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Conserved domains on  [gi|544681177|ref|WP_021113257|]
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multicopper oxidase domain-containing protein [Glaesserella parasuis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10883 super family cl32600
FtsI repressor; Provisional
 1-467 3.35e-143

FtsI repressor; Provisional


The actual alignment was detected with superfamily member PRK10883:

Pssm-ID: 182808 [Multi-domain]  Cd Length: 471  Bit Score: 418.34  E-value: 3.35e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177   1 MKLSRRQFLQRSTLAGVATVTPTSLWA-KNRPSLTIPPMIEVGRGRPVRLDFRPAQTQFNKGKLVDVWGVNGRYLAPTVR 79
Cdd:PRK10883   1 MSLSRRQFIQASGIALCAGALPLRARAaGQQQPLPVPPLLESRRGQPLFLTLQRAHWSFTGGTKASVWGINGRYLGPTIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  80 VKSGDFVKLTYTNNLPQALSINIQGLQAPTEMIGSIHRAIDKNSSWSPILSVNQSACTAWYHADTMLNSAFQVYRGLVGL 159
Cdd:PRK10883  81 VWKGDDVKLIYSNRLTEPVSMTVSGLQVPGPLMGGPARMMSPNADWAPVLPIRQNAATCWYHANTPNRMAQHVYNGLAGM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 160 WIIEDNESRKASLPNKYGVNDIPLILQDQLINSDGIQVIDTQTNQ-FFGKRLFVNGQESPYFDVPRGWVRLRIANASLSR 238
Cdd:PRK10883 161 WLVEDEVSKSLPIPNHYGVDDFPVIIQDKRLDNFGTPEYNEPGSGgFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNAR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 239 HYDLRLDNGKPLYLIATGIGFLADMVEMEHISLAPSERIEVLVDLNEGDKVSLITGKKRDFFDEIGKLFKDNNELNDNVV 318
Cdd:PRK10883 241 RYQLQMSDGRPLHVIAGDQGFLPAPVSVKQLSLAPGERREILVDMSNGDEVSITAGEAAGIVDRLRGFFEPSSILVSTLV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 319 LEFRPEGLPSAlnVTPKLPPFNVEEFNLKITQERKINLRPQDRL--INHQRFDPKRIDFTVKKGTVERWYLTTTEEVGFT 396
Cdd:PRK10883 321 LTLRPTGLLPL--VTDNLPMRLLPDEIMEGSPIRSREISLGDDLpgINGALWDMNRIDVTAQQGTWERWTVRADMPQAFH 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544681177 397 LQGAKFMVETRNRQAVPHKQLAWRDCVWLEPTQEttLLVKFEHTASEQQPFTFGVSDLMLRDRGCMGQFVV 467
Cdd:PRK10883 399 IEGVMFLIRNVNGAMPFPEDRGWKDTVWVDGQVE--LLVYFGQPSWAHFPFLFYSQTLEMADRGSIGQLLV 467
 
Name Accession Description Interval E-value
PRK10883 PRK10883
FtsI repressor; Provisional
 1-467 3.35e-143

FtsI repressor; Provisional


Pssm-ID: 182808 [Multi-domain]  Cd Length: 471  Bit Score: 418.34  E-value: 3.35e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177   1 MKLSRRQFLQRSTLAGVATVTPTSLWA-KNRPSLTIPPMIEVGRGRPVRLDFRPAQTQFNKGKLVDVWGVNGRYLAPTVR 79
Cdd:PRK10883   1 MSLSRRQFIQASGIALCAGALPLRARAaGQQQPLPVPPLLESRRGQPLFLTLQRAHWSFTGGTKASVWGINGRYLGPTIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  80 VKSGDFVKLTYTNNLPQALSINIQGLQAPTEMIGSIHRAIDKNSSWSPILSVNQSACTAWYHADTMLNSAFQVYRGLVGL 159
Cdd:PRK10883  81 VWKGDDVKLIYSNRLTEPVSMTVSGLQVPGPLMGGPARMMSPNADWAPVLPIRQNAATCWYHANTPNRMAQHVYNGLAGM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 160 WIIEDNESRKASLPNKYGVNDIPLILQDQLINSDGIQVIDTQTNQ-FFGKRLFVNGQESPYFDVPRGWVRLRIANASLSR 238
Cdd:PRK10883 161 WLVEDEVSKSLPIPNHYGVDDFPVIIQDKRLDNFGTPEYNEPGSGgFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNAR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 239 HYDLRLDNGKPLYLIATGIGFLADMVEMEHISLAPSERIEVLVDLNEGDKVSLITGKKRDFFDEIGKLFKDNNELNDNVV 318
Cdd:PRK10883 241 RYQLQMSDGRPLHVIAGDQGFLPAPVSVKQLSLAPGERREILVDMSNGDEVSITAGEAAGIVDRLRGFFEPSSILVSTLV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 319 LEFRPEGLPSAlnVTPKLPPFNVEEFNLKITQERKINLRPQDRL--INHQRFDPKRIDFTVKKGTVERWYLTTTEEVGFT 396
Cdd:PRK10883 321 LTLRPTGLLPL--VTDNLPMRLLPDEIMEGSPIRSREISLGDDLpgINGALWDMNRIDVTAQQGTWERWTVRADMPQAFH 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544681177 397 LQGAKFMVETRNRQAVPHKQLAWRDCVWLEPTQEttLLVKFEHTASEQQPFTFGVSDLMLRDRGCMGQFVV 467
Cdd:PRK10883 399 IEGVMFLIRNVNGAMPFPEDRGWKDTVWVDGQVE--LLVYFGQPSWAHFPFLFYSQTLEMADRGSIGQLLV 467
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 32-469 2.94e-127

