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Conserved domains on  [gi|1179981522|ref|WP_083503876|]
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multicopper oxidase domain-containing protein [Legionella nautarum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
copper_res_A super family cl36914
copper-resistance protein, CopA family; This model represents the CopA copper resistance ...
 20-688 1.82e-133

copper-resistance protein, CopA family; This model represents the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is observed for a large number of periplasmic proteins that cross the inner membrane with metal-containing cofactors already bound. The combination of copper-binding sites and TAT translocation motif suggests a mechansism of resistance by packaging and export. [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds]


The actual alignment was detected with superfamily member TIGR01480:

Pssm-ID: 273649 [Multi-domain]  Cd Length: 587  Bit Score: 413.12  E-value: 1.82e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  20 VDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHVSQKAIPPGGV 99
Cdd:TIGR01480  48 FDLTIGETMVNFTGRARPAITVNGSIPGPLLRWREGDTVRLRVTNTLPEDTSIHWHGILLPFQMDGVPGVSFAGIAPGET 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 100 FHYRFVLKQSGTYWYHAHAELQEQQGLYGAFVIDPIKAPKYKYMKDFVVVLSDWSNTKPEQILKNLKKEGDYYSprfPLQ 179
Cdd:TIGR01480 128 FTYRFPVRQSGTYWYHSHSGFQEQAGLYGPLIIDPAEPDPVRADREHVVLLSDWTDLDPAALFRKLKVMAGHDN---YYK 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 180 PSLVKFMHDYKKGSAgerKQLFNDYKMMQQMRMSIYDFSDV--AYDAFLLNGQPKFKPWTALVKKGDVVRLRFIGAGGST 257
Cdd:TIGR01480 205 RTVADFFRDVRNDGL---KQTLADRKMWGQMRMTPTDLADVngSTYTYLMNGTTPAGNWTGLFRPGEKVRLRFINGSAMT 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 258 IFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVKIQKNRPYIIYAESLDTVGAAYGAL-VTSSQHVvdyqKV 336
Cdd:TIGR01480 282 YFDVRIPGLKLTVVAVDGQYVHPVSVDEFRIAPAETFDVIVEPTGDDAFTIFAQDSDRTGYARGTLaVRLGLTA----PV 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 337 PPF-PEPLPVSRDmmammmgqmnqgtlpqvikssikkkgvnhspkMKMSSMSHEMSHKKlhpmqkntlsSSMSNMKmdsn 415
Cdd:TIGR01480 358 PALdPRPLLTMKD--------------------------------MGMGGMHHGMDHSK----------MSMGGMP---- 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 416 mkmdsnmkmdsnmkmdsnmkmdsnmkmdsnmKMDSNMKMDSNMKMDSSMkmdssMKMDSNMKMDSNMKMDSNMKMDSNMK 495
Cdd:TIGR01480 392 -------------------------------GMDMSMRAQSNAPMDHSQ-----MAMDASPKHPASEPLNPLVDMIVDMP 435

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 496 MDsnmKMDsnmkmdsnmkmdsnmkmdsnmkmdsnmkmptEPTIIGDKMGPPTSSYkTSMGTKYQPMiaavktnDPNTPvA 575
Cdd:TIGR01480 436 MD---RMD-------------------------------DPGIGLRDNGRRVLTY-ADLHSLFPPP-------DGRAP-G 472

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 576 HVINMELFGYMDRFIWFINGVPAYKAHPIRLEPGKRYRFVFTNTSMMHHPMHIHGHWFILRKGNDAYDPLLHTIDVPPGA 655
Cdd:TIGR01480 473 REIELHLTGNMERFAWSFDGEAFGLKTPLRFNYGERLRVVLVNDTMMAHPIHLHGMWSELEDGQGEFQVRKHTVDVPPGG 552

                         650       660       670
                  ....*....|....*....|....*....|...
gi 1179981522 656 TITADVDTDASGQWFFHCHFLYHMMTGMSRVFQ 688
Cdd:TIGR01480 553 KRSFRVTADALGRWAYHCHMLLHMEAGMFREVT 585
CopB super family cl46790
Copper resistance protein B precursor (CopB); This family consists of several bacterial copper ...
 754-940 1.87e-34

Copper resistance protein B precursor (CopB); This family consists of several bacterial copper resistance proteins. Copper is essential and serves as cofactor for more than 30 enzymes yet a surplus of copper is toxic and leads to radical formation and oxidation of biomolecules. Therefore, copper homeostasis is a key requisite for every organizm. CopB serves to extrude copper when it approaches toxic levels.


