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Conserved domains on  [gi|262089312|gb|ACY24533|]
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copper-containing nitrite reductase [uncultured crenarchaeote 57a5]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 46-172 7.18e-48

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: 162.38  E-value: 7.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  46 VKHVTLIASEKQLQVAPdnalhpgGITYNAYTFNGTIPGPVISIDQGDTLNITLKNEG--KTIHSLDFHAGYGPSKALSG 123
Cdd:cd11020    1 VVEVTLTTVEKVVEIAP-------GVTYTAWTFNGQVPGPVIRVREGDTVELTLTNPGtnTMPHSIDFHAATGPGGGEFT 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 262089312 124 SVKPGESKTWSLTGEFPGVFIYHCGADglnGIWEHISNGMYGGIVVHPK 172
Cdd:cd11020   74 TIAPGETKTFSFKALYPGVFMYHCATA---PVLMHIANGMYGAIIVEPK 119
Cu_nitrite_red super family cl42876
nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. ...
 37-342 1.04e-47

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]


The actual alignment was detected with superfamily member TIGR02376:

Pssm-ID: 131429 [Multi-domain]  Cd Length: 311  Bit Score: 168.42  E-value: 1.04e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312   37 GQEKEKGGQVKHVTLIASEKQLQVAPdnalhpgGITYNAYTFNGTIPGPVISIDQGDTLNITLKN-EGKTI-HSLDFHAG 114
Cdd:TIGR02376  18 DQIDRSGPKVVEVTMTIEEKKMVIDD-------GVTYQAMTFDGSVPGPLIRVHEGDYVELTLINpPTNTMpHNVDFHAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  115 YGPskaLSGS----VKPGESKTWSLTGEFPGVFIYHCGADGLNGiWeHISNGMYGGIVVHPKTETKA--KEFYVVFSELY 188
Cdd:TIGR02376  91 TGA---LGGAaltqVNPGETATLRFKATRPGAFVYHCAPPGMVP-W-HVVSGMNGAIMVLPREGLPEydKEYYIGESDLY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  189 NNADKGPfvgtnGTAGSFDIGKFISKNPDLVMTNGmaHKYvpAIGQVNKLelnknaelfkvKPGELTRWYIINAGPNDGV 268
Cdd:TIGR02376 166 TPKDEGE-----GGAYEDDVAAMRTLTPTHVVFNG--AVG--ALTGDNAL-----------TAGVGERVLFVHSQPNRDS 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262089312  269 SFHFIGGmlsVRDGTNQANNGLGTQDINDETWWIPPAAGSVIESTFPEAGLYVGVDHAMADVVKGAAFAVVAME 342
Cdd:TIGR02376 226 RPHLIGG---HGDYVWVTGKFANPPNRDVETWFIPGGSAAAALYTFEQPGVYAYVDHNLIEAFEKGAAAQVKVE 296
PetE COG3794
Plastocyanin [Energy production and conversion];
473-549 4.17e-30

Plastocyanin [Energy production and conversion];


:

Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 112.40  E-value: 4.17e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262089312 473 FEPPALTVKAGTTVTWKNTDSTLHTVTSGSAeggePGKDFDSSYLAGGKTFEHVFSTPGTFDYFCTLHPYMKGHVTV 549
Cdd:COG3794    3 FEPATLTVKPGDTVTWVNTDSVPHNVTSDDG----PDGAFDSGLLAPGETFSVTFDEPGTYDYYCTPHPWMVGTIVV 75
PHA03292 super family cl30052
envelope glycoprotein I; Provisional
 316-482 9.27e-03

envelope glycoprotein I; Provisional


The actual alignment was detected with superfamily member PHA03292:

Pssm-ID: 177577  Cd Length: 413  Bit Score: 38.78  E-value: 9.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 316 EAGLY---VGVDHA-MADVVKGAAFaVVAMENSTASDyPTGTCVPPKGSESVVCEEATAAEAAGGAATTEKASASANDNN 391
Cdd:PHA03292 139 DSGAYilrVKLDHApTADVFGLSAF-VYDFDSPTVPD-PEPTTARPEPAAGYVATPTPRYLNAVTTSTYSRSMSSQPAGA 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 392 DKNTNNKSNDNNNKGNDKESQTEVTQNATMLNTSASSGNATGNGTMMAGNMTGNMTGNMTGTAGSEI------DISPGSS 465
Cdd:PHA03292 217 ATATPTPTLDTGLTTVAPPNETVVTGETALLCHWFQPSTRVPTLYLHLLGTTGNLTEDVLLTEDSEIlrtpppDPSSSRS 296

                        170
                 ....*....|....*..
gi 262089312 466 SPSNAKFFEPPALTVKA 482
Cdd:PHA03292 297 PGAGDDFKQTNSTSPKR 313
 
Name Accession Description Interval E-value
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 46-172 7.18e-48

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: 162.38  E-value: 7.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  46 VKHVTLIASEKQLQVAPdnalhpgGITYNAYTFNGTIPGPVISIDQGDTLNITLKNEG--KTIHSLDFHAGYGPSKALSG 123
Cdd:cd11020    1 VVEVTLTTVEKVVEIAP-------GVTYTAWTFNGQVPGPVIRVREGDTVELTLTNPGtnTMPHSIDFHAATGPGGGEFT 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 262089312 124 SVKPGESKTWSLTGEFPGVFIYHCGADglnGIWEHISNGMYGGIVVHPK 172
Cdd:cd11020   74 TIAPGETKTFSFKALYPGVFMYHCATA---PVLMHIANGMYGAIIVEPK 119
Cu_nitrite_red TIGR02376
nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. ...
 37-342 1.04e-47

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: 168.42  E-value: 1.04e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312   37 GQEKEKGGQVKHVTLIASEKQLQVAPdnalhpgGITYNAYTFNGTIPGPVISIDQGDTLNITLKN-EGKTI-HSLDFHAG 114
Cdd:TIGR02376  18 DQIDRSGPKVVEVTMTIEEKKMVIDD-------GVTYQAMTFDGSVPGPLIRVHEGDYVELTLINpPTNTMpHNVDFHAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  115 YGPskaLSGS----VKPGESKTWSLTGEFPGVFIYHCGADGLNGiWeHISNGMYGGIVVHPKTETKA--KEFYVVFSELY 188
Cdd:TIGR02376  91 TGA---LGGAaltqVNPGETATLRFKATRPGAFVYHCAPPGMVP-W-HVVSGMNGAIMVLPREGLPEydKEYYIGESDLY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  189 NNADKGPfvgtnGTAGSFDIGKFISKNPDLVMTNGmaHKYvpAIGQVNKLelnknaelfkvKPGELTRWYIINAGPNDGV 268
Cdd:TIGR02376 166 TPKDEGE-----GGAYEDDVAAMRTLTPTHVVFNG--AVG--ALTGDNAL-----------TAGVGERVLFVHSQPNRDS 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262089312  269 SFHFIGGmlsVRDGTNQANNGLGTQDINDETWWIPPAAGSVIESTFPEAGLYVGVDHAMADVVKGAAFAVVAME 342
Cdd:TIGR02376 226 RPHLIGG---HGDYVWVTGKFANPPNRDVETWFIPGGSAAAALYTFEQPGVYAYVDHNLIEAFEKGAAAQVKVE 296
CuRO_2_CuNIR cd04208
Cupredoxin domain 2 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 177-334 2.13e-42

