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Conserved domains on  [gi|922668154|gb|ALA65616|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Eleutherozoa sp. COT033_L26]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
1-287 0e+00

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


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 444803  Cd Length: 511  Bit Score: 569.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00153  30 SLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00153 110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00153 190 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTL 269
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00153 270 GMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 316
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-287 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 569.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00153  30 SLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00153 110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00153 190 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTL 269
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00153 270 GMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 316
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-287 0e+00

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 546.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:cd01663   23 SLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:cd01663  103 LLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLIT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:cd01663  183 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYL 262
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:cd01663  263 GMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 309
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
1-287 3.15e-121

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: 355.76  E-value: 3.15e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154    1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMiGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:TIGR02891  26 VLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:TIGR02891 105 LLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVT 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYL 240
Cdd:TIGR02891 185 SILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYR 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 922668154  241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:TIGR02891 264 AMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGV 310
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-287 2.60e-117

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


Pssm-ID: 223913 [Multi-domain]  Cd Length: 566  Bit Score: 348.13  E-value: 2.60e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQP-GSLLQDDQIYNVIVTAHALVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFL 79
Cdd:COG0843   36 ALALLMRLELATPsGSQFLDPQLYNQILTLHGVIMIFFFAMP-AIGGFANYLVPLMIGARDVAFPRLNAISFWLLVVGAI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  80 LLLASAGVESGAG-TGWTIYPPLSSgLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVF 158
Cdd:COG0843  115 LLVTSFFVPGGAAdTGWTAYPPLSA-ISYSGPGVDLFILGLHLLGIGSLLGAINFIVTILNMRAPGMTMMKMPLFTWSIL 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 159 VTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEpFG 238
Cdd:COG0843  194 ITAILILLAFPVLAAALTMLLLDRNFGTSFFTPAGGGDPLLYQHLFWFFGHPEVYILILPAFGIVSEIIPTFARKPL-FG 272
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 922668154 239 YLGMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:COG0843  273 YTSMVYAFVAIGILSFIVWAHHMFTTGLPADLRAFFSITTMIIAIPTGI 321
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I;
1-287 4.11e-80

Cytochrome C and Quinol oxidase polypeptide I;


Pssm-ID: 425471  Cd Length: 432  Bit Score: 248.64  E-value: 4.11e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154    1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:pfam00115  19 LLGLLIRLQLAFPGLNFLSPLTYNRLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   81 LLASAGvesGAGTGWTIYPPLssglahagGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFdRLPLFVWSVFVT 160
Cdd:pfam00115  98 LLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILAT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  161 AFLLLLSLPVLAGAITMLLTDRNVNttffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYL 240
Cdd:pfam00115 166 AILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYR 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 922668154  241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:pfam00115 239 LSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGV 285
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-287 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 569.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00153  30 SLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00153 110 LLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLIT 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00153 190 AILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTL 269
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00153 270 GMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 316
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
1-287 0e+00

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 546.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:cd01663   23 SLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:cd01663  103 LLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLIT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:cd01663  183 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYL 262
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:cd01663  263 GMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 309
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
1-287 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 527.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00167  32 ALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00167 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVT 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00167 192 TILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYM 271
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00167 272 GMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 318
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
1-287 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 521.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00037  32 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00037 112 LLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFIT 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00037 192 AFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYL 271
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00037 272 GMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 318
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
1-287 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 520.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00116  32 ALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00116 112 LLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLIT 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00116 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYM 271
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00116 272 GMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGI 318
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
1-287 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 514.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00223  29 SLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00223 109 LLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVT 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00223 189 AFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTL 268
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00223 269 GMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 315
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
1-287 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 507.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00142  30 GLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00142 110 LLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKIT 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00142 190 AILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTL 269
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00142 270 GMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGI 316
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
1-287 5.12e-163

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 462.86  E-value: 5.12e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00183  32 ALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00183 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLIT 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00183 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYM 271
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00183 272 GMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGV 318
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
1-287 1.44e-161

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 458.96  E-value: 1.44e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00103  32 ALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00103 112 LLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLIT 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00103 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYM 271
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00103 272 GMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGV 318
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
1-287 4.25e-160

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 455.55  E-value: 4.25e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00077  32 ALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00077 112 LLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLIT 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00077 192 AVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYM 271
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00077 272 GMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGV 318
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
1-287 1.07e-157

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 449.35  E-value: 1.07e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00007  29 SMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALIL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00007 109 LVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVIT 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00007 189 VVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTL 268
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00007 269 GMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 315
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
1-287 3.04e-156

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 445.81  E-value: 3.04e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00182  34 AFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALIL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00182 114 LLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILIT 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00182 194 AFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYL 273
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00182 274 GMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
1-287 3.56e-154

