NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|808154989|gb|AKC96823|]
View 

cytochrome oxidase subunit I, partial (mitochondrion) [Arthropoda sp. NZAC 03010879]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
1-202 2.25e-132

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: 412277  Cd Length: 511  Bit Score: 380.75  E-value: 2.25e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTS 216
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-202 2.25e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 380.75  E-value: 2.25e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTS 216
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-202 1.57e-116

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: 339.84  E-value: 1.57e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:cd01663    8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:cd01663   88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:cd01663  168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTS 209
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-202 3.72e-61

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


Pssm-ID: 223913  Cd Length: 566  Bit Score: 199.44  E-value: 3.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSP-GSLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFP 79
Cdd:COG0843   21 ILYLILAIFFLLVGGALALLMRLELATPsGSQFLDPQLYNQILTLHGVIMIFFFAMP-AIGGFANYLVPLMIGARDVAFP 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  80 RMNNMSFWLLPPSLSLLLMSSIVENGAG-TGWTVYPPLSANIAHsGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPV 158
Cdd:COG0843  100 RLNAISFWLLVVGAILLVTSFFVPGGAAdTGWTAYPPLSAISYS-GPGVDLFILGLHLLGIGSLLGAINFIVTILNMRAP 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 808154989 159 GMTLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:COG0843  179 GMTMMKMPLFTWSILITAILILLAFPVLAAALTMLLLDRNFGTS 222
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I;
2-202 3.06e-39

Cytochrome C and Quinol oxidase polypeptide I;


Pssm-ID: 395065  Cd Length: 434  Bit Score: 138.85  E-value: 3.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989    2 LYFIFGAWAGMVGTSLSLLIRAELGSPGSLigddQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPLDP----LTYNQLRTLHGNLMIFGFATP-FIFGFGNYLVPLMIGARDMAFPRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   82 NNMSFWLLPPSLSLLLMSSIveNGAGTGWTVYPPLSAniahsgssVDLAIFSLHLAGISSILGAVNFITTVINMRPVGMT 161
Cdd:pfam00115  80 NALSFWLVVLGAVLLLASFF--GGATTGWTEYPPLTG--------VDLWYLGLLLAGVGSLLGAINFIVTILKRRAPGMY 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 808154989  162 LDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:pfam00115 150 LSRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSFGTH 190
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-202 2.25e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 380.75  E-value: 2.25e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTS 216
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-202 1.57e-116

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: 339.84  E-value: 1.57e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:cd01663    8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:cd01663   88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:cd01663  168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTS 209
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
1-202 1.07e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 330.87  E-value: 1.07e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00167  17 TLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00167  97 MNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGI 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00167 177 TQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTT 218
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
1-202 5.91e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 326.66  E-value: 5.91e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00116  17 TLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00116  97 MNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAM 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00116 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTT 218
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
1-202 2.45e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 322.44  E-value: 2.45e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00142  15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPR 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00142  95 MNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGM 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00142 175 KFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTS 216
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
1-202 8.00e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 318.46  E-value: 8.00e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00223  14 TLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00223  94 LNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGM 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00223 174 QLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTS 215
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
1-202 1.18e-99

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 297.56  E-value: 1.18e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00103  17 TLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00103  97 MNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAM 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00103 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTT 218
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
1-202 2.99e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 296.83  E-value: 2.99e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00183  17 TLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00183  97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAI 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00183 177 SQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTT 218
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
1-202 4.00e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 296.47  E-value: 4.00e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00077  17 TLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00077  97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSM 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00077 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTT 218
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
1-202 1.12e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 292.50  E-value: 1.12e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00037  17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00037  97 MNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGM 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00037 177 TFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTT 218
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
1-202 8.04e-96

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 287.57  E-value: 8.04e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00007  14 TLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00007  94 LNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGL 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00007 174 RLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTS 215
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
1-202 1.02e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 272.47  E-value: 1.02e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00182  19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPR 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00182  99 LNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGV 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00182 179 TFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTT 220
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
1-202 1.11e-89