The actual alignment was detected with superfamily member COG3667:

Pssm-ID: 481130  Cd Length: 268  Bit Score: 133.08  E-value: 1.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 754 HNAQRLNYKGLYGPDYNKLELFVNDAELLKGKVESADIDIFYWHLISQFWAIKAGANYTNKPANTPYWqPGIGIEGLMPY 833
Cdd:COG3667    78 GDALAWDGQAWYGGDYNRLWLKSEGEGSSGGRLEEAEVEALYSRAISPFWDLQAGVRYDFGPGPDRTW-AAFGVQGLAPY 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 834 FIDTNLRGYYYN-GSAKLDVELSRDTQITNNLFIRAGIRSILASKTVIQANIGNGLNQMRYIVRPYYRLIPGLNINVEYE 912
Cdd:COG3667   157 WFEVDATAYLSEdGDLAARLEAEYDLLLTQRLILQPRAELNLYAQDDPERGIGSGLSDVELGLRLRYEIRREFAPYVGVE 236

                         170       180
                  ....*....|....*....|....*...
gi 1179981522 913 HEQDYGAFKNIQISNGEAANQDTITFGL 940
Cdd:COG3667   237 WERKFGDTADLARAAGEDTSETRFVAGV 264
 
Name Accession Description Interval E-value
copper_res_A TIGR01480
copper-resistance protein, CopA family; This model represents the CopA copper resistance ...
 20-688 1.82e-133

copper-resistance protein, CopA family; This model represents the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is observed for a large number of periplasmic proteins that cross the inner membrane with metal-containing cofactors already bound. The combination of copper-binding sites and TAT translocation motif suggests a mechansism of resistance by packaging and export. [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273649 [Multi-domain]  Cd Length: 587  Bit Score: 413.12  E-value: 1.82e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  20 VDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHVSQKAIPPGGV 99
Cdd:TIGR01480  48 FDLTIGETMVNFTGRARPAITVNGSIPGPLLRWREGDTVRLRVTNTLPEDTSIHWHGILLPFQMDGVPGVSFAGIAPGET 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 100 FHYRFVLKQSGTYWYHAHAELQEQQGLYGAFVIDPIKAPKYKYMKDFVVVLSDWSNTKPEQILKNLKKEGDYYSprfPLQ 179
Cdd:TIGR01480 128 FTYRFPVRQSGTYWYHSHSGFQEQAGLYGPLIIDPAEPDPVRADREHVVLLSDWTDLDPAALFRKLKVMAGHDN---YYK 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 180 PSLVKFMHDYKKGSAgerKQLFNDYKMMQQMRMSIYDFSDV--AYDAFLLNGQPKFKPWTALVKKGDVVRLRFIGAGGST 257
Cdd:TIGR01480 205 RTVADFFRDVRNDGL---KQTLADRKMWGQMRMTPTDLADVngSTYTYLMNGTTPAGNWTGLFRPGEKVRLRFINGSAMT 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 258 IFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVKIQKNRPYIIYAESLDTVGAAYGAL-VTSSQHVvdyqKV 336
Cdd:TIGR01480 282 YFDVRIPGLKLTVVAVDGQYVHPVSVDEFRIAPAETFDVIVEPTGDDAFTIFAQDSDRTGYARGTLaVRLGLTA----PV 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 337 PPF-PEPLPVSRDmmammmgqmnqgtlpqvikssikkkgvnhspkMKMSSMSHEMSHKKlhpmqkntlsSSMSNMKmdsn 415
Cdd:TIGR01480 358 PALdPRPLLTMKD--------------------------------MGMGGMHHGMDHSK----------MSMGGMP---- 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 416 mkmdsnmkmdsnmkmdsnmkmdsnmkmdsnmKMDSNMKMDSNMKMDSSMkmdssMKMDSNMKMDSNMKMDSNMKMDSNMK 495
Cdd:TIGR01480 392 -------------------------------GMDMSMRAQSNAPMDHSQ-----MAMDASPKHPASEPLNPLVDMIVDMP 435

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 496 MDsnmKMDsnmkmdsnmkmdsnmkmdsnmkmdsnmkmptEPTIIGDKMGPPTSSYkTSMGTKYQPMiaavktnDPNTPvA 575
Cdd:TIGR01480 436 MD---RMD-------------------------------DPGIGLRDNGRRVLTY-ADLHSLFPPP-------DGRAP-G 472

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 576 HVINMELFGYMDRFIWFINGVPAYKAHPIRLEPGKRYRFVFTNTSMMHHPMHIHGHWFILRKGNDAYDPLLHTIDVPPGA 655
Cdd:TIGR01480 473 REIELHLTGNMERFAWSFDGEAFGLKTPLRFNYGERLRVVLVNDTMMAHPIHLHGMWSELEDGQGEFQVRKHTVDVPPGG 552

                         650       660       670
                  ....*....|....*....|....*....|...
gi 1179981522 656 TITADVDTDASGQWFFHCHFLYHMMTGMSRVFQ 688
Cdd:TIGR01480 553 KRSFRVTADALGRWAYHCHMLLHMEAGMFREVT 585
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 18-344 8.84e-64

