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Conserved domains on  [gi|30688168|ref|NP_173714|]
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Cupredoxin superfamily protein [Arabidopsis thaliana]

Protein Classification

multicopper oxidase family protein( domain architecture ID 11450234)

multicopper oxidase family protein couples the one-electron oxidation of four substrate molecules to the four electron reductive cleavage of the O-O bond of dioxygen

CATH:  2.60.40.420
EC:  1.-.-.-
PubMed:  16234932|19816718|14572631|1995346
SCOP:  4002203

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 84-580 2.72e-99

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: 308.02  E-value: 2.72e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  84 PATPVFAYGtsrskATVPGPTIETVYGVDTYVTWRNHLPKshilpwdptispatpkhggiPTVVHLHGGIHEPTSDGNAD 163
Cdd:COG2132  31 KPTTVWGYN-----GQYPGPTIRVREGDRVRVRVTNRLPE--------------------PTTVHWHGLRVPNAMDGVPG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 164 AWFTAGfrETgpkWTkttLHYENKQQPGNMWYHDHAMGLTRVNLLAGLVGAYIlrhhaVESPF-QLPTGDeFDRPLIIFD 242
Cdd:COG2132  86 DPIAPG--ET---FT---YEFPVPQPAGTYWYHPHTHGSTAEQVYRGLAGALI-----VEDPEeDLPRYD-RDIPLVLQD 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 243 RSFRKDGSIYmnatgnnpSIHPQWQPEYFGDVIIVNGKAWPRLNVRRR-KYRFRIINASNARFFKFFFSNGLDFIVVGSD 321
Cdd:COG2132 152 WRLDDDGQLL--------YPMDAAMGGRLGDTLLVNGRPNPTLEVRPGeRVRLRLLNASNARIYRLALSDGRPFTVIATD 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 322 SAYLSKPVMTKSILLSPSEIVDVVVDFYKSPSRTVVLANDAPypypsgdpvNEENGKVMKFIINNESEDDtcTIPKKLIN 401
Cdd:COG2132 224 GGLLPAPVEVDELLLAPGERADVLVDFSADPGEEVTLANPFE---------GRSGRALLTLRVTGAAASA--PLPANLAP 292

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 402 YPNADVSNAVLTRYISMyeyvSNSDEPTHLLVNGLPYE-APVTETPKSGTTEVWEVINLTEDNHPLHIHLGLFKVVEQTa 480
Cdd:COG2132 293 LPDLEDREAVRTRELVL----TGGMAGYVWTINGKAFDpDRPDLTVKLGERERWTLVNDTMMPHPFHLHGHQFQVLSRN- 367

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 481 llaagleefkecmtkqndavkcqiskyarGKKTAvtahERGWKNVFKMMPGHVTRILVRFsyihtnasypfdpTQEPG-Y 559
Cdd:COG2132 368 -----------------------------GKPPP----EGGWKDTVLVPPGETVRILFRF-------------DNYPGdW 401

                       490       500
                ....*....|....*....|.
gi 30688168 560 VYHCHILDHEDNMMMRPLKVI 580
Cdd:COG2132 402 MFHCHILEHEDAGMMGQFEVV 422
 
Name Accession Description Interval E-value
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 84-580 2.72e-99

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: 308.02  E-value: 2.72e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  84 PATPVFAYGtsrskATVPGPTIETVYGVDTYVTWRNHLPKshilpwdptispatpkhggiPTVVHLHGGIHEPTSDGNAD 163
Cdd:COG2132  31 KPTTVWGYN-----GQYPGPTIRVREGDRVRVRVTNRLPE--------------------PTTVHWHGLRVPNAMDGVPG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 164 AWFTAGfrETgpkWTkttLHYENKQQPGNMWYHDHAMGLTRVNLLAGLVGAYIlrhhaVESPF-QLPTGDeFDRPLIIFD 242
Cdd:COG2132  86 DPIAPG--ET---FT---YEFPVPQPAGTYWYHPHTHGSTAEQVYRGLAGALI-----VEDPEeDLPRYD-RDIPLVLQD 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 243 RSFRKDGSIYmnatgnnpSIHPQWQPEYFGDVIIVNGKAWPRLNVRRR-KYRFRIINASNARFFKFFFSNGLDFIVVGSD 321
Cdd:COG2132 152 WRLDDDGQLL--------YPMDAAMGGRLGDTLLVNGRPNPTLEVRPGeRVRLRLLNASNARIYRLALSDGRPFTVIATD 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 322 SAYLSKPVMTKSILLSPSEIVDVVVDFYKSPSRTVVLANDAPypypsgdpvNEENGKVMKFIINNESEDDtcTIPKKLIN 401
Cdd:COG2132 224 GGLLPAPVEVDELLLAPGERADVLVDFSADPGEEVTLANPFE---------GRSGRALLTLRVTGAAASA--PLPANLAP 292

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 402 YPNADVSNAVLTRYISMyeyvSNSDEPTHLLVNGLPYE-APVTETPKSGTTEVWEVINLTEDNHPLHIHLGLFKVVEQTa 480
Cdd:COG2132 293 LPDLEDREAVRTRELVL----TGGMAGYVWTINGKAFDpDRPDLTVKLGERERWTLVNDTMMPHPFHLHGHQFQVLSRN- 367

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 481 llaagleefkecmtkqndavkcqiskyarGKKTAvtahERGWKNVFKMMPGHVTRILVRFsyihtnasypfdpTQEPG-Y 559
Cdd:COG2132 368 -----------------------------GKPPP----EGGWKDTVLVPPGETVRILFRF-------------DNYPGdW 401

                       490       500
                ....*....|....*....|.
gi 30688168 560 VYHCHILDHEDNMMMRPLKVI 580
Cdd:COG2132 402 MFHCHILEHEDAGMMGQFEVV 422
CuRO_2_CotA_like cd13868
The second Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat ...
 234-384 1.97e-83

The second Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat component; CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and it is required for spore resistance against hydrogen peroxide and UV light. Laccase is composed of three cupredoxin-like domains and includes one mononuclear and one trinuclear copper center. It is a member of the multicopper oxidase (MCO) family, which couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water. 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259936 [Multi-domain]  Cd Length: 155  Bit Score: 257.18  E-value: 1.97e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 234 FDRPLIIFDRSFRKDGSIYMNATGNNPSIHPQWQPEYFGDVIIVNGKAWPRLNVRRRKYRFRIINASNARFFKFFFSN-- 311
Cdd:cd13868   1 YEIPLLIQDRSFNADGSLFYPATGANPSPHPSWVPEFFGDTIVVNGKAWPYLEVEPRRYRFRILNGSNARFYNLSLSNgd 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30688168 312 GLDFIVVGSDSAYLSKPVMTKSILLSPSEIVDVVVDFYKSPSRTVVLANDAPYPYPSG-DPVNEENGKVMKFII 384
Cdd:cd13868  81 GLPFWQIGTDGGFLPKPVPLDSLLIGPAERADVIVDFSDYAGQTLILKNDAPAPYPGGgAADPDTTGQVMQFRV 154
PRK10965 PRK10965
multicopper oxidase; Provisional
 101-574 1.44e-23

