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Conserved domains on  [gi|1079485409|ref|YP_009305762|]
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cytochrome c oxidase subunit II (mitochondrion) [Heteralocha acutirostris]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475905)

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 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 1.34e-171

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 470.94  E-value: 1.34e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLS-SSTVDAQEIELVvWTILPAIVLVTLALP 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELI-WTILPAIVLILLALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  80 SLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDV 159
Cdd:MTH00117   80 SLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079485409 160 LHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSSLMS 227
Cdd:MTH00117  160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 1.34e-171

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 470.94  E-value: 1.34e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLS-SSTVDAQEIELVvWTILPAIVLVTLALP 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELI-WTILPAIVLILLALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  80 SLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDV 159
Cdd:MTH00117   80 SLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079485409 160 LHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSSLMS 227
Cdd:MTH00117  160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 9.51e-98

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: 280.23  E-value: 9.51e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  93 PDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDVLHSWAVPSLGVKT 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1079485409 173 DAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.96e-86

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 250.79  E-value: 3.96e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  95 LTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDVLHSWAVPSLGVKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1079485409 175 IPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 9.06e-59

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 185.03  E-value: 9.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   6 QFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTL-------TEKLSSSTVDAQEIElVVWTILPAIVLVTLAL 78
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrrrkGDADPAQFHHNTKLE-IVWTVIPIIIVIVLAV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  79 PSLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTfdsymvpttdlplghfrllevDHRVVVPMESSVRVIVTADD 158
Cdd:COG1622    97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT---------------------VNELVLPVGRPVRFLLTSAD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1079485409 159 VLHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENW 222
Cdd:COG1622   156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 3.54e-48

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: 157.16  E-value: 3.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  12 ASSPIMEELVEFHDHALMVALAICSLVLYLMALTL-------TEKLSSSTVDAQEIElVVWTILPAIVLVTL-ALPSLRI 83
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkgDEEKPSQIHGNRRLE-YVWTVIPLIIVVGLfAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  84 LYMMDEINEPDLTLKAIGHQWYWSYEYtdfKDLTFdsymvpttdlplghfrllEVDHRVVVPMESSVRVIVTADDVLHSW 163
Cdd:TIGR02866  80 LYLERPIPKDALKVKVTGYQWWWDFEY---PESGF------------------TTVNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1079485409 164 AVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENW 222
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 1.34e-171

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 470.94  E-value: 1.34e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLS-SSTVDAQEIELVvWTILPAIVLVTLALP 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELI-WTILPAIVLILLALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  80 SLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDV 159
Cdd:MTH00117   80 SLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079485409 160 LHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSSLMS 227
Cdd:MTH00117  160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-226 4.41e-142

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 396.40  E-value: 4.41e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLS-SSTVDAQEIElVVWTILPAIVLVTLALP 79
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLThTSTMDAQEVE-TIWTILPAIILILIALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  80 SLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDV 159
Cdd:MTH00098   80 SLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1079485409 160 LHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSSLM 226
Cdd:MTH00098  160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-226 6.20e-139

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 388.30  E-value: 6.20e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLSSS-TVDAQEIElVVWTILPAIVLVTLALP 79
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKyILDSQEIE-IIWTVLPAVILILIALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  80 SLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDV 159
Cdd:MTH00129   80 SLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1079485409 160 LHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSSLM 226
Cdd:MTH00129  160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 3.02e-138

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 386.44  E-value: 3.02e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLSSS-TVDAQEIELVvWTILPAIVLVTLALP 79
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTnTMDAQEIEMV-WTIMPAIILIVIALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  80 SLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDV 159
Cdd:MTH00076   80 SLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1079485409 160 LHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSSLM 226
Cdd:MTH00076  160 LHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 3.33e-136

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 381.48  E-value: 3.33e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLSSSTV-DAQEIELVvWTILPAIVLVTLALP 79
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLlEGQEIEII-WTILPAIILIFIALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  80 SLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDV 159
Cdd:MTH00154   80 SLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079485409 160 LHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSSLMS 227
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-226 4.59e-129