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: 221.73  E-value: 8.84e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  18 RVVDLVVGYKTVSFA-GKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHvsqKAIPP 96
Cdd:COG2132    14 REYELTAQPATVELLpGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDGVPG---DPIAP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  97 GGVFHYRFVLKQ-SGTYWYHAHA----ELQEQQGLYGAFVIDPIKAPKYKYMKDFVVVLSDWSNTKPEQILknlkkegdy 171
Cdd:COG2132    91 GETFTYEFPVPQpAGTYWYHPHThgstAEQVYRGLAGALIVEDPEEDLPRYDRDIPLVLQDWRLDDDGQLL--------- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 172 ysprfplqpslvkfmhdykkgsagerkqlfndYKMMQQMRMSIYDFsdvaydaFLLNGQPkfkPWTALVKKGDVVRLRFI 251
Cdd:COG2132   162 --------------------------------YPMDAAMGGRLGDT-------LLVNGRP---NPTLEVRPGERVRLRLL 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 252 GAGGSTIFRVKIP-GSVMQMVHAQGNDVN-PYTIKDFAIASGETYDVLVKIQKN--RPYIIYAESLDTVGAAYGALVTSS 327
Cdd:COG2132   200 NASNARIYRLALSdGRPFTVIATDGGLLPaPVEVDELLLAPGERADVLVDFSADpgEEVTLANPFEGRSGRALLTLRVTG 279

                         330
                  ....*....|....*..
gi 1179981522 328 QhvvdyQKVPPFPEPLP 344
Cdd:COG2132   280 A-----AASAPLPANLA 291
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 18-133 7.74e-63

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: 207.90  E-value: 7.74e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  18 RVVDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHVSQKAIPPG 97
Cdd:cd13848     1 VEYDLVIAETPVNIGGKEGEAITVNGQVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPNDMDGVPGLSFPGIKPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1179981522  98 GVFHYRFVLKQSGTYWYHAHAELQEQQGLYGAFVID 133
Cdd:cd13848    81 ETFTYRFPVRQSGTYWYHSHSGLQEQTGLYGPIIID 116
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 24-134 4.06e-45

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: 158.18  E-value: 4.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  24 VGYKTVSFAGKPR-IAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQ--MDGVEHVSQKAIPPGGVF 100
Cdd:pfam07732   2 VTYGTVSPLGGTRqAVIGVNGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwMDGVPGVTQCPIPPGQSF 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1179981522 101 HYRF-VLKQSGTYWYHAHAELQEQQGLYGAFVIDP 134
Cdd:pfam07732  82 TYRFqVKQQAGTYWYHSHTSGQQAAGLAGAIIIED 116
PcoB COG3667
Uncharacterized conserved protein involved in copper resistance [Inorganic ion transport and ...
 754-940 1.87e-34

Uncharacterized conserved protein involved in copper resistance [Inorganic ion transport and metabolism];


Pssm-ID: 442884  Cd Length: 268  Bit Score: 133.08  E-value: 1.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 754 HNAQRLNYKGLYGPDYNKLELFVNDAELLKGKVESADIDIFYWHLISQFWAIKAGANYTNKPANTPYWqPGIGIEGLMPY 833
Cdd:COG3667    78 GDALAWDGQAWYGGDYNRLWLKSEGEGSSGGRLEEAEVEALYSRAISPFWDLQAGVRYDFGPGPDRTW-AAFGVQGLAPY 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 834 FIDTNLRGYYYN-GSAKLDVELSRDTQITNNLFIRAGIRSILASKTVIQANIGNGLNQMRYIVRPYYRLIPGLNINVEYE 912
Cdd:COG3667   157 WFEVDATAYLSEdGDLAARLEAEYDLLLTQRLILQPRAELNLYAQDDPERGIGSGLSDVELGLRLRYEIRREFAPYVGVE 236

                         170       180
                  ....*....|....*....|....*...
gi 1179981522 913 HEQDYGAFKNIQISNGEAANQDTITFGL 940
Cdd:COG3667   237 WERKFGDTADLARAAGEDTSETRFVAGV 264
PLN02191 PLN02191
L-ascorbate oxidase
 3-299 1.09e-31

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 131.67  E-value: 1.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522   3 LLTSLLVVTNVFSAK-RVVDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMD-KPTSIHWHGVL-- 78
Cdd:PLN02191    8 IVTVVAVLTHTASAAvREYTWEVEYKYWWPDCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLTtEGLVIHWHGIRqk 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  79 -VPWQmDGVEHVSQKAIPPGGVFHYRFVLKQSGTYWYHAHAELQEQQGLYGAFVIDPIKAPKYK--YMKDFVVVLSDWSN 155
Cdd:PLN02191   88 gSPWA-DGAAGVTQCAINPGETFTYKFTVEKPGTHFYHGHYGMQRSAGLYGSLIVDVAKGPKERlrYDGEFNLLLSDWWH 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 156 tkpEQIlknlkkegdyYSPRFPLQPSLVKFMhdykkgsaGERKQLFNDYKMMQQMRMSIYDFSDVAYDAFLLNGQPKFKP 235
Cdd:PLN02191  167 ---ESI----------PSQELGLSSKPMRWI--------GEAQSILINGRGQFNCSLAAQFSNGTELPMCTFKEGDQCAP 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1179981522 236 WTALVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVK 299
Cdd:PLN02191  226 QTLRVEPNKTYRIRLASTTALASLNLAVQGHKLVVVEADGNYITPFTTDDIDIYSGESYSVLLT 289
CopB pfam05275
Copper resistance protein B precursor (CopB); This family consists of several bacterial copper ...
 762-942 3.06e-17

Copper resistance protein B precursor (CopB); This family consists of several bacterial copper resistance proteins. Copper is essential and serves as cofactor for more than 30 enzymes yet a surplus of copper is toxic and leads to radical formation and oxidation of biomolecules. Therefore, copper homeostasis is a key requisite for every organizm. CopB serves to extrude copper when it approaches toxic levels.