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 104.34  E-value: 1.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  101 PGPTIETVYGVDTYVTWRNHLPKshilpwdptispatpkhggiPTVVHLHGGIHEPTSDGNADAWFTAGfretgPKWTKT 180
Cdd:PRK10965  75 LGPAVRLQRGKAVTVDITNQLPE--------------------ETTLHWHGLEVPGEVDGGPQGIIAPG-----GKRTVT 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  181 tlhYENKQQPGNMWYHDHAMGLTRVNLLAGLVGAYILRHhavESPFQLPTGDEF---DRPLIIFDRSFRKDGSI-Y---- 252
Cdd:PRK10965 130 ---FTVDQPAATCWFHPHQHGKTGRQVAMGLAGLVLIED---DESLKLGLPKQWgvdDIPVILQDKRFSADGQIdYqldv 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  253 MNAT-GnnpsihpqwqpeYFGDVIIVNGKAWPRLNVRRRKYRFRIINASNARFFKFFFSNGLDFIVVGSDSAYLSKPVMT 331
Cdd:PRK10965 204 MTAAvG------------WFGDTLLTNGAIYPQHAAPRGWLRLRLLNGCNARSLNLATSDGRPLYVIASDGGLLAEPVKV 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  332 KSILLSPSEIVDVVVDFYKSPSRTVVlandapyPYP---SGDPVNEENGKVMKFIINNESEDDTCTIPKKLINYPNADVS 408
Cdd:PRK10965 272 SELPILMGERFEVLVDTSDGKAFDLV-------TLPvsqMGMALAPFDKPLPVLRIQPLLISASGTLPDSLASLPALPSL 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  409 NAVLTRYIS-------------------------------------------MYEYVSNSDEPTHLL----VNGLPY--E 439
Cdd:PRK10965 345 EGLTVRRLQlsmdprldmmgmqmlmekygdqamagmdmdhmmghmghgnmdhMNHGAADAGPAFDFHhankINGKAFdmN 424

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  440 APVTETPKsGTTEVWeVINLTEDN--HPLHIHLGLFKVveqtallaagLEEfkecmtkqndavkcqiskyaRGKKTAvtA 517
Cdd:PRK10965 425 KPMFAAKK-GQYERW-VISGVGDMmlHPFHIHGTQFRI----------LSE--------------------NGKPPA--A 470

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30688168  518 HERGWKNVFKmMPGHVTRILVRFSYihtnasypfDPTQEPGYVYHCHILDHEDNMMM 574
Cdd:PRK10965 471 HRAGWKDTVR-VEGGRSEVLVKFDH---------DAPKEHAYMAHCHLLEHEDTGMM 517
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 418-579 2.97e-10

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: 58.60  E-value: 2.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168   418 MYEYVSNSDEPTHLLVNGLPY-EAPVTETPKSGTTEVWEVINLTEDNHPLHIHLGLFKVVEQTallaaGLEEFKECMTKQ 496
Cdd:pfam07731   9 LLQITSGNFRRNDWAINGLLFpPNTNVITLPYGTVVEWVLQNTTTGVHPFHLHGHSFQVLGRG-----GGPWPEEDPKTY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168   497 NdavkcqiskyargkktavtAHERGWKNVFKMMPGHVTRILVRFSYihtnasypfdptqePG-YVYHCHILDHEDNMMMR 575
Cdd:pfam07731  84 N-------------------LVDPVRRDTVQVPPGGWVAIRFRADN--------------PGvWLFHCHILWHLDQGMMG 130


                  ....
gi 30688168   576 PLKV 579
Cdd:pfam07731 131 QFVV 134
 
Name Accession Description Interval E-value
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 84-580 2.72e-99

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: 308.02  E-value: 2.72e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  84 PATPVFAYGtsrskATVPGPTIETVYGVDTYVTWRNHLPKshilpwdptispatpkhggiPTVVHLHGGIHEPTSDGNAD 163
Cdd:COG2132  31 KPTTVWGYN-----GQYPGPTIRVREGDRVRVRVTNRLPE--------------------PTTVHWHGLRVPNAMDGVPG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 164 AWFTAGfrETgpkWTkttLHYENKQQPGNMWYHDHAMGLTRVNLLAGLVGAYIlrhhaVESPF-QLPTGDeFDRPLIIFD 242
Cdd:COG2132  86 DPIAPG--ET---FT---YEFPVPQPAGTYWYHPHTHGSTAEQVYRGLAGALI-----VEDPEeDLPRYD-RDIPLVLQD 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 243 RSFRKDGSIYmnatgnnpSIHPQWQPEYFGDVIIVNGKAWPRLNVRRR-KYRFRIINASNARFFKFFFSNGLDFIVVGSD 321
Cdd:COG2132 152 WRLDDDGQLL--------YPMDAAMGGRLGDTLLVNGRPNPTLEVRPGeRVRLRLLNASNARIYRLALSDGRPFTVIATD 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 322 SAYLSKPVMTKSILLSPSEIVDVVVDFYKSPSRTVVLANDAPypypsgdpvNEENGKVMKFIINNESEDDtcTIPKKLIN 401
Cdd:COG2132 224 GGLLPAPVEVDELLLAPGERADVLVDFSADPGEEVTLANPFE---------GRSGRALLTLRVTGAAASA--PLPANLAP 292

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 402 YPNADVSNAVLTRYISMyeyvSNSDEPTHLLVNGLPYE-APVTETPKSGTTEVWEVINLTEDNHPLHIHLGLFKVVEQTa 480
Cdd:COG2132 293 LPDLEDREAVRTRELVL----TGGMAGYVWTINGKAFDpDRPDLTVKLGERERWTLVNDTMMPHPFHLHGHQFQVLSRN- 367

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 481 llaagleefkecmtkqndavkcqiskyarGKKTAvtahERGWKNVFKMMPGHVTRILVRFsyihtnasypfdpTQEPG-Y 559
Cdd:COG2132 368 -----------------------------GKPPP----EGGWKDTVLVPPGETVRILFRF-------------DNYPGdW 401

