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Conserved domains on  [gi|1773401166|ref|NP_001362964|]
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cytochrome c oxidase subunit 2, mitochondrial [Vigna unguiculata]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 super family cl31789
cytochrome c oxidase subunit II; Provisional
 145-384 4.27e-117

cytochrome c oxidase subunit II; Provisional


The actual alignment was detected with superfamily member MTH00051:

Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 339.83  E-value: 4.27e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 145 DAPEPWQLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALwcfrskISPIPQR-IVHGTTIEILWTILPSIIL 223
Cdd:MTH00051    2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRAL------TTKYYHKyLFEGTLIEIIWTLIPAAIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 224 MFIAIPSFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeQSLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAK 303
Cdd:MTH00051   76 IFIAFPSLKLLYLMDEVI-DPALTIKAIGHQWYWSYEYSDYGT---DTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 304 THLRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSNQI 383
Cdd:MTH00051  152 TQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQS 231


                  .
gi 1773401166 384 Q 384
Cdd:MTH00051  232 E 232
 
Name Accession Description Interval E-value
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 145-384 4.27e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 339.83  E-value: 4.27e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 145 DAPEPWQLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALwcfrskISPIPQR-IVHGTTIEILWTILPSIIL 223
Cdd:MTH00051    2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRAL------TTKYYHKyLFEGTLIEIIWTLIPAAIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 224 MFIAIPSFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeQSLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAK 303
Cdd:MTH00051   76 IFIAFPSLKLLYLMDEVI-DPALTIKAIGHQWYWSYEYSDYGT---DTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 304 THLRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSNQI 383
Cdd:MTH00051  152 TQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQS 231


                  .
gi 1773401166 384 Q 384
Cdd:MTH00051  232 E 232
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 244-378 2.59e-97

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: 285.23  E-value: 2.59e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 244 PAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLRVLITSADVLHSWAVPS 323
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1773401166 324 LGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSW 378
Cdd:cd13912    76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
246-370 3.84e-84

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 251.56  E-value: 3.84e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 246 ITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLRVLITSADVLHSWAVPSLG 325
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1773401166 326 VKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAV 370
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
134-382 2.37e-70

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 220.09  E-value: 2.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 134 MCGGFPAIALCDAPEPWQLGFQDAATPIMQGIMDLHHDIFFF--LVQILVFVLWVLsrALWCFR-SKISPIPQRIVHGTT 210
Cdd:COG1622     1 MKRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIImlVIFVLVFGLLLY--FAIRYRrRKGDADPAQFHHNTK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 211 IEILWTILPSIILMFIAIPSFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeqslafdsymvpeddlelgqlr 290
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAP-EDPLTVEVTGYQWKWLFRYPDQGI------------------------ 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 291 llEVDNRVVVPAKTHLRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAV 370
Cdd:COG1622   134 --ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVV 211

                         250
                  ....*....|..
gi 1773401166 371 STKDYGSWVSNQ 382
Cdd:COG1622   212 SPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 157-380 1.85e-53

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: 175.65  E-value: 1.85e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 157 AATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALWCFRSKIS-PIPQRIVHGTTIEILWTILPSIILMFIAIPSFTLLY 235
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGDeEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 236 SMDDVVVDPAITIKAIGHQWYWSYEYSDYnnsdeqslafdsymvpeddlelgqlrLLEVDNRVVVPAKTHLRVLITSADV 315
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1773401166 316 LHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVS 380
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 145-384 4.27e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 339.83  E-value: 4.27e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 145 DAPEPWQLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALwcfrskISPIPQR-IVHGTTIEILWTILPSIIL 223
Cdd:MTH00051    2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRAL------TTKYYHKyLFEGTLIEIIWTLIPAAIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 224 MFIAIPSFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeQSLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAK 303
Cdd:MTH00051   76 IFIAFPSLKLLYLMDEVI-DPALTIKAIGHQWYWSYEYSDYGT---DTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 304 THLRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSNQI 383
Cdd:MTH00051  152 TQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQS 231


                  .
gi 1773401166 384 Q 384
Cdd:MTH00051  232 E 232
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 145-384 1.39e-116