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 363.44  E-value: 4.59e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLSSS-TVDAQEIElVVWTILPAIVLVTLALP 79
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKyILDSQEIE-IVWTILPAIILIMIALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  80 SLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDV 159
Cdd:MTH00185   80 SLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1079485409 160 LHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSSLM 226
Cdd:MTH00185  160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 3.73e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 360.84  E-value: 3.73e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLSSSTV-DAQEIELVvWTILPAIVLVTLALP 79
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLlDSQMIEFV-WTIIPAFILISLALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  80 SLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDV 159
Cdd:MTH00168   80 SLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1079485409 160 LHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSS 224
Cdd:MTH00168  160 LHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-228 1.34e-127

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 359.64  E-value: 1.34e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLSSSTV-DAQEIElVVWTILPAIVLVTLALP 79
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTIlEAQKLE-TIWTIVPALILVFLALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  80 SLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDV 159
Cdd:MTH00140   80 SLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1079485409 160 LHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSSLMSS 228
Cdd:MTH00140  160 IHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMSE 228
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-224 3.09e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 351.31  E-value: 3.09e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLtekLSSST----VDAQEIELVvWTILPAIVLVTL 76
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLL---FSSPTnrffLEGQELETI-WTIVPAFILIFI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  77 ALPSLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTA 156
Cdd:MTH00038   77 ALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSS 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079485409 157 DDVLHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSS 224
Cdd:MTH00038  157 ADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-222 3.13e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 345.93  E-value: 3.13e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLSSST-VDAQEIElVVWTILPAIVLVTLALP 79
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSlLESQEVE-TIWTVLPAFILLFLALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  80 SLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDV 159
Cdd:MTH00139   80 SLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1079485409 160 LHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENW 222
Cdd:MTH00139  160 LHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-228 1.57e-114

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 326.43  E-value: 1.57e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLSSSTV-DAQEIElVVWTILPAIVLVTLALP 79
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYIlEAQQIE-TIWTILPALILLFLAFP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  80 SLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDV 159
Cdd:MTH00008   80 SLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1079485409 160 LHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSSLMSS 228
Cdd:MTH00008  160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-228 6.64e-105

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 302.82  E-value: 6.64e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   6 QFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEK-LSSSTVDAQEIElVVWTILPAIVLVTLALPSLRIL 84
Cdd:MTH00023   15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKfYDRFLVDGTFLE-IVWTIIPAVILVFIALPSLKLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  85 YMMDEINEPDLTLKAIGHQWYWSYEYTDFKD--LTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDVLHS 162
Cdd:MTH00023   94 YLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHS 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1079485409 163 WAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSSLMSS 228
Cdd:MTH00023  174 FAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-222 7.01e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 294.77  E-value: 7.01e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   6 QFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEK-LSSSTVDAQEIElVVWTILPAIVLVTLALPSLRIL 84
Cdd:MTH00051    8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKyYHKYLFEGTLIE-IIWTLIPAAILIFIAFPSLKLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  85 YMMDEINEPDLTLKAIGHQWYWSYEYTDF--KDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDVLHS 162
Cdd:MTH00051   87 YLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHS 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409 163 WAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENW 222
Cdd:MTH00051  167 FAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINW 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 9.51e-98

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: 280.23  E-value: 9.51e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  93 PDLTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDVLHSWAVPSLGVKT 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1079485409 173 DAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.96e-86

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 250.79  E-value: 3.96e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  95 LTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDVLHSWAVPSLGVKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1079485409 175 IPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-222 1.72e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 251.87  E-value: 1.72e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   6 QFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLSSS----TVDAQEIElVVWTILPAIVLVTLALPSL 81
Cdd:MTH00027   34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywnKLDGSLIE-VIWTLIPAFILILIAFPSL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  82 RILYMMDE-INEPDLTLKAIGHQWYWSYEYTDF--KDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADD 158
Cdd:MTH00027  113 RLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAAD 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1079485409 159 VLHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENW 222
Cdd:MTH00027  193 VLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-226 5.53e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 229.13  E-value: 5.53e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  23 FHDHALMVALAICSLV-LYLMALTLTEKLSSSTVDAQEIELVvWTILPAIVLVTLALPSLRILYMMDEIN-EPDLTLKAI 100
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVfLFLYLISNNFYFKSKKIEYQFGELL-CSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409 101 GHQWYWSYEYTDFKDLTFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDVLHSWAVPSLGVKTDAIPGRLN 180
Cdd:MTH00080  104 GHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILS 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1079485409 181 QTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENWSSLM 226
Cdd:MTH00080  184 TLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLL 229
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 9.06e-59