                       490       500
                ....*....|....*....|.
gi 30688168 560 VYHCHILDHEDNMMMRPLKVI 580
Cdd:COG2132 402 MFHCHILEHEDAGMMGQFEVV 422
CuRO_2_CotA_like cd13868
The second Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat ...
 234-384 1.97e-83

The second Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat component; CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and it is required for spore resistance against hydrogen peroxide and UV light. Laccase is composed of three cupredoxin-like domains and includes one mononuclear and one trinuclear copper center. It is a member of the multicopper oxidase (MCO) family, which couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water. 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259936 [Multi-domain]  Cd Length: 155  Bit Score: 257.18  E-value: 1.97e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 234 FDRPLIIFDRSFRKDGSIYMNATGNNPSIHPQWQPEYFGDVIIVNGKAWPRLNVRRRKYRFRIINASNARFFKFFFSN-- 311
Cdd:cd13868   1 YEIPLLIQDRSFNADGSLFYPATGANPSPHPSWVPEFFGDTIVVNGKAWPYLEVEPRRYRFRILNGSNARFYNLSLSNgd 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30688168 312 GLDFIVVGSDSAYLSKPVMTKSILLSPSEIVDVVVDFYKSPSRTVVLANDAPYPYPSG-DPVNEENGKVMKFII 384
Cdd:cd13868  81 GLPFWQIGTDGGFLPKPVPLDSLLIGPAERADVIVDFSDYAGQTLILKNDAPAPYPGGgAADPDTTGQVMQFRV 154
CuRO_1_BOD_CotA_like cd13844
The first Cupredoxin domain of Bilirubin oxidase (BOD), the bacterial endospore coat component ...
 65-221 1.36e-70

The first Cupredoxin domain of Bilirubin oxidase (BOD), the bacterial endospore coat component CotA, and similar proteins; Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and it is required for spore resistance against hydrogen peroxide and UV light. Also included in this subfamily are phenoxazinone synthase (PHS), which catalyzes the oxidative coupling of substituted o-aminophenols to produce phenoxazinones. PHS has been shown to participate in diverse biological functions such as spore pigmentation and biosynthesis of the antibiotic grixazone. These are Laccase-like multicopper oxidases (MCOs) that 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 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: 259913 [Multi-domain]  Cd Length: 162  Bit Score: 224.09  E-value: 1.36e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  65 PASLQIGMFSTKWKFHRDLPATPVFAYGTSrSKATVPGPTIETVYGVDTYVTWRNHLPKSHILPWDPT-------ISPAT 137
Cdd:cd13844   1 GDYYEIEMREFTQQLHPDLPPTTVWGYGGS-NSTSYPGPTIEARRGVPVRVTWVNNLPDKHHLPLDDTlpsteeaTPGAE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 138 PKHGGIPTVVHLHGGIHEPTSDGNADAWFTAGFREtGPKWTKTTLHYENKQQPGNMWYHDHAMGLTRVNLLAGLVGAYIL 217
Cdd:cd13844  80 PPVPPVPTVVHLHGGEVPPESDGYPEAWFTPGGEE-GPGFGSATYYYPNDQSAATLWYHDHALGITRLNVYAGLAGFYLI 158


                ....
gi 30688168 218 RHHA 221
Cdd:cd13844 159 RDEA 162
CuRO_3_CotA_like cd13891
The third Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat ...
 413-579 3.14e-65

The third Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat component; CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and is required for spore resistance against hydrogen peroxide and UV light. CotA belongs to the laccase-like multicopper oxidase (MCO) family, which 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 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259958 [Multi-domain]  Cd Length: 143  Bit Score: 209.46  E-value: 3.14e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 413 TRYISMYEYVSNSDEPTHLLVNGLPYEAPVTETPKSGTTEVWEVINLTEDNHPLHIHLGLFKVVEQTALLAAglEEFKEC 492
Cdd:cd13891   3 TRQLTLGETVDSGGRLTHLLNNLLGWHDPVTETPRLGSTEIWEIINLTPDAHPIHLHLVQFQVLDRQPFDVD--EYNATG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 493 mtkqndavkcqiSKYARGKKTAVTAHERGWKNVFKMMPGHVTRILVRFSYIhtnasypfdptqEPGYVYHCHILDHEDNM 572
Cdd:cd13891  81 ------------EIYYTGPPRPPAPNERGWKDTVRAYPGEVTRIIVRFDGP------------EGGYVWHCHILEHEDNE 136


                ....*..
gi 30688168 573 MMRPLKV 579
Cdd:cd13891 137 MMRPFRV 143
CuRO_2_BOD_CotA_like cd14448
Cupredoxin domain 2 of Bilirubin oxidase (BOD), the bacterial endospore coat component CotA, ...
 235-382 9.71e-45

Cupredoxin domain 2 of Bilirubin oxidase (BOD), the bacterial endospore coat component CotA, and similar proteins; Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and is required for spore resistance against hydrogen peroxide and UV light. Also included in this subfamily are phenoxazinone synthase (PHS), which catalyzes the oxidative coupling of substituted o-aminophenols to produce phenoxazinones, and FtsP (also named SufI), which is a component of the cell division apparatus. These proteins are laccase-like multicopper oxidases (MCOs) that 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 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259990 [Multi-domain]  Cd Length: 144  Bit Score: 155.15  E-value: 9.71e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 235 DRPLIIFDRSFRKDGSIYMNATGNNPsihpQWQPEYFGDVIIVNGKAWPRLNVRRRKYRFRIINASNARFFKFFFSNGLD 314
Cdd:cd14448   1 DLPLVITDRQFNADGTLYYPSPPTNM----EWVPGFFGDVILVNGKIWPYLEVEPGWYRLRLLNASNARHYNLALSDGLP 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30688168 315 FIVVGSDSAYLSKPVMTKSILLSPSEIVDVVVDFYKSPSRTVVLANDAPYPYPSGDPVNEENgkVMKF 382
Cdd:cd14448  77 FHVIGSDGGLLEAPVKVKELVLAPAERIDVVVDFSQYAGEEVELVNLGGASMAILPTDYDTD--VMQF 142
CuRO_2_BOD cd13866
The second cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the ...
 233-384 7.75e-39

