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Conserved domains on  [gi|1540312748|gb|AZP75122|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Mohoua novaeseelandiae]

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 ...
 3-270 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 MTH00116:

Pssm-ID: 469701  Cd Length: 515  Bit Score: 554.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   3 FINRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 82
Cdd:MTH00116    2 FITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  83 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGA 162
Cdd:MTH00116   82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 163 INFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 242
Cdd:MTH00116  162 INFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241

                         250       260
                  ....*....|....*....|....*...
gi 1540312748 243 EVYILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00116  242 EVYILILPGFGIISHIVTYYAGKKEPFG 269
 
Name Accession Description Interval E-value
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 3-270 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 554.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   3 FINRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 82
Cdd:MTH00116    2 FITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  83 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGA 162
Cdd:MTH00116   82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 163 INFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 242
Cdd:MTH00116  162 INFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241

                         250       260
                  ....*....|....*....|....*...
gi 1540312748 243 EVYILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00116  242 EVYILILPGFGIISHIVTYYAGKKEPFG 269
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 11-270 4.15e-165

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: 466.19  E-value: 4.15e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  11 TNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 90
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  91 PDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAI 170
Cdd:cd01663    81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 171 NMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILP 250
Cdd:cd01663   161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240

                         250       260
                  ....*....|....*....|
gi 1540312748 251 GFGIISHVVAYYAGKKEPFG 270
Cdd:cd01663   241 GFGIISHIISTFSGKKPVFG 260
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 8-266 8.60e-97

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: 292.59  E-value: 8.60e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   8 LFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMiGGFGNWLVPLM 87
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  88 IGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFIT 167
Cdd:TIGR02891  80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 168 TAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYIL 247
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239

                         250
                  ....*....|....*....
gi 1540312748 248 ILPGFGIISHVVAYYAGKK 266
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP 258
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-266 1.59e-95

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 290.49  E-value: 1.59e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   2 TFINRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGN 81
Cdd:COG0843     4 SGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  82 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILG 161
Cdd:COG0843    83 YLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 162 AINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 241
Cdd:COG0843   163 GVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242

                         250       260
                  ....*....|....*....|....*
gi 1540312748 242 PEVYILILPGFGIISHVVAYYAGKK 266
Cdd:COG0843   243 PEVYILILPAFGIVSEIIPTFSRKP 267
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 15-266 6.90e-60

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: 195.87  E-value: 6.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  15 DIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 94
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  95 FPRMNNMSFWLLPPSFLLLLASStveAGVGTGWTVYPPLAGnlahagasVDLAIFSLHLAGISSILGAINFITTAINMKP 174
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 175 PALSQyQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNttffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGI 254
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221

                         250
                  ....*....|..
gi 1540312748 255 ISHVVAYYAGKK 266
Cdd:pfam00115 222 IYYILPKFAGRP 233
 
Name Accession Description Interval E-value
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 3-270 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 554.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   3 FINRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 82
Cdd:MTH00116    2 FITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  83 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGA 162
Cdd:MTH00116   82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 163 INFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 242
Cdd:MTH00116  162 INFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241

                         250       260
                  ....*....|....*....|....*...
gi 1540312748 243 EVYILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00116  242 EVYILILPGFGIISHIVTYYAGKKEPFG 269
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 5-270 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 509.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   5 NRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 84
Cdd:MTH00153    2 NKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  85 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAIN 164
Cdd:MTH00153   82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAIN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 165 FITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEV 244
Cdd:MTH00153  162 FITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241

                         250       260
                  ....*....|....*....|....*.
gi 1540312748 245 YILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00153  242 YILILPGFGMISHIISQESGKKETFG 267
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 3-270 3.27e-172

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 485.34  E-value: 3.27e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   3 FINRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 82
Cdd:MTH00167    2 WINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  83 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGA 162
Cdd:MTH00167   82 LVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 163 INFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 242
Cdd:MTH00167  162 INFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241

                         250       260
                  ....*....|....*....|....*...
gi 1540312748 243 EVYILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00167  242 EVYILILPGFGMISHIVVYYSGKKEPFG 269
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 11-270 4.15e-165

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: 466.19  E-value: 4.15e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  11 TNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 90
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  91 PDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAI 170
Cdd:cd01663    81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 171 NMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILP 250
Cdd:cd01663   161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240

