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Conserved domains on  [gi|2827765|sp|P25006|]
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RecName: Full=Copper-containing nitrite reductase; AltName: Full=Cu-NIR; Flags: Precursor

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. ...
 50-376 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: 537.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765     50 LPRVKVDLVKPPFVHAHDQVAKTGPRVVEFTMTIEEKKLVIDrEGTEIHAMTFNGSVPGPLMVVHENDYVELRLINPDTN 129
Cdd:TIGR02376   1 LPRVKVDLVAPPFVHVHDQIDRSGPKVVEVTMTIEEKKMVID-DGVTYQAMTFDGSVPGPLIRVHEGDYVELTLINPPTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    130 TLLHNIDFHAATGALGGGALTQVNPGEETTLRFKATKPGVFVYHCAPEGMVPWHVTSGMNGAIMVLPRDGLKDekgqplt 209
Cdd:TIGR02376  80 TMPHNVDFHAATGALGGAALTQVNPGETATLRFKATRPGAFVYHCAPPGMVPWHVVSGMNGAIMVLPREGLPE------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    210 YDKIYYVGEQDFYVPKDEAgnykkyetPGEAYEDAVKAMRTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQANRD 289
Cdd:TIGR02376 153 YDKEYYIGESDLYTPKDEG--------EGGAYEDDVAAMRTLTPTHVVFNGAVGALTGDNALTAGVGERVLFVHSQPNRD 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    290 TRPHLIGGHGDYVWATGKFRNPPDLDQETWLIPGGTAGAAFYTFRQPGVYAYVNHNLIEAFELGAAGHFKVTGEWNDDLM 369
Cdd:TIGR02376 225 SRPHLIGGHGDYVWVTGKFANPPNRDVETWFIPGGSAAAALYTFEQPGVYAYVDHNLIEAFEKGAAAQVKVEGAWNPDLM 304


                  ....*..
gi 2827765    370 TSVVKPA 376
Cdd:TIGR02376 305 TQVVAPT 311
 
Name Accession Description Interval E-value
Cu_nitrite_red TIGR02376
nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. ...
 50-376 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: 537.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765     50 LPRVKVDLVKPPFVHAHDQVAKTGPRVVEFTMTIEEKKLVIDrEGTEIHAMTFNGSVPGPLMVVHENDYVELRLINPDTN 129
Cdd:TIGR02376   1 LPRVKVDLVAPPFVHVHDQIDRSGPKVVEVTMTIEEKKMVID-DGVTYQAMTFDGSVPGPLIRVHEGDYVELTLINPPTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    130 TLLHNIDFHAATGALGGGALTQVNPGEETTLRFKATKPGVFVYHCAPEGMVPWHVTSGMNGAIMVLPRDGLKDekgqplt 209
Cdd:TIGR02376  80 TMPHNVDFHAATGALGGAALTQVNPGETATLRFKATRPGAFVYHCAPPGMVPWHVVSGMNGAIMVLPREGLPE------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    210 YDKIYYVGEQDFYVPKDEAgnykkyetPGEAYEDAVKAMRTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQANRD 289
Cdd:TIGR02376 153 YDKEYYIGESDLYTPKDEG--------EGGAYEDDVAAMRTLTPTHVVFNGAVGALTGDNALTAGVGERVLFVHSQPNRD 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    290 TRPHLIGGHGDYVWATGKFRNPPDLDQETWLIPGGTAGAAFYTFRQPGVYAYVNHNLIEAFELGAAGHFKVTGEWNDDLM 369
Cdd:TIGR02376 225 SRPHLIGGHGDYVWVTGKFANPPNRDVETWFIPGGSAAAALYTFEQPGVYAYVDHNLIEAFEKGAAAQVKVEGAWNPDLM 304


                  ....*..
gi 2827765    370 TSVVKPA 376
Cdd:TIGR02376 305 TQVVAPT 311
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 76-197 3.80e-46