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: 375.81  E-value: 2.94e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  32 SLTIPPMIEVGRGRPVRLDFRPAQTQFNKGKLVDVWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLQAPTEM 111
Cdd:COG2132    1 PLPIPPLLESGGGREYELTAQPATVELLPGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 112 IGSIHRAIDKNSSWSPILSVNQSACTAWYHADTMLNSAFQVYRGLVGLWIIEDNESRkasLPNkyGVNDIPLILQDQLIN 191
Cdd:COG2132   81 DGVPGDPIAPGETFTYEFPVPQPAGTYWYHPHTHGSTAEQVYRGLAGALIVEDPEED---LPR--YDRDIPLVLQDWRLD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 192 SDG--IQVIDTQTNQFFGKRLFVNGQESPYFDVPRG-WVRLRIANASLSRHYDLRLDNGKPLYLIATGIGFLADMVEMEH 268
Cdd:COG2132  156 DDGqlLYPMDAAMGGRLGDTLLVNGRPNPTLEVRPGeRVRLRLLNASNARIYRLALSDGRPFTVIATDGGLLPAPVEVDE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 269 ISLAPSERIEVLVDLN--EGDKVSLITgkkrDFFDEigklfkdnnelNDNVVLEFRPEGLPSALNVTPKLPPFNVEEfNL 346
Cdd:COG2132  236 LLLAPGERADVLVDFSadPGEEVTLAN----PFEGR-----------SGRALLTLRVTGAAASAPLPANLAPLPDLE-DR 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 347 KITQERKINLRPQDR----LINHQRFDPKRIDFTVKKGTVERWYLT--TTEEVGFTLQGAKFMVETRNRQAVPHkqLAWR 420
Cdd:COG2132  300 EAVRTRELVLTGGMAgyvwTINGKAFDPDRPDLTVKLGERERWTLVndTMMPHPFHLHGHQFQVLSRNGKPPPE--GGWK 377

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 544681177 421 DCVWLEPTQETTLLVKFEHTAseqQPFTFGVSDLMLRDRGCMGQFVVAE 469
Cdd:COG2132  378 DTVLVPPGETVRILFRFDNYP---GDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_2_CueO_FtsP cd13867
The second Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 179-324 7.22e-60

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: 192.80  E-value: 7.22e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 179 NDIPLILQDQLINSDGIQV--IDTQTNQFFGKRLFVNGQESPYFDVPRGWVRLRIANASLSRHYDLRLDNGKPLYLIATG 256
Cdd:cd13867    1 DDIPLILQDRRFDEDGQLDyrMMDDMDGFLGDTLLVNGTINPYLDVPRGWVRLRLLNGSNARTYNLGFSDNRPFYQIASD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544681177 257 IGFLADMVEMEHISLAPSERIEVLVDLNEGDKVSLITGKKRDFFDEIGklFKDNNELNDNVVLEFRPE 324
Cdd:cd13867   81 GGLLPAPVELKRLLLAPGERAEILVDFSDGEPVSLRSGPDEGGLGMIG--FGDSGEDDDFDLLTLRVG 146
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 52-167 2.39e-27

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: 105.79  E-value: 2.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177   52 RPAQTQFNKGKLVDVWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLQAPTEMI-----GSIHRAIDKNSSWS 126
Cdd:pfam07732   3 TYGTVSPLGGTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWmdgvpGVTQCPIPPGQSFT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 544681177  127 PILSVNQSACTAWYHADTMlnsaFQVYRGLVGLWIIEDNES 167
Cdd:pfam07732  83 YRFQVKQQAGTYWYHSHTS----GQQAAGLAGAIIIEDRAS 119
 
Name Accession Description Interval E-value
PRK10883 PRK10883
FtsI repressor; Provisional
 1-467 3.35e-143