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 440.42  E-value: 3.56e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00184  34 AFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00184 114 LLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVT 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00184 194 TFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYL 273
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00184 274 GMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
1-287 4.45e-147

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 422.17  E-value: 4.45e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00079  33 SLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFL 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSgLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00079 113 ILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVT 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00079 192 VFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSL 271
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00079 272 GMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGV 318
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
1-287 3.09e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 392.84  E-value: 3.09e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:MTH00026  33 AFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFL 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:MTH00026 113 LLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFIT 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYL 240
Cdd:MTH00026 193 AILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYL 272
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00026 273 GMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGI 319
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
1-287 5.85e-126

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: 366.47  E-value: 5.85e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPlMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:cd00919   21 LLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:cd00919  100 LLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVT 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYL 240
Cdd:cd00919  180 AILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYK 258
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:cd00919  259 LMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGI 305
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
1-287 3.15e-121

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: 355.76  E-value: 3.15e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154    1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMiGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:TIGR02891  26 VLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:TIGR02891 105 LLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVT 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYL 240
Cdd:TIGR02891 185 SILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYR 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 922668154  241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:TIGR02891 264 AMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGV 310
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-287 2.60e-117

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


Pssm-ID: 223913 [Multi-domain]  Cd Length: 566  Bit Score: 348.13  E-value: 2.60e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQP-GSLLQDDQIYNVIVTAHALVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFL 79
Cdd:COG0843   36 ALALLMRLELATPsGSQFLDPQLYNQILTLHGVIMIFFFAMP-AIGGFANYLVPLMIGARDVAFPRLNAISFWLLVVGAI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  80 LLLASAGVESGAG-TGWTIYPPLSSgLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVF 158
Cdd:COG0843  115 LLVTSFFVPGGAAdTGWTAYPPLSA-ISYSGPGVDLFILGLHLLGIGSLLGAINFIVTILNMRAPGMTMMKMPLFTWSIL 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 159 VTAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEpFG 238
Cdd:COG0843  194 ITAILILLAFPVLAAALTMLLLDRNFGTSFFTPAGGGDPLLYQHLFWFFGHPEVYILILPAFGIVSEIIPTFARKPL-FG 272
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 922668154 239 YLGMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:COG0843  273 YTSMVYAFVAIGILSFIVWAHHMFTTGLPADLRAFFSITTMIIAIPTGI 321
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
2-287 1.50e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 323.94  E-value: 1.50e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   2 MSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLLL 81
Cdd:MTH00048  34 LSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  82 LASagVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFdRLPLFVWSVFVTA 161
Cdd:MTH00048 114 LLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTS 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 162 FLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKSEPFGYLG 241
Cdd:MTH00048 191 ILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYG 270
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 922668154 242 MVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:MTH00048 271 LVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGI 316
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
1-287 5.44e-102

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: 306.81  E-value: 5.44e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:cd01662   27 VDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  81 LLASAGVESGAGTGWTIYPPLSSGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVT 160
Cdd:cd01662  106 LNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVT 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 161 AFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYL 240
Cdd:cd01662  186 SILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYR 264
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922668154 241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:cd01662  265 SMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGV 311
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I;
1-287 4.11e-80

Cytochrome C and Quinol oxidase polypeptide I;


Pssm-ID: 425471  Cd Length: 432  Bit Score: 248.64  E-value: 4.11e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154    1 AMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPiMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLL 80
Cdd:pfam00115  19 LLGLLIRLQLAFPGLNFLSPLTYNRLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154   81 LLASAGvesGAGTGWTIYPPLssglahagGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFdRLPLFVWSVFVT 160
Cdd:pfam00115  98 LLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILAT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  161 AFLLLLSLPVLAGAITMLLTDRNVNttffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKsEPFGYL 240
Cdd:pfam00115 166 AILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYR 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 922668154  241 GMVYAIVSIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:pfam00115 239 LSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGV 285
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
23-287 1.03e-63

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 211.72  E-value: 1.03e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154  23 YNVIVTAHALVMIFFMVMPIMIGgFGNWLIPLMIGAPDMAFPRMNNMSFWLVPPSFLLLLASAGVESGAGTGWTIYPPLS 102
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 103 SGLAHAGGSVDLAIFSLHLAGASSILASINFITTVINMRTPGISFDRLPLFVWSVFVTAFLLLLSLPVLAGAITMLLTDR 182
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922668154 183 NVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSgKSEPFGYLGMVYAIVSIGILGFLVWAHHMF 262
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFF 336
                        250       260
                 ....*....|....*....|....*
gi 922668154 263 TVGMDVDTRAYFTAATMIIAVPTGI 287
Cdd:PRK15017 337 TMGAGANVNAFFGITTMIIAIPTGV 361
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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