The second cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. It is used in diagnosing jaundice through the determination of bilirubin in serum. BOD is a member of the multicopper oxidase (MCO) family that also includes laccase, ascorbate oxidase and ceruloplasmin. 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259934 [Multi-domain]  Cd Length: 152  Bit Score: 139.70  E-value: 7.75e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 233 EFDRPLIIFDRSFRKDGSIYMNatgnnpsihPQWQPEYFGDVIIVNGKAWPRLNVRRRKYRFRIINASNARFFKFFFSNG 312
Cdd:cd13866   3 DYDIPLVLADKQFDPNGQLMFD---------EFNLDGLLGDVILVNGVPWPFLNVEPRKYRFRLLNASVSRFFQLALVDG 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30688168 313 LD-----FIVVGSDSAYLSKPVMTKSILLSPSEIVDVVVDFYKSPS-RTVVLANDAPYPYPSG-DPVNEENGKVMKFII 384
Cdd:cd13866  74 DNptripFTVIASDGGLLSHPVETTLLRLGMAERYDIVVDFSKYAAgTRLYLVNRLEHDDGRGpDNDYPATDKVMRFRV 152
CuRO_2_CueO_FtsP cd13867
The second Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 235-382 2.47e-32

The second Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins; CueO is a multicopper oxidase (MCO) that 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. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the second domain. 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259935 [Multi-domain]  Cd Length: 146  Bit Score: 121.53  E-value: 2.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 235 DRPLIIFDRSFRKDGSIYMNATGNNPSihpqwqpeYFGDVIIVNGKAWPRLNVRRRKYRFRIINASNARFFKFFFSNGLD 314
Cdd:cd13867   2 DIPLILQDRRFDEDGQLDYRMMDDMDG--------FLGDTLLVNGTINPYLDVPRGWVRLRLLNGSNARTYNLGFSDNRP 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30688168 315 FIVVGSDSAYLSKPVMTKSILLSPSEIVDVVVDFykSPSRTVVLANDaPYPYPSGDPVNEENGKVMKF 382
Cdd:cd13867  74 FYQIASDGGLLPAPVELKRLLLAPGERAEILVDF--SDGEPVSLRSG-PDEGGLGMIGFGDSGEDDDF 138
CuRO_2_McoP_like cd13879
The second cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 234-365 1.39e-26

The second cupredoxin domain of multicopper oxidase McoP and similar proteins; This family includes archaeal and bacterial multicopper oxidases (MCOs), represented by the extremely thermostable McoP from the hyperthermophilic archaeon Pyrobaculum aerophilum. McoP is an efficient metallo-oxidase that catalyzes the oxidation of cuprous and ferrous ions. It is noteworthy that McoP has three-fold higher catalytic efficiency when using nitrous oxide as electron acceptor than when using dioxygen, the typical oxidizing substrate of multicopper oxidases. McoP may function as a novel archaeal nitrous oxide reductase that is probably involved in the denitrification pathway in archaea. 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259946 [Multi-domain]  Cd Length: 162  Bit Score: 105.82  E-value: 1.39e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 234 FDRPLIIFDRSFRKDGS-IYmnatgnNPSIHPQWQpEYFGDVIIVNGKAWPRLNVRRRKYRFRIINASNARFFKFFFSNG 312
Cdd:cd13879   1 YDLPLVIQDRRFDANNQlVY------LPNGMDRMM-GFLGDRILVNGTPDPTLSVATRAYRLRLLNGSNARIYKLAWSDG 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 30688168 313 LDFIVVGSDSAYLSKPVMTKSILLSPSEIVDVVVDFYKSPSRTVVLANDAPYP 365
Cdd:cd13879  74 SPLTVIGTDGGLLEAPKTVPYVMLAPGERVDLWVDFSGRPVGTELKLKSLPFS 126
PRK10965 PRK10965
multicopper oxidase; Provisional
 101-574 1.44e-23

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 104.34  E-value: 1.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  101 PGPTIETVYGVDTYVTWRNHLPKshilpwdptispatpkhggiPTVVHLHGGIHEPTSDGNADAWFTAGfretgPKWTKT 180
Cdd:PRK10965  75 LGPAVRLQRGKAVTVDITNQLPE--------------------ETTLHWHGLEVPGEVDGGPQGIIAPG-----GKRTVT 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  181 tlhYENKQQPGNMWYHDHAMGLTRVNLLAGLVGAYILRHhavESPFQLPTGDEF---DRPLIIFDRSFRKDGSI-Y---- 252
Cdd:PRK10965 130 ---FTVDQPAATCWFHPHQHGKTGRQVAMGLAGLVLIED---DESLKLGLPKQWgvdDIPVILQDKRFSADGQIdYqldv 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  253 MNAT-GnnpsihpqwqpeYFGDVIIVNGKAWPRLNVRRRKYRFRIINASNARFFKFFFSNGLDFIVVGSDSAYLSKPVMT 331
Cdd:PRK10965 204 MTAAvG------------WFGDTLLTNGAIYPQHAAPRGWLRLRLLNGCNARSLNLATSDGRPLYVIASDGGLLAEPVKV 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  332 KSILLSPSEIVDVVVDFYKSPSRTVVlandapyPYP---SGDPVNEENGKVMKFIINNESEDDTCTIPKKLINYPNADVS 408
Cdd:PRK10965 272 SELPILMGERFEVLVDTSDGKAFDLV-------TLPvsqMGMALAPFDKPLPVLRIQPLLISASGTLPDSLASLPALPSL 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  409 NAVLTRYIS-------------------------------------------MYEYVSNSDEPTHLL----VNGLPY--E 439
Cdd:PRK10965 345 EGLTVRRLQlsmdprldmmgmqmlmekygdqamagmdmdhmmghmghgnmdhMNHGAADAGPAFDFHhankINGKAFdmN 424

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  440 APVTETPKsGTTEVWeVINLTEDN--HPLHIHLGLFKVveqtallaagLEEfkecmtkqndavkcqiskyaRGKKTAvtA 517
Cdd:PRK10965 425 KPMFAAKK-GQYERW-VISGVGDMmlHPFHIHGTQFRI----------LSE--------------------NGKPPA--A 470

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30688168  518 HERGWKNVFKmMPGHVTRILVRFSYihtnasypfDPTQEPGYVYHCHILDHEDNMMM 574
Cdd:PRK10965 471 HRAGWKDTVR-VEGGRSEVLVKFDH---------DAPKEHAYMAHCHLLEHEDTGMM 517
CuRO_3_PHS cd13892
The third Cupredoxin domain of phenoxazinone synthase (PHS); Phenoxazinone synthase (PHS, ...
 438-579 3.87e-23

The third Cupredoxin domain of phenoxazinone synthase (PHS); Phenoxazinone synthase (PHS, 2-aminophenol:oxygen oxidoreductase) catalyzes the oxidative coupling of substituted o-aminophenols to produce phenoxazinones. PHS has been shown to participate in diverse biological functions such as spore pigmentation and biosynthesis of the antibiotic grixazone. PHS is a member of the laccase-like multicopper oxidase (MCO) family, which 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 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259959 [Multi-domain]  Cd Length: 184  Bit Score: 96.83  E-value: 3.87e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 438 YEAPVTETPKSGTTEVWEVINLTEDN-HPLHIHLGLFKVVEQTALLAAGLEEFKECMTKQNDAvkcqiskyarGKKTAVT 516
Cdd:cd13892  60 FDDDVNFTAAAGSWERWTFVNLGEGHpHPMHIHLAEFQVLERQPYDVTGFDTTVGGTDRPITP----------GEAAPLE 129

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30688168 517 AHERGWKNVFKMMPGHVTRILVRFsyihtnasypfdPTQEPGYVYHCHILDHEDNMMMRPLKV 579
Cdd:cd13892 130 PVELGWKDTVVVGPGELVTVLVQF------------DGATGRFMYHCHILEHEDHDMMRPFVV 180
CuRO_3_CueO_FtsP cd13890
The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 413-579 1.43e-19

The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins; CueO is a multicopper oxidase (MCO) that 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. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. FtsP does not contain any copper binding sites.