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 338.65  E-value: 1.39e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 145 DAPEPWQLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALwcfrsKISPIPQRIVHGTTIEILWTILPSIILM 224
Cdd:MTH00023    9 DIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEAL-----NGKFYDRFLVDGTFLEIVWTIIPAVILV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 225 FIAIPSFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYnnsDEQSLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKT 304
Cdd:MTH00023   84 FIALPSLKLLYLMDEVV-SPALTIKAIGHQWYWSYEYSDY---EGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 305 HLRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSNQIQ 384
Cdd:MTH00023  160 HVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 151-383 2.29e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 324.86  E-value: 2.29e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 151 QLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALwcFRSKISpipQRIVHGTTIEILWTILPSIILMFIAIPS 230
Cdd:MTH00154    6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLL--FNKFTN---RFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 231 FTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLRVLI 310
Cdd:MTH00154   81 LRLLYLLDEVN-NPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILI 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1773401166 311 TSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSNQI 383
Cdd:MTH00154  155 TAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 147-382 5.44e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 321.48  E-value: 5.44e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 147 PEPWQLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALwcfRSKISpipqrivHGTT-----IEILWTILPSI 221
Cdd:MTH00117    2 ANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLML---TTKLT-------HTNTvdaqeVELIWTILPAI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 222 ILMFIAIPSFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVP 301
Cdd:MTH00117   72 VLILLALPSLRILYLMDEIN-NPHLTIKAIGHQWYWSYEYTDYKD-----LSFDSYMIPTQDLPNGHFRLLEVDHRMVIP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 302 AKTHLRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSN 381
Cdd:MTH00117  146 MESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225


                  .
gi 1773401166 382 Q 382
Cdd:MTH00117  226 L 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 151-381 3.55e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 311.49  E-value: 3.55e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 151 QLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALWcfrSKISPIpqRIVHGTTIEILWTILPSIILMFIAIPS 230
Cdd:MTH00140    6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLF---NKFSCR--TILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 231 FTLLYSMDdVVVDPAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLRVLI 310
Cdd:MTH00140   81 LRLLYLLD-ETNNPLLTVKAIGHQWYWSYEYSDFSV-----IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1773401166 311 TSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSN 381
Cdd:MTH00140  155 TSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 149-384 3.95e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 311.64  E-value: 3.95e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 149 PWQLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALWcfrskISPIPQRIVHGTTIEILWTILPSIILMFIAI 228
Cdd:MTH00038    4 WLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLF-----SSPTNRFFLEGQELETIWTIVPAFILIFIAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 229 PSFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLRV 308
Cdd:MTH00038   79 PSLQLLYLMDEVN-NPFLTIKAIGHQWYWSYEYTDYND-----LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRV 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1773401166 309 LITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSNQIQ 384
Cdd:MTH00038  153 LVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLE 228
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 151-381 5.18e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 306.26  E-value: 5.18e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 151 QLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALW-CFRSKiSPIPQRIVhgttiEILWTILPSIILMFIAIP 229
Cdd:MTH00139    6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSnKFTSR-SLLESQEV-----ETIWTVLPAFILLFLALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 230 SFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLRVL 309
Cdd:MTH00139   80 SLRLLYLMDEVS-DPYLTFKAVGHQWYWSYEYSDFKN-----LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRAL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1773401166 310 ITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSN 381
Cdd:MTH00139  154 ITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 151-381 1.33e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 302.67  E-value: 1.33e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 151 QLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLsraLWCFRSKisPIPQRIVHGTTIEILWTILPSIILMFIAIPS 230
Cdd:MTH00168    6 QLGLQDAASPVMEELILFHDHALLILVLILTLVLYSL---LVLVTSK--YTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 231 FTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLRVLI 310
Cdd:MTH00168   81 LRLLYLMDEID-KPDLTIKAVGHQWYWSYEYTDYND-----LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1773401166 311 TSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSN 381
Cdd:MTH00168  155 TSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 147-380 5.10e-100

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 295.86  E-value: 5.10e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 147 PEPWQLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALwcfrskispiPQRIVHGTT-----IEILWTILPSI 221
Cdd:MTH00098    2 AYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLML----------TTKLTHTSTmdaqeVETIWTILPAI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 222 ILMFIAIPSFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVP 301
Cdd:MTH00098   72 ILILIALPSLRILYMMDEIN-NPSLTVKTMGHQWYWSYEYTDYED-----LSFDSYMIPTSDLKPGELRLLEVDNRVVLP 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1773401166 302 AKTHLRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVS 380
Cdd:MTH00098  146 MEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSA 224
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 244-378 2.59e-97

