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Conserved domains on  [gi|2777215752|pdb|8RGB|A]
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Chain A, Copper-containing nitrite reductase

Protein Classification

copper-containing nitrite reductase( domain architecture ID 11494189)

copper-containing nitrite reductase catalyzes the reduction of nitrite to nitric oxide (NO)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cu_nitrite_red TIGR02376
nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. ...
 6-333 0e+00

nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. It reduces nitrite to nitric oxide, the first step in denitrification. [Central intermediary metabolism, Nitrogen metabolism]


:

Pssm-ID: 131429 [Multi-domain]  Cd Length: 311  Bit Score: 525.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A          6 LPRQRVDLVAPPFVHVHEQATKQGPKIMEFKLVVQEKKMVIDEkGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATN 85
Cdd:TIGR02376   1 LPRVKVDLVAPPFVHVHDQIDRSGPKVVEVTMTIEEKKMVIDD-GVTYQAMTFDGSVPGPLIRVHEGDYVELTLINPPTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A         86 TMPHNIDFHSATGALGGGALTLINPGEQVVLRWKATRTGVFVYHCAPGGpMIPWHVVSGMNGAVMVLPRDGLNdghghsl 165
Cdd:TIGR02376  80 TMPHNVDFHAATGALGGAALTQVNPGETATLRFKATRPGAFVYHCAPPG-MVPWHVVSGMNGAIMVLPREGLP------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A        166 RYDRIYYIGEQDLYVPRDEKgnfksydsPGEAYSDTEEVMRKLTPTHVVFNGKAGALTGKNALNANVGENVLIVHSQANR 245
Cdd:TIGR02376 152 EYDKEYYIGESDLYTPKDEG--------EGGAYEDDVAAMRTLTPTHVVFNGAVGALTGDNALTAGVGERVLFVHSQPNR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A        246 DSRPHLIGGHGDYVWETGKFSNAPETGLETWFIRGGSAGAALYKFLQPGIYAYVTHNLIEAANLGATAHFKVEGKWNDDL 325
Cdd:TIGR02376 224 DSRPHLIGGHGDYVWVTGKFANPPNRDVETWFIPGGSAAAALYTFEQPGVYAYVDHNLIEAFEKGAAAQVKVEGAWNPDL 303


                  ....*...
8RGB_A        326 MTQVKAPA 333
Cdd:TIGR02376 304 MTQVVAPT 311
 
Name Accession Description Interval E-value
Cu_nitrite_red TIGR02376
nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. ...
 6-333 0e+00

nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. It reduces nitrite to nitric oxide, the first step in denitrification. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 131429 [Multi-domain]  Cd Length: 311  Bit Score: 525.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A          6 LPRQRVDLVAPPFVHVHEQATKQGPKIMEFKLVVQEKKMVIDEkGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATN 85
Cdd:TIGR02376   1 LPRVKVDLVAPPFVHVHDQIDRSGPKVVEVTMTIEEKKMVIDD-GVTYQAMTFDGSVPGPLIRVHEGDYVELTLINPPTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A         86 TMPHNIDFHSATGALGGGALTLINPGEQVVLRWKATRTGVFVYHCAPGGpMIPWHVVSGMNGAVMVLPRDGLNdghghsl 165
Cdd:TIGR02376  80 TMPHNVDFHAATGALGGAALTQVNPGETATLRFKATRPGAFVYHCAPPG-MVPWHVVSGMNGAIMVLPREGLP------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A        166 RYDRIYYIGEQDLYVPRDEKgnfksydsPGEAYSDTEEVMRKLTPTHVVFNGKAGALTGKNALNANVGENVLIVHSQANR 245
Cdd:TIGR02376 152 EYDKEYYIGESDLYTPKDEG--------EGGAYEDDVAAMRTLTPTHVVFNGAVGALTGDNALTAGVGERVLFVHSQPNR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A        246 DSRPHLIGGHGDYVWETGKFSNAPETGLETWFIRGGSAGAALYKFLQPGIYAYVTHNLIEAANLGATAHFKVEGKWNDDL 325
Cdd:TIGR02376 224 DSRPHLIGGHGDYVWVTGKFANPPNRDVETWFIPGGSAAAALYTFEQPGVYAYVDHNLIEAFEKGAAAQVKVEGAWNPDL 303


                  ....*...
8RGB_A        326 MTQVKAPA 333
Cdd:TIGR02376 304 MTQVVAPT 311
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 34-154 1.20e-54

Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center, which serves as the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis.