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 272.09  E-value: 1.11e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00184  19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00184  99 LNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGI 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00184 179 TMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTT 220
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
1-202 2.58e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 265.78  E-value: 2.58e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00079  18 TLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSaNIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00079  98 LNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSI 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00079 177 SLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTS 218
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
1-202 1.15e-80

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 249.55  E-value: 1.15e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 80
Cdd:MTH00026  18 SLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:MTH00026  98 LNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGM 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:MTH00026 178 TMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTT 219
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
1-202 2.04e-71

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: 223.56  E-value: 2.04e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPR 80
Cdd:cd00919    6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  81 MNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGM 160
Cdd:cd00919   85 LNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGM 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 808154989 161 TLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:cd00919  165 TLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTS 206
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-202 3.72e-61

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


Pssm-ID: 223913  Cd Length: 566  Bit Score: 199.44  E-value: 3.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   1 TLYFIFGAWAGMVGTSLSLLIRAELGSP-GSLIGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFP 79
Cdd:COG0843   21 ILYLILAIFFLLVGGALALLMRLELATPsGSQFLDPQLYNQILTLHGVIMIFFFAMP-AIGGFANYLVPLMIGARDVAFP 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  80 RMNNMSFWLLPPSLSLLLMSSIVENGAG-TGWTVYPPLSANIAHsGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPV 158
Cdd:COG0843  100 RLNAISFWLLVVGAILLVTSFFVPGGAAdTGWTAYPPLSAISYS-GPGVDLFILGLHLLGIGSLLGAINFIVTILNMRAP 178
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 808154989 159 GMTLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:COG0843  179 GMTMMKMPLFTWSILITAILILLAFPVLAAALTMLLLDRNFGTS 222
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
2-201 1.79e-50

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 170.24  E-value: 1.79e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   2 LYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:MTH00048  19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  82 NNMSFWLLPPSLSLLLMSSIVenGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGMT 161
Cdd:MTH00048  99 NALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 808154989 162 LdKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNT 201
Cdd:MTH00048 177 S-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGS 215
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
2-201 5.53e-46

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: 158.13  E-value: 5.53e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   2 LYFIFGAWAGMVGTSLSLLIRAELGSPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRM 81
Cdd:cd01662   13 MYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  82 NNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLSANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGMT 161
Cdd:cd01662   92 NALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMT 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 808154989 162 LDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNT 201
Cdd:cd01662  172 LMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGT 211
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I;
2-202 3.06e-39

Cytochrome C and Quinol oxidase polypeptide I;


Pssm-ID: 395065  Cd Length: 434  Bit Score: 138.85  E-value: 3.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989    2 LYFIFGAWAGMVGTSLSLLIRAELGSPGSLigddQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRM 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPLDP----LTYNQLRTLHGNLMIFGFATP-FIFGFGNYLVPLMIGARDMAFPRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989   82 NNMSFWLLPPSLSLLLMSSIveNGAGTGWTVYPPLSAniahsgssVDLAIFSLHLAGISSILGAVNFITTVINMRPVGMT 161
Cdd:pfam00115  80 NALSFWLVVLGAVLLLASFF--GGATTGWTEYPPLTG--------VDLWYLGLLLAGVGSLLGAINFIVTILKRRAPGMY 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 808154989  162 LDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTT 202
Cdd:pfam00115 150 LSRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSFGTH 190
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
38-201 1.31e-29

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 114.65  E-value: 1.31e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989  38 YNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLSLLLMSSIVENGAGTGWTVYPPLS 117
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808154989 118 ANIAHSGSSVDLAIFSLHLAGISSILGAVNFITTVINMRPVGMTLDKTPLFVWSVAITALLLLLSLPVLAGAITMLLTDR 197
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                 ....
gi 808154989 198 NLNT 201
Cdd:PRK15017 258 YLGT 261
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH