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Conserved domains on  [gi|45469|emb|CAA29268|]
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unnamed protein product [Paracoccus denitrificans]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11446855)

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

CATH:  1.10.287.90|2.60.40.420
EC:  7.1.1.9
Gene Ontology:  GO:0042773|GO:0004129|GO:0005507
SCOP:  4002011|4002191

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
45-281 9.91e-80

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


:

Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 241.27  E-value: 9.91e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     45 GGMNFQPASSPLAHDQQWLDHFVLYIITAVTIFVCLLLLICIVRFNRRANP-VPARFTHNTPIEVIWTLVPVLILVAIGA 123
Cdd:COG1622  17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    124 FSLPILFRSQEMPNDPdLVIKAIGHQWYWSYEYPNDGVAfdalmlekealadagysedeyllaTDNPVVVPVGKKVLVQV 203
Cdd:COG1622  97 PTLRVLHALDDAPEDP-LTVEVTGYQWKWLFRYPDQGIA------------------------TVNELVLPVGRPVRFLL 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45469    204 TATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLAGAKEEFAA 281
Cdd:COG1622 152 TSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAAT 229
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
45-281 9.91e-80

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 241.27  E-value: 9.91e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     45 GGMNFQPASSPLAHDQQWLDHFVLYIITAVTIFVCLLLLICIVRFNRRANP-VPARFTHNTPIEVIWTLVPVLILVAIGA 123
Cdd:COG1622  17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    124 FSLPILFRSQEMPNDPdLVIKAIGHQWYWSYEYPNDGVAfdalmlekealadagysedeyllaTDNPVVVPVGKKVLVQV 203
Cdd:COG1622  97 PTLRVLHALDDAPEDP-LTVEVTGYQWKWLFRYPDQGIA------------------------TVNELVLPVGRPVRFLL 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45469    204 TATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLAGAKEEFAA 281
Cdd:COG1622 152 TSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAAT 229
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 139-271 5.40e-67

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: 205.11  E-value: 5.40e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    139 PDLVIKAIGHQWYWSYEYP-NDGVAFDALMLEKEALADAGYsedeYLLATDNPVVVPVGKKVLVQVTATDVIHAWTIPAF 217
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSdFNDLEFDSYMIPEDDLEKGQL----RLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSL 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 45469    218 AVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAW 271
Cdd:cd13912  77 GIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 47-272 1.30e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 205.06  E-value: 1.30e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      47 MNFQPASSPLA------HDqqwldhFVLYIITAVTIFV--CLLLLICIVRFNRRanpvparFTHNTPIEVIWTLVPVLIL 118
Cdd:MTH00154   7 LSFQDSASPLMeqliffHD------HTMMILIMITILVgyMMISLLFNKFTNRF-------LLEGQEIEIIWTILPAIIL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     119 VAIGAFSLPILFRSQEMpNDPDLVIKAIGHQWYWSYEYPN-DGVAFDALMLEKEALADAGYSedeyLLATDNPVVVPVGK 197
Cdd:MTH00154  74 IFIALPSLRLLYLLDEV-NNPSITLKTIGHQWYWSYEYSDfKNIEFDSYMIPTNELENNGFR----LLDVDNRLVLPMNT 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45469     198 KVLVQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWL 272
Cdd:MTH00154 149 QIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
141-263 1.72e-61

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 190.70  E-value: 1.72e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      141 LVIKAIGHQWYWSYEYPNDG-VAFDALMLEKEALADAGYSedeyLLATDNPVVVPVGKKVLVQVTATDVIHAWTIPAFAV 219
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGdLEFDSYMIPTEDLEEGQLR----LLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 45469      220 KQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAV 263
Cdd:pfam00116  77 KTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 66-273 1.64e-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: 160.24  E-value: 1.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469       66 FVLYIITAVTIFVCLLLLICIVRFNRRA-NPVPARFTHNTPIEVIWTLVPVLILVAIGAFSLPILFRSQEMPNDPDLVIK 144
Cdd:TIGR02866  15 FVLAVSTLISLLVAALLAYVVWKFRRKGdEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYLERPIPKDALKVK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      145 AIGHQWYWSYEYPNDGVAfdalmlekealadagysedeyllaTDNPVVVPVGKKVLVQVTATDVIHAWTIPAFAVKQDAV 224
Cdd:TIGR02866  95 VTGYQWWWDFEYPESGFT------------------------TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAI 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 45469      225 PGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLA 273
Cdd:TIGR02866 151 PGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
45-281 9.91e-80