Pssm-ID: 259957 [Multi-domain]  Cd Length: 124  Bit Score: 84.61  E-value: 1.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 413 TRYISMyeyvsnSDEPTHLLVNGLPYE-APVTETPKSGTTEVWEVINLTEDNHPLHIHLGLFKVVEQtallaagleefke 491
Cdd:cd13890   4 ERTFTL------SGDPHAFTINGKRFDmNRIDFTVKLGTTEIWEVTNTDGMPHPFHIHGVQFRILSR------------- 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 492 cmtkqndavkcqiskyaRGKKtaVTAHERGWKNVFKMMPGHVTRILVRFSYiHTNASYPfdptqepgYVYHCHILDHEDN 571
Cdd:cd13890  65 -----------------NGQP--PPPNEAGWKDTVWVPPGETVRILVKFDH-YADPTGP--------FMYHCHILEHEDN 116


                ....*...
gi 30688168 572 MMMRPLKV 579
Cdd:cd13890 117 GMMGQFVV 124
CuRO_2_PHS cd13869
The second Cupredoxin domain of phenoxazinone synthase (PHS); Phenoxazinone synthase (PHS, ...
 237-382 2.80e-18

The second Cupredoxin domain of phenoxazinone synthase (PHS); Phenoxazinone synthase (PHS, 2-aminophenol:oxygen oxidoreductase) catalyzes the oxidative coupling of substituted o-aminophenols to produce phenoxazinones. PHS participates in diverse biological functions such as spore pigmentation and biosynthesis of the antibiotic grixazone. It is a member of the multicopper oxidase (MCO) family, which couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water. 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259937 [Multi-domain]  Cd Length: 166  Bit Score: 82.23  E-value: 2.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 237 PLIIFDRSFRKDGS--------------IYMNATGNNPSIHPqwqpeYFGDVIIVNGKAWPRLNVRRRKYRFRIINASNA 302
Cdd:cd13869   3 PLVIRDRNLDTDADgaltgrllhkllykQAGVGTGDAALEIP-----FTGPYTLVNGVIWPYLEVRPGWYRLRLLNASNA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 303 RFFKFFFSNGLD-------FIVVGSDSAYLSKPVMT--KSILLSPSEIVDVVVDFYKSPSRTVVLANDAPYPYPSGDPVN 373
Cdd:cd13869  78 RIYRLALLDETDehpvpgaLVVIGTDAGLLPRPVPVpgGAVNLGPGERADVLVDFAALRGRRLRLVNESPGALNGQPGQT 157


                ....*....
gi 30688168 374 EENgkVMKF 382
Cdd:cd13869 158 DPD--VMQF 164
CuRO_2_McoC_like cd13881
The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 235-382 5.05e-18

The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family includes bacterial multicopper oxidases (MCOs) represented by McoC from the pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic MCO, 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 the 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. They are 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259948 [Multi-domain]  Cd Length: 142  Bit Score: 80.73  E-value: 5.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 235 DRPLIIFDRSFRKDGSIymnatgnNPSIHPQWQ--PEyfGDVIIVNGKAWPRLNVRRRKY-RFRIINASNARFFKFFFsN 311
Cdd:cd13881   1 ERVLVLSDLTLDGDGQL-------AEPSAADWMfgRE--GDLVLVNGQLNPTITVRPGEVqRWRIVNAASARYFRLAL-D 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30688168 312 GLDFIVVGSDSAYLSKPVMTKSILLSPSEIVDVVVDFYKSPSRTVVLANdapyPYPSGDPVNEENGKVMKF 382
Cdd:cd13881  71 GHKFRLIGTDGGLLEAPREVDELLLAPGERAEVLVTAGEPGGRLVLLAL----PYDRGHMGGMEPRPPLTL 137
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 413-574 2.86e-16

The third 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259967 [Multi-domain]  Cd Length: 123  Bit Score: 75.36  E-value: 2.86e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 413 TRYISMYEYVSNSDEPThLLVNGLPYEAP-VTETPKSGTTEVWEVINLTEDNHPLHIHLGLFKVVEqtallaagleefke 491
Cdd:cd13900   3 TRRLVFSEGMSPGGGGA-FTINGKPFDPDrPDRTVRLGTVEEWTLINTSGEDHPFHIHVNPFQVVS-------------- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 492 cmtkqndavkcqiskyargkKTAVTAHERGWKNVFKMMPGHVTRILVRFsyihtnasypFDPTQEpgYVYHCHILDHEDN 571
Cdd:cd13900  68 --------------------INGKPGLPPVWRDTVNVPAGGSVTIRTRF----------RDFTGE--FVLHCHILDHEDQ 115


                ...
gi 30688168 572 MMM 574
Cdd:cd13900 116 GMM 118
CuRO_3_BOD cd13889
The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the ...
 433-574 1.82e-15

The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. It is used in diagnosing jaundice through the determination of bilirubin in serum. BOD is a member of the multicopper oxidase (MCO) family that also includes laccase, ascorbate oxidase and ceruloplasmin. 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259956 [Multi-domain]  Cd Length: 124  Bit Score: 73.12  E-value: 1.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 433 VNGLPYEAP--VTETPKSGTTEVWEVINLTED-NHPLHIHLglfkvveqtallaaglEEFkecmtkqndavkcQISKYAR 509
Cdd:cd13889  17 INGKTWADPnrIDAAPQLGTVEIWTLINGGGGwSHPIHIHL----------------EDF-------------QILSRNG 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30688168 510 GKKtAVTAHERGWKNVFKMMPGHVTRILVRFSyihtnasyPFDPTqepgYVYHCHILDHEDNMMM 574
Cdd:cd13889  68 GSR-AVPPYERGRKDVVYLGPGEEVRVLMRFR--------PFRGK----YMMHCHNLVHEDHDMM 119
PRK10883 PRK10883
FtsI repressor; Provisional
 187-350 3.21e-14