Pssm-ID: 428404  Cd Length: 208  Bit Score: 81.42  E-value: 3.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 762 KGLYGPDYNKLELfvnDAE---LLKGKVESADIDIFYWHLISQFWAIKAGANYTNKPANTPYWQpGIGIEGLMPYFIDTN 838
Cdd:pfam05275  26 QAWYGGDYNRLWL---KSEgerSFGGGLEEAELQLLYSRAISPFWDLQAGVRQDFGPGPDRTWA-ALGVQGLAPYWFEVD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 839 LRGYYYN-GSAKLDVELSRDTQITNNLFIRAGIRSILASKTVIQANIGNGLN------QMRY-IVR---PYyrlipglni 907
Cdd:pfam05275 102 ATLYVSEdGDTAARLEAEYELLLTQRLILQPRLELNLYGQDDPERGIGSGLSdleaglRLRYeISRefaPY--------- 172

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1179981522 908 nVEYEHEQDYGAFKNIQISNGEAANQDTITFGLTV 942
Cdd:pfam05275 173 -IGVEWERKFGDTADFARAEGESTSDTRFVAGLRF 206
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 401-529 1.61e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 74.95  E-value: 1.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 401 NTLSSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDS 480
Cdd:NF033609  585 DSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDS 664

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1179981522 481 NMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  665 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 713
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.79e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 74.95  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  594 SASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 673

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  674 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 719
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.85e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 74.95  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  606 SASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 685

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  686 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 731
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 2.00e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 74.56  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  600 SASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 679

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  680 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 725
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-573 6.05e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 73.02  E-value: 6.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  718 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 797

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMPTEPTIIGDKMGPPTSSYKTSMGTKYQPmia 563
Cdd:NF033609  798 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVP--- 874

                         170
                  ....*....|
gi 1179981522 564 avktndPNTP 573
Cdd:NF033609  875 ------PNSP 878
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 7.18e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 73.02  E-value: 7.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  582 SGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSD 661

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  662 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 707
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 8.88e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 72.63  E-value: 8.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  576 SDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSD 655

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  656 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 701
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.23e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 72.25  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  688 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 767

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  768 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 813
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.56e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.86  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  694 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 773

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  774 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 819
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.70e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.48  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  700 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 779

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  780 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 825
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.76e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.48  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  682 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 761

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  762 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 807
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.90e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.48  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  618 SASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 697

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMkmDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  698 SDSDSDSDSDS--DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 741
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 2.39e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.09  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  676 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 755

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  756 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 801
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 2.41e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.09  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  706 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 785

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  786 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 831
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 2.67e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.09  E-value: 2.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  612 SASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 691

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMkmDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  692 SDSDSDSDSDSDSDSDS--DSDSDSDSDSDSDSDSDSDSDSDSDSD 735
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 405-529 2.83e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.09  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 405 SSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMKM 484
Cdd:NF033609  571 SDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDS 650

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1179981522 485 DSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  651 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 695
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 2.98e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 70.71  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  624 SASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 703

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMkmDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  704 SDSDS--DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 747
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 3.11e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 70.71  E-value: 3.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  712 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 791

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  792 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 837
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 3.53e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 70.71  E-value: 3.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  670 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 749

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  750 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 795
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 4.02e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 70.32  E-value: 4.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  664 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 743

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  744 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 789
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 5.60e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 69.94  E-value: 5.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  658 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 737

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  738 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 783
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 6.31e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 69.94  E-value: 6.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMk 483
Cdd:NF033609  630 SASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS- 708

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 mDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  709 -DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 753
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 8.22e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 69.55  E-value: 8.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMk 483
Cdd:NF033609  648 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS- 726

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 mDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  727 -DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 771
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 8.22e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 69.55  E-value: 8.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  652 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 731

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  732 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 777
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 9.58e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 69.17  E-value: 9.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMkmDSNMK 483
Cdd:NF033609  636 SASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS--DSDSD 713

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  714 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 759
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.18e-11

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 68.78  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMkmDSNMKMDSNMK 483
Cdd:NF033609  642 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS--DSDSDSDSDSD 719

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  720 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 765
 
Name Accession Description Interval E-value
copper_res_A TIGR01480
copper-resistance protein, CopA family; This model represents the CopA copper resistance ...
 20-688 1.82e-133

