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Conserved domains on  [gi|1511931899|gb|AYV60943|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Glyphotmethis efe]

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
 1-151 2.46e-99

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 284.80  E-value: 2.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   1 TVLTLITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSY 80
Cdd:MTH00154   29 MILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSY 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511931899  81 EYSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00154  109 EYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-151 2.46e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 284.80  E-value: 2.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   1 TVLTLITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSY 80
Cdd:MTH00154   29 MILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSY 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511931899  81 EYSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00154  109 EYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 67-151 1.98e-53

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: 165.05  E-value: 1.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  67 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDA 146
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82


                  ....*
gi 1511931899 147 TPGRI 151
Cdd:cd13912    83 VPGRL 87
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
67-151 2.77e-48

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 151.79  E-value: 2.77e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  67 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDA 146
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80


                  ....*
gi 1511931899 147 TPGRI 151
Cdd:pfam00116  81 VPGRL 85
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-151 8.88e-29

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 105.30  E-value: 8.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   2 VLTLITIVVgysLSYML--MIKYSNR-------YVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTI 72
Cdd:COG1622    42 IMLVIFVLV---FGLLLyfAIRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVT 118

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1511931899  73 GRQWYWSYEYsdfvdvefdtymtPESDLEvdgfrlldVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:COG1622   119 GYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRV 176
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-150 4.50e-23

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: 89.75  E-value: 4.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   2 VLTLITIVVGYSLSYMlMIKYSNR-------YVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSID-ALITIKTIG 73
Cdd:TIGR02866  19 VSTLISLLVAALLAYV-VWKFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYLERPIPkDALKVKVTG 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1511931899  74 RQWYWSYEYSDFvdvefdtymtpesdlevdGFRlldVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGR 150
Cdd:TIGR02866  98 YQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQ 153
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-151 2.46e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 284.80  E-value: 2.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   1 TVLTLITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSY 80
Cdd:MTH00154   29 MILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSY 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511931899  81 EYSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00154  109 EYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 2-152 8.48e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 225.20  E-value: 8.48e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   2 VLTLITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSYE 81
Cdd:MTH00140   30 VLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYE 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511931899  82 YSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRIK 152
Cdd:MTH00140  110 YSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLN 180
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 2-150 4.32e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 213.24  E-value: 4.32e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   2 VLTLITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSYE 81
Cdd:MTH00117   30 VALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYE 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1511931899  82 YSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGR 150
Cdd:MTH00117  110 YTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGR 178
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 2-151 6.42e-71

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 213.18  E-value: 6.42e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   2 VLTLITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSYE 81
Cdd:MTH00008   30 ILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYE 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  82 YSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00008  110 YSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRL 179
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-150 1.75e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 211.76  E-value: 1.75e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   1 TVLTLITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSY 80
Cdd:MTH00168   29 LILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSY 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  81 EYSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGR 150
Cdd:MTH00168  109 EYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGR 178
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 2-151 9.00e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 209.94  E-value: 9.00e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   2 VLTLITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSYE 81
Cdd:MTH00038   30 ILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYE 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  82 YSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00038  110 YTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRL 179
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-151 9.75e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 209.96  E-value: 9.75e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   1 TVLTLITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSY 80
Cdd:MTH00139   29 VILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSY 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511931899  81 EYSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00139  109 EYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRL 179
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 5-151 5.10e-62

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 190.31  E-value: 5.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   5 LITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSYEYSD 84
Cdd:MTH00098   33 LISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTD 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1511931899  85 FVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00098  113 YEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRL 179
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-151 8.04e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 189.99  E-value: 8.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   2 VLTLITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSYE 81
Cdd:MTH00051   32 ILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYE 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1511931899  82 YSDF--VDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00051  112 YSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRL 183
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-151 2.36e-61

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 189.19  E-value: 2.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   2 VLTLITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSYE 81
Cdd:MTH00023   39 LLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYE 118

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1511931899  82 YSDFVD--VEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00023  119 YSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRL 190
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-151 4.17e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 185.69  E-value: 4.17e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   2 VLTLITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSYE 81
Cdd:MTH00129   30 IVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYE 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  82 YSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00129  110 YTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRL 179
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-151 1.86e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 183.93  E-value: 1.86e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   1 TVLTLITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSY 80
Cdd:MTH00185   29 MIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSY 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511931899  81 EYSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00185  109 EYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRL 179
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 5-151 3.43e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 183.06  E-value: 3.43e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   5 LITIVVGYSLSYMLMIKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTIGRQWYWSYEYSD 84
Cdd:MTH00076   33 LISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTD 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1511931899  85 FVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00076  113 YEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRL 179
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 67-151 1.98e-53

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: 165.05  E-value: 1.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  67 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDA 146
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82


                  ....*
gi 1511931899 147 TPGRI 151
Cdd:cd13912    83 VPGRL 87
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
67-151 2.77e-48

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 151.79  E-value: 2.77e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  67 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDA 146
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80