FtsI repressor; Provisional


Pssm-ID: 182808 [Multi-domain]  Cd Length: 471  Bit Score: 418.34  E-value: 3.35e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177   1 MKLSRRQFLQRSTLAGVATVTPTSLWA-KNRPSLTIPPMIEVGRGRPVRLDFRPAQTQFNKGKLVDVWGVNGRYLAPTVR 79
Cdd:PRK10883   1 MSLSRRQFIQASGIALCAGALPLRARAaGQQQPLPVPPLLESRRGQPLFLTLQRAHWSFTGGTKASVWGINGRYLGPTIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  80 VKSGDFVKLTYTNNLPQALSINIQGLQAPTEMIGSIHRAIDKNSSWSPILSVNQSACTAWYHADTMLNSAFQVYRGLVGL 159
Cdd:PRK10883  81 VWKGDDVKLIYSNRLTEPVSMTVSGLQVPGPLMGGPARMMSPNADWAPVLPIRQNAATCWYHANTPNRMAQHVYNGLAGM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 160 WIIEDNESRKASLPNKYGVNDIPLILQDQLINSDGIQVIDTQTNQ-FFGKRLFVNGQESPYFDVPRGWVRLRIANASLSR 238
Cdd:PRK10883 161 WLVEDEVSKSLPIPNHYGVDDFPVIIQDKRLDNFGTPEYNEPGSGgFVGDTLLVNGVQSPYVEVSRGWVRLRLLNASNAR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 239 HYDLRLDNGKPLYLIATGIGFLADMVEMEHISLAPSERIEVLVDLNEGDKVSLITGKKRDFFDEIGKLFKDNNELNDNVV 318
Cdd:PRK10883 241 RYQLQMSDGRPLHVIAGDQGFLPAPVSVKQLSLAPGERREILVDMSNGDEVSITAGEAAGIVDRLRGFFEPSSILVSTLV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 319 LEFRPEGLPSAlnVTPKLPPFNVEEFNLKITQERKINLRPQDRL--INHQRFDPKRIDFTVKKGTVERWYLTTTEEVGFT 396
Cdd:PRK10883 321 LTLRPTGLLPL--VTDNLPMRLLPDEIMEGSPIRSREISLGDDLpgINGALWDMNRIDVTAQQGTWERWTVRADMPQAFH 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544681177 397 LQGAKFMVETRNRQAVPHKQLAWRDCVWLEPTQEttLLVKFEHTASEQQPFTFGVSDLMLRDRGCMGQFVV 467
Cdd:PRK10883 399 IEGVMFLIRNVNGAMPFPEDRGWKDTVWVDGQVE--LLVYFGQPSWAHFPFLFYSQTLEMADRGSIGQLLV 467
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 32-469 2.94e-127

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: 375.81  E-value: 2.94e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  32 SLTIPPMIEVGRGRPVRLDFRPAQTQFNKGKLVDVWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLQAPTEM 111
Cdd:COG2132    1 PLPIPPLLESGGGREYELTAQPATVELLPGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 112 IGSIHRAIDKNSSWSPILSVNQSACTAWYHADTMLNSAFQVYRGLVGLWIIEDNESRkasLPNkyGVNDIPLILQDQLIN 191
Cdd:COG2132   81 DGVPGDPIAPGETFTYEFPVPQPAGTYWYHPHTHGSTAEQVYRGLAGALIVEDPEED---LPR--YDRDIPLVLQDWRLD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 192 SDG--IQVIDTQTNQFFGKRLFVNGQESPYFDVPRG-WVRLRIANASLSRHYDLRLDNGKPLYLIATGIGFLADMVEMEH 268
Cdd:COG2132  156 DDGqlLYPMDAAMGGRLGDTLLVNGRPNPTLEVRPGeRVRLRLLNASNARIYRLALSDGRPFTVIATDGGLLPAPVEVDE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 269 ISLAPSERIEVLVDLN--EGDKVSLITgkkrDFFDEigklfkdnnelNDNVVLEFRPEGLPSALNVTPKLPPFNVEEfNL 346
Cdd:COG2132  236 LLLAPGERADVLVDFSadPGEEVTLAN----PFEGR-----------SGRALLTLRVTGAAASAPLPANLAPLPDLE-DR 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 347 KITQERKINLRPQDR----LINHQRFDPKRIDFTVKKGTVERWYLT--TTEEVGFTLQGAKFMVETRNRQAVPHkqLAWR 420
Cdd:COG2132  300 EAVRTRELVLTGGMAgyvwTINGKAFDPDRPDLTVKLGERERWTLVndTMMPHPFHLHGHQFQVLSRNGKPPPE--GGWK 377

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 544681177 421 DCVWLEPTQETTLLVKFEHTAseqQPFTFGVSDLMLRDRGCMGQFVVAE 469
Cdd:COG2132  378 DTVLVPPGETVRILFRFDNYP---GDWMFHCHILEHEDAGMMGQFEVVP 423
PRK10965 PRK10965
multicopper oxidase; Provisional
 3-468 5.34e-92

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 288.85  E-value: 5.34e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177   3 LSRRQFLQRSTLAGVATVTPT---SLWAKNRPSLTIPPMIEV-GRGRpVRLDFRPAQTQFNKGKLVDVWGVNGRYLAPTV 78
Cdd:PRK10965   1 MQRRDFLKLSAALGAASALPLwsrAAFAAERPALPIPPLLTPdARGR-IQLTIQAGQSSFAGKTATATWGYNGNLLGPAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  79 RVKSGDFVKLTYTNNLPQALSINIQGLQAPTEMIGSIHRAIDKNSSWSPILSVNQSACTAWYHADTMLNSAFQVYRGLVG 158
Cdd:PRK10965  80 RLQRGKAVTVDITNQLPEETTLHWHGLEVPGEVDGGPQGIIAPGGKRTVTFTVDQPAATCWFHPHQHGKTGRQVAMGLAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 159 LWIIEDNESRKASLPNKYGVNDIPLILQDQLINSDGiqVIDTQTN------QFFGKRLFVNGQESPYFDVPRGWVRLRIA 232
Cdd:PRK10965 160 LVLIEDDESLKLGLPKQWGVDDIPVILQDKRFSADG--QIDYQLDvmtaavGWFGDTLLTNGAIYPQHAAPRGWLRLRLL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 233 NASLSRHYDLRLDNGKPLYLIATGIGFLADMVEMEHISLAPSERIEVLVDLNEGDKVSLITGKKRDFFDEIGKLFKDNNE 312
Cdd:PRK10965 238 NGCNARSLNLATSDGRPLYVIASDGGLLAEPVKVSELPILMGERFEVLVDTSDGKAFDLVTLPVSQMGMALAPFDKPLPV 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 313 LNDNVVLEFRPEGLPSALNVTPKLPPFnveefnLKITQeRKINLRPQDRL------------------------------ 362
Cdd:PRK10965 318 LRIQPLLISASGTLPDSLASLPALPSL------EGLTV-RRLQLSMDPRLdmmgmqmlmekygdqamagmdmdhmmghmg 390