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: 285.23  E-value: 2.59e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 244 PAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLRVLITSADVLHSWAVPS 323
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1773401166 324 LGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSW 378
Cdd:cd13912    76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 149-384 1.42e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 287.38  E-value: 1.42e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 149 PWQLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALwcfRSKISPipQRIVHGTTIEILWTILPSIILMFIAI 228
Cdd:MTH00129    4 PSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMV---STKLTN--KYILDSQEIEIIWTVLPAVILILIAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 229 PSFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLRV 308
Cdd:MTH00129   79 PSLRILYLMDEIN-DPHLTIKAMGHQWYWSYEYTDYED-----LGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRV 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1773401166 309 LITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSNQIQ 384
Cdd:MTH00129  153 LVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLE 228
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 149-382 6.22e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 285.52  E-value: 6.22e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 149 PWQLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALWCFRSKISPIPQRivhgtTIEILWTILPSIILMFIAI 228
Cdd:MTH00076    4 PSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQ-----EIEMVWTIMPAIILIVIAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 229 PSFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLRV 308
Cdd:MTH00076   79 PSLRILYLMDEIN-DPHLTVKAIGHQWYWSYEYTDYED-----LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRM 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1773401166 309 LITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSNQ 382
Cdd:MTH00076  153 LITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 151-381 6.92e-94

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 280.59  E-value: 6.92e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 151 QLGFQDAATPIMQGIMDLH-HDIFfflvqILVFVLWVLSRALWC--FRSKISpipQRIVHGTTIEILWTILPSIILMFIA 227
Cdd:MTH00008    6 QLMFQDAASPVMLQLISFHdHALL-----ILTLVLTVVGYAMTSlmFNKLSN---RYILEAQQIETIWTILPALILLFLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 228 IPSFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLR 307
Cdd:MTH00008   78 FPSLRLLYLMDEVS-NPSITLKTIGHQWYWSYEYSDFSN-----LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIR 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1773401166 308 VLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSN 381
Cdd:MTH00008  152 VLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 148-384 6.19e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 275.61  E-value: 6.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 148 EPWQLGFQDAATPIMQGIMDLH-HDIFF-FLVQILVFVLwVLSRALWCFRSKIspipqrIVHGTTIEILWTILPSIILMF 225
Cdd:MTH00185    3 HPSQLGLQDAASPVMEELIHFHdHTLMIvFLISTLVLYI-IVAMVTTKLTNKY------ILDSQEIEIVWTILPAIILIM 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 226 IAIPSFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTH 305
Cdd:MTH00185   76 IALPSLRILYLMDEIN-DPHLTIKAMGHQWYWSYEYTDYEQ-----LEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESP 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1773401166 306 LRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVSNQIQ 384
Cdd:MTH00185  150 IRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLE 228
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 139-382 1.11e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 276.14  E-value: 1.11e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 139 PAIALCDAPEPWQLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALwcFRSKISPIPQRIVHGTTIEILWTIL 218
Cdd:MTH00027   22 VASMIKDANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRIL--LGNNYYSYYWNKLDGSLIEVIWTLI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 219 PSIILMFIAIPSFTLLYSMDDVVVDPAITIKAIGHQWYWSYEYSDYNnsdEQSLAFDSYMVPEDDLELGQLRLLEVDNRV 298
Cdd:MTH00027  100 PAFILILIAFPSLRLLYIMDECGFSANITIKVTGHQWYWSYSYEDYG---EKNIEFDSYMIPTADLEFGDLRLLEVDNRL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 299 VVPAKTHLRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSW 378
Cdd:MTH00027  177 ILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256


                  ....
gi 1773401166 379 VSNQ 382
Cdd:MTH00027  257 IGRE 260
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
246-370 3.84e-84

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 251.56  E-value: 3.84e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 246 ITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLRVLITSADVLHSWAVPSLG 325
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1773401166 326 VKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAV 370
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 166-378 6.63e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 221.81  E-value: 6.63e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 166 MDLHHDIFFFLVQILVFVLWV---LSRALWCFRSKISpipqrivHGTTIEILWTILPSIILMFIAIPSFTLLYSMDDVVV 242
Cdd:MTH00080   22 FHNFNCSLLFGEFVLAFVVFLflyLISNNFYFKSKKI-------EYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 243 DPAITIKAIGHQWYWSYEYSDYNNsdeqsLAFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLRVLITSADVLHSWAVP 322
Cdd:MTH00080   95 DSNLTVKVTGHQWYWSYEFSDIPG-----LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALP 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1773401166 323 SLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSW 378
Cdd:MTH00080  170 SLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEW 225
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
134-382 2.37e-70

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 220.09  E-value: 2.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 134 MCGGFPAIALCDAPEPWQLGFQDAATPIMQGIMDLHHDIFFF--LVQILVFVLWVLsrALWCFR-SKISPIPQRIVHGTT 210
Cdd:COG1622     1 MKRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIImlVIFVLVFGLLLY--FAIRYRrRKGDADPAQFHHNTK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 211 IEILWTILPSIILMFIAIPSFTLLYSMDDVVvDPAITIKAIGHQWYWSYEYSDYNNsdeqslafdsymvpeddlelgqlr 290
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAP-EDPLTVEVTGYQWKWLFRYPDQGI------------------------ 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 291 llEVDNRVVVPAKTHLRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAV 370
Cdd:COG1622   134 --ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVV 211

                         250
                  ....*....|..
gi 1773401166 371 STKDYGSWVSNQ 382
Cdd:COG1622   212 SPEEFDAWLAEQ 223
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 273-375 3.62e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 178.86  E-value: 3.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 273 AFDSYMVPEDDLELGQLRLLEVDNRVVVPAKTHLRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQC 352
Cdd:PTZ00047   50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                          90       100
                  ....*....|....*....|...
gi 1773401166 353 SEICGTNHAFMPIVVEAVSTKDY 375
Cdd:PTZ00047  130 SEMCGTLHGFMPIVVEAVSPEAY 152
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 157-380 1.85e-53

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: 175.65  E-value: 1.85e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 157 AATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALWCFRSKIS-PIPQRIVHGTTIEILWTILPSIILMFIAIPSFTLLY 235
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGDeEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 236 SMDDVVVDPAITIKAIGHQWYWSYEYSDYnnsdeqslafdsymvpeddlelgqlrLLEVDNRVVVPAKTHLRVLITSADV 315
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1773401166 316 LHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWVS 380
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 210-370 2.41e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 149.33  E-value: 2.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 210 TIEILWTILPSIILMFIAipSFTLLYSMDDVVVDPAITIKAIGHQWYWSYEYSDynnsdeqSLAFDSYMVpeDDLELgql 289
Cdd:MTH00047   48 VLELLWTVVPTLLVLVLC--FLNLNFITSDLDCFSSETIKVIGHQWYWSYEYSF-------GGSYDSFMT--DDIFG--- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 290 rlleVDNRVVVPAKTHLRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEA 369
Cdd:MTH00047  114 ----VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEV 189


                  .
gi 1773401166 370 V 370
Cdd:MTH00047  190 V 190
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 146-233 2.74e-35

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: 124.75  E-value: 2.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 146 APEPWQLGFQDAATPIMQGIMDLHHDIFFFLVQILVFVLWVLSRALWCFRSKISPIPQR-IVHGTTIEILWTILPSIILM 224
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARyTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1773401166 225 FIAIPSFTL 233
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 246-368 1.66e-26

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: 101.60  E-value: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 246 ITIKAIGHQWYWSYEYSDynnsdeqslafdsymvpeddlelgqlrlLEVDNRVVVPAKTHLRVLITSADVLHSWAVPSLG 325
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN----------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLG 52

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1773401166 326 VKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVE 368
Cdd:cd13842    53 VKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 245-370 2.97e-26

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: 101.16  E-value: 2.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 245 AITIKAIGHQWYWSYEYSDYnnsdeqslafdsymvPEDDLELGqlrllevdNRVVVPAKTHLRVLITSADVLHSWAVPSL 324
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDE---------------PGRGIVTA--------NELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1773401166 325 GVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAV 370
Cdd:cd04213    58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 246-379 2.06e-23

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: 93.63  E-value: 2.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 246 ITIKAIGHQWYWSYEYSDYNNSDEQSLafdsymvpeddlelgqlrllevdnrvVVPAKTHLRVLITSADVLHSWAVPSLG 325
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEANVTTSEQL--------------------------VIPADRPVYFRITSRDVIHAFHVPELG 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1773401166 326 VKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAVSTKDYGSWV 379
Cdd:cd13914    55 LKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 245-368 2.34e-23