copper-resistance protein, CopA family; This model represents the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is observed for a large number of periplasmic proteins that cross the inner membrane with metal-containing cofactors already bound. The combination of copper-binding sites and TAT translocation motif suggests a mechansism of resistance by packaging and export. [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273649 [Multi-domain]  Cd Length: 587  Bit Score: 413.12  E-value: 1.82e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  20 VDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHVSQKAIPPGGV 99
Cdd:TIGR01480  48 FDLTIGETMVNFTGRARPAITVNGSIPGPLLRWREGDTVRLRVTNTLPEDTSIHWHGILLPFQMDGVPGVSFAGIAPGET 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 100 FHYRFVLKQSGTYWYHAHAELQEQQGLYGAFVIDPIKAPKYKYMKDFVVVLSDWSNTKPEQILKNLKKEGDYYSprfPLQ 179
Cdd:TIGR01480 128 FTYRFPVRQSGTYWYHSHSGFQEQAGLYGPLIIDPAEPDPVRADREHVVLLSDWTDLDPAALFRKLKVMAGHDN---YYK 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 180 PSLVKFMHDYKKGSAgerKQLFNDYKMMQQMRMSIYDFSDV--AYDAFLLNGQPKFKPWTALVKKGDVVRLRFIGAGGST 257
Cdd:TIGR01480 205 RTVADFFRDVRNDGL---KQTLADRKMWGQMRMTPTDLADVngSTYTYLMNGTTPAGNWTGLFRPGEKVRLRFINGSAMT 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 258 IFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVKIQKNRPYIIYAESLDTVGAAYGAL-VTSSQHVvdyqKV 336
Cdd:TIGR01480 282 YFDVRIPGLKLTVVAVDGQYVHPVSVDEFRIAPAETFDVIVEPTGDDAFTIFAQDSDRTGYARGTLaVRLGLTA----PV 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 337 PPF-PEPLPVSRDmmammmgqmnqgtlpqvikssikkkgvnhspkMKMSSMSHEMSHKKlhpmqkntlsSSMSNMKmdsn 415
Cdd:TIGR01480 358 PALdPRPLLTMKD--------------------------------MGMGGMHHGMDHSK----------MSMGGMP---- 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 416 mkmdsnmkmdsnmkmdsnmkmdsnmkmdsnmKMDSNMKMDSNMKMDSSMkmdssMKMDSNMKMDSNMKMDSNMKMDSNMK 495
Cdd:TIGR01480 392 -------------------------------GMDMSMRAQSNAPMDHSQ-----MAMDASPKHPASEPLNPLVDMIVDMP 435

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 496 MDsnmKMDsnmkmdsnmkmdsnmkmdsnmkmdsnmkmptEPTIIGDKMGPPTSSYkTSMGTKYQPMiaavktnDPNTPvA 575
Cdd:TIGR01480 436 MD---RMD-------------------------------DPGIGLRDNGRRVLTY-ADLHSLFPPP-------DGRAP-G 472

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 576 HVINMELFGYMDRFIWFINGVPAYKAHPIRLEPGKRYRFVFTNTSMMHHPMHIHGHWFILRKGNDAYDPLLHTIDVPPGA 655
Cdd:TIGR01480 473 REIELHLTGNMERFAWSFDGEAFGLKTPLRFNYGERLRVVLVNDTMMAHPIHLHGMWSELEDGQGEFQVRKHTVDVPPGG 552

                         650       660       670
                  ....*....|....*....|....*....|...
gi 1179981522 656 TITADVDTDASGQWFFHCHFLYHMMTGMSRVFQ 688
Cdd:TIGR01480 553 KRSFRVTADALGRWAYHCHMLLHMEAGMFREVT 585
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 18-344 8.84e-64

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: 221.73  E-value: 8.84e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  18 RVVDLVVGYKTVSFA-GKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHvsqKAIPP 96
Cdd:COG2132    14 REYELTAQPATVELLpGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDGVPG---DPIAP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  97 GGVFHYRFVLKQ-SGTYWYHAHA----ELQEQQGLYGAFVIDPIKAPKYKYMKDFVVVLSDWSNTKPEQILknlkkegdy 171
Cdd:COG2132    91 GETFTYEFPVPQpAGTYWYHPHThgstAEQVYRGLAGALIVEDPEEDLPRYDRDIPLVLQDWRLDDDGQLL--------- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 172 ysprfplqpslvkfmhdykkgsagerkqlfndYKMMQQMRMSIYDFsdvaydaFLLNGQPkfkPWTALVKKGDVVRLRFI 251
Cdd:COG2132   162 --------------------------------YPMDAAMGGRLGDT-------LLVNGRP---NPTLEVRPGERVRLRLL 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 252 GAGGSTIFRVKIP-GSVMQMVHAQGNDVN-PYTIKDFAIASGETYDVLVKIQKN--RPYIIYAESLDTVGAAYGALVTSS 327
Cdd:COG2132   200 NASNARIYRLALSdGRPFTVIATDGGLLPaPVEVDELLLAPGERADVLVDFSADpgEEVTLANPFEGRSGRALLTLRVTG 279

                         330
                  ....*....|....*..
gi 1179981522 328 QhvvdyQKVPPFPEPLP 344
Cdd:COG2132   280 A-----AASAPLPANLA 291
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 18-133 7.74e-63

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: 207.90  E-value: 7.74e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  18 RVVDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHVSQKAIPPG 97
Cdd:cd13848     1 VEYDLVIAETPVNIGGKEGEAITVNGQVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPNDMDGVPGLSFPGIKPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1179981522  98 GVFHYRFVLKQSGTYWYHAHAELQEQQGLYGAFVID 133
Cdd:cd13848    81 ETFTYRFPVRQSGTYWYHSHSGLQEQTGLYGPIIID 116
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 576-689 7.19e-52