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: 148.47  E-value: 2.13e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 177 AKEFYVVFSELYNNADKGpfvgtngTAGSFDIGKFISKNPDLVMTNGMAHKYVPAigqvnklelnknaELFKVKPGELTR 256
Cdd:cd04208    2 DREYYLVQSELYTGGDDG-------GVGLFDYAKMLDEKPDYVVFNGRVFAYTGT-------------NPLQAKVGERVR 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 257 WYIINAGPNDGVSFHFIGGMLSV--RDGTNQANnglgtQDINDETWWIPPAAGSVIESTFPEAGLYVGVDHAMADVVKGA 334
Cdd:cd04208   62 IYVVNAGPNLTSSFHVIGGIFDRvyPEGSNPNN-----PLRGVQTVLVPPGGGAIVEFTFPVPGNYALVDHALSRAEKGA 136
PetE COG3794
Plastocyanin [Energy production and conversion];
473-549 4.17e-30

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 112.40  E-value: 4.17e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262089312 473 FEPPALTVKAGTTVTWKNTDSTLHTVTSGSAeggePGKDFDSSYLAGGKTFEHVFSTPGTFDYFCTLHPYMKGHVTV 549
Cdd:COG3794    3 FEPATLTVKPGDTVTWVNTDSVPHNVTSDDG----PDGAFDSGLLAPGETFSVTFDEPGTYDYYCTPHPWMVGTIVV 75
Amicyanin cd13921
Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; ...
 473-549 1.55e-29

Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; In Paracoccus denitrificans bacteria, amicyanin acts as an intermediary of a three-member redox complex along with methylamine dehydrogenase (MADH) and cytochrome c-551i. The electron is transferred from the active site of MADH via the amicyanin copper ion to the cytochrome heme iron. The electron transfer from MADH to cytochrome c-551i does not involve a ternary complex but occurs via a ping-pong mechanism in which amicyanin uses the same interface for the reactions with MADH and cytochrome c-551i.


Pssm-ID: 259988 [Multi-domain]  Cd Length: 81  Bit Score: 111.27  E-value: 1.55e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262089312 473 FEPPALTVKAGTTVTWKNTDSTLHTVTSgsaeggePGKDFDSSYLAGGKTFEHVFSTPGTFDYFCTLHPYMKGHVTV 549
Cdd:cd13921   11 FNPAEVTVKVGDTVTWTNKDSVPHTVTA-------EDGAFDSGMLATGKSFSYTFTAAGTYDYFCTIHPFMKGTVTV 80
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 42-277 2.95e-19

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: 90.38  E-value: 2.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  42 KGGQVKHVTLIASEKQLQVAPdnalhpgGITYNAYTFNGTIPGPVISIDQGDTLNITLKN---EGKTIHsldFHAGYGPS 118
Cdd:COG2132    9 ESGGGREYELTAQPATVELLP-------GKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNrlpEPTTVH---WHGLRVPN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 119 kALSG----SVKPGESKTWSLT-GEFPGVFIYHCGADGLNGiwEHISNGMYGGIVVHPKTET---KAKEFYVVFSE-LYN 189
Cdd:COG2132   79 -AMDGvpgdPIAPGETFTYEFPvPQPAGTYWYHPHTHGSTA--EQVYRGLAGALIVEDPEEDlprYDRDIPLVLQDwRLD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 190 NADKGPFVGTNGTAGSFdigkfisknPDLVMTNGMAHKYvpaigqvnklelnknaelFKVKPGELTRWYIINAGP----- 264
Cdd:COG2132  156 DDGQLLYPMDAAMGGRL---------GDTLLVNGRPNPT------------------LEVRPGERVRLRLLNASNariyr 208

                        250
                 ....*....|....*...
gi 262089312 265 ---NDGVSFHFIG--GML 277
Cdd:COG2132  209 lalSDGRPFTVIAtdGGL 226
halo_cynanin TIGR03102
halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic ...
 439-549 1.45e-12

halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronobacterium pharaonis. This model represents a domain duplicated in some halocyanins, while appearing once in others. This domain includes the characteristic copper ligand residues. This family does not include plastocyanins, and does not include certain divergent paralogs of halocyanin.


Pssm-ID: 274429 [Multi-domain]  Cd Length: 115  Bit Score: 64.41  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  439 AGNMTGNMTgNMTGTagSEIDISPGSSSPSNAKFFEPPALTVKAGTTVTWKNT-DSTLHTVTSgsaeggEPGKDFDSSYL 517
Cdd:TIGR03102   8 VSNYDGSIV-DRTGQ--DEVTVDVGAEANGGGFAFDPPAIRVDPGTTVVWEWTgEGGGHNVVS------DGDGDLDESER 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 262089312  518 AG--GKTFEHVFSTPGTFDYFCTLHPY--MKGHVTV 549
Cdd:TIGR03102  79 VSeeGTTYEHTFEEPGIYLYVCVPHEAlgMKGAVVV 114
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 473-549 1.53e-12

Cupredoxin-like domain; 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.


Pssm-ID: 379208 [Multi-domain]  Cd Length: 104  Bit Score: 63.76  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  473 FEPPALTVKAGT--TVTWKNTDSTLHTVTSgsaeggepgKDFD-SSYLAGGKTFEHVFST--PGTFDYFCTLHPYMKGHV 547
Cdd:pfam13473  32 FSPSRITVPAGTpvKLEFKNKDKTPAEFES---------PDLGiEKVLAPGKTSTITIPPlkPGEYDFFCDMHMDAKGKL 102


                  ..
gi 262089312  548 TV 549
Cdd:pfam13473 103 IV 104
PLN02191 PLN02191
L-ascorbate oxidase
 77-191 1.19e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 51.17  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  77 TFNGTIPGPVISIDQGDTLNITLKN----EGKTIHsldFHA--------GYGPSKALSGSVKPGESKTWSLTGEFPGVFI 144
Cdd:PLN02191  46 TVNGQFPGPTIDAVAGDTIVVHLTNklttEGLVIH---WHGirqkgspwADGAAGVTQCAINPGETFTYKFTVEKPGTHF 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 262089312 145 YHcGADGLNGiwehiSNGMYGGIVVHPKTETKAK-----EFYVVFSELYNNA 191
Cdd:PLN02191 123 YH-GHYGMQR-----SAGLYGSLIVDVAKGPKERlrydgEFNLLLSDWWHES 168
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 60-172 1.57e-05

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: 44.16  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312   60 VAPDNALHPGGITYNAYTFNGTIPGPVISIDQGDTLNITLKN---EGKTIHsldFH------------AGYGPSKALsgs 124
Cdd:pfam07732   2 VTYGTVSPLGGTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNnldEPTSIH---WHglqqrgtpwmdgVPGVTQCPI--- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 262089312  125 vKPGESKTWSLTGEFP-GVFIYHCGADGlngiweHISNGMYGGIVVHPK 172
Cdd:pfam07732  76 -PPGQSFTYRFQVKQQaGTYWYHSHTSG------QQAAGLAGAIIIEDR 117
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 77-171 6.53e-05