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: 93.47  E-value: 2.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 245 AITIKAIGHQWYWSYEYSDYnnsdeqslafDSYMVPEDDLELGQLRLlEVDNRVvvpakthlRVLITSADVLHSWAVPSL 324
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGG----------DGKLGTDDDVTSPELHL-PVGRPV--------LFNLRSKDVIHSFWVPEF 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1773401166 325 GVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFM--PIVVE 368
Cdd:cd13919    62 RVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 245-369 2.66e-20

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: 84.60  E-value: 2.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 245 AITIKAIGHQWYWSYEYSDynnsdeqslafdsymvpeddlelGQlrllEVDNRVVVPAKTHLRVLITSADVLHSWAVPSL 324
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPN-----------------------GK----REINELHVPVGKPVRLILTSKDVIHSFYVPAF 53

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1773401166 325 GVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEA 369
Cdd:cd13915    54 RIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 217-379 4.90e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 82.50  E-value: 4.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 217 ILPSIILM-FIAIPSFTLLY--SMDDVVVDPAITIKAIGHQWYWSYEYSDynnsdeqslafdsymvpeddlELGQLrlle 293
Cdd:cd13918     1 GLSAIIVIsLIVWTYGMLLYveDPPDEADEDALEVEVEGFQFGWQFEYPN---------------------GVTTG---- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 294 vdNRVVVPAKTHLRVLITSADVLHSWAVPSLGVKCDAVPGRLNqiSTFIQRE--GVYYGQCSEICGTNHAFMPIVVEAVS 371
Cdd:cd13918    56 --NTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYT--STWFEADepGTYEAKCYELCGSGHSLMTGDVIVMD 131


                  ....*...
gi 1773401166 372 TKDYGSWV 379
Cdd:cd13918   132 EEEFEAWY 139
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 296-368 7.33e-09

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: 52.57  E-value: 7.33e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1773401166 296 NRVVVPAKTHLRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFM--PIVVE 368
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 289-368 1.66e-05

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: 43.37  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 289 LRLLEVDNRVVVPAKTHLRVLITS-ADVLHSWAVPSLGVKCDA---------------VPGRLNQISTFIQREGVYYGQC 352
Cdd:cd00920    16 GVLLFGPPVLVVPVGDTVRVQFVNkLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVYWFYC 95

                          90
                  ....*....|....*.
gi 1773401166 353 SEICGtNHAFMPIVVE 368
Cdd:cd00920    96 TIPGH-NHAGMVGTIN 110
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 246-363 7.08e-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: 41.21  E-value: 7.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 246 ITIKAIGHQWYWSyeysdynnsdeqslafdsymVPEDDLELGQLrlleVDNRVvvpakthlrvliTSADVLHSWAVPS-- 323
Cdd:cd13916     1 QVVAVTGHQWYWE--------------------LSRTEIPAGKP----VEFRV------------TSADVNHGFGIYDpd 44

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1773401166 324 --LGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFM 363
Cdd:cd13916    45 mrLLAQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 246-370 1.99e-04

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: 40.22  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 246 ITIKAIGHQWYWSYEYSDYNnsdeqslafdsymvpeddlelgqlrlLEVDNRVVVPAKTHLRVLITSADVLHSWAVPSLG 325
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQG--------------------------IATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLG 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1773401166 326 VKCDAVPGRLNQISTFIQREGVYYGQCSEICGTNHAFMPIVVEAV 370
Cdd:cd04212    55 GQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 207-381 6.80e-04

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 41.32  E-value: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 207 HGTTIE-ILWTIlPSIILMFIAIPSFTLLYSMD-----DVVVDPaITIKAIGHQWYWSYEYSDYNNSDEQSLAFdsymvp 280
Cdd:PRK10525   84 HSNKVEaVVWTV-PILIIIFLAVLTWKTTHALEpskplAHDEKP-ITIEVVSMDWKWFFIYPEQGIATVNEIAF------ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1773401166 281 eddlelgqlrllevdnrvvvPAKTHLRVLITSADVLHSWAVPSLGVKCDAVPGRLNQISTFIQREGVYYGQCSEICGtnH 360
Cdd:PRK10525  156 --------------------PANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSG--P 213

                         170       180
                  ....*....|....*....|....
gi 1773401166 361 AFMPIVVEAVSTKD---YGSWVSN 381
Cdd:PRK10525  214 GFSGMKFKAIATPDraeFDQWVAK 237
 
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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