The third 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 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: 259963 [Multi-domain]  Cd Length: 115  Bit Score: 177.06  E-value: 7.19e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 576 HVINMELFGYMDRFIWFINGVPAYKAHPIRLEPGKRYRFVFTNTSMMHHPMHIHGHWFILRKGNDAYDPLLHTIDVPPGA 655
Cdd:cd13896     2 REIELHLTGNMERYVWTINGKAYPDADPLRVREGERVRIVFVNDTMMAHPMHLHGHFFQVENGNGEYGPRKDTVLVPPGE 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1179981522 656 TITADVDTDASGQWFFHCHFLYHMMTGMSRVFQY 689
Cdd:cd13896    82 TVSVDFDADNPGRWAFHCHNLYHMEAGMMRVVEY 115
CuRO_2_CopA cd13874
The second cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 212-323 6.89e-46

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: 160.15  E-value: 6.89e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 212 MSIYDFSDVAYDAFLLNGQPKFKPWTALVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASG 291
Cdd:cd13874     1 MDPMDISDVYYDTYLINGKPPEDNWTGLFKPGERVRLRFINAAASTYFDVRIPGGKMTVVAADGQDVRPVEVDEFRIGVA 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1179981522 292 ETYDVLVKIQKNRPYIIYAESLDTVGAAYGAL 323
Cdd:cd13874    81 ETYDVIVTIPENGAYTIRATSQDRSGYASGTL 112
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 24-134 4.06e-45

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: 158.18  E-value: 4.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  24 VGYKTVSFAGKPR-IAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQ--MDGVEHVSQKAIPPGGVF 100
Cdd:pfam07732   2 VTYGTVSPLGGTRqAVIGVNGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTpwMDGVPGVTQCPIPPGQSF 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1179981522 101 HYRF-VLKQSGTYWYHAHAELQEQQGLYGAFVIDP 134
Cdd:pfam07732  82 TYRFqVKQQAGTYWYHSHTSGQQAAGLAGAIIIED 116
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 16-133 1.70e-42

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: 150.46  E-value: 1.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  16 AKRVVDLVVGYKTVSfagkpriAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHVSQKAIP 95
Cdd:cd13861     7 AAPAELLDLGGPTTR-------TWGYNGQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGVPGLTQPPVP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1179981522  96 PGGVFHYRFVLKQSGTYWYHAHAELQEQQ--GLYGAFVID 133
Cdd:cd13861    80 PGESFTYEFTPPDAGTYWYHPHVGSQEQLdrGLYGPLIVE 119
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 18-132 2.27e-41

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: 147.43  E-value: 2.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  18 RVVDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMD-KPTSIHWHGVLVPWQ--MDGVEHVSQKAI 94
Cdd:cd04206     1 REYELTITETTVNPDGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNLPnEPTSIHWHGLRQPGTndGDGVAGLTQCPI 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1179981522  95 PPGGVFHYRFVLK-QSGTYWYHAHAELQEQQGLYGAFVI 132
Cdd:cd04206    81 PPGESFTYRFTVDdQAGTFWYHSHVGGQRADGLYGPLIV 119
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 38-133 4.41e-37

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: 135.02  E-value: 4.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  38 AIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHVSQKAIPPGGVFHYRFVLKQSGTYWYHAH 117
Cdd:cd13860    22 AWGYNGSVPGPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGVPGITQPPIQPGETFTYEFTAKQAGTYMYHSH 101

                          90
                  ....*....|....*...
gi 1179981522 118 AELQEQQ--GLYGAFVID 133
Cdd:cd13860   102 VDEAKQEdmGLYGAFIVH 119
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 18-132 1.17e-35

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: 131.23  E-value: 1.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  18 RVVDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVL---VPWqMDGVEHVSQKAI 94
Cdd:cd13857     1 REYNFTISEITGAPDGFVRPMLVINGQFPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFqngTNW-MDGTAGITQCPI 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1179981522  95 PPGGVFHYRFVL-KQSGTYWYHAHAELQEQQGLYGAFVI 132
Cdd:cd13857    80 PPGGSFTYNFTVdGQYGTYWYHSHYSTQYADGLVGPLIV 118
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 24-303 1.46e-35

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


Pssm-ID: 274555 [Multi-domain]  Cd Length: 541  Bit Score: 142.97  E-value: 1.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  24 VGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNH-MDKPTSIHWHGVL---VPWqMDGVEHVSQKAIPPGGV 99
Cdd:TIGR03388   8 VEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKlHTEGVVIHWHGIRqigTPW-ADGTAGVTQCAINPGET 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 100 FHYRFVLKQSGTYWYHAHAELQEQQGLYGAFVIDPIKAPK--YKYMKDFVVVLSDWSNTK-PEQILknlkkegdYYSPRf 176
Cdd:TIGR03388  87 FIYNFVVDRPGTYFYHGHYGMQRSAGLYGSLIVDVPDGEKepFHYDGEFNLLLSDWWHKSiHEQEV--------GLSSK- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 177 PLQpslvkfmhdykkgSAGERKQLFNDYKmmQQMRMSI-YDFSDVAYDAFLLNGQPKFKPWTALVKKGDVVRLRFIGAGG 255
Cdd:TIGR03388 158 PMR-------------WIGEPQSLLINGR--GQFNCSLaAKFSSTNLPQCNLKGNEQCAPQILHVEPGKTYRLRIASTTA 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1179981522 256 STIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVKIQKN 303
Cdd:TIGR03388 223 LAALNFAIEGHKLTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQD 270
PcoB COG3667
Uncharacterized conserved protein involved in copper resistance [Inorganic ion transport and ...
 754-940 1.87e-34