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 174.71  E-value: 1.20e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       34 EFKLVVQEKKMVIDeKGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATNTMPHNIDFHSATGAlGGGALTLINPGEQ 113
Cdd:cd11020   3 EVTLTTVEKVVEIA-PGVTYTAWTFNGQVPGPVIRVREGDTVELTLTNPGTNTMPHSIDFHAATGP-GGGEFTTIAPGET 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
8RGB_A      114 VVLRWKATRTGVFVYHCAPGGpmIPWHVVSGMNGAVMVLPR 154
Cdd:cd11020  81 KTFSFKALYPGVFMYHCATAP--VLMHIANGMYGAIIVEPK 119
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 169-321 4.77e-28

Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 106.63  E-value: 4.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A        169 RIYYIGEQDLYvPRDEKGNFKSYDSPGEAYSDTEevmrkLTPTHVVFNGKAGALTGKNALNANVGENVLIVhSQANRDSR 248
Cdd:pfam00394   1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFP-----PVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
8RGB_A        249 PHLIGGHGDY-VWETGKFSNAPETglETWFIRGGSAGAALYKFLQ-PGIYAYVTHNLIEAANLGATAHFKVEGKW 321
Cdd:pfam00394  74 NFSIEGHKMTvVEVDGVYVNPFTV--DSLDIFPGQRYSVLVTANQdPGNYWIVASPNIPAFDNGTAAAILRYSGA 146
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 38-153 2.51e-07

Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis;


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 51.86  E-value: 2.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       38 VVQEKKMVIDEkGTTFQAMTFNG---SMPGPLMVVHEGDYVEVTLVNpaTNTMPHNIDFH-------SATGA-LGGGAL- 105
Cdd:COG2132 301 AVRTRELVLTG-GMAGYVWTINGkafDPDRPDLTVKLGERERWTLVN--DTMMPHPFHLHghqfqvlSRNGKpPPEGGWk 377

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
8RGB_A      106 --TLINPGEQVVLRWKATR-TGVFVYHCapggpMIPWHVVSGMNGAVMVLP 153
Cdd:COG2132 378 dtVLVPPGETVRILFRFDNyPGDWMFHC-----HILEHEDAGMMGQFEVVP 423
PLN02191 PLN02191
L-ascorbate oxidase
 56-168 3.26e-04

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 42.31  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A        56 MTFNGSMPGPLMVVHEGDYVEVTLVNPATN----TMPHNIDFHSATGALGGGALT--LINPGEQVVLRWKATRTGVFVYH 129
Cdd:PLN02191  45 MTVNGQFPGPTIDAVAGDTIVVHLTNKLTTeglvIHWHGIRQKGSPWADGAAGVTqcAINPGETFTYKFTVEKPGTHFYH 124

                         90       100       110
                 ....*....|....*....|....*....|....*....
8RGB_A       130 CAPGgpmipWHVVSGMNGAVMVlprdGLNDGHGHSLRYD 168
Cdd:PLN02191 125 GHYG-----MQRSAGLYGSLIV----DVAKGPKERLRYD 154
 
Name Accession Description Interval E-value
Cu_nitrite_red TIGR02376
nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. ...
 6-333 0e+00

nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. It reduces nitrite to nitric oxide, the first step in denitrification. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 131429 [Multi-domain]  Cd Length: 311  Bit Score: 525.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A          6 LPRQRVDLVAPPFVHVHEQATKQGPKIMEFKLVVQEKKMVIDEkGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATN 85
Cdd:TIGR02376   1 LPRVKVDLVAPPFVHVHDQIDRSGPKVVEVTMTIEEKKMVIDD-GVTYQAMTFDGSVPGPLIRVHEGDYVELTLINPPTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A         86 TMPHNIDFHSATGALGGGALTLINPGEQVVLRWKATRTGVFVYHCAPGGpMIPWHVVSGMNGAVMVLPRDGLNdghghsl 165
Cdd:TIGR02376  80 TMPHNVDFHAATGALGGAALTQVNPGETATLRFKATRPGAFVYHCAPPG-MVPWHVVSGMNGAIMVLPREGLP------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A        166 RYDRIYYIGEQDLYVPRDEKgnfksydsPGEAYSDTEEVMRKLTPTHVVFNGKAGALTGKNALNANVGENVLIVHSQANR 245
Cdd:TIGR02376 152 EYDKEYYIGESDLYTPKDEG--------EGGAYEDDVAAMRTLTPTHVVFNGAVGALTGDNALTAGVGERVLFVHSQPNR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A        246 DSRPHLIGGHGDYVWETGKFSNAPETGLETWFIRGGSAGAALYKFLQPGIYAYVTHNLIEAANLGATAHFKVEGKWNDDL 325
Cdd:TIGR02376 224 DSRPHLIGGHGDYVWVTGKFANPPNRDVETWFIPGGSAAAALYTFEQPGVYAYVDHNLIEAFEKGAAAQVKVEGAWNPDL 303


                  ....*...
8RGB_A        326 MTQVKAPA 333
Cdd:TIGR02376 304 MTQVVAPT 311
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 34-154 1.20e-54

Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center, which serves as the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis.


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 174.71  E-value: 1.20e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       34 EFKLVVQEKKMVIDeKGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATNTMPHNIDFHSATGAlGGGALTLINPGEQ 113
Cdd:cd11020   3 EVTLTTVEKVVEIA-PGVTYTAWTFNGQVPGPVIRVREGDTVELTLTNPGTNTMPHSIDFHAATGP-GGGEFTTIAPGET 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
8RGB_A      114 VVLRWKATRTGVFVYHCAPGGpmIPWHVVSGMNGAVMVLPR 154
Cdd:cd11020  81 KTFSFKALYPGVFMYHCATAP--VLMHIANGMYGAIIVEPK 119
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 32-154 2.01e-54

Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center, which serves as the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis. The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles two domain nitrite reductase in both sequence homology and structure similarity. It consists of two domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of larger laccases.


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 174.22  E-value: 2.01e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       32 IMEFKLVVQEKKMVIDEkGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATNTMPHNIDFHSATGALGGGALTLINPG 111
Cdd:cd04201   1 KVEVDMETVEKTMQLDD-GVEYRYWTFDGDIPGPMLRVREGDTVELHFSNNPSSTMPHNIDFHAATGAGGGAGATFIAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
8RGB_A      112 EQVVLRWKATRTGVFVYHCAPGGPmiPWHVVSGMNGAVMVLPR 154
Cdd:cd04201  80 ETSTFSFKATQPGLYVYHCAVAPV--PMHIANGMYGLILVEPK 120
CuRO_2_CuNIR cd04208
Cupredoxin domain 2 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 167-318 8.05e-45

Cupredoxin domain 2 of Copper-containing nitrite reductase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center in the protein. The type 2 copper center of a copper nitrite reductase is the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis.


Pssm-ID: 259871 [Multi-domain]  Cd Length: 143  Bit Score: 150.40  E-value: 8.05e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A      167 YDRIYYIGEQDLYVPRDEkgnfksydspGEAYSDTEEVMRKLTPTHVVFNGKAGALTGKNALNANVGENVLIVHSQA--N 244
Cdd:cd04208   1 VDREYYLVQSELYTGGDD----------GGVGLFDYAKMLDEKPDYVVFNGRVFAYTGTNPLQAKVGERVRIYVVNAgpN 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
8RGB_A      245 RDSRPHLIGGHGDYVWETGKFSNAPETGLETWFIRGGSAGAALYKFLQPGIYAYVTHNLIEaANLGATAHFKVE 318
Cdd:cd04208  71 LTSSFHVIGGIFDRVYPEGSNPNNPLRGVQTVLVPPGGGAIVEFTFPVPGNYALVDHALSR-AEKGALGVLKVE 143
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 169-321 4.77e-28

Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 106.63  E-value: 4.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A        169 RIYYIGEQDLYvPRDEKGNFKSYDSPGEAYSDTEevmrkLTPTHVVFNGKAGALTGKNALNANVGENVLIVhSQANRDSR 248
Cdd:pfam00394   1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFP-----PVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
8RGB_A        249 PHLIGGHGDY-VWETGKFSNAPETglETWFIRGGSAGAALYKFLQ-PGIYAYVTHNLIEAANLGATAHFKVEGKW 321
Cdd:pfam00394  74 NFSIEGHKMTvVEVDGVYVNPFTV--DSLDIFPGQRYSVLVTANQdPGNYWIVASPNIPAFDNGTAAAILRYSGA 146
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 34-154 5.10e-20

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. Three copper ions of type 1 lie close to one another near the surface of the central part of the trimer, and, effectively, a trimeric substrate binding site is formed in their vicinity. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities.


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 84.24  E-value: 5.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       34 EFKLVVQEKKMVIDEkGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLVNpaTNTMPHNIDFH-SATGALGGGALTLINPGE 112
Cdd:cd11024   3 EFTLVAEDAEIEIAP-GVVFKAWTYNGTVPGPTLRATEGDLVRIHFIN--TGDHPHTIHFHgIHDAAMDGTGLGPIMPGE 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
8RGB_A      113 QVVLRWKATRTGVFVYHC--APGGPmipwHVVSGMNGAVMVLPR 154
Cdd:cd11024  80 SFTYEFVAEPAGTHLYHChvQPLKE----HIAMGLYGAFIVDPK 119
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 34-151 2.01e-19

Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins; Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 82.72  E-value: 2.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       34 EFKLVVQEKKMVIDekGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLVNpATNTMPHNIDFH-----SATGALGGGALT-- 106
Cdd:cd04206   2 EYELTITETTVNPD--GVLRQVITVNGQFPGPTIRVKEGDTVEVTVTN-NLPNEPTSIHWHglrqpGTNDGDGVAGLTqc 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
8RGB_A      107 LINPGEQVVLRWKAT-RTGVFVYHCAPGGpmipwHVVSGMNGAVMV 151
Cdd:cd04206  79 PIPPGESFTYRFTVDdQAGTFWYHSHVGG-----QRADGLYGPLIV 119
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 41-151 5.27e-12

The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins; This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. Its biological function has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals.


Pssm-ID: 259928 [Multi-domain]  Cd Length: 122  Bit Score: 62.11  E-value: 5.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       41 EKKMVIDE------KGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLVNpaTNTMPHNIDFHSA-------TGALGGGALTL 107
Cdd:cd13859   2 EFEMTIDEtvitvvPGLDFKTFAFNGQVPGPLIHVKEGDDLVVHVTN--NTTLPHTIHWHGVlqmgswkMDGVPGVTQPA 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
8RGB_A      108 INPGEQVVLRWKATRTGVFVYHCAPGgpmIPWHV-VSGMNGAVMV 151
Cdd:cd13859  80 IEPGESFTYKFKAERPGTLWYHCHVN---VNEHVgMRGMWGPLIV 121
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 50-156 2.12e-08

Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 51.86  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A         50 GTTFQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATNTMP---HNIDFHSATGALG--GGALTLINPGEQVVLRWKATRT- 123
Cdd:pfam07732  12 GTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNLDEPTSihwHGLQQRGTPWMDGvpGVTQCPIPPGQSFTYRFQVKQQa 91

                          90       100       110
                  ....*....|....*....|....*....|...
8RGB_A        124 GVFVYHcapggPMIPWHVVSGMNGAVMVLPRDG 156
Cdd:pfam07732  92 GTYWYH-----SHTSGQQAAGLAGAIIIEDRAS 119
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 41-155 4.52e-08

Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are not recognized by the pfam00394 model.