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 185.03  E-value: 9.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   6 QFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTL-------TEKLSSSTVDAQEIElVVWTILPAIVLVTLAL 78
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrrrkGDADPAQFHHNTKLE-IVWTVIPIIIVIVLAV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  79 PSLRILYMMDEINEPDLTLKAIGHQWYWSYEYTDFKDLTfdsymvpttdlplghfrllevDHRVVVPMESSVRVIVTADD 158
Cdd:COG1622    97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT---------------------VNELVLPVGRPVRFLLTSAD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1079485409 159 VLHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENW 222
Cdd:COG1622   156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 3.54e-48

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: 157.16  E-value: 3.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  12 ASSPIMEELVEFHDHALMVALAICSLVLYLMALTL-------TEKLSSSTVDAQEIElVVWTILPAIVLVTL-ALPSLRI 83
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkgDEEKPSQIHGNRRLE-YVWTVIPLIIVVGLfAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  84 LYMMDEINEPDLTLKAIGHQWYWSYEYtdfKDLTFdsymvpttdlplghfrllEVDHRVVVPMESSVRVIVTADDVLHSW 163
Cdd:TIGR02866  80 LYLERPIPKDALKVKVTGYQWWWDFEY---PESGF------------------TTVNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1079485409 164 AVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENW 222
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 26-214 3.72e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 146.64  E-value: 3.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  26 HALMVALAICSLVLYLMALTLTEKLSSSTV--DAQEIELVvWTILPA-IVLVTLALPSLRILYMMDeiNEPDLTLKAIGH 102
Cdd:MTH00047   13 YILALCVFIPCWVYIMLCWQVVSGNGSVNFgsENQVLELL-WTVVPTlLVLVLCFLNLNFITSDLD--CFSSETIKVIGH 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409 103 QWYWSYEYTDfkDLTFDSYMVPTTDLplghfrlleVDHRVVVPMESSVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQT 182
Cdd:MTH00047   90 QWYWSYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHL 158

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1079485409 183 SFTASRPGVFYGQCSEICGANHSFMPIVVEAI 214
Cdd:MTH00047  159 FFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-214 3.44e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 135.33  E-value: 3.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409 117 TFDSYMVPTTDLPLGHFRLLEVDHRVVVPMESSVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQC 196
Cdd:PTZ00047   50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                          90
                  ....*....|....*...
gi 1079485409 197 SEICGANHSFMPIVVEAI 214
Cdd:PTZ00047  130 SEMCGTLHGFMPIVVEAV 147
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.81e-31

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: 110.85  E-value: 1.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  95 LTLKAIGHQWYWSYEYTDfkdltfdsymvpttdlplghfrlLEVDHRVVVPMESSVRVIVTADDVLHSWAVPSLGVKTDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1079485409 175 IPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVE 212
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-213 8.28e-30

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: 106.94  E-value: 8.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  94 DLTLKAIGHQWYWSYEYTDFKDLTFdsymVPTTDLplghfrllevdhrvVVPMESSVRVIVTADDVLHSWAVPSLGVKTD 173
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGI----VTANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1079485409 174 AIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEA 213
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIA 102
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 60-222 1.10e-25

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: 97.14  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  60 IELVVWTILpaivlvtlalpslRILYMMD---EINEPDLTLKAIGHQWYWSYEYTDfkDLTFDSYMVpttdlplghfrll 136
Cdd:cd13918     8 ISLIVWTYG-------------MLLYVEDppdEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTLR------------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409 137 evdhrvvVPMESSVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPL 216
Cdd:cd13918    60 -------VPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDE 132


                  ....*.
gi 1079485409 217 ANFENW 222
Cdd:cd13918   133 EEFEAW 138
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 2.20e-25

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: 95.09  E-value: 2.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409   1 MANHSQFGFQDASSPIMEELVEFHDHALMVALAICSLVLYLMALTLTEKLSSS-------TVDAQEIElVVWTILPAIVL 73
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKnpitaryTTHGQTIE-IIWTIIPAVIL 79

                          90
                  ....*....|
gi 1079485409  74 VTLALPSLRI 83
Cdd:pfam02790  80 ILIALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-212 1.86e-24

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: 93.09  E-value: 1.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  94 DLTLKAIGHQWYWSYEY--TDFKDLTFDSYMVPTTDLPLGHfrllevdhrvvvpmesSVRVIVTADDVLHSWAVPSLGVK 171
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYpgGDGKLGTDDDVTSPELHLPVGR----------------PVLFNLRSKDVIHSFWVPEFRVK 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1079485409 172 TDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13919    65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-213 2.92e-22

