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Conserved domains on  [gi|970839877|gb|ALU66372|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Prosphena scudderi]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-149 5.18e-86

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 250.90  E-value: 5.18e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00154  32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839877  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00154 112 DFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLN 180
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-149 5.18e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 250.90  E-value: 5.18e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00154  32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839877  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00154 112 DFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLN 180
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-149 1.53e-55

C-terminal domain of Cytochrome c Oxidase subunit II; 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 170.44  E-value: 1.53e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877  64 ITIKTIGRQWYWSYEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82


                 ....*.
gi 970839877 144 TPGRLN 149
Cdd:cd13912   83 VPGRLN 88
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
64-149 2.41e-50

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 156.80  E-value: 2.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   64 ITIKTIGRQWYWSYEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80


                  ....*.
gi 970839877  144 TPGRLN 149
Cdd:pfam00116  81 VPGRLN 86
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
20-149 6.00e-24

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 92.58  E-value: 6.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877  20 KARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYsdfmnvefdtymlPEKElks 99
Cdd:COG1622   69 DPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQG--- 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 970839877 100 nnfrlLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:COG1622  133 -----IATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVT 177
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-149 8.24e-20

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 81.27  E-value: 8.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   13 YIILIKFKARN--------MLHGHM-IEMIWTLIPA-ITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSDF 82
Cdd:TIGR02866  30 LLAYVVWKFRRkgdeekpsQIHGNRrLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970839877   83 mnvefdtymlpekelksnnfrLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:TIGR02866 110 ---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTN 155
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-149 5.18e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 250.90  E-value: 5.18e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00154  32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839877  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00154 112 DFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLN 180
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-149 4.13e-64

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 195.52  E-value: 4.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00117  32 LLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYT 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839877  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00117 112 DYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLN 180
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-149 4.28e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 193.01  E-value: 4.28e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00139  32 IMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYS 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839877  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00139 112 DFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLN 180
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-149 2.86e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 190.92  E-value: 2.86e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00140  32 VLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYS 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839877  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00140 112 DFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLN 180
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-149 8.58e-61

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 186.99  E-value: 8.58e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00008  32 TLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839877  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00008 112 DFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLN 180
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-149 8.58e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 181.72  E-value: 8.58e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00168  32 VLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYT 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839877  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00168 112 DYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLN 180
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-149 8.41e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 179.51  E-value: 8.41e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00038  32 TLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYT 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839877  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00038 112 DYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLN 180
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-149 1.53e-55

C-terminal domain of Cytochrome c Oxidase subunit II; 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 170.44  E-value: 1.53e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877  64 ITIKTIGRQWYWSYEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82


                 ....*.
gi 970839877 144 TPGRLN 149
Cdd:cd13912   83 VPGRLN 88
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-149 2.50e-53

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 168.03  E-value: 2.50e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00076  32 FLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYT 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839877  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00076 112 DYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLN 180
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-149 8.23e-53

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 166.98  E-value: 8.23e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   2 MITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSD 81
Cdd:MTH00185  33 LISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTD 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 970839877  82 FMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00185 113 YEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLN 180
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-149 1.73e-52

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 166.46  E-value: 1.73e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00023  41 IIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYS 120

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 970839877  81 DFM--NVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00023 121 DYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLN 191
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 2-149 2.16e-52

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 165.66  E-value: 2.16e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   2 MITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSD 81
Cdd:MTH00098  33 LISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTD 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 970839877  82 FMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00098 113 YEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLN 180
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-149 4.40e-52

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 164.89  E-value: 4.40e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   1 IMITIIVGYNLSYIIL----IKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWS 76
Cdd:MTH00129  28 LMIVFLISTLVLYIIVamvsTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWS 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970839877  77 YEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00129 108 YEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLN 180
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
64-149 2.41e-50

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 156.80  E-value: 2.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   64 ITIKTIGRQWYWSYEYSDFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80