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 51.28  E-value: 4.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A         41 EKKMVIDEKGTTFQAMTFNG---SMPGPLMVVHEGDYVEVTLVNpaTNTMPHNIDFHSATGAL---GGGALT-------- 106
Cdd:pfam07731   7 PTLLQITSGNFRRNDWAINGllfPPNTNVITLPYGTVVEWVLQN--TTTGVHPFHLHGHSFQVlgrGGGPWPeedpktyn 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
8RGB_A        107 ----------LINPGEQVVLRWKATRTGVFVYHCApggpmIPWHVVSGMNGAVMVLPRD 155
Cdd:pfam07731  85 lvdpvrrdtvQVPPGGWVAIRFRADNPGVWLFHCH-----ILWHLDQGMMGQFVVRPGD 138
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 38-153 2.51e-07

Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis;


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 51.86  E-value: 2.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       38 VVQEKKMVIDEkGTTFQAMTFNG---SMPGPLMVVHEGDYVEVTLVNpaTNTMPHNIDFH-------SATGA-LGGGAL- 105
Cdd:COG2132 301 AVRTRELVLTG-GMAGYVWTINGkafDPDRPDLTVKLGERERWTLVN--DTMMPHPFHLHghqfqvlSRNGKpPPEGGWk 377

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
8RGB_A      106 --TLINPGEQVVLRWKATR-TGVFVYHCapggpMIPWHVVSGMNGAVMVLP 153
Cdd:COG2132 378 dtVLVPPGETVRILFRFDNyPGDWMFHC-----HILEHEDAGMMGQFEVVP 423
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 34-129 6.70e-07

The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily includes bacterial two domain multicopper oxidases (2dMCOs) with similarity to McoN from Nitrosomonas europaea. 2dMCO is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals.


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 47.58  E-value: 6.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       34 EFKLVVQEKKMVIdEKGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLvnpaTNTMPH--NIDFHSAT---GALGGGALT-- 106
Cdd:cd13860   2 VFHLVAEPVKWEI-APGVKVEAWGYNGSVPGPTIEVTEGDRVRILV----TNELPEptTVHWHGLPvpnGMDGVPGITqp 76

                        90       100
                ....*....|....*....|...
8RGB_A      107 LINPGEQVVLRWKATRTGVFVYH 129
Cdd:cd13860  77 PIQPGETFTYEFTAKQAGTYMYH 99
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 34-155 1.09e-06

Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis;


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 49.93  E-value: 1.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       34 EFKLVVQEKKMVIDeKGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLVN---PATNTMPHNIdfHSAtGALGGGALTLINP 110
Cdd:COG2132  15 EYELTAQPATVELL-PGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNrlpEPTTVHWHGL--RVP-NAMDGVPGDPIAP 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
8RGB_A      111 GEQVVLRWKAT-RTGVFVYHCAPGGPMiPWHVVSGMNGAVMVLPRD 155
Cdd:COG2132  91 GETFTYEFPVPqPAGTYWYHPHTHGST-AEQVYRGLAGALIVEDPE 135
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 34-129 1.54e-06

The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces; The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 46.47  E-value: 1.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       34 EFKLVVQEKKMVIDekGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLvnpaTNTMPHN---IDFH-----SATGALGGGAL 105
Cdd:cd13854   5 KYTLTITNSTLAPD--GVEKEVMLINGQYPGPLIEANWGDTIEVTV----INKLQDNgtsIHWHgirqlNTNWQDGVPGV 78

                        90       100
                ....*....|....*....|....*.
8RGB_A      106 TL--INPGEQVVLRWKATRTGVFVYH 129
Cdd:cd13854  79 TEcpIAPGDTRTYRFRATQYGTSWYH 104
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 46-151 1.02e-05

The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family includes bacteria multicopper oxidases (MCOs) represented by McoC from pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic multicopper oxidase, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. They are capable of oxidizing a vast range of substrates, varying from aromatic compunds to inorganic compounds such as metals. Most MCOs have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 44.39  E-value: 1.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       46 IDEKGTTFqaMTFNGSMPGPLMVVHEGDYVEVTLVN----PAT---NTMPHNIDFHsatgalgGGALTLINPGEQVVLRW 118
Cdd:cd13855  16 LPGKPTEF--WAYNGSVPGPLIEVFEGDTVEITFRNrlpePTTvhwHGLPVPPDQD-------GNPHDPVAPGNDRVYRF 86

                        90       100       110
                ....*....|....*....|....*....|....*
8RGB_A      119 K--ATRTGVFVYHCAPGGpMIPWHVVSGMNGAVMV 151
Cdd:cd13855  87 TlpQDSAGTYWYHPHPHG-HTAEQVYRGLAGAFVV 120
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 207-308 1.23e-05