Uncharacterized conserved protein involved in copper resistance [Inorganic ion transport and metabolism];


Pssm-ID: 442884  Cd Length: 268  Bit Score: 133.08  E-value: 1.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 754 HNAQRLNYKGLYGPDYNKLELFVNDAELLKGKVESADIDIFYWHLISQFWAIKAGANYTNKPANTPYWqPGIGIEGLMPY 833
Cdd:COG3667    78 GDALAWDGQAWYGGDYNRLWLKSEGEGSSGGRLEEAEVEALYSRAISPFWDLQAGVRYDFGPGPDRTW-AAFGVQGLAPY 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 834 FIDTNLRGYYYN-GSAKLDVELSRDTQITNNLFIRAGIRSILASKTVIQANIGNGLNQMRYIVRPYYRLIPGLNINVEYE 912
Cdd:COG3667   157 WFEVDATAYLSEdGDLAARLEAEYDLLLTQRLILQPRAELNLYAQDDPERGIGSGLSDVELGLRLRYEIRREFAPYVGVE 236

                         170       180
                  ....*....|....*....|....*...
gi 1179981522 913 HEQDYGAFKNIQISNGEAANQDTITFGL 940
Cdd:COG3667   237 WERKFGDTADLARAAGEDTSETRFVAGV 264
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 33-132 2.28e-34

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


Pssm-ID: 259927 [Multi-domain]  Cd Length: 105  Bit Score: 126.88  E-value: 2.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  33 GKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMD-KPTSIHWHGVL---VPWqMDGVEHVSQKAIPPGGVFHYRFVLKQ 108
Cdd:cd13858     2 GVERPVITVNGQLPGPSIEVCEGDTVVVDVKNRLPgESTTIHWHGIHqrgTPY-MDGVPMVTQCPILPGQTFRYKFKADP 80

                          90       100
                  ....*....|....*....|....
gi 1179981522 109 SGTYWYHAHAELQEQQGLYGAFVI 132
Cdd:cd13858    81 AGTHWYHSHSGTQRADGLFGALIV 104
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 570-689 9.10e-34

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: 135.06  E-value: 9.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 570 PNTPVAHVINMELFGYMDRFIWFINGVPaYKAHPIRLEP--GKRYRFVFTNTSMMHHPMHIHGHWFIL--RKGNDAYDPL 645
Cdd:COG2132   297 EDREAVRTRELVLTGGMAGYVWTINGKA-FDPDRPDLTVklGERERWTLVNDTMMPHPFHLHGHQFQVlsRNGKPPPEGG 375

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 646 L-HTIDVPPGATITADVD-TDASGQWFFHCHFLYHMMTGMSRVFQY 689
Cdd:COG2132   376 WkDTVLVPPGETVRILFRfDNYPGDWMFHCHILEHEDAGMMGQFEV 421
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 21-132 2.62e-33

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: 124.33  E-value: 2.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  21 DLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVL---VPWqMDGVEHVSQKAIPPG 97
Cdd:cd13850     2 TLTVTEGSPDGDGGEREVILINGQFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGILqrgTPW-SDGVPGVTQWPIQPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1179981522  98 GVFHYRFVLK-QSGTYWYHAHAELQEQQGLYGAFVI 132
Cdd:cd13850    81 GSFTYRWKAEdQYGLYWYHSHYRGYYMDGLYGPIYI 116
CuRO_1_LCC_like_3 cd13865
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 22-134 8.61e-33

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: 259933 [Multi-domain]  Cd Length: 115  Bit Score: 122.80  E-value: 8.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  22 LVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHVSQKAIPPGGVFH 101
Cdd:cd13865     3 LTVASRTIEVNGKAATVYGIRQPDGTEGLRLTEGDRFDVELENRLDEPTTIHWHGLIPPNLQDGVPDVTQPPIPPGQSQR 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1179981522 102 YRFVLKQSGTYWYHAHAELQEQQGLYGAFVIDP 134
Cdd:cd13865    83 YDFPLVQPGTFWMHSHYGLQEQKLLAAPLIIRS 115
PLN02191 PLN02191
L-ascorbate oxidase
 3-299 1.09e-31