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 241.27  E-value: 9.91e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     45 GGMNFQPASSPLAHDQQWLDHFVLYIITAVTIFVCLLLLICIVRFNRRANP-VPARFTHNTPIEVIWTLVPVLILVAIGA 123
Cdd:COG1622  17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    124 FSLPILFRSQEMPNDPdLVIKAIGHQWYWSYEYPNDGVAfdalmlekealadagysedeyllaTDNPVVVPVGKKVLVQV 203
Cdd:COG1622  97 PTLRVLHALDDAPEDP-LTVEVTGYQWKWLFRYPDQGIA------------------------TVNELVLPVGRPVRFLL 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45469    204 TATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLAGAKEEFAA 281
Cdd:COG1622 152 TSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAAT 229
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 139-271 5.40e-67

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: 205.11  E-value: 5.40e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    139 PDLVIKAIGHQWYWSYEYP-NDGVAFDALMLEKEALADAGYsedeYLLATDNPVVVPVGKKVLVQVTATDVIHAWTIPAF 217
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSdFNDLEFDSYMIPEDDLEKGQL----RLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSL 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 45469    218 AVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAW 271
Cdd:cd13912  77 GIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 47-272 1.30e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 205.06  E-value: 1.30e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      47 MNFQPASSPLA------HDqqwldhFVLYIITAVTIFV--CLLLLICIVRFNRRanpvparFTHNTPIEVIWTLVPVLIL 118
Cdd:MTH00154   7 LSFQDSASPLMeqliffHD------HTMMILIMITILVgyMMISLLFNKFTNRF-------LLEGQEIEIIWTILPAIIL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     119 VAIGAFSLPILFRSQEMpNDPDLVIKAIGHQWYWSYEYPN-DGVAFDALMLEKEALADAGYSedeyLLATDNPVVVPVGK 197
Cdd:MTH00154  74 IFIALPSLRLLYLLDEV-NNPSITLKTIGHQWYWSYEYSDfKNIEFDSYMIPTNELENNGFR----LLDVDNRLVLPMNT 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45469     198 KVLVQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWL 272
Cdd:MTH00154 149 QIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 45-273 3.30e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 204.06  E-value: 3.30e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      45 GGMNFQPASSPLAHDQQWLDHFVLYIITAVTIFVCLLLLIC-----IVRFNRRANPvparfthntpIEVIWTLVPVLILV 119
Cdd:MTH00168   5 SQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLvtskyTNRFLLDSQM----------IEFVWTIIPAFILI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     120 AIGAFSLPILFRSQEmPNDPDLVIKAIGHQWYWSYEYpND--GVAFDALMLEKEALADAGYSedeyLLATDNPVVVPVGK 197
Cdd:MTH00168  75 SLALPSLRLLYLMDE-IDKPDLTIKAVGHQWYWSYEY-TDynDLEFDSYMVPTQDLSPGQFR----LLEVDNRLVLPMDS 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45469     198 KVLVQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLA 273
Cdd:MTH00168 149 KIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 45-277 9.90e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 202.86  E-value: 9.90e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      45 GGMNFQPASSPLAHDQQWLDHFVLYIITAVTIFVCLLLLICIVrfnrraNPVPARFTHNTP-IEVIWTLVPVLILVAIGA 123
Cdd:MTH00140   5 GQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLF------NKFSCRTILEAQkLETIWTIVPALILVFLAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     124 FSLPILFRSQEmPNDPDLVIKAIGHQWYWSYEYPN-DGVAFDALMLEKEALADAGYSedeyLLATDNPVVVPVGKKVLVQ 202
Cdd:MTH00140  79 PSLRLLYLLDE-TNNPLLTVKAIGHQWYWSYEYSDfSVIEFDSYMVPENELELGDFR----LLEVDNRLVLPYSVDTRVL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45469     203 VTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLAGAKE 277
Cdd:MTH00140 154 VTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMSE 228
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 47-278 5.22e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 196.08  E-value: 5.22e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      47 MNFQPASSPLAHDQQWLDHFVLYIITAVTIFVC--LLLLICIVRFNRRanpvparFTHNTPIEVIWTLVPVLILVAIGAF 124
Cdd:MTH00038   7 LGLQDASSPLMEELIYFHDYALIILTLITILVFygLASLLFSSPTNRF-------FLEGQELETIWTIVPAFILIFIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     125 SLPILFRSQEMpNDPDLVIKAIGHQWYWSYEY-PNDGVAFDALMLEKEALAdagySEDEYLLATDNPVVVPVGKKVLVQV 203
Cdd:MTH00038  80 SLQLLYLMDEV-NNPFLTIKAIGHQWYWSYEYtDYNDLEFDSYMVPTSDLS----TGLPRLLEVDNRLVLPYQTPIRVLV 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45469     204 TATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLAGAKEE 278
Cdd:MTH00038 155 SSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
141-263 1.72e-61