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: 45.51  E-value: 6.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312   77 TFNGTIPGPVISIDQGDTLNITLKN----EGKTIHsldFHA--------GYGPSKALSGSVKPGESKTWSLTGEFPGVFI 144
Cdd:TIGR03388  24 GINGQFPGPTIRAQAGDTIVVELTNklhtEGVVIH---WHGirqigtpwADGTAGVTQCAINPGETFIYNFVVDRPGTYF 100

                          90       100
                  ....*....|....*....|....*..
gi 262089312  145 YHcGADGLNGiwehiSNGMYGGIVVHP 171
Cdd:TIGR03388 101 YH-GHYGMQR-----SAGLYGSLIVDV 121
PHA03292 PHA03292
envelope glycoprotein I; Provisional
 316-482 9.27e-03

envelope glycoprotein I; Provisional


Pssm-ID: 177577  Cd Length: 413  Bit Score: 38.78  E-value: 9.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 316 EAGLY---VGVDHA-MADVVKGAAFaVVAMENSTASDyPTGTCVPPKGSESVVCEEATAAEAAGGAATTEKASASANDNN 391
Cdd:PHA03292 139 DSGAYilrVKLDHApTADVFGLSAF-VYDFDSPTVPD-PEPTTARPEPAAGYVATPTPRYLNAVTTSTYSRSMSSQPAGA 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 392 DKNTNNKSNDNNNKGNDKESQTEVTQNATMLNTSASSGNATGNGTMMAGNMTGNMTGNMTGTAGSEI------DISPGSS 465
Cdd:PHA03292 217 ATATPTPTLDTGLTTVAPPNETVVTGETALLCHWFQPSTRVPTLYLHLLGTTGNLTEDVLLTEDSEIlrtpppDPSSSRS 296

                        170
                 ....*....|....*..
gi 262089312 466 SPSNAKFFEPPALTVKA 482
Cdd:PHA03292 297 PGAGDDFKQTNSTSPKR 313
 
Name Accession Description Interval E-value
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 46-172 7.18e-48

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: 162.38  E-value: 7.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  46 VKHVTLIASEKQLQVAPdnalhpgGITYNAYTFNGTIPGPVISIDQGDTLNITLKNEG--KTIHSLDFHAGYGPSKALSG 123
Cdd:cd11020    1 VVEVTLTTVEKVVEIAP-------GVTYTAWTFNGQVPGPVIRVREGDTVELTLTNPGtnTMPHSIDFHAATGPGGGEFT 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 262089312 124 SVKPGESKTWSLTGEFPGVFIYHCGADglnGIWEHISNGMYGGIVVHPK 172
Cdd:cd11020   74 TIAPGETKTFSFKALYPGVFMYHCATA---PVLMHIANGMYGAIIVEPK 119
Cu_nitrite_red TIGR02376
nitrite reductase, copper-containing; This family consists of copper-type nitrite reductase. ...
 37-342 1.04e-47

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: 168.42  E-value: 1.04e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312   37 GQEKEKGGQVKHVTLIASEKQLQVAPdnalhpgGITYNAYTFNGTIPGPVISIDQGDTLNITLKN-EGKTI-HSLDFHAG 114
Cdd:TIGR02376  18 DQIDRSGPKVVEVTMTIEEKKMVIDD-------GVTYQAMTFDGSVPGPLIRVHEGDYVELTLINpPTNTMpHNVDFHAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  115 YGPskaLSGS----VKPGESKTWSLTGEFPGVFIYHCGADGLNGiWeHISNGMYGGIVVHPKTETKA--KEFYVVFSELY 188
Cdd:TIGR02376  91 TGA---LGGAaltqVNPGETATLRFKATRPGAFVYHCAPPGMVP-W-HVVSGMNGAIMVLPREGLPEydKEYYIGESDLY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  189 NNADKGPfvgtnGTAGSFDIGKFISKNPDLVMTNGmaHKYvpAIGQVNKLelnknaelfkvKPGELTRWYIINAGPNDGV 268
Cdd:TIGR02376 166 TPKDEGE-----GGAYEDDVAAMRTLTPTHVVFNG--AVG--ALTGDNAL-----------TAGVGERVLFVHSQPNRDS 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 262089312  269 SFHFIGGmlsVRDGTNQANNGLGTQDINDETWWIPPAAGSVIESTFPEAGLYVGVDHAMADVVKGAAFAVVAME 342
Cdd:TIGR02376 226 RPHLIGG---HGDYVWVTGKFANPPNRDVETWFIPGGSAAAALYTFEQPGVYAYVDHNLIEAFEKGAAAQVKVE 296
CuRO_2_CuNIR cd04208
Cupredoxin domain 2 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 177-334 2.13e-42

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: 148.47  E-value: 2.13e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 177 AKEFYVVFSELYNNADKGpfvgtngTAGSFDIGKFISKNPDLVMTNGMAHKYVPAigqvnklelnknaELFKVKPGELTR 256
Cdd:cd04208    2 DREYYLVQSELYTGGDDG-------GVGLFDYAKMLDEKPDYVVFNGRVFAYTGT-------------NPLQAKVGERVR 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 257 WYIINAGPNDGVSFHFIGGMLSV--RDGTNQANnglgtQDINDETWWIPPAAGSVIESTFPEAGLYVGVDHAMADVVKGA 334
Cdd:cd04208   62 IYVVNAGPNLTSSFHVIGGIFDRvyPEGSNPNN-----PLRGVQTVLVPPGGGAIVEFTFPVPGNYALVDHALSRAEKGA 136
PetE COG3794
Plastocyanin [Energy production and conversion];
473-549 4.17e-30

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 112.40  E-value: 4.17e-30
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262089312 473 FEPPALTVKAGTTVTWKNTDSTLHTVTSGSAeggePGKDFDSSYLAGGKTFEHVFSTPGTFDYFCTLHPYMKGHVTV 549
Cdd:COG3794    3 FEPATLTVKPGDTVTWVNTDSVPHNVTSDDG----PDGAFDSGLLAPGETFSVTFDEPGTYDYYCTPHPWMVGTIVV 75
Amicyanin cd13921
Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; ...
 473-549 1.55e-29

Amicyanin is a type I blue copper protein that plays an essential role in electron transfer; In Paracoccus denitrificans bacteria, amicyanin acts as an intermediary of a three-member redox complex along with methylamine dehydrogenase (MADH) and cytochrome c-551i. The electron is transferred from the active site of MADH via the amicyanin copper ion to the cytochrome heme iron. The electron transfer from MADH to cytochrome c-551i does not involve a ternary complex but occurs via a ping-pong mechanism in which amicyanin uses the same interface for the reactions with MADH and cytochrome c-551i.