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 363 -------------------------INHQRFDPKRIDFTVKKGTVERWYLTTTEEV---GFTLQGAKFMVETRNRQAVPH 414
Cdd:PRK10965 391 hgnmdhmnhgaadagpafdfhhankINGKAFDMNKPMFAAKKGQYERWVISGVGDMmlhPFHIHGTQFRILSENGKPPAA 470

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 544681177 415 KQLAWRDCVWLEpTQETTLLVKFEHTASEQQPFTFGVSDLMLRDRGCMGQFVVA 468
Cdd:PRK10965 471 HRAGWKDTVRVE-GGRSEVLVKFDHDAPKEHAYMAHCHLLEHEDTGMMLGFTVS 523
CuRO_2_CueO_FtsP cd13867
The second Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 179-324 7.22e-60

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: 192.80  E-value: 7.22e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 179 NDIPLILQDQLINSDGIQV--IDTQTNQFFGKRLFVNGQESPYFDVPRGWVRLRIANASLSRHYDLRLDNGKPLYLIATG 256
Cdd:cd13867    1 DDIPLILQDRRFDEDGQLDyrMMDDMDGFLGDTLLVNGTINPYLDVPRGWVRLRLLNGSNARTYNLGFSDNRPFYQIASD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544681177 257 IGFLADMVEMEHISLAPSERIEVLVDLNEGDKVSLITGKKRDFFDEIGklFKDNNELNDNVVLEFRPE 324
Cdd:cd13867   81 GGLLPAPVELKRLLLAPGERAEILVDFSDGEPVSLRSGPDEGGLGMIG--FGDSGEDDDFDLLTLRVG 146
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 45-164 3.13e-58

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: 187.78  E-value: 3.13e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  45 RPVRLDFRPAQTQFNKGKLVDVWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLQAPTEMIGSIHRAIDKNSS 124
Cdd:cd04232    1 KPFTLTAQKGETEFLPGKKTATWGYNGSYLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDGGPHQPIAPGQT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 544681177 125 WSPILSVNQSACTAWYHADTMLNSAFQVYRGLVGLWIIED 164
Cdd:cd04232   81 WSPTFTIDQPAATLWYHPHTHGKTAEQVYRGLAGLFIIED 120
CuRO_3_CueO_FtsP cd13890
The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 348-467 2.06e-50

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: 167.43  E-value: 2.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 348 ITQERKINL--RPQDRLINHQRFDPKRIDFTVKKGTVERWYLTTT--EEVGFTLQGAKFMVETRNRQAVPHKQLAWRDCV 423
Cdd:cd13890    1 PTQERTFTLsgDPHAFTINGKRFDMNRIDFTVKLGTTEIWEVTNTdgMPHPFHIHGVQFRILSRNGQPPPPNEAGWKDTV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 544681177 424 WLEPTQETTLLVKFEHTASEQQPFTFGVSDLMLRDRGCMGQFVV 467
Cdd:cd13890   81 WVPPGETVRILVKFDHYADPTGPFMYHCHILEHEDNGMMGQFVV 124
CuRO_2_BOD_CotA_like cd14448
Cupredoxin domain 2 of Bilirubin oxidase (BOD), the bacterial endospore coat component CotA, ...
 180-323 2.41e-33

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: 122.80  E-value: 2.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 180 DIPLILQDQLINSDG------IQVIDTQTNQFFGKRLFVNGQESPYFDVPRGWVRLRIANASLSRHYDLRLDNGKPLYLI 253
Cdd:cd14448    1 DLPLVITDRQFNADGtlyypsPPTNMEWVPGFFGDVILVNGKIWPYLEVEPGWYRLRLLNASNARHYNLALSDGLPFHVI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544681177 254 ATGIGFLADMVEMEHISLAPSERIEVLVDLN--EGDKVSLITGKkrdfFDEIGKLfkdnNELNDNVVLEFRP 323
Cdd:cd14448   81 GSDGGLLEAPVKVKELVLAPAERIDVVVDFSqyAGEEVELVNLG----GASMAIL----PTDYDTDVMQFRV 144
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 52-167 2.39e-27

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: 105.79  E-value: 2.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177   52 RPAQTQFNKGKLVDVWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLQAPTEMI-----GSIHRAIDKNSSWS 126
Cdd:pfam07732   3 TYGTVSPLGGTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWmdgvpGVTQCPIPPGQSFT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 544681177  127 PILSVNQSACTAWYHADTMlnsaFQVYRGLVGLWIIEDNES 167
Cdd:pfam07732  83 YRFQVKQQAGTYWYHSHTS----GQQAAGLAGAIIIEDRAS 119
CuRO_2_McoP_like cd13879
The second cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 180-293 1.42e-23