FtsI repressor; Provisional


Pssm-ID: 182808 [Multi-domain]  Cd Length: 471  Bit Score: 75.13  E-value: 3.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  187 KQQPGNMWYHDHAMGLTRVNLLAGLVGAYILRHhAVESPFQLPTG---DEFdrPLIIFDRSFRKDGSiymnatgnnpsih 263
Cdd:PRK10883 133 RQNAATCWYHANTPNRMAQHVYNGLAGMWLVED-EVSKSLPIPNHygvDDF--PVIIQDKRLDNFGT------------- 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  264 PQWQPE----YFGDVIIVNGKAWPRLNVRRRKYRFRIINASNARFFKFFFSNGLDFIVVGSDSAYLSKPVMTKSILLSPS 339
Cdd:PRK10883 197 PEYNEPgsggFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNARRYQLQMSDGRPLHVIAGDQGFLPAPVSVKQLSLAPG 276

                        170
                 ....*....|.
gi 30688168  340 EIVDVVVDFYK 350
Cdd:PRK10883 277 ERREILVDMSN 287
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 431-579 3.96e-14

The third 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259969 [Multi-domain]  Cd Length: 125  Bit Score: 69.35  E-value: 3.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 431 LLVNGLPYEAPVTE-TPKSGTTEVWEVINLTEDNHPLHIHLGLFKVVEQTALLAAgleefkecmtkqndavkcqiskyar 509
Cdd:cd13902  21 FLINGKTFDMNRIDfVAKVGEVEVWEVTNTSHMDHPFHLHGTQFQVLEIDGNPQK------------------------- 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30688168 510 gkktavtAHERGWKNVFKMMPGHVTRILVRFSyihtnasypfdptqEPG-YVYHCHILDHEDNMMMRPLKV 579
Cdd:cd13902  76 -------PEYRAWKDTVNLPPGEAVRIATRQD--------------DPGmWMYHCHILEHEDAGMMGMLHV 125
CuRO_3_McoP_like cd13888
The third cupredoxin domain of multicopper oxidase McoP and similar proteins; This subfamily ...
 425-579 1.28e-13

The third cupredoxin domain of multicopper oxidase McoP and similar proteins; This subfamily includes archaeal and bacterial multicopper oxidases (MCOs), represented by the extremely thermostable McoP from the hyperthermophilic archaeon Pyrobaculum aerophilum. McoP is an efficient metallo-oxidase that catalyzes the oxidation of cuprous and ferrous ions. It is noteworthy that McoP has three-fold higher catalytic efficiency when using nitrous oxide as electron acceptor than when using dioxygen, the typical oxidizing substrate of multicopper oxidases. McoP may function as a novel archaeal nitrous oxide reductase that is probably involved in the denitrification pathway in archaea. Members of this subfamily contain three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259955 [Multi-domain]  Cd Length: 139  Bit Score: 68.36  E-value: 1.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 425 SDEPTHLLVNGLPYEAPVTETP---KSGTTEVWEVINLTED-NHPLHIHLGLFKVVEQTALLAagleefkecmtkqndav 500
Cdd:cd13888   9 SMGRMQWTINGETWADDPDAFPverVGGTVEIWELVNDAASmPHPMHIHGFQFQVLERSDSPP----------------- 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30688168 501 kcQISKYARGKKtAVTAHERGWKNVFKMMPGHVTRILVRFSYihtnasyPFDPTQEpgYVYHCHILDHEDNMMMRPLKV 579
Cdd:cd13888  72 --QVAELAVAPS-GRTATDLGWKDTVLVWPGETVRIAVDFTH-------DYPGDQL--YLLHCHNLEHEDDGMMVNVRV 138
CuRO_3_MCO_like_1 cd13907
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 432-579 4.52e-13

The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259974 [Multi-domain]  Cd Length: 154  Bit Score: 67.12  E-value: 4.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 432 LVNGLPYE----APvTETPKSGTTEVWEVINLTEDN---------------------HPLHIHLGLFKVVEQTAL--LAA 484
Cdd:cd13907  16 TINGRSFEmddvTP-DETVKLNTTEVWEIINDLGGMgggggmmggggmmmggmmampHPIHLHGVQFQVLERSVGpkDRA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 485 GLEEFKECMTkqndavkcqiskyargkktavtahERGWKNVFKMMPGHVTRILVRFsyihtnasypfdpTQEPG-YVYHC 563
Cdd:cd13907  95 YWATVKDGFI------------------------DEGWKDTVLVMPGERVRIIKPF-------------DDYKGlFLYHC 137

                       170
                ....*....|....*.
gi 30688168 564 HILDHEDNMMMRPLKV 579
Cdd:cd13907 138 HNLEHEDMGMMRNFLV 153
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 99-218 8.99e-13

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: 65.00  E-value: 8.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  99 TVPGPTIETVYGVDTYVTWRNHLPkshilpwdptispatpkhgGIPTVVHLHGGIHEPTSDGNADAWFTAGfreTGPKWT 178
Cdd:cd04206  27 QFPGPTIRVKEGDTVEVTVTNNLP-------------------NEPTSIHWHGLRQPGTNDGDGVAGLTQC---PIPPGE 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 30688168 179 KTTLHYENKQQPGNMWYHDHAMGltrvNLLAGLVGAYILR 218
Cdd:cd04206  85 SFTYRFTVDDQAGTFWYHSHVGG----QRADGLYGPLIVE 120
CuRO_3_MCO_like_5 cd13911
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 433-574 2.39e-12

The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259978 [Multi-domain]  Cd Length: 119  Bit Score: 64.10  E-value: 2.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 433 VNGLPYE-APVTETPKSGTTEVWEVinLTEDNHPLHIHLGLFKVVeqtallaagleefkecmtkqndavkcqiskyARGK 511
Cdd:cd13911  19 VNGKVFDpDHIAARPRLGTTEIWVF--SSDGRHPVHLHGAHFQVV-------------------------------SRTG 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30688168 512 KtAVTAHERGWKNVFKMMPGHVTRILVRFSyihtnaSYpfdptqEPGYVYHCHILDHEDNMMM 574
Cdd:cd13911  66 G-RPGEWDAGWKDTVLLRPRESVTVIIRFD------GY------RGRYVFHCHNLEHEDMGMM 115
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 429-577 2.14e-10