Pssm-ID: 259988 [Multi-domain]  Cd Length: 81  Bit Score: 111.27  E-value: 1.55e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262089312 473 FEPPALTVKAGTTVTWKNTDSTLHTVTSgsaeggePGKDFDSSYLAGGKTFEHVFSTPGTFDYFCTLHPYMKGHVTV 549
Cdd:cd13921   11 FNPAEVTVKVGDTVTWTNKDSVPHTVTA-------EDGAFDSGMLATGKSFSYTFTAAGTYDYFCTIHPFMKGTVTV 80
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 46-172 1.65e-27

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: 106.97  E-value: 1.65e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  46 VKHVTLIASEKQLQVAPdnalhpgGITYNAYTFNGTIPGPVISIDQGDTLNITLKNEGKTIHSLDFHagyGPSKAL---- 121
Cdd:cd11024    1 VREFTLVAEDAEIEIAP-------GVVFKAWTYNGTVPGPTLRATEGDLVRIHFINTGDHPHTIHFH---GIHDAAmdgt 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 262089312 122 -SGSVKPGESKTWSLTGEFPGVFIYHCGADGLNgiwEHISNGMYGGIVVHPK 172
Cdd:cd11024   71 gLGPIMPGESFTYEFVAEPAGTHLYHCHVQPLK---EHIAMGLYGAFIVDPK 119
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 49-172 1.03e-25

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: 101.80  E-value: 1.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  49 VTLIASEKQLQVAPdnalhpgGITYNAYTFNGTIPGPVISIDQGDTLNITLKNEGKTI--HSLDFHAGYGPSKALS-GSV 125
Cdd:cd04201    4 VDMETVEKTMQLDD-------GVEYRYWTFDGDIPGPMLRVREGDTVELHFSNNPSSTmpHNIDFHAATGAGGGAGaTFI 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 262089312 126 KPGESKTWSLTGEFPGVFIYHCGADGLNgiwEHISNGMYGGIVVHPK 172
Cdd:cd04201   77 APGETSTFSFKATQPGLYVYHCAVAPVP---MHIANGMYGLILVEPK 120
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 42-277 2.95e-19

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: 90.38  E-value: 2.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  42 KGGQVKHVTLIASEKQLQVAPdnalhpgGITYNAYTFNGTIPGPVISIDQGDTLNITLKN---EGKTIHsldFHAGYGPS 118
Cdd:COG2132    9 ESGGGREYELTAQPATVELLP-------GKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNrlpEPTTVH---WHGLRVPN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 119 kALSG----SVKPGESKTWSLT-GEFPGVFIYHCGADGLNGiwEHISNGMYGGIVVHPKTET---KAKEFYVVFSE-LYN 189
Cdd:COG2132   79 -AMDGvpgdPIAPGETFTYEFPvPQPAGTYWYHPHTHGSTA--EQVYRGLAGALIVEDPEEDlprYDRDIPLVLQDwRLD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 190 NADKGPFVGTNGTAGSFdigkfisknPDLVMTNGMAHKYvpaigqvnklelnknaelFKVKPGELTRWYIINAGP----- 264
Cdd:COG2132  156 DDGQLLYPMDAAMGGRL---------GDTLLVNGRPNPT------------------LEVRPGERVRLRLLNASNariyr 208

                        250
                 ....*....|....*...
gi 262089312 265 ---NDGVSFHFIG--GML 277
Cdd:COG2132  209 lalSDGRPFTVIAtdGGL 226
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 47-170 3.00e-17

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: 77.62  E-value: 3.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  47 KHVTLIASEKQLQVAPdnalhpgGITYNAYTFNGTIPGPVISIDQGDTLNITLKN---EGKTIHsldFHaGY-------G 116
Cdd:cd13860    1 KVFHLVAEPVKWEIAP-------GVKVEAWGYNGSVPGPTIEVTEGDRVRILVTNelpEPTTVH---WH-GLpvpngmdG 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 262089312 117 PSKALSGSVKPGESKTWSLTGEFPGVFIYHCGADGLNgiweHISNGMYGGIVVH 170
Cdd:cd13860   70 VPGITQPPIQPGETFTYEFTAKQAGTYMYHSHVDEAK----QEDMGLYGAFIVH 119
Halocyanin cd04220
Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) ...
 467-550 2.83e-15

Halocyanin is an archaea blue (type I) copper redox protein; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronomonas pharaonis (Natronobacterium pharaonis). Halocyanin may serve as a mobile electron carrier at a peripheral membrane protein. The copper-binding domain is present only once in some halocyanins and is duplicated in others.


Pssm-ID: 259882 [Multi-domain]  Cd Length: 92  Bit Score: 71.26  E-value: 2.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 467 PSNAKFFEPPALTVKAGTTVTWKNTDS-TLHTVTSGSaeggEPGKDFDSSYLAG--GKTFEHVFSTPGTFDYFCTLHPY- 542
Cdd:cd04220    8 MNGGFAFDPAAIRVSPGTTVTWEWTGEgGGHNVVAYE----DPITAFDSGSTDSseGETYEHTFEETGEYRYVCVPHEAl 83


                 ....*....
gi 262089312 543 -MKGHVTVN 550
Cdd:cd04220   84 gMKGAIVVE 92
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 68-170 1.79e-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: 70.01  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  68 PGGITYNAYTFNGTIPGPVISIDQGDTLNITLKNEGKTI-HSLDFHA--------GYGPSKALSGSVKPGESKTWSLTGE 138
Cdd:cd04206   14 PDGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNLPNEpTSIHWHGlrqpgtndGDGVAGLTQCPIPPGESFTYRFTVD 93

                         90       100       110
                 ....*....|....*....|....*....|...
gi 262089312 139 F-PGVFIYHCGADGlngiweHISNGMYGGIVVH 170
Cdd:cd04206   94 DqAGTFWYHSHVGG------QRADGLYGPLIVE 120
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 55-169 1.02e-12

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: 64.95  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  55 EKQLQVAPDNALHPGGITYNAYTFNGTIPGPVISIDQGDTLNITLKN---EGKTIHsldFHaGYGPSKALSG-------S 124
Cdd:cd13861    2 EYTLTAAPAELLDLGGPTTRTWGYNGQVPGPELRVRQGDTLRVRLTNrlpEPTTIH---WH-GLRLPNAMDGvpgltqpP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 262089312 125 VKPGESKTWSLTGEFPGVFIYH--CGADglngiwEHISNGMYGGIVV 169
Cdd:cd13861   78 VPPGESFTYEFTPPDAGTYWYHphVGSQ------EQLDRGLYGPLIV 118
halo_cynanin TIGR03102
halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic ...
 439-549 1.45e-12

halocyanin domain; Halocyanins are blue (type I) copper redox proteins found in halophilic archaea such as Natronobacterium pharaonis. This model represents a domain duplicated in some halocyanins, while appearing once in others. This domain includes the characteristic copper ligand residues. This family does not include plastocyanins, and does not include certain divergent paralogs of halocyanin.


Pssm-ID: 274429 [Multi-domain]  Cd Length: 115  Bit Score: 64.41  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  439 AGNMTGNMTgNMTGTagSEIDISPGSSSPSNAKFFEPPALTVKAGTTVTWKNT-DSTLHTVTSgsaeggEPGKDFDSSYL 517
Cdd:TIGR03102   8 VSNYDGSIV-DRTGQ--DEVTVDVGAEANGGGFAFDPPAIRVDPGTTVVWEWTgEGGGHNVVS------DGDGDLDESER 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 262089312  518 AG--GKTFEHVFSTPGTFDYFCTLHPY--MKGHVTV 549
Cdd:TIGR03102  79 VSeeGTTYEHTFEEPGIYLYVCVPHEAlgMKGAVVV 114
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 473-549 1.53e-12

Cupredoxin-like domain; 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.