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 43.76  E-value: 1.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A      207 KLTPTHVVFNGKAGALTGKNALNANVGENVLIVHSqaNRDSRPH--LIGGHGDYVWETGKFSNAPETglETWFIRGGSAG 284
Cdd:cd00920   4 TASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVQFV--NKLGENHsvTIAGFGVPVVAMAGGANPGLV--NTLVIGPGESA 79

                        90       100
                ....*....|....*....|....
8RGB_A      285 AALYKFLQPGIYAYVTHNLIEAAN 308
Cdd:cd00920  80 EVTFTTDQAGVYWFYCTIPGHNHA 103
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 34-81 8.93e-05

The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity, and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259917 [Multi-domain]  Cd Length: 116  Bit Score: 41.50  E-value: 8.93e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
8RGB_A       34 EFKLVVQEKKMVIDEKGTTfqAMTFNGSMPGPLMVVHEGDYVEVTLVN 81
Cdd:cd13848   2 EYDLVIAETPVNIGGKEGE--AITVNGQVPGPLLRFKEGDDATIRVHN 47
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 35-94 2.16e-04

The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Plants usually express multiple laccase genes, but their precise physiological/biochemical roles remain largely unclear. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259918 [Multi-domain]  Cd Length: 117  Bit Score: 40.32  E-value: 2.16e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       35 FKLVVQEKKmvIDEKGTTFQAMTFNGSMPGPLMVVHEGDYVEVTlvnpATNTMPHNIDFH 94
Cdd:cd13849   1 YTFVVQEKN--VTRLCSTKSILTVNGQFPGPTIRVHEGDTVVVN----VTNRSPYNITIH 54
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 50-152 2.26e-04

The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi, plants and insects. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259927 [Multi-domain]  Cd Length: 105  Bit Score: 39.83  E-value: 2.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       50 GTTFQAMTFNGSMPGPLMVVHEGDYVEVTLVNpatntmphnidfhsatgALGGGALTL---------------------- 107
Cdd:cd13858   2 GVERPVITVNGQLPGPSIEVCEGDTVVVDVKN-----------------RLPGESTTIhwhgihqrgtpymdgvpmvtqc 64

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
8RGB_A      108 -INPGEQVVLRWKATRTGVFVYHCAPGgpmipWHVVSGMNGAVMVL 152
Cdd:cd13858  65 pILPGQTFRYKFKADPAGTHWYHSHSG-----TQRADGLFGALIVR 105
PLN02191 PLN02191
L-ascorbate oxidase
 56-168 3.26e-04

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 42.31  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A        56 MTFNGSMPGPLMVVHEGDYVEVTLVNPATN----TMPHNIDFHSATGALGGGALT--LINPGEQVVLRWKATRTGVFVYH 129
Cdd:PLN02191  45 MTVNGQFPGPTIDAVAGDTIVVHLTNKLTTeglvIHWHGIRQKGSPWADGAAGVTqcAINPGETFTYKFTVEKPGTHFYH 124

                         90       100       110
                 ....*....|....*....|....*....|....*....
8RGB_A       130 CAPGgpmipWHVVSGMNGAVMVlprdGLNDGHGHSLRYD 168
Cdd:PLN02191 125 GHYG-----MQRSAGLYGSLIV----DVAKGPKERLRYD 154
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 68-150 4.01e-04

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: 39.52  E-value: 4.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       68 VVHEGDYVEVTLVNPatNTMPHNI---DFHSATGALGGGALTLIN------PGEQVVLRWKATRTGVFVYHCAPGGpmip 138
Cdd:cd00920  26 VVPVGDTVRVQFVNK--LGENHSVtiaGFGVPVVAMAGGANPGLVntlvigPGESAEVTFTTDQAGVYWFYCTIPG---- 99

                        90
                ....*....|..
8RGB_A      139 wHVVSGMNGAVM 150
Cdd:cd00920 100 -HNHAGMVGTIN 110
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 44-129 4.98e-04