                  ....*
gi 1511931899 147 TPGRI 151
Cdd:pfam00116  81 VPGRL 85
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-151 1.08e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 155.18  E-value: 1.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   2 VLTLITIVVGYSLSYMLMIKYSNRYV------LHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSI-DALITIKTIGR 74
Cdd:MTH00027   55 ILFILTIIVGVVLWLIIRILLGNNYYsyywnkLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSANITIKVTGH 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1511931899  75 QWYWSYEYSDF--VDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00027  135 QWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRI 213
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 5-151 6.72e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 149.39  E-value: 6.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   5 LITIVVGYSLSYMLMIKYSNRYVlHGHLIETIWTTLPAITLIFIALPSLRLLYMLD-DSIDALITIKTIGRQWYWSYEYS 83
Cdd:MTH00080   36 LAFVVFLFLYLISNNFYFKSKKI-EYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVTGHQWYWSYEFS 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1511931899  84 DFVDVEFDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00080  115 DIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGIL 182
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-151 8.88e-29

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 105.30  E-value: 8.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   2 VLTLITIVVgysLSYML--MIKYSNR-------YVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSIDALITIKTI 72
Cdd:COG1622    42 IMLVIFVLV---FGLLLyfAIRYRRRkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVT 118

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1511931899  73 GRQWYWSYEYsdfvdvefdtymtPESDLEvdgfrlldVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:COG1622   119 GYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRV 176
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 32-151 4.47e-24

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 92.32  E-value: 4.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  32 LIETIWTTLPaiTLIFIALPSLRLLYMLDDSID-ALITIKTIGRQWYWSYEYSDfvDVEFDTYMTPESDLevdgfrlldV 110
Cdd:MTH00047   48 VLELLWTVVP--TLLVLVLCFLNLNFITSDLDCfSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG---------V 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1511931899 111 DNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:MTH00047  115 DKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRI 155
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-150 4.50e-23

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: 89.75  E-value: 4.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899   2 VLTLITIVVGYSLSYMlMIKYSNR-------YVLHGHLIETIWTTLPAITLIFIALPSLRLLYMLDDSID-ALITIKTIG 73
Cdd:TIGR02866  19 VSTLISLLVAALLAYV-VWKFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYLERPIPkDALKVKVTG 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1511931899  74 RQWYWSYEYSDFvdvefdtymtpesdlevdGFRlldVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGR 150
Cdd:TIGR02866  98 YQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQ 153
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 90-151 7.89e-18

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 75.24  E-value: 7.89e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1511931899  90 FDTYMTPESDLEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDATPGRI 151
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRL 112
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-55 1.59e-12

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: 59.65  E-value: 1.59e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511931899   1 TVLTLITIVVGYSLSYMLM------IKYSNRYVLHGHLIETIWTTLPAITLIFIALPSLRL 55
Cdd:pfam02790  29 FILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-153 3.09e-11

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: 56.88  E-value: 3.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  67 ITIKTIGRQWYWSYEYsdfvdvefdtymtPESDlEVDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDA 146
Cdd:cd13919     2 LVVEVTAQQWAWTFRY-------------PGGD-GKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67


                  ....*..
gi 1511931899 147 TPGRIKP 153
Cdd:cd13919    68 VPGRTTR 74
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 67-151 4.19e-11

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: 56.09  E-value: 4.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  67 ITIKTIGRQWYWSYEYSDFVDVEFDTymtpesdlevdgfrlldvDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDA 146
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63


                  ....*
gi 1511931899 147 TPGRI 151
Cdd:cd04213    64 IPGRT 68
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 67-150 8.39e-11

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: 55.38  E-value: 8.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  67 ITIKTIGRQWYWSYEYSDfvdvefdtymtpesdlevdgfrlLDVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDA 146
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57


                  ....
gi 1511931899 147 TPGR 150
Cdd:cd13842    58 VPGY 61
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-150 1.64e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 54.56  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  67 ITIKTIGRQWYWSYEYsdfvdvefdtymtpesdleVDGFRlldVDNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDA 146
Cdd:cd13915     2 LEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59


                  ....
gi 1511931899 147 TPGR 150
Cdd:cd13915    60 VPGR 63
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-150 7.45e-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: 53.18  E-value: 7.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  67 ITIKTIGRQWYWSYEYsdfvdvefdtymtPESdlEVDGFrlldvdNRTILPMNTEVRILTSASDVLHSWAVPSMGIKIDA 146
Cdd:cd13914     1 VEIEVEAYQWGWEFSY-------------PEA--NVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59


                  ....
gi 1511931899 147 TPGR 150
Cdd:cd13914    60 FPGQ 63
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 55-149 1.26e-04

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: 39.75  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511931899  55 LLYM----LDDSIDALiTIKTIGRQWYWSYEYSDFVDvefdtymtpesdlEVDGFRLldvdnrtilPMNTEVRILTSASD 130
Cdd:cd13918    18 LLYVedppDEADEDAL-EVEVEGFQFGWQFEYPNGVT-------------TGNTLRV---------PADTPIALRVTSTD 74

                          90
                  ....*....|....*....
gi 1511931899 131 VLHSWAVPSMGIKIDATPG 149
Cdd:cd13918    75 VFHTFGIPELRVKADAIPG 93
 
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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