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 190.70  E-value: 1.72e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      141 LVIKAIGHQWYWSYEYPNDG-VAFDALMLEKEALADAGYSedeyLLATDNPVVVPVGKKVLVQVTATDVIHAWTIPAFAV 219
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGdLEFDSYMIPTEDLEEGQLR----LLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 45469      220 KQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAV 263
Cdd:pfam00116  77 KTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 45-275 3.19e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 188.77  E-value: 3.19e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      45 GGMNFQPASSPLAHDQQWLDHFVLYIITAVTIFVCLLLLICIVRfnrranpvpaRFTHNTPI-----EVIWTLVPVLILV 119
Cdd:MTH00139   5 GQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSN----------KFTSRSLLesqevETIWTVLPAFILL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     120 AIGAFSLPILFRSQEMpNDPDLVIKAIGHQWYWSYEYPN-DGVAFDALMLEKEALADAGYSedeyLLATDNPVVVPVGKK 198
Cdd:MTH00139  75 FLALPSLRLLYLMDEV-SDPYLTFKAVGHQWYWSYEYSDfKNLSFDSYMIPTEDLSSGEFR----LLEVDNRLVLPYKSN 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45469     199 VLVQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLAGA 275
Cdd:MTH00139 150 IRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 47-273 2.55e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 183.96  E-value: 2.55e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      47 MNFQPASSPLAHDQQWLDHFVLYIITAVTIFVCLLLLICIVrfnrranpvpARFTHNTP-----IEVIWTLVPVLILVAI 121
Cdd:MTH00117   7 LGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLT----------TKLTHTNTvdaqeVELIWTILPAIVLILL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     122 GAFSLPILFRSQEMpNDPDLVIKAIGHQWYWSYEYPN-DGVAFDALMLEKEALADAGYSedeyLLATDNPVVVPVGKKVL 200
Cdd:MTH00117  77 ALPSLRILYLMDEI-NNPHLTIKAIGHQWYWSYEYTDyKDLSFDSYMIPTQDLPNGHFR----LLEVDHRMVIPMESPIR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45469     201 VQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLA 273
Cdd:MTH00117 152 ILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSS 224
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 46-278 7.38e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 183.06  E-value: 7.38e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      46 GMNFQPASSPLAHDQQWLDHFVLYIITAVTIFVclllLICIVRFNRRANPVPArFTHNTPIEVIWTLVPVLILVAIGAFS 125
Cdd:MTH00051   8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTV----LWLIIRALTTKYYHKY-LFEGTLIEIIWTLIPAAILIFIAFPS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     126 LPILFRSQEMPnDPDLVIKAIGHQWYWSYEYPNDG---VAFDALMLEKEALAdagySEDEYLLATDNPVVVPVGKKVLVQ 202
Cdd:MTH00051  83 LKLLYLMDEVI-DPALTIKAIGHQWYWSYEYSDYGtdtIEFDSYMIPTSDLN----SGDLRLLEVDNRLIVPIQTQVRVL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45469     203 VTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLAGAKEE 278
Cdd:MTH00051 158 VTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 47-278 1.00e-53