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: 96.58  E-value: 1.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 180 DIPLILQDQLINSDGIQVIDTQTNQ----FFGKRLFVNGQESPYFDVPRGWVRLRIANASLSRHYDLRLDNGKPLYLIAT 255
Cdd:cd13879    2 DLPLVIQDRRFDANNQLVYLPNGMDrmmgFLGDRILVNGTPDPTLSVATRAYRLRLLNGSNARIYKLAWSDGSPLTVIGT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 544681177 256 GIGFLADMVEMEHISLAPSERIEVLVDLN---EGDKVSLIT 293
Cdd:cd13879   82 DGGLLEAPKTVPYVMLAPGERVDLWVDFSgrpVGTELKLKS 122
CuRO_2_BOD cd13866
The second cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the ...
 180-322 2.20e-21

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: 90.39  E-value: 2.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 180 DIPLILQDQLINSDGIQVIDTQ-TNQFFGKRLFVNGQESPYFDVPRGWVRLRIANASLSRHYDLRLDNG-----KPLYLI 253
Cdd:cd13866    5 DIPLVLADKQFDPNGQLMFDEFnLDGLLGDVILVNGVPWPFLNVEPRKYRFRLLNASVSRFFQLALVDGdnptrIPFTVI 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544681177 254 ATGIGFLADMVEMEHISLAPSERIEVLVD---LNEGDKVSLITGkkRDFFDEIGKLFKDNNElndNVVLEFR 322
Cdd:cd13866   85 ASDGGLLSHPVETTLLRLGMAERYDIVVDfskYAAGTRLYLVNR--LEHDDGRGPDNDYPAT---DKVMRFR 151
CuRO_2_CotA_like cd13868
The second Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat ...
 180-322 2.28e-20

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: 87.69  E-value: 2.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 180 DIPLILQDQLINSDGIQVIDTQTN----------QFFGKRLFVNGQESPYFDV-PRGWvRLRIANASLSRHYDLRLDNGK 248
Cdd:cd13868    2 EIPLLIQDRSFNADGSLFYPATGAnpsphpswvpEFFGDTIVVNGKAWPYLEVePRRY-RFRILNGSNARFYNLSLSNGD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544681177 249 --PLYLIATGIGFLADMVEMEHISLAPSERIEVLVDLN--EGDKVSLITGKKRDFFDEigklfKDNNELNDNVVLEFR 322
Cdd:cd13868   81 glPFWQIGTDGGFLPKPVPLDSLLIGPAERADVIVDFSdyAGQTLILKNDAPAPYPGG-----GAADPDTTGQVMQFR 153
CuRO_2_McoC_like cd13881
The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 183-285 1.26e-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: 82.27  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 183 LILQDQLINSDGIQVIDTQTNQFFGKR---LFVNGQESPYFDVPRG-WVRLRIANASLSRHYDLRLDnGKPLYLIATGIG 258
Cdd:cd13881    4 LVLSDLTLDGDGQLAEPSAADWMFGREgdlVLVNGQLNPTITVRPGeVQRWRIVNAASARYFRLALD-GHKFRLIGTDGG 82

                         90       100
                 ....*....|....*....|....*..
gi 544681177 259 FLADMVEMEHISLAPSERIEVLVDLNE 285
Cdd:cd13881   83 LLEAPREVDELLLAPGERAEVLVTAGE 109
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 71-164 1.44e-15

The first 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 the electron acceptor than when using dioxygen, the typical oxidizing substrate of MCOs. 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 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: 259921 [Multi-domain]  Cd Length: 114  Bit Score: 72.71  E-value: 1.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  71 GRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLQAPTEMIGSIHRAIDKNSSWSPILSVNQSACTAWYHADTMLNSAF 150
Cdd:cd13852   20 DSYLGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDGHPRYAIDPGETYVYEFEVLNRAGTYWYHPHPHGLTAK 99

                         90
                 ....*....|....
gi 544681177 151 QVYRGLVGLWIIED 164
Cdd:cd13852  100 QVYRGLAGLFLVTD 113
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 53-163 2.22e-15

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: 72.23  E-value: 2.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  53 PAQTQFNKGKLVDVWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLQAPTEM--IGSI-HRAIDKNSSWSPIL 129
Cdd:cd13860    9 PVKWEIAPGVKVEAWGYNGSVPGPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMdgVPGItQPPIQPGETFTYEF 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 544681177 130 SVNQSAcTAWYHADTmlNSAFQVYRGLVGLWIIE 163
Cdd:cd13860   89 TAKQAG-TYMYHSHV--DEAKQEDMGLYGAFIVH 119
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 49-162 5.35e-13

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: 65.57  E-value: 5.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  49 LDFRPAQTQFNKGKLVDVWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLQAPTEMIGSIHRAI----DKNSS 124
Cdd:cd13855    6 LTAAEVRIRLLPGKPTEFWAYNGSVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDGNPHDPVapgnDRVYR 85

