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Conserved domains on  [gi|636841652|ref|WP_024363396|]
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MULTISPECIES: cytochrome b5 [Lysinibacillus]

Protein Classification

cupredoxin domain-containing protein( domain architecture ID 139548)

cupredoxin domain-containing protein may contain a type I copper center and be involved in inter-molecular electron transfer reactions

CATH:  2.60.40.420
Gene Ontology:  GO:0005507|GO:0009055
PubMed:  21258692|35994119
SCOP:  3000886

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 57-157 2.05e-44

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.


The actual alignment was detected with superfamily member cd13913:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 99  Bit Score: 141.55  E-value: 2.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  57 PGVHKVEGKDwdYEVVILASAFFYNPPEIEVPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFL 136
Cdd:cd13913    1 PGVRKIGPNE--YEVYVVAQAFAFNPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYL 78

                         90       100
                 ....*....|....*....|.
gi 636841652 137 IVCNEYCGTGHTLMHSMLKVV 157
Cdd:cd13913   79 IICNEYCGAGHHNMYGKIIVE 99
 
Name Accession Description Interval E-value
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 57-157 2.05e-44

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: 141.55  E-value: 2.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  57 PGVHKVEGKDwdYEVVILASAFFYNPPEIEVPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFL 136
Cdd:cd13913    1 PGVRKIGPNE--YEVYVVAQAFAFNPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYL 78

                         90       100
                 ....*....|....*....|.
gi 636841652 137 IVCNEYCGTGHTLMHSMLKVV 157
Cdd:cd13913   79 IICNEYCGAGHHNMYGKIIVE 99
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
10-161 7.66e-20

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 82.18  E-value: 7.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  10 WLVFGVATLVAFLIILGIGAFhqgshpnSNKKTIDYEKVKEiAPFTnpgVhKVEGKDWDYEvvilasaFFY------NPP 83
Cdd:COG1622   77 TKLEIVWTVIPIIIVIVLAVP-------TLRVLHALDDAPE-DPLT---V-EVTGYQWKWL-------FRYpdqgiaTVN 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  84 EIEVPLGSKVKFIATSEDVIHGF---EIAGTnINMMlePGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVVDPN 160
Cdd:COG1622  138 ELVLPVGRPVRFLLTSADVIHSFwvpALGGK-QDAI--PGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPE 214


                 .
gi 636841652 161 E 161
Cdd:COG1622  215 E 215
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
87-150 1.77e-10

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 55.11  E-value: 1.77e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636841652   87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLM 150
Cdd:pfam00116  50 LPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 95-161 5.43e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 49.95  E-value: 5.43e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 636841652  95 FIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVVDPNE 161
Cdd:MTH00047 128 LLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
 
Name Accession Description Interval E-value
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 57-157 2.05e-44

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: 141.55  E-value: 2.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  57 PGVHKVEGKDwdYEVVILASAFFYNPPEIEVPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFL 136
Cdd:cd13913    1 PGVRKIGPNE--YEVYVVAQAFAFNPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYL 78

                         90       100
                 ....*....|....*....|.
gi 636841652 137 IVCNEYCGTGHTLMHSMLKVV 157
Cdd:cd13913   79 IICNEYCGAGHHNMYGKIIVE 99
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 61-150 9.22e-23

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: 86.20  E-value: 9.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  61 KVEGKDWDYEVVILASAffyNPPEIEVPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCN 140
Cdd:cd13842    4 YVTGVQWSWTFIYPNVR---TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTIICA 80

                         90
                 ....*....|
gi 636841652 141 EYCGTGHTLM 150
Cdd:cd13842   81 EYCGLGHSYM 90
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
10-161 7.66e-20

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 82.18  E-value: 7.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  10 WLVFGVATLVAFLIILGIGAFhqgshpnSNKKTIDYEKVKEiAPFTnpgVhKVEGKDWDYEvvilasaFFY------NPP 83
Cdd:COG1622   77 TKLEIVWTVIPIIIVIVLAVP-------TLRVLHALDDAPE-DPLT---V-EVTGYQWKWL-------FRYpdqgiaTVN 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  84 EIEVPLGSKVKFIATSEDVIHGF---EIAGTnINMMlePGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVVDPN 160
Cdd:COG1622  138 ELVLPVGRPVRFLLTSADVIHSFwvpALGGK-QDAI--PGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPE 214


                 .
gi 636841652 161 E 161
Cdd:COG1622  215 E 215
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 61-157 2.71e-18

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: 75.37  E-value: 2.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  61 KVEGKDWDY------EVVILASAFFYNPPEIEVPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGE 134
Cdd:cd13919    5 EVTAQQWAWtfrypgGDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTREGE 84

                         90       100
                 ....*....|....*....|...
gi 636841652 135 FLIVCNEYCGTGHTLMHSMLKVV 157
Cdd:cd13919   85 YEVRCAELCGLGHYRMRATVKVV 107
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 70-157 5.91e-18

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: 73.94  E-value: 5.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  70 EVVILASAFFYNPPeIEVPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYisEYVAEI--NQTGEFLIVCNEYCGTGH 147
Cdd:cd13917    2 DVYLVARAWQWRPV-LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGY--EWVITMtpNETGEFHIICNEYCGIGH 78

                         90
                 ....*....|
gi 636841652 148 TLMHSMLKVV 157
Cdd:cd13917   79 HTMHGRIIVE 88
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 61-156 5.81e-17

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: 71.51  E-value: 5.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  61 KVEGKDWDYEvvilasaFFY-----NPPEIEVPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEF 135
Cdd:cd13915    5 QVTGRQWMWE-------FTYpngkrEINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEY 77