The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus; Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259919 [Multi-domain]  Cd Length: 117  Bit Score: 39.20  E-value: 4.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       44 MVIDEKGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLvnpaTNTMPHN--IDFHS--------ATGALGggaLT--LINPG 111
Cdd:cd13850   8 GSPDGDGGEREVILINGQFPGPPIILDEGDEVEILV----TNNLPVNttIHFHGilqrgtpwSDGVPG---VTqwPIQPG 80

                        90
                ....*....|....*....
8RGB_A      112 EQVVLRWKATR-TGVFVYH 129
Cdd:cd13850  81 GSFTYRWKAEDqYGLYWYH 99
PetE COG3794
Plastocyanin [Energy production and conversion];
69-151 5.16e-04

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 38.05  E-value: 5.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       69 VHEGDyvEVTLVNpaTNTMPHNIdfHSATGALGGGALTLINPGEQVvlRWKATRTGVFVYHCAPggpmipwHvvSGMNGA 148
Cdd:COG3794  10 VKPGD--TVTWVN--TDSVPHNV--TSDDGPDGAFDSGLLAPGETF--SVTFDEPGTYDYYCTP-------H--PWMVGT 72


                ...
8RGB_A      149 VMV 151
Cdd:COG3794  73 IVV 75
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 50-145 6.06e-04

Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins; Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 2, 4, and 6 of the 6-domain MCO ceruloplasmin and similar proteins.


Pssm-ID: 259870 [Multi-domain]  Cd Length: 132  Bit Score: 39.37  E-value: 6.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       50 GTTFQAMTFNGSMpgplMVVHEGDYVEVTLVNPATNTMPHNIDFH-------SATGALGGGALTLINP----------GE 112
Cdd:cd04207  24 GMPFKEGDANTDI----FSVEAGDVVEIVLINAGNHDMQHPFHLHghsfwvlGSGGGPFDAPLNLTNPpwrdtvlvppGG 99

                        90       100       110
                ....*....|....*....|....*....|...
8RGB_A      113 QVVLRWKATRTGVFVYHCapggpMIPWHVVSGM 145
Cdd:cd04207 100 WVVIRFKADNPGVWMLHC-----HILEHEDAGM 127
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 55-129 6.66e-04

The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259914 [Multi-domain]  Cd Length: 120  Bit Score: 38.97  E-value: 6.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       55 AMTFNGSMPGPLMVVHEGDYVEVTLVNpatNTMPHNIDFH------SATGALGGGALT---LINPGEQVVLRWKATRTGV 125
Cdd:cd13845  21 VIGINGQFPGPTIRATAGDTIVVELEN---KLPTEGVAIHwhgirqRGTPWADGTASVsqcPINPGETFTYQFVVDRPGT 97


                ....
8RGB_A      126 FVYH 129
Cdd:cd13845  98 YFYH 101
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 55-168 8.97e-04

L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 40.89  E-value: 8.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A         55 AMTFNGSMPGPLMVVHEGDYVEVTLVNPAT--NTMP--HNIDFHSATGALGGGALT--LINPGEQVVLRWKATRTGVFVY 128
Cdd:TIGR03388  22 VIGINGQFPGPTIRAQAGDTIVVELTNKLHteGVVIhwHGIRQIGTPWADGTAGVTqcAINPGETFIYNFVVDRPGTYFY 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
8RGB_A        129 HCAPGgpMipwHVVSGMNGAVMVLPRDGLNDghghSLRYD 168
Cdd:TIGR03388 102 HGHYG--M---QRSAGLYGSLIVDVPDGEKE----PFHYD 132
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 34-152 1.15e-03

The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins; This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. The biological function of McoN has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals.