                  ....*.
gi 970839877  144 TPGRLN 149
Cdd:pfam00116  81 VPGRLN 86
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-149 8.92e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 156.86  E-value: 8.92e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   1 IMITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00051  34 TIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYS 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 970839877  81 DF--MNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00051 114 DYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLN 184
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-149 2.63e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 135.92  E-value: 2.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   2 MITIIVGYNLSYIILIKFKAR------NMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSN-ETMITIKTIGRQWY 74
Cdd:MTH00027  58 ILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSANITIKVTGHQWY 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970839877  75 WSYEYSDF--MNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00027 138 WSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRIN 214
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 2-149 1.15e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 128.20  E-value: 1.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   2 MITIIVGYNLSYIILIKFKARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSN-ETMITIKTIGRQWYWSYEYS 80
Cdd:MTH00080  35 VLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFS 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839877  81 DFMNVEFDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00080 115 DIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILS 183
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
20-149 6.00e-24

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 92.58  E-value: 6.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877  20 KARNMLHGHMIEMIWTLIPAITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYsdfmnvefdtymlPEKElks 99
Cdd:COG1622   69 DPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQG--- 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 970839877 100 nnfrlLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:COG1622  133 -----IATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVT 177
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 30-149 8.54e-21

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 83.47  E-value: 8.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877  30 IEMIWTLIPAItLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSDfmNVEFDTYMlpekelksNNFRLLdVDN 109
Cdd:MTH00047  49 LELLWTVVPTL-LVLVLCFLNLNFITSDLDCFSSETIKVIGHQWYWSYEYSF--GGSYDSFM--------TDDIFG-VDK 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 970839877 110 RTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:MTH00047 117 PLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRIN 156
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-149 8.24e-20

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 81.27  E-value: 8.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877   13 YIILIKFKARN--------MLHGHM-IEMIWTLIPA-ITLIFIALPSLRLLYLLDDSNETMITIKTIGRQWYWSYEYSDF 82
Cdd:TIGR02866  30 LLAYVVWKFRRkgdeekpsQIHGNRrLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970839877   83 mnvefdtymlpekelksnnfrLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRLN 149
Cdd:TIGR02866 110 ---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTN 155
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 87-148 8.46e-19

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 77.55  E-value: 8.46e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 970839877  87 FDTYMLPEKELKSNNFRLLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDATPGRL 148
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRL 112
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 64-149 1.66e-12

Cupredoxin domain of Heme-copper oxidase subunit II; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 59.62  E-value: 1.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877  64 ITIKTIGRQWYWSYEYSDfmnvefdtymlpekelksnnfrlLDVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57


                 ....*.
gi 970839877 144 TPGRLN 149
Cdd:cd13842   58 VPGYTS 63
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-149 6.96e-12

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 58.02  E-value: 6.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877  64 ITIKTIGRQWYWSYEYSdfmnvefdtymlpekelksNNFRlldVDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13915    2 LEIQVTGRQWMWEFTYP-------------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59


                 ....*.
gi 970839877 144 TPGRLN 149
Cdd:cd13915   60 VPGRYT 65
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-149 1.85e-10

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 54.57  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877  64 ITIKTIGRQWYWSYEYsdfmnvefdtymlPEKELKSNNFRLLDVdNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13919    2 LVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67


                 ....*.
gi 970839877 144 TPGRLN 149
Cdd:cd13919   68 VPGRTT 73
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-150 4.01e-10

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 53.57  E-value: 4.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877  64 ITIKTIGRQWYWSYEYSDfmnvefdtymlpekelkSNNFRlldvDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPE-----------------ANVTT----SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59


                 ....*..
gi 970839877 144 TPGRLNL 150
Cdd:cd13914   60 FPGQYNT 66
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 64-149 6.73e-10

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 53.01  E-value: 6.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877  64 ITIKTIGRQWYWSYEYSDFMNVEFDTymlpekelksnnfrlldvDNRTVVPMNSEIRMLTSASDVLHSWTIPALGIKVDA 143
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63


                 ....*.
gi 970839877 144 TPGRLN 149
Cdd:cd04213   64 IPGRTN 69
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-46 1.05e-06

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 44.24  E-value: 1.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 970839877    1 IMITIIVGYNLSYIIL------IKFKARNMLHGHMIEMIWTLIPAITLIFIA 46
Cdd:pfam02790  32 TLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 57-149 5.21e-06

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 43.60  E-value: 5.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839877  57 DDSNETMITIKTIGRQWYWSYEYSDfmNVEFDTYMlpekelksnnfrlldvdnrtVVPMNSEIRMLTSASDVLHSWTIPA 136
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPE 83

                         90
                 ....*....|...
gi 970839877 137 LGIKVDATPGRLN 149
Cdd:cd13918   84 LRVKADAIPGEYT 96
 
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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