                         90       100
                 ....*....|....*....|.
gi 636841652 136 LIVCNEYCGTGHTLMHSMLKV 156
Cdd:cd13915   78 DLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 62-161 2.94e-12

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 59.73  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  62 VEGKDWDYEVvILASAFFYNPPEIEVPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNE 141
Cdd:cd13914    5 VEAYQWGWEF-SYPEANVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYCAE 83

                         90       100
                 ....*....|....*....|
gi 636841652 142 YCGTGHTLMHSMLKVVDPNE 161
Cdd:cd13914   84 YCGAGHSQMLSTVTVVSQDE 103
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 61-157 4.19e-12

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: 59.17  E-value: 4.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  61 KVEGKDWDYEVVILASAF--FYNPPEIEVPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIV 138
Cdd:cd04213    5 EVTGHQWWWEFRYPDEPGrgIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVYRGQ 84

                         90
                 ....*....|....*....
gi 636841652 139 CNEYCGTGHTLMhsMLKVV 157
Cdd:cd04213   85 CAEFCGASHALM--RFKVI 101
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 86-157 5.29e-12

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 58.55  E-value: 5.29e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636841652  86 EVPLGSKVKFIATSEDVIHGFEIAGTNINMMLE----PGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVV 157
Cdd:cd13916   18 EIPAGKPVEFRVTSADVNHGFGIYDPDMRLLAQtqamPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFTVV 93
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
87-150 1.77e-10

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 55.11  E-value: 1.77e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636841652   87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLM 150
Cdd:pfam00116  50 LPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 80-156 1.03e-09

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: 52.62  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  80 YNPPEIEVPLGSKVKFIAT----SEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLK 155
Cdd:cd04223   13 FTPDIIEVKEGDEVTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLI 92


                 .
gi 636841652 156 V 156
Cdd:cd04223   93 V 93
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
61-156 5.40e-09

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 53.76  E-value: 5.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  61 KVEGKDWDYEVVILASAFFYNPPEIEVPLGSKVKFIATS----EDVIHGFEIAGTNINMMLEPGYIS--EYVAeiNQTGE 134
Cdd:COG4263  520 KVIRDGNKVRVYMTSIAPHFGPDEFEVKQGDEVTVHVTNldqvEDLTHGFAIPGYNINMEIMPQETAsvTFVA--DKPGV 597

                         90       100
                 ....*....|....*....|..
gi 636841652 135 FLIVCNEYCGTGHTLMHSMLKV 156
Cdd:COG4263  598 YWYYCTWFCHALHMEMRGRMLV 619
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 95-161 5.43e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 49.95  E-value: 5.43e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 636841652  95 FIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVVDPNE 161
Cdd:MTH00047 128 LLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 87-156 6.04e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 50.01  E-value: 6.04e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKV 156
Cdd:MTH00080 147 LPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEV 216
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 87-157 2.35e-07

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: 47.18  E-value: 2.35e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636841652  87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVV 157
Cdd:cd13912   52 VPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAV 122
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 87-160 6.20e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 47.24  E-value: 6.20e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636841652  87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVVDPN 160
Cdd:MTH00140 144 LPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLE 217
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 87-160 9.03e-07

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 46.77  E-value: 9.03e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636841652  87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVVDPN 160
Cdd:MTH00008 144 LPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTK 217
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 84-161 1.19e-06

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 45.52  E-value: 1.19e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636841652  84 EIEVPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVVDPNE 161
Cdd:cd13918   57 TLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEE 134
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 87-161 2.47e-06

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 45.51  E-value: 2.47e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 636841652  87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVVDPNE 161
Cdd:MTH00023 155 VPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDK 229
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 85-157 2.88e-06

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 45.65  E-value: 2.88e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 636841652  85 IEVPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVV 157
Cdd:MTH00185 142 MVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAV 214
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 87-150 6.27e-06

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 44.39  E-value: 6.27e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636841652  87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLM 150
Cdd:MTH00051 148 VPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 211
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 87-159 4.96e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 41.34  E-value: 4.96e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 636841652  87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVVDP 159
Cdd:PTZ00047  77 LPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVSP 149
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 87-150 5.35e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 41.61  E-value: 5.35e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636841652  87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLM 150
Cdd:MTH00038 144 LPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFM 207
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 87-157 5.41e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 41.93  E-value: 5.41e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636841652  87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVV 157
Cdd:MTH00027 178 LPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESV 248
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 87-150 8.64e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 41.30  E-value: 8.64e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636841652  87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLM 150
Cdd:MTH00076 144 VPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFM 207
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 70-159 1.33e-04

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 41.12  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636841652  70 EVVILASAFFYNPPEIEVPLGSKVKFIATS----EDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGT 145
Cdd:PRK02888 542 RVYMTSQAPAFGLREFTVKQGDEVTVIVTNldkvEDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHA 621

                         90
                 ....*....|....*
gi 636841652 146 GHTLMHS-MLkvVDP 159
Cdd:PRK02888 622 LHMEMRGrML--VEP 634
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 87-150 2.10e-04

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 40.08  E-value: 2.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636841652  87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLM 150
Cdd:MTH00129 144 VPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFM 207
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 87-161 3.33e-04

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 39.43  E-value: 3.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 636841652  87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVVDPNE 161
Cdd:MTH00154 144 LPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNN 218
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 87-161 5.01e-04

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 38.93  E-value: 5.01e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 636841652  87 VPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVVDPNE 161
Cdd:MTH00139 144 LPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKF 218
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 85-160 1.28e-03

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 37.65  E-value: 1.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636841652  85 IEVPLGSKVKFIATSEDVIHGFEIAGTNINMMLEPGYISEYVAEINQTGEFLIVCNEYCGTGHTLMHSMLKVVDPN 160
Cdd:MTH00168 142 LVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWE 217
 
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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