Pssm-ID: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 38.77  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       34 EFKLVVQE-----KKMVIDEKGTTFQAMTFNG-SMPG-PLMVVHEGDYVEVTLVNpaTNTMPHNIDFH-------SATGA 99
Cdd:cd04202   3 DYTLVLQEwfvdpGTTPMPPEGMDFNYFTINGkSFPAtPPLVVKEGDRVRIRLIN--LSMDHHPMHLHghfflvtATDGG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
8RGB_A      100 -LGGGA-----LTLINPGEQVVLRWKATRTGVFVYHCapggpMIPWHVVSGMNGAVMVL 152
Cdd:cd04202  81 pIPGSApwpkdTLNVAPGERYDIEFVADNPGDWMFHC-----HKLHHAMNGMGGGMMTL 134
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 34-81 1.19e-03

The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus; The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259922 [Multi-domain]  Cd Length: 139  Bit Score: 38.77  E-value: 1.19e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
8RGB_A       34 EFKLVVQEKKMVIDEKGTTFQamTFNGSMPGPLMVVHEGDYVEVTLVN 81
Cdd:cd13853   3 EVTLTVEYGRVTLAGLPVTLR--TYNGSIPGPTLRVRPGDTLRITLKN 48
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 108-151 1.87e-03

The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259966 [Multi-domain]  Cd Length: 160  Bit Score: 38.39  E-value: 1.87e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
8RGB_A      108 INPGEQVVLRWKATRTGVFVYHCapggpMIPWHVVSGMnGAVMV 151
Cdd:cd13899 120 VPPGGSVVIRFRADNPGVWFFHC-----HIEWHLEAGL-AATFI 157
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 55-94 2.06e-03

laccase, plant; Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.


Pssm-ID: 274556 [Multi-domain]  Cd Length: 539  Bit Score: 39.72  E-value: 2.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
8RGB_A         55 AMTFNGSMPGPLMVVHEGDYVEVTLVNPATNtmphNIDFH 94
Cdd:TIGR03389  24 ILTVNGKFPGPTLYAREGDTVIVNVTNNVQY----NVTIH 59
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 44-129 3.25e-03

The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida, which is involved in the oxidation of Mn(II). However, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCO catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 36.83  E-value: 3.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       44 MVIDEKGTTFQAMTFNGSMPGPLMVVHEGDYVEVTLVN--PATNT-------MPHNIDfhsatgalGGGALT--LINPGE 112
Cdd:cd13861  11 ELLDLGGPTTRTWGYNGQVPGPELRVRQGDTLRVRLTNrlPEPTTihwhglrLPNAMD--------GVPGLTqpPVPPGE 82

                        90
                ....*....|....*..
8RGB_A      113 QVVLRWKATRTGVFVYH 129
Cdd:cd13861  83 SFTYEFTPPDAGTYWYH 99
PLN02604 PLN02604
oxidoreductase
 42-169 3.78e-03

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 39.07  E-value: 3.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A        42 KKMVIdekgttfqamTFNGSMPGPLMVVHEGDYVEVTLVNpatNTMPHNIDFH-SATGALG--------GGALTLINPGE 112
Cdd:PLN02604  42 KKLVI----------TINGRSPGPTILAQQGDTVIVELKN---SLLTENVAIHwHGIRQIGtpwfdgteGVTQCPILPGE 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
8RGB_A       113 QVVLRWKATRTGVFVYHCAPGgpmipWHVVSGMNGAVMVLPRDGLNDghGHSLRYDR 169
Cdd:PLN02604 109 TFTYEFVVDRPGTYLYHAHYG-----MQREAGLYGSIRVSLPRGKSE--PFSYDYDR 158
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 108-151 4.27e-03

Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction only];


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 37.25  E-value: 4.27e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
8RGB_A      108 INPGEQVVLRWKATRTGVFVYHCapggpMIPWHVVSGMNGAVMV 151
Cdd:COG4454 112 LAPGETGELVWTFTKAGTFEFAC-----LIPGHYEAGMTGKIVV 150
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 55-129 7.66e-03

The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259925 [Multi-domain]  Cd Length: 125  Bit Score: 36.16  E-value: 7.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8RGB_A       55 AMTFNGSMPGPLMVVHEGDYVEVTLVNPATN-TMP-------HNIDFHSATGALGGGALTL--INPGEQVVLRWKAT-RT 123
Cdd:cd13856  21 AVLANGQFPGPLITANKGDTFRITVVNQLTDpTMRrstsihwHGIFQHGTNYADGPAFVTQcpIAPNHSFTYDFTAGdQA 100


                ....*.
8RGB_A      124 GVFVYH 129
Cdd:cd13856 101 GTFWYH 106
 
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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