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 544681177 125 WS-PilsvNQSACTAWYHADTMLNSAFQVYRGLVGLWII 162
Cdd:cd13855   86 FTlP----QDSAGTYWYHPHPHGHTAEQVYRGLAGAFVV 120
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 362-467 6.39e-12

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: 62.42  E-value: 6.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 362 LINHQRFDPKRIDFTVKKGTVERWYLTTTEEVG--FTLQGAKFMVETRNRQAVPHKQLAWRDCVWLEPTQETTLLVKFEH 439
Cdd:cd13902   22 LINGKTFDMNRIDFVAKVGEVEVWEVTNTSHMDhpFHLHGTQFQVLEIDGNPQKPEYRAWKDTVNLPPGEAVRIATRQDD 101

                         90       100
                 ....*....|....*....|....*...
gi 544681177 440 TAseqqPFTFGVSDLMLRDRGCMGQFVV 467
Cdd:cd13902  102 PG----MWMYHCHILEHEDAGMMGMLHV 125
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 60-163 1.36e-11

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: 61.53  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  60 KGKLVDVWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQA-LSINIQGLQAP-----TEMIGSIHRAIDKNSSWSPILSVNQ 133
Cdd:cd04206   15 DGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNLPNEpTSIHWHGLRQPgtndgDGVAGLTQCPIPPGESFTYRFTVDD 94

                         90       100       110
                 ....*....|....*....|....*....|
gi 544681177 134 SACTAWYHADTMlnsaFQVYRGLVGLWIIE 163
Cdd:cd04206   95 QAGTFWYHSHVG----GQRADGLYGPLIVE 120
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 45-163 3.45e-11

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: 60.33  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  45 RPVRLDFRPAQTQFNKGKLVDVWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLQAPTEMIGSIH---RAIDK 121
Cdd:cd13861    1 VEYTLTAAPAELLDLGGPTTRTWGYNGQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPGltqPPVPP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 544681177 122 NSSWSPILSVnQSACTAWYHADtmLNSAFQVYRGLVGLWIIE 163
Cdd:cd13861   81 GESFTYEFTP-PDAGTYWYHPH--VGSQEQLDRGLYGPLIVE 119
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 363-438 4.14e-10

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: 57.26  E-value: 4.14e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544681177 363 INHQRFDPKRIDFTVKKGTVERWYLTTTEEVG--FTLQGAKFMVETRNRQAVPhkQLAWRDCVWLEPTQETTLLVKFE 438
Cdd:cd13900   22 INGKPFDPDRPDRTVRLGTVEEWTLINTSGEDhpFHIHVNPFQVVSINGKPGL--PPVWRDTVNVPAGGSVTIRTRFR 97
CuRO_3_MCO_like_5 cd13911
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 363-465 4.64e-10

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: 57.17  E-value: 4.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 363 INHQRFDPKRIDFTVKKGTVERWYLTTTEEVGFTLQGAKFMVETRNRQAVPHKQLAWRDCVWLEPTQETTLLVKFEhtaS 442
Cdd:cd13911   19 VNGKVFDPDHIAARPRLGTTEIWVFSSDGRHPVHLHGAHFQVVSRTGGRPGEWDAGWKDTVLLRPRESVTVIIRFD---G 95

                         90       100
                 ....*....|....*....|...
gi 544681177 443 EQQPFTFGVSDLMLRDRGCMGQF 465
Cdd:cd13911   96 YRGRYVFHCHNLEHEDMGMMANF 118
CuRO_2_PHS cd13869
The second Cupredoxin domain of phenoxazinone synthase (PHS); Phenoxazinone synthase (PHS, ...
 205-322 4.81e-10

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: 58.35  E-value: 4.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 205 FFGKRLFVNGQESPYFDVPRGWVRLRIANASLSRHYDLRL---DNGKP----LYLIATGIGFLAD--MVEMEHISLAPSE 275
Cdd:cd13869   45 FTGPYTLVNGVIWPYLEVRPGWYRLRLLNASNARIYRLALldeTDEHPvpgaLVVIGTDAGLLPRpvPVPGGAVNLGPGE 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 544681177 276 RIEVLVDLnegdkvSLITGKKRDFFDEIGKLFKDNNELNDNVVLEFR 322
Cdd:cd13869  125 RADVLVDF------AALRGRRLRLVNESPGALNGQPGQTDPDVMQFR 165
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 47-163 6.44e-10

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: 57.26  E-value: 6.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  47 VRLDFRPAQTQFNKGKLVdVWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLQA------------------P 108
Cdd:cd13853    4 VTLTVEYGRVTLAGLPVT-LRTYNGSIPGPTLRVRPGDTLRITLKNDLPPEGAANEAPAPNtphcpnttnlhfhglhvsP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 544681177 109 TEMIGSIHRAIDKNSSWSPI--LSVNQSACTAWYHADTMLNSAFQVYRGLVGLWIIE 163
Cdd:cd13853   83 TGNSDNVFLTIAPGESFTYEydIPADHPPGTYWYHPHLHGSTALQVAGGMAGALVVE 139
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 212-293 2.75e-09

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: 55.83  E-value: 2.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 212 VNGQESPYFDVPRG-WVRLRIANASLSRHYDLRLDNGkPLYLIATGiGFLADMVEMEHISLAPSERIEVLVDLNEGDKVS 290
Cdd:cd04205   50 NSGCPLPVITVEPGkTYRLRLINAGSFASFNFAIDGH-NMTVIEVD-GGYVEPLEVDNLDLAPGQRYDVLVKADQPPGNY 127