Pssm-ID: 379208 [Multi-domain]  Cd Length: 104  Bit Score: 63.76  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  473 FEPPALTVKAGT--TVTWKNTDSTLHTVTSgsaeggepgKDFD-SSYLAGGKTFEHVFST--PGTFDYFCTLHPYMKGHV 547
Cdd:pfam13473  32 FSPSRITVPAGTpvKLEFKNKDKTPAEFES---------PDLGiEKVLAPGKTSTITIPPlkPGEYDFFCDMHMDAKGKL 102


                  ..
gi 262089312  548 TV 549
Cdd:pfam13473 103 IV 104
Pseudoazurin_like cd04204
Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin; The ...
 469-548 1.88e-12

Small blue copper proteins including pseudocyanin, plastocyanin, halocyanin and amicyanin; The Pseudocyanin-like family of copper-binding proteins (or blue (type 1) copper domain) is a family of small proteins that bind a single copper atom and are characterized by an intense electronic absorption band near 600 nm. Pseudoazurin (PAz) has been identified as a electron donor in the denitrification pathway. For example, PAz acts as an electron donor to cytochrome c peroxidase and N2OR from Paracoccus pantotrophus (Pp), and to the copper containing nitrite reductase (NiR) that catalyzes the second step of denitrification. Plastocyanin is found in cyanobacteria, higher plants, and some algae where it plays a role in photosynthesis. Plastocyanin is responsible for transporting electrons from PSII to PSI. This family also includes halocyanins found in halophilic archaea such as Natronomonas pharaonis (Natronobacterium pharaonis) and amicyanin found in bacteria Paracoccus denitrificans.


Pssm-ID: 259867 [Multi-domain]  Cd Length: 92  Bit Score: 63.35  E-value: 1.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 469 NAKFFEPPALTVKAGTTVTWKNTDSTLHTVTSGSAEGGEPGKDFDSSYL-AGGKTFEHVFSTPGTFDYFCTLHPY--MKG 545
Cdd:cd04204   10 GAMAFEPAAIRVDAGETVEFVNTGGGPHNVVFDKEIVPDGDAEFESDRVdEEGFTYEQTFDEPGVYGYYCTPHRGagMVG 89


                 ...
gi 262089312 546 HVT 548
Cdd:cd04204   90 TVI 92
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 69-169 2.52e-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: 64.04  E-value: 2.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  69 GGITYNAYTFNGTIPGPVISIDQGDTLNITLKNEGKTIHSLDFHAGY--------GPSKALSGSVKPGESKTWSLTGEFP 140
Cdd:cd13859   16 PGLDFKTFAFNGQVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLqmgswkmdGVPGVTQPAIEPGESFTYKFKAERP 95

                         90       100       110
                 ....*....|....*....|....*....|
gi 262089312 141 GVFIYHCGADglngIWEHIS-NGMYGGIVV 169
Cdd:cd13859   96 GTLWYHCHVN----VNEHVGmRGMWGPLIV 121
Copper-bind pfam00127
Copper binding proteins, plastocyanin/azurin family;
465-550 5.49e-12

Copper binding proteins, plastocyanin/azurin family;


Pssm-ID: 395076 [Multi-domain]  Cd Length: 99  Bit Score: 62.00  E-value: 5.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  465 SSPSNAKFFEPPALTVKAGTTVTWKNTDSTLHTVTsgSAEGGEPGKdFDSSYL---------AGGKTFEHVFSTPGTFDY 535
Cdd:pfam00127   6 GVDSGDMVFEPKEITVKKGEKVTFVNNAGMPHNVV--FDKDGVPAG-VDADKVkmgdhtkliGGGETYSVTFDLAGTYGF 82

                          90
                  ....*....|....*..
gi 262089312  536 FCTLHP--YMKGHVTVN 550
Cdd:pfam00127  83 FCTPHQgaGMVGKVTVE 99
Plastocyanin cd04219
Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to ...
 473-550 7.97e-11

Plastocyanin is a type I copper protein and functions in the electron transfer from PSII to PSI; Plastocyanin is a small copper-containing protein found in cyanobacteria, higher plants, and some algae, where it plays a role in photosynthesis. The two photosystems that are primarily responsible for photosynthesis are photosystem I (PSI) and photosystem II (PSII). The flow of electrons begins in PSII, which acts as a proton pump. Plastocyanin is responsible for transporting electrons from PSII to PSI.


Pssm-ID: 259881 [Multi-domain]  Cd Length: 97  Bit Score: 58.92  E-value: 7.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 473 FEPPALTVKAGTTVTWKNTDSTLHTVTSGSAEGGEPGKDFDSSY----LAGGKTFEHVFSTPGTFDYFCTLH--PYMKGH 546
Cdd:cd04219   14 FEPKELTVKAGDTVEFVNNKGGPHNVVFDEDAVPSAVDAAALSHkdllNAPGETFSVTFPAPGTYTFYCEPHrgAGMVGK 93


                 ....
gi 262089312 547 VTVN 550
Cdd:cd04219   94 ITVQ 97
cyanin_plasto TIGR02656
plastocyanin; Members of this family are plastocyanin, a blue copper protein related to ...
 473-550 1.11e-09

plastocyanin; Members of this family are plastocyanin, a blue copper protein related to pseudoazurin, halocyanin, amicyanin, etc. This protein, located in the thylakoid luman, performs electron transport to photosystem I in Cyanobacteria and chloroplasts. [Energy metabolism, Electron transport, Energy metabolism, Photosynthesis]


Pssm-ID: 274247 [Multi-domain]  Cd Length: 99  Bit Score: 55.58  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  473 FEPPALTVKAGTTVTWKNTDSTLHTVTSGSAEGGEPGKDFDSSY------LAGGKTFEHVFSTPGTFDYFCTLH--PYMK 544
Cdd:TIGR02656  14 FEPAKISIAAGDTVEWVNNKGGPHNVVFDEDAVPAGVKELAKSLshkdllNSPGESYEVTFSTPGTYTFYCEPHrgAGMV 93


                  ....*.
gi 262089312  545 GHVTVN 550
Cdd:TIGR02656  94 GKITVE 99
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 68-170 7.94e-08

The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. 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. 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: 259926 [Multi-domain]  Cd Length: 119  Bit Score: 50.72  E-value: 7.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  68 PGGITYNAYTFNGTIPGPVISIDQGDTLNITLKNEGKTIHSLDFHAGY--------GPSKALSGSVKPGESKT--WSLTG 137
Cdd:cd13857   14 PDGFVRPMLVINGQFPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFqngtnwmdGTAGITQCPIPPGGSFTynFTVDG 93