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: 153.91  E-value: 3.80e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   76 VVEFTMTIEEKKLVIDrEGTEIHAMTFNGSVPGPLMVVHENDYVELRLINPDTNTLLHNIDFHaATGALGGGALTQVNPG 155
Cdd:cd11020   1 VVEVTLTTVEKVVEIA-PGVTYTAWTFNGQVPGPVIRVREGDTVELTLTNPGTNTMPHSIDFH-AATGPGGGEFTTIAPG 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 2827765  156 EETTLRFKATKPGVFVYHCAPEGMvPWHVTSGMNGAIMVLPR 197
Cdd:cd11020  79 ETKTFSFKALYPGVFMYHCATAPV-LMHIANGMYGAIIVEPK 119
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 212-364 2.50e-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: 107.79  E-value: 2.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    212 KIYYVGEQDFYvPKDEAGNYKKYETPGEAYEDAvkamrTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVhSQANRDTR 291
Cdd:pfam00394   1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDF-----PPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2827765    292 PHLIGGHGDY-VWATGKFRNPpdLDQETWLIPGGTAGAAFYTFRQ-PGVYAYVNHNLIEAFELGAAGHFKVTGEW 364
Cdd:pfam00394  74 NFSIEGHKMTvVEVDGVYVNP--FTVDSLDIFPGQRYSVLVTANQdPGNYWIVASPNIPAFDNGTAAAILRYSGA 146
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 74-198 1.08e-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: 50.32  E-value: 1.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   74 PRVVEFTMTIEEKKLVIDReGTEIHAMTFNGSVPGPLMVVHENDYVELRLIN---PDTNTLLHNI------DFHAATGal 144
Cdd:COG2132  11 GGGREYELTAQPATVELLP-GKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNrlpEPTTVHWHGLrvpnamDGVPGDP-- 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 2827765  145 gggaltqVNPGEETTLRFKATKP-GVFVYHCAPEGMVPWHVTSGMNGAIMVLPRD 198
Cdd:COG2132  88 -------IAPGETFTYEFPVPQPaGTYWYHPHTHGSTAEQVYRGLAGALIVEDPE 135
PLN02191 PLN02191
L-ascorbate oxidase
 76-229 1.60e-05

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 46.93  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    76 VVEFTMTIEEKKLVID-REGTeihAMTFNGSVPGPLMVVHENDYVELRLINPDTNTLL----HNIDFHAATGALGGGALT 150
Cdd:PLN02191  23 VREYTWEVEYKYWWPDcKEGA---VMTVNGQFPGPTIDAVAGDTIVVHLTNKLTTEGLvihwHGIRQKGSPWADGAAGVT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   151 Q--VNPGEETTLRFKATKPGVFVYHcapeGMVPWHVTSGMNGAIMVLPRDGlkdeKGQPLTYDKIYYVGEQDFY---VPK 225
Cdd:PLN02191 100 QcaINPGETFTYKFTVEKPGTHFYH----GHYGMQRSAGLYGSLIVDVAKG----PKERLRYDGEFNLLLSDWWhesIPS 171


                 ....
gi 2827765   226 DEAG 229
Cdd:PLN02191 172 QELG 175
 
Name Accession Description Interval E-value
Cu_nitrite_red TIGR02376
nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. ...
 50-376 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: 537.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765     50 LPRVKVDLVKPPFVHAHDQVAKTGPRVVEFTMTIEEKKLVIDrEGTEIHAMTFNGSVPGPLMVVHENDYVELRLINPDTN 129
Cdd:TIGR02376   1 LPRVKVDLVAPPFVHVHDQIDRSGPKVVEVTMTIEEKKMVID-DGVTYQAMTFDGSVPGPLIRVHEGDYVELTLINPPTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    130 TLLHNIDFHAATGALGGGALTQVNPGEETTLRFKATKPGVFVYHCAPEGMVPWHVTSGMNGAIMVLPRDGLKDekgqplt 209
Cdd:TIGR02376  80 TMPHNVDFHAATGALGGAALTQVNPGETATLRFKATRPGAFVYHCAPPGMVPWHVVSGMNGAIMVLPREGLPE------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    210 YDKIYYVGEQDFYVPKDEAgnykkyetPGEAYEDAVKAMRTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQANRD 289
Cdd:TIGR02376 153 YDKEYYIGESDLYTPKDEG--------EGGAYEDDVAAMRTLTPTHVVFNGAVGALTGDNALTAGVGERVLFVHSQPNRD 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    290 TRPHLIGGHGDYVWATGKFRNPPDLDQETWLIPGGTAGAAFYTFRQPGVYAYVNHNLIEAFELGAAGHFKVTGEWNDDLM 369
Cdd:TIGR02376 225 SRPHLIGGHGDYVWVTGKFANPPNRDVETWFIPGGSAAAALYTFEQPGVYAYVDHNLIEAFEKGAAAQVKVEGAWNPDLM 304


