168 N---KLTLLTWSIFLTTVLLLLSIPVLAGAITMLLLDrnMNTSFFDPSgggDPILFQHLFWFFGHPEVYILILPGFGIIS 244
Cdd:cd01660 154 NpgkKVPLATFMVVTTMILWLVASLGVALEVLFQLLP--WSLGLVDTV---DVLLSRTLFWWFGHPLVYFWLLPAYIAWY 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60476514 245 HIIfnemnkPSTFGPISMIYALISISFLGFIVWG-----HHMFT-VGMDVDTRAYFTSATMIIAIPTGIKIFSWLASF-- 316
Cdd:cd01660 229 TIL------PKIAGGKLFSDPLARLAFILFLLFStpvgfHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLei 302

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60476514 317 ----------YG--SKFDIYNPSLLWAMGFITMFTIGGLSGIILSNSSLDISLHDTYYVVAHFH 368
Cdd:cd01660 303 agrlrggkglFGwiRALPWGDPMFLALFLAMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFH 366
 
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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