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Conserved domains on  [gi|1748173289|gb|QER92461|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Koreoleptoxis davidi]

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 ...
 1-253 4.53e-174

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


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 488.99  E-value: 4.53e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00153   38 ELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00153  118 SGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSL 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00153  198 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLA 277

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00153  278 IGLLGFIVWAHHM 290
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-253 4.53e-174

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 488.99  E-value: 4.53e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00153   38 ELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00153  118 SGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSL 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00153  198 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLA 277

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00153  278 IGLLGFIVWAHHM 290
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-253 1.23e-161

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: 456.94  E-value: 1.23e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:cd01663    31 ELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:cd01663   111 GGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSL 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:cd01663   191 PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLS 270

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:cd01663   271 IGILGFIVWAHHM 283
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-253 4.16e-98

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: 295.29  E-value: 4.16e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMiGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:TIGR02891  34 QLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:TIGR02891 113 GAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAF 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYsSKKETFGTLGMIYAMLA 240
Cdd:TIGR02891 193 PVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTF-ARKPIFGYRAMVYATVA 271

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:TIGR02891 272 IGFLSFGVWAHHM 284
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-253 3.76e-95

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 288.95  E-value: 3.76e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMmIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:COG0843    43 QLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:COG0843   122 GAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAF 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKeTFGTLGMIYAMLA 240
Cdd:COG0843   202 PVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVA 280

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:COG0843   281 IAFLSFLVWAHHM 293
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-253 9.06e-61

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: 197.41  E-value: 9.06e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMmIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAve 80
Cdd:pfam00115  27 QLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG-- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 sGAGTGWTVYPPLSGnlahaggsVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFeRLPLFVWSVKITAILLLLSL 160
Cdd:pfam00115 104 -GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNtaffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYsSKKETFGTLGMIYAMLA 240
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKF-AGRPLFGYKLSVLAFWL 246

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:pfam00115 247 IAFLGFLVWAHHL 259
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-253 4.53e-174

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 488.99  E-value: 4.53e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00153   38 ELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00153  118 SGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSL 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00153  198 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLA 277

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00153  278 IGLLGFIVWAHHM 290
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-253 1.23e-161

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: 456.94  E-value: 1.23e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:cd01663    31 ELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:cd01663   111 GGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSL 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:cd01663   191 PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLS 270

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:cd01663   271 IGILGFIVWAHHM 283
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-253 2.93e-158

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 449.04  E-value: 2.93e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00223   37 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00223  117 SGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSL 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00223  197 PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLS 276

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00223  277 IGVLGFIVWAHHM 289
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-253 5.26e-158

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 448.40  E-value: 5.26e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00142   38 ELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00142  118 SGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSL 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00142  198 PVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLS 277

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00142  278 IGLLGFIVWAHHM 290
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-253 1.24e-152

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 434.87  E-value: 1.24e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00167   40 ELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00167  120 AGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00167  200 PVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMA 279

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00167  280 IGLLGFIVWAHHM 292
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-253 2.17e-150

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 429.13  E-value: 2.17e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00116   40 ELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00116  120 AGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00116  200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLS 279

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00116  280 IGFLGFIVWAHHM 292
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-253 2.69e-140

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 403.51  E-value: 2.69e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00007   37 ELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00007  117 KGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSL 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00007  197 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLG 276

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00007  277 IGVLGFIVWAHHM 289
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-253 1.51e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 394.20  E-value: 1.51e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00037   40 ELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00037  120 SGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00037  200 PVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIA 279

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00037  280 IGILGFLVWAHHM 292
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-253 9.26e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 384.66  E-value: 9.26e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00183   40 ELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00183  120 AGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00183  200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMA 279

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00183  280 IGLLGFIVWAHHM 292
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-253 1.11e-132

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 384.23  E-value: 1.11e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00103   40 ELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00103  120 AGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00103  200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMS 279

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00103  280 IGFLGFIVWAHHM 292
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-253 3.31e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 383.14  E-value: 3.31e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00077   40 ELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00077  120 AGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00077  200 PVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMS 279

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00077  280 IGLLGFIVWAHHM 292
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-253 1.87e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 373.77  E-value: 1.87e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00182   42 ELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00182  122 QGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSL 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00182  202 PVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLS 281

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00182  282 IGILGFIVWAHHM 294
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-253 3.21e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 365.30  E-value: 3.21e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00184   42 ELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00184  122 QGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSL 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00184  202 PVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVS 281