                         90       100       110
                 ....*....|....*....|....*....|...
gi 262089312 138 EFpGVFIYHCGADGLNgiwehiSNGMYGGIVVH 170
Cdd:cd13857   94 QY-GTYWYHSHYSTQY------ADGLVGPLIVH 119
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 69-169 1.49e-07

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: 50.71  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  69 GGITYNAYTFNGTIPGPVISIDQGDTLNITLKNE-GKTIHSLDFHAGYGPSKALS------G--------------SVKP 127
Cdd:cd13853   16 AGLPVTLRTYNGSIPGPTLRVRPGDTLRITLKNDlPPEGAANEAPAPNTPHCPNTtnlhfhGlhvsptgnsdnvflTIAP 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 262089312 128 GESKTWSLT---GEFPGVFIYHCGADGLNGiwEHISNGMYGGIVV 169
Cdd:cd13853   96 GESFTYEYDipaDHPPGTYWYHPHLHGSTA--LQVAGGMAGALVV 138
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 68-170 2.34e-07

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: 49.94  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  68 PGGITYNAYTFNG-TIPG-PVISIDQGDTLNITLKNEGKTIHSLDFHaGY--------GpsKALSGS---------VKPG 128
Cdd:cd04202   22 PEGMDFNYFTINGkSFPAtPPLVVKEGDRVRIRLINLSMDHHPMHLH-GHfflvtatdG--GPIPGSapwpkdtlnVAPG 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 262089312 129 ESKTWSLTGEFPGVFIYHCgadglnGIWEHISNGMYGGIVVH 170
Cdd:cd04202   99 ERYDIEFVADNPGDWMFHC------HKLHHAMNGMGGGMMTL 134
Cupredoxin_Fibrocystin-L_like cd04217
Cupredoxin domain of PKHDL1, a homolog of the autosomal recessive polycystic kidney disease ...
 473-549 9.43e-07

Cupredoxin domain of PKHDL1, a homolog of the autosomal recessive polycystic kidney disease protein; One member of this family is Fibrocystin-L, a homolog of the autosomal recessive polycystic kidney disease protein PKHD1. Human fibrocystin-L is predicted to be a large receptor protein (466 kDa) with a signal peptide, a single transmembrane domain and a short cytoplasmic tail. Fibrocystin-L is widely expressed at a low level in most tissues but is up-regulated specifically in T lymphocytes following activation signals. It may play roles in immunity.


Pssm-ID: 259879 [Multi-domain]  Cd Length: 86  Bit Score: 46.78  E-value: 9.43e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262089312 473 FEPPALTVKAGTTVTWKNTDSTLHTVTSGSAEGgepgkDFDSSYLAGGKTFEHVFSTPGTFDYFCTLHPYMKGHVTV 549
Cdd:cd04217   15 ISPSELEINVGDTVTWHNFKRPKGRIVLVSEEG-----LFEDQTLYYGKAFSYTFTEPGTYYFSVKDVPEMKGTINV 86
PLN02191 PLN02191
L-ascorbate oxidase
 77-191 1.19e-06

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 51.17  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  77 TFNGTIPGPVISIDQGDTLNITLKN----EGKTIHsldFHA--------GYGPSKALSGSVKPGESKTWSLTGEFPGVFI 144
Cdd:PLN02191  46 TVNGQFPGPTIDAVAGDTIVVHLTNklttEGLVIH---WHGirqkgspwADGAAGVTQCAINPGETFTYKFTVEKPGTHF 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 262089312 145 YHcGADGLNGiwehiSNGMYGGIVVHPKTETKAK-----EFYVVFSELYNNA 191
Cdd:PLN02191 123 YH-GHYGMQR-----SAGLYGSLIVDVAKGPKERlrydgEFNLLLSDWWHES 168
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 48-146 1.40e-06

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: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  48 HVTLIASEKQLQVAPdnalhpgGITYNAYTFNGTIPGPVISIDQGDTLNITLKN---EGKTIHsldFHAGYGPSKAlSGS 124
Cdd:cd13855    3 RATLTAAEVRIRLLP-------GKPTEFWAYNGSVPGPLIEVFEGDTVEITFRNrlpEPTTVH---WHGLPVPPDQ-DGN 71

                         90       100
                 ....*....|....*....|....*...
gi 262089312 125 ----VKPGESKT--WSLTGEFPGVFIYH 146
Cdd:cd13855   72 phdpVAPGNDRVyrFTLPQDSAGTYWYH 99
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 77-171 1.92e-06

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: 47.06  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  77 TFNGTIPGPVISIDQGDTLNITLKN----EGKTIHSLDFHAGYGPSKALSGSVK-----PGESKTWSLTGEFPGVFIYHc 147
Cdd:cd13845   23 GINGQFPGPTIRATAGDTIVVELENklptEGVAIHWHGIRQRGTPWADGTASVSqcpinPGETFTYQFVVDRPGTYFYH- 101

                         90       100
                 ....*....|....*....|....
gi 262089312 148 GADGLNGiwehiSNGMYGGIVVHP 171
Cdd:cd13845  102 GHYGMQR-----SAGLYGSLIVDP 120
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 81-172 3.50e-06

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. 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. This subfamily has lost the type 1 (T1) copper binding site in domain 1 that is present in other two-domain laccases.


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 46.49  E-value: 3.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  81 TIPGPVISIDQGDTLNITLKNEGKTIHSLDFHA-GYGPSKALSG----SVKPGESK--TWSLTGEF-----------PGV 142
Cdd:cd14449   26 TVPGPVIEVREGDTLKILFRNTLDVPASLHPHGvDYTTASDGTGmnasIVAPGDTRiyTWRTHGGYrradgswaegtAGY 105

                         90       100       110
                 ....*....|....*....|....*....|
gi 262089312 143 FIYHCGADGLNGIWEHISNGMYGGIVVHPK 172
Cdd:cd14449  106 WHYHDHVFGTEHGTEGLSRGLYGALIVRRV 135
MauL cd04221
Methylamine utilization protein MauL; MauL is one of the products from the methylamine ...
 469-549 1.16e-05

Methylamine utilization protein MauL; MauL is one of the products from the methylamine utilization gene cluster in Methylobacterium extorquens AM1. Mutants generated by insertions in mauL were not able to grow on methylamine or any other primary amine as carbon sources. MauL belongs to the blue or type I copper protein family. They are involved in electron transfer reactions with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form.