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


Pssm-ID: 259870 [Multi-domain]  Cd Length: 132  Bit Score: 58.63  E-value: 2.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 429 THLLVNGLPYEAPVTET----PKSGTTEVWEVINLTE--DNHPLHIHLGLFKVVEQTALLAAGleefkecmtkqndavkc 502
Cdd:cd04207  18 TRWVINGMPFKEGDANTdifsVEAGDVVEIVLINAGNhdMQHPFHLHGHSFWVLGSGGGPFDA----------------- 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30688168 503 qiskyargkktAVTAHERGWKNVFKMMPGHVTRILVRFsyihtnasypfdptQEPG-YVYHCHILDHEDNMMMRPL 577
Cdd:cd04207  81 -----------PLNLTNPPWRDTVLVPPGGWVVIRFKA--------------DNPGvWMLHCHILEHEDAGMMTVF 131
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 418-579 2.97e-10

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: 58.60  E-value: 2.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168   418 MYEYVSNSDEPTHLLVNGLPY-EAPVTETPKSGTTEVWEVINLTEDNHPLHIHLGLFKVVEQTallaaGLEEFKECMTKQ 496
Cdd:pfam07731   9 LLQITSGNFRRNDWAINGLLFpPNTNVITLPYGTVVEWVLQNTTTGVHPFHLHGHSFQVLGRG-----GGPWPEEDPKTY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168   497 NdavkcqiskyargkktavtAHERGWKNVFKMMPGHVTRILVRFSYihtnasypfdptqePG-YVYHCHILDHEDNMMMR 575
Cdd:pfam07731  84 N-------------------LVDPVRRDTVQVPPGGWVAIRFRADN--------------PGvWLFHCHILWHLDQGMMG 130


                  ....
gi 30688168   576 PLKV 579
Cdd:pfam07731 131 QFVV 134
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 236-347 6.68e-10

Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins; Laccase-like multicopper oxidases (MCOs) 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 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259868 [Multi-domain]  Cd Length: 152  Bit Score: 57.75  E-value: 6.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 236 RPLIIFDRSFRKDGSIYMNATGNNPSIHPQWqpeyfgDVIIVNGKAW--------------PRLNVRRRK-YRFRIINAS 300
Cdd:cd04205   1 RVLLLSDWYHDSAEDVLAGYMPNSFGNEPVP------DSLLINGRGRfncsmavcnsgcplPVITVEPGKtYRLRLINAG 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 30688168 301 NARFFKFFFsNGLDFIVVGSDsAYLSKPVMTKSILLSPSEIVDVVVD 347
Cdd:cd04205  75 SFASFNFAI-DGHNMTVIEVD-GGYVEPLEVDNLDLAPGQRYDVLVK 119
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 100-216 1.48e-08

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: 53.41  E-value: 1.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 100 VPGPTIETVYGVDTYVTWRNHLPKSHILPWDPtiSPATPkHGGIPTVVHLHGGIHEPTsdGNADAWFtagfRETGPKwtk 179
Cdd:cd13853  29 IPGPTLRVRPGDTLRITLKNDLPPEGAANEAP--APNTP-HCPNTTNLHFHGLHVSPT--GNSDNVF----LTIAPG--- 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 30688168 180 TTLHYE----NKQQPGNMWYHDHAMGLTRVNLLAGLVGAYI 216
Cdd:cd13853  97 ESFTYEydipADHPPGTYWYHPHLHGSTALQVAGGMAGALV 137
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
 284-372 1.53e-08

The second cupredoxin domain of the plant laccases; 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. Plants usually express multiple laccase genes, but their precise physiological/biochemical roles remain largely unclear. 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259943 [Multi-domain]  Cd Length: 148  Bit Score: 53.76  E-value: 1.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 284 RLNVRRRK-YRFRIINAsnARFFKFFFS-NGLDFIVVGSDSAYLsKPVMTKSILLSPSEIVDVVVDFYKSPSRTVVLANd 361
Cdd:cd13875  52 VLTVEPGKtYLLRIINA--ALNEELFFKiANHTLTVVAVDASYT-KPFTTDYILIAPGQTTDVLLTADQPPGRYYMAAR- 127

                        90
                ....*....|.
gi 30688168 362 apyPYPSGDPV 372
Cdd:cd13875 128 ---PYQSAPPV 135
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 273-348 3.04e-07

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


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 50.01  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168   273 DVIIVNGKAW---PRLNVRRRK-YRFRIINASNARFFKFFFSnGLDFIVVGSDSAYLsKPVMTKSILLSPSEIVDVVVDF 348
Cdd:pfam00394  37 DAVLINGKDGaslATLTVTPGKtYRLRIINVALDDSLNFSIE-GHKMTVVEVDGVYV-NPFTVDSLDIFPGQRYSVLVTA 114
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 84-218 4.83e-07

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 48.63  E-value: 4.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  84 PATPVFAYGTSrskatVPGPTIETVYGVDTYVTWRNHLPKshilpwdptispatpkhggiPTVVHLHGGIHEPTSDGNAD 163
Cdd:cd13855  19 KPTEFWAYNGS-----VPGPLIEVFEGDTVEITFRNRLPE--------------------PTTVHWHGLPVPPDQDGNPH 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30688168 164 AWFTAG----FRETGPkwtkttlhyenKQQPGNMWYHDHAMGLTRVNLLAGLVGAYILR 218
Cdd:cd13855  74 DPVAPGndrvYRFTLP-----------QDSAGTYWYHPHPHGHTAEQVYRGLAGAFVVK 121
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 99-218 7.05e-07

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 48.40  E-value: 7.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168    99 TVPGPTIETVYGVDTYVTWRNHLPKshilpwdptispatpkhggiPTVVHLHGgIHEPtsdGNADAWFTAG--FRETGPK 176
Cdd:pfam07732  23 QFPGPTIRVREGDTVVVNVTNNLDE--------------------PTSIHWHG-LQQR---GTPWMDGVPGvtQCPIPPG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 30688168   177 WTKTtLHYENKQQPGNMWYHDHAMGLTrvnlLAGLVGAYILR 218
Cdd:pfam07732  79 QSFT-YRFQVKQQAGTYWYHSHTSGQQ----AAGLAGAIIIE 115
CuRO_2_CumA_like cd13885
The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 235-367 3.59e-06