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00184  282 IGILGFIVWAHHM 294
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-253 2.14e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 350.13  E-value: 2.14e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00079   41 ELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVD 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSgNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00079  121 MGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00079  200 PVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILS 279

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00079  280 IGLIGCVVWAHHM 292
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-253 2.71e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 343.15  E-value: 2.71e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:MTH00026   41 ELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:MTH00026  121 QGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSL 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLA 240
Cdd:MTH00026  201 PVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLA 280

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:MTH00026  281 IGVLGFIVWAHHM 293
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-253 7.25e-103

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: 7.25e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPlMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:cd00919    29 ELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:cd00919   108 GGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLAL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYsSKKETFGTLGMIYAMLA 240
Cdd:cd00919   188 PVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTF-SGKPLFGYKLMVYAFLA 266

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:cd00919   267 IGFLSFLVWAHHM 279
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-253 4.16e-98

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: 295.29  E-value: 4.16e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMiGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:TIGR02891  34 QLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:TIGR02891 113 GAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAF 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYsSKKETFGTLGMIYAMLA 240
Cdd:TIGR02891 193 PVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTF-ARKPIFGYRAMVYATVA 271

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:TIGR02891 272 IGFLSFGVWAHHM 284
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-253 3.76e-95

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 288.95  E-value: 3.76e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMmIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:COG0843    43 QLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:COG0843   122 GAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAF 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKeTFGTLGMIYAMLA 240
Cdd:COG0843   202 PVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVA 280

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:COG0843   281 IAFLSFLVWAHHM 293
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 15-253 2.29e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 270.78  E-value: 2.29e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  15 YNVIVTAHAFVMIFFLVMPMMIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVesGAGTGWTVYPPLS 94
Cdd:MTH00048   55 YNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLS 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  95 GNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMrWRGMQFERLPLFVWSVKITAILLLLSLPVLAGAITMLLTDR 174
Cdd:MTH00048  133 SSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSA-FMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDR 211

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1748173289 175 NFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHM 253
Cdd:MTH00048  212 NFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHM 290
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-253 5.98e-82

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: 254.04  E-value: 5.98e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVE 80
Cdd:cd01662    35 QLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 SGAGTGWTVYPPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSL 160
Cdd:cd01662   114 GFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAF 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYsSKKETFGTLGMIYAMLA 240
Cdd:cd01662   194 PVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTF-SRKPLFGYRSMVYATVA 272

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:cd01662   273 IGFLSFGVWVHHM 285
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-253 9.06e-61

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: 197.41  E-value: 9.06e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289   1 ELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMmIGGFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAve 80
Cdd:pfam00115  27 QLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG-- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  81 sGAGTGWTVYPPLSGnlahaggsVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFeRLPLFVWSVKITAILLLLSL 160
Cdd:pfam00115 104 -GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 161 PVLAGAITMLLTDRNFNtaffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYsSKKETFGTLGMIYAMLA 240
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKF-AGRPLFGYKLSVLAFWL 246

                         250
                  ....*....|...
gi 1748173289 241 IGVLGFIVWAHHM 253
Cdd:pfam00115 247 IAFLGFLVWAHHL 259
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-252 2.32e-52

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: 179.66  E-value: 2.32e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  11 DDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGAGTGWTVY 90
Cdd:TIGR02882  88 DAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNY 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  91 PPLSGNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSLPVLAGAITML 170
Cdd:TIGR02882 167 APLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALM 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289 171 LTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYsSKKETFGTLGMIYAMLAIGVLGFIVWA 250
Cdd:TIGR02882 247 TTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTF-AQKRLFGYKSMVWSTVGIAFLSFLVWV 325


                  ..
gi 1748173289 251 HH 252
Cdd:TIGR02882 326 HH 327
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 15-252 4.52e-52

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 178.98  E-value: 4.52e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  15 YNVIVTAHAFVMIFFLVMPMMIGgFGNWLIPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLS 94
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1748173289  95 GNLAHAGGSVDLAIFSLHLAGASSILGAVNFITTIINMRWRGMQFERLPLFVWSVKITAILLLLSLPVLAGAITMLLTDR 174
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1748173289 175 NFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYsSKKETFGTLGMIYAMLAIGVLGFIVWAHH 252
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATF-SRKRLFGYTSLVWATVCITVLSFIVWLHH 334
 
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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