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 174.69  E-value: 1.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      47 MNFQPASSPLAHDqqwLDHFVLYIITAVTIFVCLLLLICIVRfnrranpVPARFTH-----NTPIEVIWTLVPVLILVAI 121
Cdd:MTH00185   7 LGLQDAASPVMEE---LIHFHDHTLMIVFLISTLVLYIIVAM-------VTTKLTNkyildSQEIEIVWTILPAIILIMI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     122 GAFSLPILFRSQEMpNDPDLVIKAIGHQWYWSYEYPN-DGVAFDALMLEKEALADAGYSedeyLLATDNPVVVPVGKKVL 200
Cdd:MTH00185  77 ALPSLRILYLMDEI-NDPHLTIKAMGHQWYWSYEYTDyEQLEFDSYMTPTQDLTPGQFR----LLETDHRMVVPMESPIR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45469     201 VQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLAGAKEE 278
Cdd:MTH00185 152 VLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEE 229
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 47-272 1.86e-53

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 174.55  E-value: 1.86e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      47 MNFQPASSPLAHDQQWLDHFVLYIItaVTIFVCLLLLICIVRFNRRANpvpaRF-THNTPIEVIWTLVPVLILVAIGAFS 125
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLL--IIIITVVLWLIVEALNGKFYD----RFlVDGTFLEIVWTIIPAVILVFIALPS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     126 LPILFRSQEMPnDPDLVIKAIGHQWYWSYEYPN---DGVAFDALMLEKEALAdagySEDEYLLATDNPVVVPVGKKVLVQ 202
Cdd:MTH00023  90 LKLLYLMDEVV-SPALTIKAIGHQWYWSYEYSDyegETLEFDSYMVPTSDLN----SGDFRLLEVDNRLVVPINTHVRIL 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     203 VTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWL 272
Cdd:MTH00023 165 VTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 47-271 3.95e-53

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 173.36  E-value: 3.95e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      47 MNFQPASSPLAHDqqwLDHF---VLYIITAVTIFVcLLLLICIVrfnrrANPVPARFTHNT-PIEVIWTLVPVLILVAIG 122
Cdd:MTH00129   7 LGFQDAASPVMEE---LLHFhdhALMIVFLISTLV-LYIIVAMV-----STKLTNKYILDSqEIEIIWTVLPAVILILIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     123 AFSLPILFRSQEMpNDPDLVIKAIGHQWYWSYEYPN-DGVAFDALMLEKEALADAGYSedeyLLATDNPVVVPVGKKVLV 201
Cdd:MTH00129  78 LPSLRILYLMDEI-NDPHLTIKAMGHQWYWSYEYTDyEDLGFDSYMIPTQDLTPGQFR----LLEADHRMVVPVESPIRV 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     202 QVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAW 271
Cdd:MTH00129 153 LVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 45-277 1.07e-52