                  ....*..
gi 2827765    370 TSVVKPA 376
Cdd:TIGR02376 305 TQVVAPT 311
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 76-197 3.80e-46

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: 153.91  E-value: 3.80e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   76 VVEFTMTIEEKKLVIDrEGTEIHAMTFNGSVPGPLMVVHENDYVELRLINPDTNTLLHNIDFHaATGALGGGALTQVNPG 155
Cdd:cd11020   1 VVEVTLTTVEKVVEIA-PGVTYTAWTFNGQVPGPVIRVREGDTVELTLTNPGTNTMPHSIDFH-AATGPGGGEFTTIAPG 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 2827765  156 EETTLRFKATKPGVFVYHCAPEGMvPWHVTSGMNGAIMVLPR 197
Cdd:cd11020  79 ETKTFSFKALYPGVFMYHCATAPV-LMHIANGMYGAIIVEPK 119
CuRO_2_CuNIR cd04208
Cupredoxin domain 2 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 210-361 5.58e-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: 151.56  E-value: 5.58e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765  210 YDKIYYVGEQDFYVPKDEagnykkyetpGEAYEDAVKAMRTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQA--N 287
Cdd:cd04208   1 VDREYYLVQSELYTGGDD----------GGVGLFDYAKMLDEKPDYVVFNGRVFAYTGTNPLQAKVGERVRIYVVNAgpN 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2827765  288 RDTRPHLIGGHGDYVWATGKFRNPPDLDQETWLIPGGTAGAAFYTFRQPGVYAYVNHNLIEAfELGAAGHFKVT 361
Cdd:cd04208  71 LTSSFHVIGGIFDRVYPEGSNPNNPLRGVQTVLVPPGGGAIVEFTFPVPGNYALVDHALSRA-EKGALGVLKVE 143
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 76-197 9.95e-42

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: 142.24  E-value: 9.95e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   76 VVEFTMTIEEKKLVIDrEGTEIHAMTFNGSVPGPLMVVHENDYVELRLINPDTNTLLHNIDFHAATGALGGGALTQVNPG 155
Cdd:cd04201   1 KVEVDMETVEKTMQLD-DGVEYRYWTFDGDIPGPMLRVREGDTVELHFSNNPSSTMPHNIDFHAATGAGGGAGATFIAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 2827765  156 EETTLRFKATKPGVFVYHCAPEGmVPWHVTSGMNGAIMVLPR 197
Cdd:cd04201  80 ETSTFSFKATQPGLYVYHCAVAP-VPMHIANGMYGLILVEPK 120
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 212-364 2.50e-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: 107.79  E-value: 2.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    212 KIYYVGEQDFYvPKDEAGNYKKYETPGEAYEDAvkamrTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVhSQANRDTR 291
Cdd:pfam00394   1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDF-----PPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2827765    292 PHLIGGHGDY-VWATGKFRNPpdLDQETWLIPGGTAGAAFYTFRQ-PGVYAYVNHNLIEAFELGAAGHFKVTGEW 364
Cdd:pfam00394  74 NFSIEGHKMTvVEVDGVYVNP--FTVDSLDIFPGQRYSVLVTANQdPGNYWIVASPNIPAFDNGTAAAILRYSGA 146
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 76-197 7.58e-17