                 ...
gi 544681177 291 LIT 293
Cdd:cd04205  128 WIR 130
CuRO_1_BOD_CotA_like cd13844
The first Cupredoxin domain of Bilirubin oxidase (BOD), the bacterial endospore coat component ...
 44-166 2.17e-08

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: 53.45  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  44 GRPVRLDFRPAQTQFNKGKL-VDVWG----VNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLQAPTEMIG----- 113
Cdd:cd13844    1 GDYYEIEMREFTQQLHPDLPpTTVWGyggsNSTSYPGPTIEARRGVPVRVTWVNNLPDKHHLPLDDTLPSTEEATpgaep 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 114 -------SIH-------------------RAIDKNSSWSPILSV---NQSACTAWYHADTMLNSAFQVYRGLVGLWIIED 164
Cdd:cd13844   81 pvppvptVVHlhggevppesdgypeawftPGGEEGPGFGSATYYypnDQSAATLWYHDHALGITRLNVYAGLAGFYLIRD 160


                 ..
gi 544681177 165 NE 166
Cdd:cd13844  161 EA 162
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 61-163 3.11e-07

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: 48.82  E-value: 3.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  61 GKLVDVWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLQAPTEMIGS---IHRAIDKNSSWSPILSVNQSAcT 137
Cdd:cd13848   16 GKEGEAITVNGQVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPNDMDGVpglSFPGIKPGETFTYRFPVRQSG-T 94

                         90       100
                 ....*....|....*....|....*.
gi 544681177 138 AWYHADTMLnsafQVYRGLVGLWIIE 163
Cdd:cd13848   95 YWYHSHSGL----QEQTGLYGPIIID 116
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 53-163 1.49e-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. 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: 46.88  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  53 PAQTQFNKGKLVDVWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGlqaptemigsIHRAIDKNSSWSPILS-- 130
Cdd:cd11024   10 DAEIEIAPGVVFKAWTYNGTVPGPTLRATEGDLVRIHFINTGDHPHTIHFHG----------IHDAAMDGTGLGPIMPge 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 544681177 131 ------VNQSACTAWYHADTMLNSAfQVYRGLVGLWIIE 163
Cdd:cd11024   80 sftyefVAEPAGTHLYHCHVQPLKE-HIAMGLYGAFIVD 117
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 331-469 1.46e-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: 44.73  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  331 NVTPKLPPfnveefNLKITQerkINLRPQDRLINHQRFDPKRIDFTVKKGTVERWYLTTTEEVG--FTLQGAKFMVETRN 408
Cdd:pfam07731   1 DTPPKLPT------LLQITS---GNFRRNDWAINGLLFPPNTNVITLPYGTVVEWVLQNTTTGVhpFHLHGHSFQVLGRG 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544681177  409 RQAVPHKQLA--------WRDCVWLEPTQETTLLVKFEHTaseqqpftfGVsdLMLR-------DRGCMGQFVVAE 469
Cdd:pfam07731  72 GGPWPEEDPKtynlvdpvRRDTVQVPPGGWVAIRFRADNP---------GV--WLFHchilwhlDQGMMGQFVVRP 136
CuRO_3_BOD cd13889
The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the ...
 363-467 2.83e-05

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: 43.46  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 363 INHQRF-DPKRIDFTVKKGTVERWYLtTTEEVGFT------LQGAKFMVETRNRQAVPHKQLAWRDCVWLEPTQETTLLV 435
Cdd:cd13889   17 INGKTWaDPNRIDAAPQLGTVEIWTL-INGGGGWShpihihLEDFQILSRNGGSRAVPPYERGRKDVVYLGPGEEVRVLM 95

                         90       100       110
                 ....*....|....*....|....*....|..
gi 544681177 436 KFehtASEQQPFTFGVSDLMLRDRGCMGQFVV 467
Cdd:cd13889   96 RF---RPFRGKYMMHCHNLVHEDHDMMLRFEV 124
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
 210-286 6.57e-05

The second cupredoxin domain of CopA copper resistance protein like family; The members of this family are copper resistance protein (CopA) homologs. CopA is multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. CopA 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259938 [Multi-domain]  Cd Length: 117  Bit Score: 42.32  E-value: 6.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 210 LFVNGQ---ESPYFDVPRG-WVRLRIANASLSRHYDLRLDnGKPLYLIATGiGFLADMVEMEHISLAPSERIEVLVDLNE 285
Cdd:cd13870   18 YLINGRppeDPAVFTARPGdRLRLRLINAAGDTAFRVALA-GHRLTVTHTD-GFPVEPVEVDALLIGMGERYDAIVTANN 95


                 .
gi 544681177 286 G 286
Cdd:cd13870   96 G 96
CuRO_2_CopA cd13874
The second cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 207-286 1.79e-04

The second 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 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 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259942 [Multi-domain]  Cd Length: 112  Bit Score: 40.74  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 207 GKRLFVNGQESPYFDVPRG----WVRLRIANASLSRHYDLRLDNGKPLYLIATGIgflaDM--VEMEHISLAPSERIEVL 280
Cdd:cd13874   11 YDTYLINGKPPEDNWTGLFkpgeRVRLRFINAAASTYFDVRIPGGKMTVVAADGQ----DVrpVEVDEFRIGVAETYDVI 86