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 171.96  E-value: 1.07e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      45 GGMNFQPASSPLA------HDQQWLdhfVLYIITAVTIFVCLLLLicivrFNRRANpvpaRFT-HNTPIEVIWTLVPVLI 117
Cdd:MTH00008   5 GQLMFQDAASPVMlqlisfHDHALL---ILTLVLTVVGYAMTSLM-----FNKLSN----RYIlEAQQIETIWTILPALI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     118 LVAIGAFSLPILFRSQEMPNdPDLVIKAIGHQWYWSYEYPN-DGVAFDALMLEKEALAdagySEDEYLLATDNPVVVPVG 196
Cdd:MTH00008  73 LLFLAFPSLRLLYLMDEVSN-PSITLKTIGHQWYWSYEYSDfSNLEFDSYMLPTSDLS----PGQFRLLEVDNRAVLPMQ 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     197 KKVLVQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLAGAK 276
Cdd:MTH00008 148 TEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFA 227


                 .
gi 45469     277 E 277
Cdd:MTH00008 228 E 228
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 47-277 5.62e-52

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 170.34  E-value: 5.62e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      47 MNFQPASSPLAHDqqwLDHFVLYIITAVTIFVCLLLLICIVRFNRR---ANPVPARfthntPIEVIWTLVPVLILVAIGA 123
Cdd:MTH00076   7 LGFQDAASPIMEE---LLHFHDHALMAVFLISTLVLYIITIMMTTKltnTNTMDAQ-----EIEMVWTIMPAIILIVIAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     124 FSLPILFRSQEMpNDPDLVIKAIGHQWYWSYEYPN-DGVAFDALMLEKEALADAGYSedeyLLATDNPVVVPVGKKVLVQ 202
Cdd:MTH00076  79 PSLRILYLMDEI-NDPHLTVKAIGHQWYWSYEYTDyEDLSFDSYMIPTQDLTPGQFR----LLEVDNRMVVPMESPIRML 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45469     203 VTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLAGAKE 277
Cdd:MTH00076 154 ITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 47-273 1.43e-50

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 166.43  E-value: 1.43e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      47 MNFQPASSPLAHD-QQWLDH--FVLYIITAVTIFVCLLLLIcivrfnrranpvpARFTHNT-----PIEVIWTLVPVLIL 118
Cdd:MTH00098   7 LGFQDATSPIMEElLHFHDHtlMIVFLISSLVLYIISLMLT-------------TKLTHTStmdaqEVETIWTILPAIIL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     119 VAIGAFSLPILFRSQEMpNDPDLVIKAIGHQWYWSYEYPN-DGVAFDALMLEKEALADAgyseDEYLLATDNPVVVPVGK 197
Cdd:MTH00098  74 ILIALPSLRILYMMDEI-NNPSLTVKTMGHQWYWSYEYTDyEDLSFDSYMIPTSDLKPG----ELRLLEVDNRVVLPMEM 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45469     198 KVLVQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLA 273
Cdd:MTH00098 149 PIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSA 224
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 66-273 1.64e-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: 160.24  E-value: 1.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469       66 FVLYIITAVTIFVCLLLLICIVRFNRRA-NPVPARFTHNTPIEVIWTLVPVLILVAIGAFSLPILFRSQEMPNDPDLVIK 144
Cdd:TIGR02866  15 FVLAVSTLISLLVAALLAYVVWKFRRKGdEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYLERPIPKDALKVK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      145 AIGHQWYWSYEYPNDGVAfdalmlekealadagysedeyllaTDNPVVVPVGKKVLVQVTATDVIHAWTIPAFAVKQDAV 224
Cdd:TIGR02866  95 VTGYQWWWDFEYPESGFT------------------------TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAI 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 45469      225 PGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLA 273
Cdd:TIGR02866 151 PGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 62-272 8.74e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 157.09  E-value: 8.74e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      62 WLDHF---VLYIITAVTIFVCLLLLICIVRFNRRANpvparFTHNTPIEVIWTLVPVLILVAIGAFSLPILFRSQEMPND 138
Cdd:MTH00080  21 WFHNFncsLLFGEFVLAFVVFLFLYLISNNFYFKSK-----KIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNLD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     139 PDLVIKAIGHQWYWSYEYPND-GVAFDALMlekEALADAGYSEDEyLLATDNPVVVPVGKKVLVQVTATDVIHAWTIPAF 217
Cdd:MTH00080  96 SNLTVKVTGHQWYWSYEFSDIpGLEFDSYM---KSLDQLRLGEPR-LLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSL 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 45469     218 AVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWL 272
Cdd:MTH00080 172 SIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 47-273 5.50e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 153.26  E-value: 5.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      47 MNFQPASSP------LAHDQQWldhFVLYIITAVTIFVCLLLLICIVRFNRRANPVPARFthntpIEVIWTLVPVLILVA 120
Cdd:MTH00027  35 LGFQDAGSPvmeeiiMLHDQIL---FILTIIVGVVLWLIIRILLGNNYYSYYWNKLDGSL-----IEVIWTLIPAFILIL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     121 IGAFSLPILFRSQEMPNDPDLVIKAIGHQWYWSYEYPNDG---VAFDALMLEKealADAGYSeDEYLLATDNPVVVPVGK 197
Cdd:MTH00027 107 IAFPSLRLLYIMDECGFSANITIKVTGHQWYWSYSYEDYGeknIEFDSYMIPT---ADLEFG-DLRLLEVDNRLILPVDT 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45469     198 KVLVQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWLA 273
Cdd:MTH00027 183 NVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIG 258
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 67-263 1.05e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 140.09  E-value: 1.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469      67 VLYIItAVTIFVCLL--LLICIVRFNRRANPVPArfTHNTPIEVIWTLVPVLILVAIGAFSLPilFRSQEMPNDPDLVIK 144
Cdd:MTH00047  11 VCYIL-ALCVFIPCWvyIMLCWQVVSGNGSVNFG--SENQVLELLWTVVPTLLVLVLCFLNLN--FITSDLDCFSSETIK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469     145 AIGHQWYWSYEYPNDGVaFDALMlekealADAGYSEDEYLLATDNPVVVPVgkkvlvqVTATDVIHAWTIPAFAVKQDAV 224
Cdd:MTH00047  86 VIGHQWYWSYEYSFGGS-YDSFM------TDDIFGVDKPLRLVYGVPYHLL-------VTSSDVIHSFSVPDLNLKMDAI 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 45469     225 PGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAV 263
Cdd:MTH00047 152 PGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 42-128 1.07e-33