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: 75.77  E-value: 7.58e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   76 VVEFTMTIEEKKLVIDrEGTEIHAMTFNGSVPGPLMVVHENDYVELRLINpdTNTLLHNIDFH-AATGALGGGALTQVNP 154
Cdd:cd11024   1 VREFTLVAEDAEIEIA-PGVVFKAWTYNGTVPGPTLRATEGDLVRIHFIN--TGDHPHTIHFHgIHDAAMDGTGLGPIMP 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 2827765  155 GEETTLRFKATKPGVFVYHC--APEGMvpwHVTSGMNGAIMVLPR 197
Cdd:cd11024  78 GESFTYEFVAEPAGTHLYHChvQPLKE---HIAMGLYGAFIVDPK 119
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 77-194 2.16e-14

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: 68.85  E-value: 2.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   77 VEFTMTIEEKKLVIDreGTEIHAMTFNGSVPGPLMVVHENDYVELRLIN--PDTNTLL--HNIDFHAATGALGGGALTQ- 151
Cdd:cd04206   1 REYELTITETTVNPD--GVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNnlPNEPTSIhwHGLRQPGTNDGDGVAGLTQc 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 2827765  152 -VNPGEETTLRFKAT-KPGVFVYHCApegmVPWHVTSGMNGAIMV 194
Cdd:cd04206  79 pIPPGESFTYRFTVDdQAGTFWYHSH----VGGQRADGLYGPLIV 119
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 78-194 9.32e-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: 61.73  E-value: 9.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   78 EFTMTIEEKKLViDREGTEIHAMTFNGSVPGPLMVVHENDYVELRLINpdTNTLLHNIDFHAATGALG-------GGALT 150
Cdd:cd13859   2 EFEMTIDETVIT-VVPGLDFKTFAFNGQVPGPLIHVKEGDDLVVHVTN--NTTLPHTIHWHGVLQMGSwkmdgvpGVTQP 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 2827765  151 QVNPGEETTLRFKATKPGVFVYHCAPEgmVPWHVT-SGMNGAIMV 194
Cdd:cd13859  79 AIEPGESFTYKFKAERPGTLWYHCHVN--VNEHVGmRGMWGPLIV 121
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 94-199 2.05e-07

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: 49.17  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765     94 GTEIHAMTFNGSVPGPLMVVHENDYVELRLINP-DTNTLLH----NIDFHAATGALGGGALTQVNPGEETTLRFKATKP- 167
Cdd:pfam07732  12 GTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNlDEPTSIHwhglQQRGTPWMDGVPGVTQCPIPPGQSFTYRFQVKQQa 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2827765    168 GVFVYHcapeGMVPWHVTSGMNGAIMVLPRDG 199
Cdd:pfam07732  92 GTYWYH----SHTSGQQAAGLAGAIIIEDRAS 119
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 78-194 3.80e-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: 48.35  E-value: 3.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   78 EFTMTIEEKKLVIDReGTEIHAMTFNGSVPGPLMVVHENDYVELRLIN--PDTNTL-LHNIDFHAATGALGGGALTQVNP 154
Cdd:cd13860   2 VFHLVAEPVKWEIAP-GVKVEAWGYNGSVPGPTIEVTEGDRVRILVTNelPEPTTVhWHGLPVPNGMDGVPGITQPPIQP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 2827765  155 GEETTLRFKATKPGVFVYHCAPEGMVpwHVTSGMNGAIMV 194
Cdd:cd13860  81 GETFTYEFTAKQAGTYMYHSHVDEAK--QEDMGLYGAFIV 118
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 250-346 5.55e-07

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: 47.61  E-value: 5.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765  250 TLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQ-ANRDTRPHLIGGHGDYVWATGKFRNPpdlDQETWLIPGGTAGA 328
Cdd:cd00920   4 TASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVQFVNkLGENHSVTIAGFGVPVVAMAGGANPG---LVNTLVIGPGESAE 80

                        90
                ....*....|....*...
gi 2827765  329 AFYTFRQPGVYAYVNHNL 346
Cdd:cd00920  81 VTFTTDQAGVYWFYCTIP 98
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 80-194 8.36e-07