Pssm-ID: 259883 [Multi-domain]  Cd Length: 83  Bit Score: 43.51  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 469 NAKFFEPPALTVKAGTTVTWKNTDSTLHTVTSGSaeggePGKDFDSSYLAGGKTFE-HVFSTPGTFDYFCTLHPYMKGHV 547
Cdd:cd04221    7 KDKEFEPHVLVIKPGDTVSFPNSDDIRHNVYSFS-----PAKIFELLDQPPGTTKDvVLFDKAGVVVVGCNIHPIMRAWI 81


                 ..
gi 262089312 548 TV 549
Cdd:cd04221   82 LV 83
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 60-172 1.57e-05

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: 44.16  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312   60 VAPDNALHPGGITYNAYTFNGTIPGPVISIDQGDTLNITLKN---EGKTIHsldFH------------AGYGPSKALsgs 124
Cdd:pfam07732   2 VTYGTVSPLGGTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNnldEPTSIH---WHglqqrgtpwmdgVPGVTQCPI--- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 262089312  125 vKPGESKTWSLTGEFP-GVFIYHCGADGlngiweHISNGMYGGIVVHPK 172
Cdd:pfam07732  76 -PPGQSFTYRFQVKQQaGTYWYHSHTSG------QQAAGLAGAIIIEDR 117
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 66-107 1.58e-05

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: 44.54  E-value: 1.58e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 262089312  66 LHPGGITYNAYTFNGTIPGPVISIDQGDTLNITLKN----EGKTIH 107
Cdd:cd13854   15 LAPDGVEKEVMLINGQYPGPLIEANWGDTIEVTVINklqdNGTSIH 60
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 66-169 2.18e-05

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: 44.35  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312   66 LHPGGITYNAYTFNGTIPGP---VISIDQGDTLNITLKNEGKTIHSLDFHA------GYGPSKALSGS------------ 124
Cdd:pfam07731  12 ITSGNFRRNDWAINGLLFPPntnVITLPYGTVVEWVLQNTTTGVHPFHLHGhsfqvlGRGGGPWPEEDpktynlvdpvrr 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 262089312  125 ----VKPGESKTWSLTGEFPGVFIYHCGadglngIWEHISNGMYGGIVV 169
Cdd:pfam07731  92 dtvqVPPGGWVAIRFRADNPGVWLFHCH------ILWHLDQGMMGQFVV 134
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 75-170 3.22e-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: 43.42  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  75 AYTFNGTIPGPVISIDQGDTLNITLKNEGKTIHSLDFHAGYGPSK-----ALSG-SVKPGESKTWsltgEFP----GVFI 144
Cdd:cd13848   21 AITVNGQVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPNDmdgvpGLSFpGIKPGETFTY----RFPvrqsGTYW 96

                         90       100
                 ....*....|....*....|....*.
gi 262089312 145 YHCGAdglnGIWEHIsnGMYGGIVVH 170
Cdd:cd13848   97 YHSHS----GLQEQT--GLYGPIIID 116
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 72-171 6.44e-05

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: 42.63  E-value: 6.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  72 TYNAYTFNGTIPGPVISIDQGDTLNITLKNEGK---TIHsldFHAGY--------GPSKALSGSVKPGESKTW--SLTGE 138
Cdd:cd13849   16 TKSILTVNGQFPGPTIRVHEGDTVVVNVTNRSPyniTIH---WHGIRqlrsgwadGPAYITQCPIQPGQSYTYrfTVTGQ 92

                         90       100       110
                 ....*....|....*....|....*....|...
gi 262089312 139 fPGVFIYHCGADGLNGIwehisngMYGGIVVHP 171
Cdd:cd13849   93 -EGTLWWHAHISWLRAT-------VYGAFIIRP 117
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 77-171 6.53e-05

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: 45.51  E-value: 6.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312   77 TFNGTIPGPVISIDQGDTLNITLKN----EGKTIHsldFHA--------GYGPSKALSGSVKPGESKTWSLTGEFPGVFI 144
Cdd:TIGR03388  24 GINGQFPGPTIRAQAGDTIVVELTNklhtEGVVIH---WHGirqigtpwADGTAGVTQCAINPGETFIYNFVVDRPGTYF 100

                          90       100
                  ....*....|....*....|....*..
gi 262089312  145 YHcGADGLNGiwehiSNGMYGGIVVHP 171
Cdd:TIGR03388 101 YH-GHYGMQR-----SAGLYGSLIVDV 121
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 60-154 7.58e-05

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: 42.32  E-value: 7.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  60 VAPDnalhpgGITYNAYTFNGTIPGPVISIDQGDTLNITLKNE--------GKTIHsldFHAGY--------GPSKALSG 123
Cdd:cd13856   12 LAPD------GFERSAVLANGQFPGPLITANKGDTFRITVVNQltdptmrrSTSIH---WHGIFqhgtnyadGPAFVTQC 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 262089312 124 SVKPGESKTWSLT-GEFPGVFIYH-------CgaDGLNG 154
Cdd:cd13856   83 PIAPNHSFTYDFTaGDQAGTFWYHshlstqyC--DGLRG 119
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 75-170 7.61e-05

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: 42.29  E-value: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  75 AYTFNGTIPGPVISIDQGDTLNITLKN---EGKTIHsldFHA----GYGPSKALSG----SVKPGESKT--WSLTGEFpG 141
Cdd:cd13850   19 VILINGQFPGPPIILDEGDEVEILVTNnlpVNTTIH---FHGilqrGTPWSDGVPGvtqwPIQPGGSFTyrWKAEDQY-G 94

                         90       100
                 ....*....|....*....|....*....
gi 262089312 142 VFIYHCGADGLngiwehISNGMYGGIVVH 170
Cdd:cd13850   95 LYWYHSHYRGY------YMDGLYGPIYIR 117
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 69-170 8.07e-05

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: 41.76  E-value: 8.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  69 GGITYNAYTFNGTIPGPVISIDQGDTLNITLKN----EGKTIHsldFHagyGPSKalSGS-------------VKPGESK 131
Cdd:cd13858    1 DGVERPVITVNGQLPGPSIEVCEGDTVVVDVKNrlpgESTTIH---WH---GIHQ--RGTpymdgvpmvtqcpILPGQTF 72

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 262089312 132 TWSLTGEFPGVFIYHcGADGLngiweHISNGMYGGIVVH 170
Cdd:cd13858   73 RYKFKADPAGTHWYH-SHSGT-----QRADGLFGALIVR 105
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 419-550 1.27e-04

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


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 42.25  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 419 ATMLNTSASSGNATGNGTMMAGNMTGNmtgnmTGTAGSEIDISPGssspsNAKFFEPPALTVKAGTTV--TWKNTDSTLH 496
Cdd:COG4454   10 ALALALLATAALAAGDSHASAIGKPGD-----AAKVTRTITVTMG-----DTMRFTPDSIEVKAGETVrfVVTNPGKLKH 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262089312 497 TVTSGS-AEGGEPGK-----------DFDSSYLAGGKTFEHV--FSTPGTFDYFCTL--HpY---MKGHVTVN 550
Cdd:COG4454   80 EFVLGTfAELAEHAKvmakmpdmehgDPNEVELAPGETGELVwtFTKAGTFEFACLIpgH-YeagMTGKIVVK 151
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 473-548 1.39e-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: 41.45  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 473 FEPPALTVKAGTTVTW--KNTDSTLHTVT-------SGSAEGGEPGKDFDSSYLAGGKTFEHVFST--PGTFDYFCT--- 538
Cdd:cd00920   20 FGPPVLVVPVGDTVRVqfVNKLGENHSVTiagfgvpVVAMAGGANPGLVNTLVIGPGESAEVTFTTdqAGVYWFYCTipg 99