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: 87.30  E-value: 2.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  94 DLTLKAIGHQWYWSYEYTDFKdltfdsymvpttdlplghfrllEVDHRVVVPMESSVRVIVTADDVLHSWAVPSLGVKTD 173
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGK----------------------REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1079485409 174 AIPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEA 213
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 3.01e-19

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: 79.76  E-value: 3.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  96 TLKAIGHQWYWSYEYTDFKDLTFDsymvpttdlplghfrllevdhRVVVPMESSVRVIVTADDVLHSWAVPSLGVKTDAI 175
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEANVTTSE---------------------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1079485409 176 PGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAIPLANFENW 222
Cdd:cd13914    61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 142-212 1.08e-10

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 56.42  E-value: 1.08e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1079485409 142 VVVPMESSVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13913    27 IEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 150-207 7.18e-07

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 46.07  E-value: 7.18e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1079485409 150 VRVIVT----ADDVLHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFM 207
Cdd:cd04223    26 VTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 133-212 1.18e-06

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 46.07  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409 133 FRLLEVDHRVVVPMESSVRVIVT-ADDVLHSWAVPSLGVKTDAI---------------PGRLNQTSFTASRPGVFYGQC 196
Cdd:cd00920    16 GVLLFGPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYWFYC 95

                          90
                  ....*....|....*.
gi 1079485409 197 SEICGaNHSFMPIVVE 212
Cdd:cd00920    96 TIPGH-NHAGMVGTIN 110
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 41-222 3.73e-06

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 46.72  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  41 LMALTLTEKLSSSTVDAQ---------EIELVVWTIlPAIVLVTLALPSLRILYMMDEI-----NEPDLTLKAIGHQWYW 106
Cdd:PRK10525   60 LMAVGFAWKYRASNKDAKyspnwshsnKVEAVVWTV-PILIIIFLAVLTWKTTHALEPSkplahDEKPITIEVVSMDWKW 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409 107 SYEYTDFKDLTFDSYMVPTTdlplghfrllevdhrvvVPmessVRVIVTADDVLHSWAVPSLGVKTDAIPGRLNQTSFTA 186
Cdd:PRK10525  139 FFIYPEQGIATVNEIAFPAN-----------------VP----VYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIA 197

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1079485409 187 SRPGVFYGQCSEICGANHSFMPIVVEAIP-LANFENW 222
Cdd:PRK10525  198 NEPGTYDGISASYSGPGFSGMKFKAIATPdRAEFDQW 234
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 1.04e-05

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: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 42.75  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  96 TLKAIGHQWYWSyeytdfkdltfdsyMVPTTdlplghfrllevdhrvvVPMESSVRVIVTADDVLHSWAVPS----LGVK 171
Cdd:cd13916     2 VVAVTGHQWYWE--------------LSRTE-----------------IPAGKPVEFRVTSADVNHGFGIYDpdmrLLAQ 50

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1079485409 172 TDAIPGRLNQTSFTASRPGVFYGQCSEICGANHSFM 207
Cdd:cd13916    51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 121-213 3.86e-05

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 44.20  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409 121 YMV---PTTDLPlgHFRLLEVDHrvvvpmessVRVIVT----ADDVLHSWAVPSLGVKTDAIPGRLNQTSFTASRPGVFY 193
Cdd:PRK02888  544 YMTsqaPAFGLR--EFTVKQGDE---------VTVIVTnldkVEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYW 612

                          90       100
                  ....*....|....*....|..
gi 1079485409 194 GQCSEICGANHSFMP--IVVEA 213
Cdd:PRK02888  613 YYCTWFCHALHMEMRgrMLVEP 634
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 95-214 1.60e-03

The cupredoxin domain of Ubiquinol oxidase subunit II; 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. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 36.76  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079485409  95 LTLKAIGHQWYWSYEYTDFKDLTFDSYMVPTtDLPLgHFRLlevdhrvvvpmessvrvivTADDVLHSWAVPSLGVKTDA 174
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQGIATVNELVIPV-GRPV-NFRL-------------------TSDSVMNSFFIPQLGGQIYA 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1079485409 175 IPGRLNQTSFTASRPGVFYGQCSEICGANHSFMPIVVEAI 214
Cdd:cd04212    60 MAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
 
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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