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: 118.20  E-value: 1.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469       42 PVNGGMNFQPASSPLAHDQQWLDHFVLYIITAVTIFVCLLLLICIVRFNRRANPVPARFT-HNTPIEVIWTLVPVLILVA 120
Cdd:pfam02790   2 PTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARYTtHGQTIEIIWTIIPAVILIL 81


                  ....*...
gi 45469      121 IGAFSLPI 128
Cdd:pfam02790  82 IALPSFKL 89
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 203-270 7.05e-28

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 105.67  E-value: 7.05e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45469     203 VTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEA 270
Cdd:PTZ00047  87 ITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVSPEAYAA 154
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 140-263 2.76e-26

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: 99.64  E-value: 2.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    140 DLVIKAIGHQWYWSYEYPNDGVAFDAlmlekealADAGYSEDEYLLAtdnpvvvpvGKKVLVQVTATDVIHAWTIPAFAV 219
Cdd:cd13919   1 ALVVEVTAQQWAWTFRYPGGDGKLGT--------DDDVTSPELHLPV---------GRPVLFNLRSKDVIHSFWVPEFRV 63

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 45469    220 KQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAV 263
Cdd:cd13919  64 KQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKVV 107
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 115-272 3.29e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 95.21  E-value: 3.29e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    115 VLILVAIGAFSLPILFRSQEMPNDPDLVIKAIGHQWYWSYEYPNDGVAFDALMLEKEALadagysedeyllatdnpvvvp 194
Cdd:cd13918   7 VISLIVWTYGMLLYVEDPPDEADEDALEVEVEGFQFGWQFEYPNGVTTGNTLRVPADTP--------------------- 65