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: 47.47  E-value: 8.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   80 TMTIEEKKL-VIDREGTEIhaMTFNGSVPGPLMVVHENDYVELRLIN--PDTNTL-LHNIDfhaATGALGGGALTQVNPG 155
Cdd:cd13855   5 TLTAAEVRIrLLPGKPTEF--WAYNGSVPGPLIEVFEGDTVEITFRNrlPEPTTVhWHGLP---VPPDQDGNPHDPVAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 2827765  156 EETTLRFK--ATKPGVFVYHCAPEGMVPWHVTSGMNGAIMV 194
Cdd:cd13855  80 NDRVYRFTlpQDSAGTYWYHPHPHGHTAEQVYRGLAGAFVV 120
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 74-198 1.08e-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: 50.32  E-value: 1.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   74 PRVVEFTMTIEEKKLVIDReGTEIHAMTFNGSVPGPLMVVHENDYVELRLIN---PDTNTLLHNI------DFHAATGal 144
Cdd:COG2132  11 GGGREYELTAQPATVELLP-GKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNrlpEPTTVHWHGLrvpnamDGVPGDP-- 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 2827765  145 gggaltqVNPGEETTLRFKATKP-GVFVYHCAPEGMVPWHVTSGMNGAIMVLPRD 198
Cdd:COG2132  88 -------IAPGETFTYEFPVPQPaGTYWYHPHTHGSTAEQVYRGLAGALIVEDPE 135
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 85-198 2.31e-06

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: 46.66  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765     85 EKKLVIDREGTEIHAMTFNG---SVPGPLMVVHENDYVELRLINPDTNTL---LHNIDFHAATGALGGGALT-------- 150
Cdd:pfam07731   7 PTLLQITSGNFRRNDWAINGllfPPNTNVITLPYGTVVEWVLQNTTTGVHpfhLHGHSFQVLGRGGGPWPEEdpktynlv 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2827765    151 --------QVNPGEETTLRFKATKPGVFVYHCApegmVPWHVTSGMNGAIMVLPRD 198
Cdd:pfam07731  87 dpvrrdtvQVPPGGWVAIRFRADNPGVWLFHCH----ILWHLDQGMMGQFVVRPGD 138
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 99-211 7.59e-06

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: 47.82  E-value: 7.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765     99 AMTFNGSVPGPLMVVHENDYVELRLinpdTNTLL--------HNIDFHAATGALGGGALTQ--VNPGEETTLRFKATKPG 168
Cdd:TIGR03388  22 VIGINGQFPGPTIRAQAGDTIVVEL----TNKLHtegvvihwHGIRQIGTPWADGTAGVTQcaINPGETFIYNFVVDRPG 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2827765    169 VFVYHcAPEGMvpwHVTSGMNGAIMVLPRDGLKdekgQPLTYD 211
Cdd:TIGR03388  98 TYFYH-GHYGM---QRSAGLYGSLIVDVPDGEK----EPFHYD 132
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 77-133 9.92e-06

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: 44.19  E-value: 9.92e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 2827765   77 VEFTMTIEEKKLVIDreGTEIHAMTFNGSVPGPLMVVHENDYVELRLINP-DTNTLLH 133
Cdd:cd13848   1 VEYDLVIAETPVNIG--GKEGEAITVNGQVPGPLLRFKEGDDATIRVHNRlDEDTSIH 56
PLN02191 PLN02191
L-ascorbate oxidase
 76-229 1.60e-05

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 46.93  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    76 VVEFTMTIEEKKLVID-REGTeihAMTFNGSVPGPLMVVHENDYVELRLINPDTNTLL----HNIDFHAATGALGGGALT 150
Cdd:PLN02191  23 VREYTWEVEYKYWWPDcKEGA---VMTVNGQFPGPTIDAVAGDTIVVHLTNKLTTEGLvihwHGIRQKGSPWADGAAGVT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   151 Q--VNPGEETTLRFKATKPGVFVYHcapeGMVPWHVTSGMNGAIMVLPRDGlkdeKGQPLTYDKIYYVGEQDFY---VPK 225
Cdd:PLN02191 100 QcaINPGETFTYKFTVEKPGTHFYH----GHYGMQRSAGLYGSLIVDVAKG----PKERLRYDGEFNLLLSDWWhesIPS 171