                         90
                 ....*....|.
gi 262089312 539 -LHPYMKGHVT 548
Cdd:cd00920  100 hNHAGMVGTIN 110
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 65-165 8.62e-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: 39.14  E-value: 8.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  65 ALHPGGITYNAYTFNGTIPgPVISIDQGDTLNITLKNEGKTIHSLDFHAGYGPSKALSGS----------VKPGESKTWS 134
Cdd:cd00920    4 TASDWGWSFTYNGVLLFGP-PVLVVPVGDTVRVQFVNKLGENHSVTIAGFGVPVVAMAGGanpglvntlvIGPGESAEVT 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 262089312 135 LTGEFPGVFIYHCgadglnGIWEHISNGMYG 165
Cdd:cd00920   83 FTTDQAGVYWFYC------TIPGHNHAGMVG 107
Cupredoxin_like_2 cd04211
Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are ...
 468-549 1.39e-03

Uncharacterized Cupredoxin-like subfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins because they have 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. Majority of family members contain multiple cupredoxin domain repeats; ceruloplasmin and coagulation factors V/VIII have six repeats; Laccase, ascorbate oxidase, and 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: 259873 [Multi-domain]  Cd Length: 110  Bit Score: 38.43  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 468 SNAKFFEPPALTVKAGTTVTW--KNTDSTLHTVTSGSAEGGE---------PGKDFDSSY---LAGGKTFEHV--FSTPG 531
Cdd:cd04211    9 SDTMRFTPDSIQVKQGETVRFvvTNNGKIPHEFVIGTAAELKehaemmrkhPGMEHDEPNmvsLAPGKSGEIVwtFTKAG 88

                         90       100
                 ....*....|....*....|..
gi 262089312 532 TFDYFCTL--H--PYMKGHVTV 549
Cdd:cd04211   89 TFEFACLIpgHyeAGMVGKVTV 110
PetE COG3794
Plastocyanin [Energy production and conversion];
85-169 1.72e-03

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 37.28  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  85 PVISIDQGDTlnITLKNEGKTIHslDFHAGYGPSKAL-SGSVKPGEskTWSLTGEFPGVFIYHCgadglngiweHISNGM 163
Cdd:COG3794    6 ATLTVKPGDT--VTWVNTDSVPH--NVTSDDGPDGAFdSGLLAPGE--TFSVTFDEPGTYDYYC----------TPHPWM 69


                 ....*.
gi 262089312 164 YGGIVV 169
Cdd:COG3794   70 VGTIVV 75
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 73-138 3.99e-03

Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the first, third, and fifth cupredoxin domains of ceruloplasmin and similar proteins including the first, third and fifth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. It functions in copper transport, amine oxidation 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: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 38.54  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  73 YNAYTFNGTIP--------GPVISIDQGDTLNITLKNegKTIHSLDFHA-GYGPSKALSG---------------SVKPG 128
Cdd:cd04199   50 YTDESFTTPGPqpehlgilGPTIRAEVGDTIKVHFKN--KASRPYSIHPhGVSYEKDSEGasysdqtgpdekkddAVAPG 127

                         90
                 ....*....|..
gi 262089312 129 ESKT--WSLTGE 138
Cdd:cd04199  128 ETYTyvWIVTEE 139
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 78-170 5.29e-03

The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) and a four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the exocellular space and the carboxyl terminus in the cytoplasm. The periplamic 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 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: 259920 [Multi-domain]  Cd Length: 121  Bit Score: 37.25  E-value: 5.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  78 FNGTIPGPVISIDQGDTLNITLKNE-GKTIHSLDFHAGY--------GPSKALSGSVKPGESKTWSLTGEFP-GVFIYHC 147
Cdd:cd13851   25 INGQWPPPPIEVNKGDTVVIHATNSlGDQPTSLHFHGLFqngtnymdGPVGVTQCPIPPGQSFTYEFTVDTQvGTYWYHS 104

                         90       100
                 ....*....|....*....|...
gi 262089312 148 GADGLNGiwehisNGMYGGIVVH 170
Cdd:cd13851  105 HDGGQYP------DGLRGPFIIH 121
COG4454 COG4454
Uncharacterized copper-binding protein, cupredoxin-like subfamily [General function prediction ...
 87-170 6.42e-03

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


Pssm-ID: 443552 [Multi-domain]  Cd Length: 151  Bit Score: 37.63  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312  87 ISIDQGDTLNITLKNEGKTIH--------SLDFHA---------GYGPSKALSgsVKPGESKTWSLTGEFPGVFIYHCGA 149
Cdd:COG4454   59 IEVKAGETVRFVVTNPGKLKHefvlgtfaELAEHAkvmakmpdmEHGDPNEVE--LAPGETGELVWTFTKAGTFEFACLI 136

                         90       100
                 ....*....|....*....|.
gi 262089312 150 DGlngiweHISNGMYGGIVVH 170
Cdd:COG4454  137 PG------HYEAGMTGKIVVK 151
PHA03292 PHA03292
envelope glycoprotein I; Provisional
 316-482 9.27e-03

envelope glycoprotein I; Provisional


Pssm-ID: 177577  Cd Length: 413  Bit Score: 38.78  E-value: 9.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 316 EAGLY---VGVDHA-MADVVKGAAFaVVAMENSTASDyPTGTCVPPKGSESVVCEEATAAEAAGGAATTEKASASANDNN 391
Cdd:PHA03292 139 DSGAYilrVKLDHApTADVFGLSAF-VYDFDSPTVPD-PEPTTARPEPAAGYVATPTPRYLNAVTTSTYSRSMSSQPAGA 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 392 DKNTNNKSNDNNNKGNDKESQTEVTQNATMLNTSASSGNATGNGTMMAGNMTGNMTGNMTGTAGSEI------DISPGSS 465
Cdd:PHA03292 217 ATATPTPTLDTGLTTVAPPNETVVTGETALLCHWFQPSTRVPTLYLHLLGTTGNLTEDVLLTEDSEIlrtpppDPSSSRS 296

                        170
                 ....*....|....*..
gi 262089312 466 SPSNAKFFEPPALTVKA 482
Cdd:PHA03292 297 PGAGDDFKQTNSTSPKR 313
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 473-549 9.91e-03

Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B from the photosynthetic bacterium Chloroflexus aurantiacus and similar proteins. Auracyanins A and B are very similar blue copper proteins with 38% sequence identity and are homologous to the bacterial redox protein Azurin. However, auracyanin A is expressed only when C. aurantiacus cells are grown in light, whereas auracyanin B is expressed in both dark and light conditions. Thus, auracyanin A may function as a redox partner in photosynthesis, while auracyanin B may function in aerobic respiration.


Pssm-ID: 259895 [Multi-domain]  Cd Length: 121  Bit Score: 36.46  E-value: 9.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089312 473 FEPPALTVKAGTTV--TWKNTDSTLHT---VTSGSAEG-GE---------PGKDF--DSSY-------LAGGKTFEHVF- 527
Cdd:cd04233   15 FDKTRLTVKAGSKVtlTFENPDDMPHNlviVKPGSLEKvGEaalamgadgPAKNYvpDSPDvlaatplVNPGETETLTFt 94

                         90       100
                 ....*....|....*....|....*..
gi 262089312 528 --STPGTFDYFCTL---HPYMKGHVTV 549
Cdd:cd04233   95 apTEPGTYPYVCTYpghWAIMKGVLIV 121
 
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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