                 ....*.
gi 544681177 281 VDLNEG 286
Cdd:cd13874   87 VTIPEN 92
CuRO_1_MCO_like_2 cd13864
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 76-163 5.73e-04

The second 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 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: 259932 [Multi-domain]  Cd Length: 139  Bit Score: 40.21  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  76 PTVRVKSGDFVKLTYTNNLP------------QALSINIQGL--QAPTEMIGSIH--------RAIDKNSSWSPILSVNQ 133
Cdd:cd13864   32 PTIRVKSGDTLNLLVTNHLCneqelskiwqdyCPTSIHFHGLvlENFGKQLANLVdgvpgltqYPIGVGESYWYNFTIPE 111

                         90       100       110
                 ....*....|....*....|....*....|.
gi 544681177 134 SAC-TAWYHAdtmlNSAFQVYRGLVGLWIIE 163
Cdd:cd13864  112 DTCgTFWYHS----HSSVQYGDGLRGVFIVD 138
CuRO_3_McoP_like cd13888
The third cupredoxin domain of multicopper oxidase McoP and similar proteins; This subfamily ...
 349-467 1.73e-03

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: 38.70  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177 349 TQERKINL--RPQDRLINHQRFDPKRIDFTVKK--GTVERWYLTTT------------------EEVGFTLQGAKFMVET 406
Cdd:cd13888    1 ATPRRIHLsmGRMQWTINGETWADDPDAFPVERvgGTVEIWELVNDaasmphpmhihgfqfqvlERSDSPPQVAELAVAP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544681177 407 RNRQAVphkQLAWRDCVWLEPTQETTLLVKFEHTASEQQPFTFGVSDLMLRDRGCMGQFVV 467
Cdd:cd13888   81 SGRTAT---DLGWKDTVLVWPGETVRIAVDFTHDYPGDQLYLLHCHNLEHEDDGMMVNVRV 138
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 66-162 2.04e-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: 38.02  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  66 VWGVNGRYLAPTVRVKSGDFVKLTYTNNLP-QALSINIQGL---------------QAPtemigsihraIDKNSSWSPIL 129
Cdd:cd13851   22 VIGINGQWPPPPIEVNKGDTVVIHATNSLGdQPTSLHFHGLfqngtnymdgpvgvtQCP----------IPPGQSFTYEF 91

                         90       100       110
                 ....*....|....*....|....*....|...
gi 544681177 130 SVNQSACTAWYHADTMlnsaFQVYRGLVGLWII 162
Cdd:cd13851   92 TVDTQVGTYWYHSHDG----GQYPDGLRGPFII 120
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 69-162 2.16e-03

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: 38.01  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  69 VNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGL-QAPT-EMIGSIHR---AIDKNSSWSPILSVNQSACTAWYHAd 143
Cdd:cd13857   24 INGQFPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLfQNGTnWMDGTAGItqcPIPPGGSFTYNFTVDGQYGTYWYHS- 102

                         90
                 ....*....|....*....
gi 544681177 144 tmlNSAFQVYRGLVGLWII 162
Cdd:cd13857  103 ---HYSTQYADGLVGPLIV 118
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 66-160 2.28e-03

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: 37.84  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  66 VWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQG-LQAPT----EMIGSIHRAIDKNSSWSPILSVNQSAcTAWY 140
Cdd:cd13859   22 TFAFNGQVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGvLQMGSwkmdGVPGVTQPAIEPGESFTYKFKAERPG-TLWY 100

                         90       100
                 ....*....|....*....|
gi 544681177 141 HADTMLNSafqvYRGLVGLW 160
Cdd:cd13859  101 HCHVNVNE----HVGMRGMW 116
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 69-164 7.37e-03

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: 36.47  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  69 VNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLQAP-------TEMIgsIHRAIDKNSSWSPILSVNQSACTAWYH 141
Cdd:cd13849   22 VNGQFPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLrsgwadgPAYI--TQCPIQPGQSYTYRFTVTGQEGTLWWH 99

                         90       100
                 ....*....|....*....|....
gi 544681177 142 AdtmlNSAFQvyRGLV-GLWIIED 164
Cdd:cd13849  100 A----HISWL--RATVyGAFIIRP 117
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 59-142 8.21e-03

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: 36.12  E-value: 8.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544681177  59 NKGKLVDVWGVNGRYLAPTVRVKSGDFVKLTYTNNLPQALSINIQGLqaptEMIGSI---------HRAIDKNSSWSPIL 129
Cdd:cd13850   12 GDGGEREVILINGQFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGI----LQRGTPwsdgvpgvtQWPIQPGGSFTYRW 87

                         90
                 ....*....|...
gi 544681177 130 SVNQSACTAWYHA 142
Cdd:cd13850   88 KAEDQYGLYWYHS 100
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 66-95 8.94e-03

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: 36.27  E-value: 8.94e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 544681177  66 VWGVNGRYLAPTVRVKSGDFVKLTYTNNLP 95
Cdd:cd13845   21 VIGINGQFPGPTIRATAGDTIVVELENKLP 50
 
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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