                 ....
gi 2827765   226 DEAG 229
Cdd:PLN02191 172 QELG 175
PLN02604 PLN02604
oxidoreductase
 86-211 3.45e-05

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 45.62  E-value: 3.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765    86 KKLVIdregteihamTFNGSVPGPLMVVHENDYVELRLINpdtNTLLHNIDFHAA---------TGALGGGALTQVNPGE 156
Cdd:PLN02604  42 KKLVI----------TINGRSPGPTILAQQGDTVIVELKN---SLLTENVAIHWHgirqigtpwFDGTEGVTQCPILPGE 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 2827765   157 ETTLRFKATKPGVFVYHcAPEGMvpwHVTSGMNGAIMVLPRDGlkdeKGQPLTYD 211
Cdd:PLN02604 109 TFTYEFVVDRPGTYLYH-AHYGM---QREAGLYGSIRVSLPRG----KSEPFSYD 155
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 76-194 1.26e-04

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: 41.47  E-value: 1.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   76 VVEFTMTIEEKKLVIDreGTEIHAMTFNGSVPGPLMVVHENDYVELRLIN-----------PDTNTLLH----NIDFH-- 138
Cdd:cd13853   1 VLEVTLTVEYGRVTLA--GLPVTLRTYNGSIPGPTLRVRPGDTLRITLKNdlppegaaneaPAPNTPHCpnttNLHFHgl 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765  139 -AATGALGGGALTQVNPGEETTLRFKATK---PGVFVYHCAPEGMVPWHVTSGMNGAIMV 194
Cdd:cd13853  79 hVSPTGNSDNVFLTIAPGESFTYEYDIPAdhpPGTYWYHPHLHGSTALQVAGGMAGALVV 138
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 151-194 1.50e-04

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: 41.86  E-value: 1.50e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 2827765  151 QVNPGEETTLRFKATKPGVFVYHCAPEgmvpWHVTSGMnGAIMV 194
Cdd:cd13899 119 MVPPGGSVVIRFRADNPGVWFFHCHIE----WHLEAGL-AATFI 157
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 79-173 1.59e-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: 40.74  E-value: 1.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   79 FTMTIEEKklVIDREGTEIHAMTFNGSVPGPLMVVHENDYVELRLINP-DTNTLLHnidFHaatgalgggALTQVN---- 153
Cdd:cd13850   1 FTLTVTEG--SPDGDGGEREVILINGQFPGPPIILDEGDEVEILVTNNlPVNTTIH---FH---------GILQRGtpws 66

                        90       100       110
                ....*....|....*....|....*....|...
gi 2827765  154 ------------PGEETTLRFKATKP-GVFVYH 173
Cdd:cd13850  67 dgvpgvtqwpiqPGGSFTYRWKAEDQyGLYWYH 99
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 152-174 1.18e-03

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


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 37.98  E-value: 1.18e-03
                        10        20
                ....*....|....*....|...
gi 2827765  152 VNPGEETTLRFKATKPGVFVYHC 174
Cdd:cd04223  54 LEPGETATVTFVADKPGVYPYYC 76
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 152-194 1.40e-03

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


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 38.79  E-value: 1.40e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 2827765  152 VNPGEETTLRFKATKPGVFVYHCapegMVPWHVTSGMNGAIMV 194
Cdd:COG4454 112 LAPGETGELVWTFTKAGTFEFAC----LIPGHYEAGMTGKIVV 150
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 100-195 1.42e-03

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: 37.90  E-value: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765  100 MTFNGSVPGPLMVVHENDYVELRLIN--PDTNTLLHnidFHaatgalgggALTQ----------------VNPGEETTLR 161
Cdd:cd13858   8 ITVNGQLPGPSIEVCEGDTVVVDVKNrlPGESTTIH---WH---------GIHQrgtpymdgvpmvtqcpILPGQTFRYK 75