The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida. CumA is involved in the oxidation of Mn(II) in Pseudomonas putida; 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. MCOs catalyze 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. The MCOs in this subfamily are 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259952 [Multi-domain]  Cd Length: 132  Bit Score: 46.55  E-value: 3.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 235 DRPLIIFDRSFRKDGSiymnATGNNPSIHPQWQPEYFGDVIIVNGKAWPRLNVRR-RKYRFRIINASNARFFKFFFSnGL 313
Cdd:cd13885   2 DLVWVLDDWRLDPDGQ----AVPGFGTPHDAAHAGRIGNLYTINGRVQPDFTVRAgERVRLRLINAANARVFALKFP-GH 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30688168 314 DFIVVGSDSAYLSK-PVMTKSILLSPSEIVDVVVDFYKSP-SRTVVLANDAPYPYP 367
Cdd:cd13885  77 EARVIALDGQPAEPfVARNGAVVLAPGMRIDLVIDAPQAAgTRFAVLDHDGRRAAP 132
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
 235-347 4.32e-06

The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; This multicopper oxidase (MCO) subfamily includes the majority of insect laccases. One member is laccase 2 from Tribolium castaneum, which 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. 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259951 [Multi-domain]  Cd Length: 150  Bit Score: 46.84  E-value: 4.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 235 DRPLIIFDRsFRKDGSIYMNATGNNPSIHPQWqpeyfgdVIIVNGKA-WP-------------RLNVRR-RKYRFRIINA 299
Cdd:cd13884   1 EHVILIQDW-THELSSERFVGRGHNGGGQPPD-------SILINGKGrYYdpktgntnntpleVFTVEQgKRYRFRLINA 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 30688168 300 SNARF-FKFFFSNGlDFIVVGSDSAYLsKPVMTKSILLSPSEIVDVVVD 347
Cdd:cd13884  73 GATNCpFRVSIDGH-TLTVIASDGNDV-EPVEVDSIIIYPGERYDFVLN 119
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 89-218 1.31e-04

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: 42.25  E-value: 1.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  89 FAYGTSRSKATVPGPTIETVYGVDTYVTWRNHLPkshilpwdptispatpkhggIPTVVHLHGGIHEPTSDGNAD----- 163
Cdd:cd14449  16 WGYGLKGGVATVPGPVIEVREGDTLKILFRNTLD--------------------VPASLHPHGVDYTTASDGTGMnasiv 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30688168 164 --------AWFTAG-FRETGPKWTKTTlhyenkqqPGNMWYHDHAMGLTR--VNLLAGLVGAYILR 218
Cdd:cd14449  76 apgdtriyTWRTHGgYRRADGSWAEGT--------AGYWHYHDHVFGTEHgtEGLSRGLYGALIVR 133
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 254-346 2.75e-04

The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259945 [Multi-domain]  Cd Length: 148  Bit Score: 41.38  E-value: 2.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 254 NATGNNPSIhpqwqpeyfgDVIIVNGKAWPRLNVRR-RKYRFRIINASNarFFKFFFS-NGLDFIVVGSDSAYLsKPVMT 331
Cdd:cd13877  27 NPTGAEPIP----------DSSLFNDTQNATINFEPgKTYLLRIINMGA--FASQYFHiEGHDMTIIEVDGVYV-KPYPV 93

                        90
                ....*....|....*
gi 30688168 332 KSILLSPSEIVDVVV 346
Cdd:cd13877  94 DTLYIAVGQRYSVLV 108
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 83-198 7.48e-04

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: 39.77  E-value: 7.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  83 LPATPVFAYGTSRSKATVPGPTIETVYGVDTYVTWRNHLPKSHILPWDPTISPATPKHGGIPTVVhlhggiHEPTSDGNA 162
Cdd:cd13859  12 ITVVPGLDFKTFAFNGQVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSWKMDGVPGVT------QPAIEPGES 85

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 30688168 163 dawFTAGFRetgpkwtkttlhyenKQQPGNMWYHDH 198
Cdd:cd13859  86 ---FTYKFK---------------AERPGTLWYHCH 103
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 99-216 1.32e-03

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: 38.79  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  99 TVPGPTIETVYGVDTYVTWRNHLPKSHILpwdptispatpkhggiptvvHLHgGIHEPTSDGNadawftaGFRETGPKWT 178
Cdd:cd11024  29 TVPGPTLRATEGDLVRIHFINTGDHPHTI--------------------HFH-GIHDAAMDGT-------GLGPIMPGES 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 30688168 179 KTtlhYENKQQP-GNMWYHDHAMGLTRvNLLAGLVGAYI 216
Cdd:cd11024  81 FT---YEFVAEPaGTHLYHCHVQPLKE-HIAMGLYGAFI 115
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 102-218 1.62e-03

The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins; CueO is a multicopper oxidase (MCO) that 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. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. 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. FtsP does not contain any copper binding sites.


Pssm-ID: 259894 [Multi-domain]  Cd Length: 120  Bit Score: 38.71  E-value: 1.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 102 GPTIETVYGVDTYVTWRNHLPKShilpwdptispatpkhggipTVVHLHGGIHEPTSDGNADAWFTAGfretgpkwTKTT 181
Cdd:cd04232  31 GPTIRVKKGDTVRINVTNNLDEE--------------------TTVHWHGLHVPGEMDGGPHQPIAPG--------QTWS 82

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 30688168 182 LHYENKQQPGNMWYHDHAMGLTRVNLLAGLVGAYILR 218
Cdd:cd04232  83 PTFTIDQPAATLWYHPHTHGKTAEQVYRGLAGLFIIE 119
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 75-216 2.68e-03

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: 37.95  E-value: 2.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168  75 TKWKFhrdLPATPVFAYGTSRSkatVPGPTIETVYG--VDTYVTwrNHLPKshilpwdptispatpkhggiPTVVHLHGG 152
Cdd:cd13860  10 VKWEI---APGVKVEAWGYNGS---VPGPTIEVTEGdrVRILVT--NELPE--------------------PTTVHWHGL 61

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30688168 153 IHEPTSDGNADawFTAgfRETGPKWTKTtlhYENK-QQPGNMWYHDHAMGLTRVNLlaGLVGAYI 216
Cdd:cd13860  62 PVPNGMDGVPG--ITQ--PPIQPGETFT---YEFTaKQAGTYMYHSHVDEAKQEDM--GLYGAFI 117
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 273-346 3.66e-03

The second cupredoxin domain of the 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. Laccase is a multicopper oxidase (MCO) 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259949 [Multi-domain]  Cd Length: 159  Bit Score: 38.54  E-value: 3.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30688168 273 DVIIVNGK---------AWPRLNVRRRK-YRFRIINASNARFFKFFFsNGLDFIVVGSDSAYlSKPVMTKSILLSPSEIV 342
Cdd:cd13882  28 DSGTINGKgrfdggptsPLAVINVKRGKrYRFRVINISCIPSFTFSI-DGHNLTVIEADGVE-TKPLTVDSVQIYAGQRY 105


                ....
gi 30688168 343 DVVV 346
Cdd:cd13882 106 SVVV 109
 
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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