                         250       260
                  ....*....|....*....|
gi 1540312748 251 GFGIISHVVAYYAGKKEPFG 270
Cdd:cd01663   241 GFGIISHIISTFSGKKPVFG 260
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 3-270 1.11e-164

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 466.28  E-value: 1.11e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   3 FINRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 82
Cdd:MTH00103    2 FINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  83 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGA 162
Cdd:MTH00103   82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 163 INFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 242
Cdd:MTH00103  162 INFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241

                         250       260
                  ....*....|....*....|....*...
gi 1540312748 243 EVYILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00103  242 EVYILILPGFGMISHIVTYYSGKKEPFG 269
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 4-270 5.63e-162

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 459.41  E-value: 5.63e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   4 INRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 83
Cdd:MTH00077    3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  84 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAI 163
Cdd:MTH00077   83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 164 NFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 243
Cdd:MTH00077  163 NFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 242

                         250       260
                  ....*....|....*....|....*..
gi 1540312748 244 VYILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00077  243 VYILILPGFGMISHIVTYYSAKKEPFG 269
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 4-270 8.18e-162

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 459.00  E-value: 8.18e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   4 INRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 83
Cdd:MTH00183    3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  84 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAI 163
Cdd:MTH00183   83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 164 NFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 243
Cdd:MTH00183  163 NFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242

                         250       260
                  ....*....|....*....|....*..
gi 1540312748 244 VYILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00183  243 VYILILPGFGMISHIVAYYSGKKEPFG 269
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 4-270 1.03e-157

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 448.40  E-value: 1.03e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   4 INRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 83
Cdd:MTH00142    1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  84 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAI 163
Cdd:MTH00142   81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 164 NFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 243
Cdd:MTH00142  161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240

                         250       260
                  ....*....|....*....|....*..
gi 1540312748 244 VYILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00142  241 VYILILPGFGMISHIINHYSGKKEVFG 267
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 6-270 2.81e-157

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 447.50  E-value: 2.81e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   6 RWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 85
Cdd:MTH00223    2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  86 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINF 165
Cdd:MTH00223   82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 166 ITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVY 245
Cdd:MTH00223  162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241

                         250       260
                  ....*....|....*....|....*
gi 1540312748 246 ILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00223  242 ILILPGFGMISHIVSHYSSKKEVFG 266
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-270 6.90e-145

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 416.15  E-value: 6.90e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   2 TFINRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 81
Cdd:MTH00037    1 MQLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  82 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILG 161
Cdd:MTH00037   81 WLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 162 AINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 241
Cdd:MTH00037  161 SINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGH 240

                         250       260
                  ....*....|....*....|....*....
gi 1540312748 242 PEVYILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00037  241 PEVYILILPGFGMISHVIAHYSGKQEPFG 269
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 6-270 1.50e-139

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 402.36  E-value: 1.50e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   6 RWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 85
Cdd:MTH00007    2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  86 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINF 165
Cdd:MTH00007   82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 166 ITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVY 245
Cdd:MTH00007  162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241

                         250       260
                  ....*....|....*....|....*
gi 1540312748 246 ILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00007  242 ILILPGFGAISHIVTHYAGKLEPFG 266
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 3-270 9.13e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 375.31  E-value: 9.13e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   3 FINRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 82
Cdd:MTH00182    4 YLTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNW 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  83 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGA 162
Cdd:MTH00182   84 LVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 163 INFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 242
Cdd:MTH00182  164 INFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHP 243

                         250       260
                  ....*....|....*....|....*...
gi 1540312748 243 EVYILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00182  244 EVYILILPGFGMISQIIPTFVAKKQIFG 271
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 3-270 9.40e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 374.93  E-value: 9.40e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   3 FINRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 82
Cdd:MTH00184    4 YLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNW 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  83 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGA 162
Cdd:MTH00184   84 FVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 163 INFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 242
Cdd:MTH00184  164 MNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243

                         250       260
                  ....*....|....*....|....*...
gi 1540312748 243 EVYILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00184  244 EVYILILPGFGIISQIIPTFAAKKQIFG 271
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 7-270 6.67e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 362.46  E-value: 6.67e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   7 WLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 86
Cdd:MTH00079    7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  87 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAgNLAHAGASVDLAIFSLHLAGISSILGAINFI 166
Cdd:MTH00079   87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFM 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 167 TTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYI 246
Cdd:MTH00079  166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245