                        90       100       110
                ....*....|....*....|....*....|....
gi 2827765  162 FKATKPGVFVYHcapeGMVPWHVTSGMNGAIMVL 195
Cdd:cd13858  76 FKADPAGTHWYH----SHSGTQRADGLFGALIVR 105
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 77-194 3.42e-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: 37.21  E-value: 3.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   77 VEFTMTIEEKKLVIDrEGTEIHAMTFNGSVPGPLMVVHENDYVELRLIN--PDTNTL-LHNIDFHAATGALGGGALTQVN 153
Cdd:cd13861   1 VEYTLTAAPAELLDL-GGPTTRTWGYNGQVPGPELRVRQGDTLRVRLTNrlPEPTTIhWHGLRLPNAMDGVPGLTQPPVP 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 2827765  154 PGEETTLRFKATKPGVFVYHcaPEGMVPWHVTSGMNGAIMV 194
Cdd:cd13861  80 PGESFTYEFTPPDAGTYWYH--PHVGSQEQLDRGLYGPLIV 118
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 151-188 6.25e-03

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: 36.67  E-value: 6.25e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 2827765  151 QVNPGEETTLRFKATKPGVFVYHCAPEgmvpWHVTSGM 188
Cdd:cd04207  94 LVPPGGWVVIRFKADNPGVWMLHCHIL----EHEDAGM 127
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 112-193 6.48e-03

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: 36.05  E-value: 6.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765  112 VVHENDYVELRLINPDTNTllHNIDFH---------AATGALGGGALTQVNPGEETTLRFKATKPGVFVYHCAPEGmvpw 182
Cdd:cd00920  26 VVPVGDTVRVQFVNKLGEN--HSVTIAgfgvpvvamAGGANPGLVNTLVIGPGESAEVTFTTDQAGVYWFYCTIPG---- 99

                        90
                ....*....|.
gi 2827765  183 HVTSGMNGAIM 193
Cdd:cd00920 100 HNHAGMVGTIN 110
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 75-173 7.67e-03

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: 36.07  E-value: 7.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   75 RVVEFTMTIEEKKLVIDreGTEIHAMTFNGSVPGPLMVVHENDYVELRLIN--PDTNTLLHnidFHaatgalgggALTQV 152
Cdd:cd13854   2 VTRKYTLTITNSTLAPD--GVEKEVMLINGQYPGPLIEANWGDTIEVTVINklQDNGTSIH---WH---------GIRQL 67

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 2827765  153 N----------------PGEETTLRFKATKPGVFVYH 173
Cdd:cd13854  68 NtnwqdgvpgvtecpiaPGDTRTYRFRATQYGTSWYH 104
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 92-188 7.74e-03

Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the second, fourth and sixth cupredoxin domains of ceruloplasmin and similar proteins, including the second, fourth, and sixth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. Ceruloplasmin also functions in copper transport, amine oxidase and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. Human Factor VIII facilitates blood clotting by acting as a cofactor for factor IXa Factor VIII and IXa forms a complex in the presence of Ca+2 and phospholipids that converts factor X to the activated form Xa.


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 36.62  E-value: 7.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2827765   92 REGTEIHAMtfNGSVPG--PLMVVHENDYVELRLINPDTNTLLHNIDFHAATGALGGGALTQVN--PGEETTLRFKATKP 167
Cdd:cd04200  41 QESNKMHAI--NGYVFGnlPGLTMCAGDRVRWHLLGMGNEVDVHSIHFHGQTFLYKGYRIDTLTlfPATFETVEMVPSNP 118

                        90       100
                ....*....|....*....|.
gi 2827765  168 GVFVYHCapegMVPWHVTSGM 188
Cdd:cd04200 119 GTWLLHC----HNSDHRHAGM 135
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
152-174 9.96e-03

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 37.96  E-value: 9.96e-03
                        10        20
                ....*....|....*....|...
gi 2827765  152 VNPGEETTLRFKATKPGVFVYHC 174
Cdd:COG4263 580 IMPQETASVTFVADKPGVYWYYC 602
 
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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