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45469    195 vgkkVLVQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWL 272
Cdd:cd13918  66 ----IALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 140-263 5.85e-24

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: 93.45  E-value: 5.85e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    140 DLVIKAIGHQWYWSYEYPNdgvafdalmlekealadagysEDEYLLATDNPVVVPVGKKVLVQVTATDVIHAWTIPAFAV 219
Cdd:cd04213   1 ALTIEVTGHQWWWEFRYPD---------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAG 59

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 45469    220 KQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAV 263
Cdd:cd04213  60 KMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 141-261 7.04e-24

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: 92.74  E-value: 7.04e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    141 LVIKAIGHQWYWSYEYPNDGVaFDALMLEKEaladagyseDEYLLatdnpvvvpvgkkvlvQVTATDVIHAWTIPAFAVK 220
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPNVRT-PNEIVVPAG---------TPVRF----------------RVTSPDVIHGFYIPNLGVK 54

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 45469    221 QDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVK 261
Cdd:cd13842  55 VDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 140-262 1.51e-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: 89.61  E-value: 1.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    140 DLVIKAIGHQWYWSYEYPNDGVAFDALMLEkealadAGYSedeyllatdnpvvvpvgkkVLVQVTATDVIHAWTIPAFAV 219
Cdd:cd13915   1 ALEIQVTGRQWMWEFTYPNGKREINELHVP------VGKP-------------------VRLILTSKDVIHSFYVPAFRI 55

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 45469    220 KQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKA 262
Cdd:cd13915  56 KQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 142-272 1.58e-21

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: 87.08  E-value: 1.58e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    142 VIKAIGHQWYWSYEYPNDGVAfdalmlekealadagySEDEYLLATDNPVVVpvgkkvlvQVTATDVIHAWTIPAFAVKQ 221
Cdd:cd13914   2 EIEVEAYQWGWEFSYPEANVT----------------TSEQLVIPADRPVYF--------RITSRDVIHAFHVPELGLKQ 57

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 45469    222 DAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAVSQEKYEAWL 272
Cdd:cd13914  58 DAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 195-261 1.68e-06

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: 45.64  E-value: 1.68e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45469    195 VGKKVLVQVTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYM--PIVVK 261
Cdd:cd13913  31 AGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 207-261 3.46e-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: 42.22  E-value: 3.46e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    207 DVIHAWTIPAFAVKQDA---------------VPGRIAQLWFSVDQEGVYFGQCSELCGiNHAYMPIVVK 261
Cdd:cd00920  42 GENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 141-263 2.05e-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: 39.84  E-value: 2.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    141 LVIKAIGHQWYWSYEYPNDGVAfdalmlekealadagysedeyllaTDNPVVVPVGKKVLVQVTATDVIHAWTIPAFAVK 220
Cdd:cd04212   1 LEIQVVSLDWKWLFIYPEQGIA------------------------TVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQ 56

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 45469    221 QDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYMPIVVKAV 263
Cdd:cd04212  57 IYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 142-256 4.68e-04

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 38.52  E-value: 4.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45469    142 VIKAIGHQWYWSY---EYP-NDGVAFdalmlekealadagysedeyllatdnpvvvpvgkkvlvQVTATDVIHAWTI--P 215
Cdd:cd13916   2 VVAVTGHQWYWELsrtEIPaGKPVEF--------------------------------------RVTSADVNHGFGIydP 43

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 45469    216 AFA-VKQ-DAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYM 256
Cdd:cd13916  44 DMRlLAQtQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 203-261 4.99e-03

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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 35.42  E-value: 4.99e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45469    203 VTATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYM--PIVVK 261
Cdd:cd13917  28 LSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMhgRIIVE 88
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 205-256 8.31e-03

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: 34.90  E-value: 8.31e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 45469    205 ATDVIHAWTIPAFAVKQDAVPGRIAQLWFSVDQEGVYFGQCSELCGINHAYM 256
Cdd:cd04223  36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
 
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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