                         250       260
                  ....*....|....*....|....
gi 1540312748 247 LILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00079  246 LILPAFGIISQSTLYLTGKKEVFG 269
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 6-270 4.73e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 340.84  E-value: 4.73e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   6 RWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 85
Cdd:MTH00026    6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  86 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINF 165
Cdd:MTH00026   86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 166 ITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVY 245
Cdd:MTH00026  166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245

                         250       260
                  ....*....|....*....|....*
gi 1540312748 246 ILILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00026  246 ILILPGFGIISQILSLFSYKKQIFG 270
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 13-266 1.28e-102

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: 306.38  E-value: 1.28e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  13 HKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPlMIGAPD 92
Cdd:cd00919     1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  93 MAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFITTAINM 172
Cdd:cd00919    80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 173 KPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGF 252
Cdd:cd00919   160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239

                         250
                  ....*....|....
gi 1540312748 253 GIISHVVAYYAGKK 266
Cdd:cd00919   240 GAISEIIPTFSGKP 253
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 8-266 8.60e-97

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: 292.59  E-value: 8.60e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   8 LFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMiGGFGNWLVPLM 87
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  88 IGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFIT 167
Cdd:TIGR02891  80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 168 TAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYIL 247
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239

                         250
                  ....*....|....*....
gi 1540312748 248 ILPGFGIISHVVAYYAGKK 266
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP 258
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-266 1.59e-95

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 290.49  E-value: 1.59e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   2 TFINRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGN 81
Cdd:COG0843     4 SGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  82 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILG 161
Cdd:COG0843    83 YLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 162 AINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 241
Cdd:COG0843   163 GVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242

                         250       260
                  ....*....|....*....|....*
gi 1540312748 242 PEVYILILPGFGIISHVVAYYAGKK 266
Cdd:COG0843   243 PEVYILILPAFGIVSEIIPTFSRKP 267
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 7-270 1.16e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 266.93  E-value: 1.16e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   7 WLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 86
Cdd:MTH00048    7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  87 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASstVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFI 166
Cdd:MTH00048   87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 167 TTAINMKPPALSqYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYI 246
Cdd:MTH00048  165 CTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243

                         250       260
                  ....*....|....*....|....
gi 1540312748 247 LILPGFGIISHVVAYYAGKKEPFG 270
Cdd:MTH00048  244 LILPGFGIISHICLSLSNNDDPFG 267
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 7-265 1.04e-78

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: 246.34  E-value: 1.04e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   7 WLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVPL 86
Cdd:cd01662     1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  87 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAINFI 166
Cdd:cd01662    80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 167 TTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYI 246
Cdd:cd01662   160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239

                         250
                  ....*....|....*....
gi 1540312748 247 LILPGFGIISHVVAYYAGK 265
Cdd:cd01662   240 LILPAFGIFSEIVPTFSRK 258
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 15-266 6.90e-60

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: 195.87  E-value: 6.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  15 DIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 94
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  95 FPRMNNMSFWLLPPSFLLLLASStveAGVGTGWTVYPPLAGnlahagasVDLAIFSLHLAGISSILGAINFITTAINMKP 174
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 175 PALSQyQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNttffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGI 254
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221

                         250
                  ....*....|..
gi 1540312748 255 ISHVVAYYAGKK 266
Cdd:pfam00115 222 IYYILPKFAGRP 233
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 5-266 9.20e-54

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: 183.90  E-value: 9.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   5 NRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLV 84
Cdd:TIGR02882  42 NEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  85 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSILGAIN 164
Cdd:TIGR02882 121 PLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGIN 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 165 FITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEV 244
Cdd:TIGR02882 201 FFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEV 280

                         250       260
                  ....*....|....*....|..
gi 1540312748 245 YILILPGFGIISHVVAYYAGKK 266
Cdd:TIGR02882 281 YIVILPAFGIYSEIISTFAQKR 302
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 5-270 3.88e-50

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 174.74  E-value: 3.88e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748   5 NRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIR-----AELGQPGALlgDDQIYNVIVTAHAFVMIFFMVMPIMIGgF 79
Cdd:PRK15017   46 KEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRsqqalASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-L 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748  80 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGISSI 159
Cdd:PRK15017  123 MNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTT 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540312748 160 LGAINFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFF 239
Cdd:PRK15017  203 LTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAW 282

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1540312748 240 GHPEVYILILPGFGIISHVVAYYAgKKEPFG 270
Cdd:PRK15017  283 GHPEVYILILPVFGVFSEIAATFS-RKRLFG 312
 
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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