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 131.67  E-value: 1.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522   3 LLTSLLVVTNVFSAK-RVVDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMD-KPTSIHWHGVL-- 78
Cdd:PLN02191    8 IVTVVAVLTHTASAAvREYTWEVEYKYWWPDCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLTtEGLVIHWHGIRqk 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  79 -VPWQmDGVEHVSQKAIPPGGVFHYRFVLKQSGTYWYHAHAELQEQQGLYGAFVIDPIKAPKYK--YMKDFVVVLSDWSN 155
Cdd:PLN02191   88 gSPWA-DGAAGVTQCAINPGETFTYKFTVEKPGTHFYHGHYGMQRSAGLYGSLIVDVAKGPKERlrYDGEFNLLLSDWWH 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 156 tkpEQIlknlkkegdyYSPRFPLQPSLVKFMhdykkgsaGERKQLFNDYKMMQQMRMSIYDFSDVAYDAFLLNGQPKFKP 235
Cdd:PLN02191  167 ---ESI----------PSQELGLSSKPMRWI--------GEAQSILINGRGQFNCSLAAQFSNGTELPMCTFKEGDQCAP 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1179981522 236 WTALVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVK 299
Cdd:PLN02191  226 QTLRVEPNKTYRIRLASTTALASLNLAVQGHKLVVVEADGNYITPFTTDDIDIYSGESYSVLLT 289
PLN02604 PLN02604
oxidoreductase
 36-303 1.12e-30

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 128.44  E-value: 1.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  36 RIAIAVNNQIPAPTLRFKEGDEITINVSNH-MDKPTSIHWHGVL---VPWqMDGVEHVSQKAIPPGGVFHYRFVLKQSGT 111
Cdd:PLN02604   43 KLVITINGRSPGPTILAQQGDTVIVELKNSlLTENVAIHWHGIRqigTPW-FDGTEGVTQCPILPGETFTYEFVVDRPGT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 112 YWYHAHAELQEQQGLYGAFVIDPI--KAPKYKYMKDFVVVLSDW-SNTKPEQILKnlkkegdyysprfplqPSLVKFmhd 188
Cdd:PLN02604  122 YLYHAHYGMQREAGLYGSIRVSLPrgKSEPFSYDYDRSIILTDWyHKSTYEQALG----------------LSSIPF--- 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 189 ykkGSAGERKQLFNDYKmmqqmrmSIYDFSDVA---YDAFLLNG-QPKFKPWTALVKKGDVVRLRFIGAGGSTIFRVKIP 264
Cdd:PLN02604  183 ---DWVGEPQSLLIQGK-------GRYNCSLVSspyLKAGVCNAtNPECSPYVLTVVPGKTYRLRISSLTALSALSFQIE 252

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1179981522 265 GSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVKIQKN 303
Cdd:PLN02604  253 GHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQD 291
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 569-687 6.85e-30

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: 115.23  E-value: 6.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 569 DPNTPVAHVInmeLFGYMDRFIWFINGVP-AYKAHPIRLEPGKRYRFVFTNTSMMHHPMHIHGHWF-ILRKGNDAYD--- 643
Cdd:pfam07731   3 PPKLPTLLQI---TSGNFRRNDWAINGLLfPPNTNVITLPYGTVVEWVLQNTTTGVHPFHLHGHSFqVLGRGGGPWPeed 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1179981522 644 ---------PLLHTIDVPPGATITADVDTDASGQWFFHCHFLYHMMTGMSRVF 687
Cdd:pfam07731  80 pktynlvdpVRRDTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQF 132
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 36-134 2.02e-28

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: 110.61  E-value: 2.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  36 RIAIAVNNQIPAPTLRFKEGDEITINVSNHMdkPT---SIHWHGVL---VPWqMDGVEHVSQKAIPPGGVFHYRFVLKQS 109
Cdd:cd13845    19 KLVIGINGQFPGPTIRATAGDTIVVELENKL--PTegvAIHWHGIRqrgTPW-ADGTASVSQCPINPGETFTYQFVVDRP 95

                          90       100
                  ....*....|....*....|....*
gi 1179981522 110 GTYWYHAHAELQEQQGLYGAFVIDP 134
Cdd:cd13845    96 GTYFYHGHYGMQRSAGLYGSLIVDP 120
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 18-133 2.03e-28

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


Pssm-ID: 259923 [Multi-domain]  Cd Length: 122  Bit Score: 110.41  E-value: 2.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  18 RVVDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHM-DKPTSIHWHGVL---VPWQmDGVEHVSQKA 93
Cdd:cd13854     4 RKYTLTITNSTLAPDGVEKEVMLINGQYPGPLIEANWGDTIEVTVINKLqDNGTSIHWHGIRqlnTNWQ-DGVPGVTECP 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1179981522  94 IPPGGVFHYRFVLKQSGTYWYHAHAELQEQQGLYGAFVID 133
Cdd:cd13854    83 IAPGDTRTYRFRATQYGTSWYHSHYSAQYGDGVVGPIVIH 122
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 18-132 4.87e-28

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: 109.28  E-value: 4.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  18 RVVDLVVGYKTVSFAG-KPRIAIAVNNQIPAPTLRFKEGDEITINVSNHM-DKPTSIHWHGVL---VPWqMDGVEHVSQK 92
Cdd:cd13851     1 VEFDWNITWVTANPDGlFERRVIGINGQWPPPPIEVNKGDTVVIHATNSLgDQPTSLHFHGLFqngTNY-MDGPVGVTQC 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1179981522  93 AIPPGGVFHYRF-VLKQSGTYWYHAHAELQEQQGLYGAFVI 132
Cdd:cd13851    80 PIPPGQSFTYEFtVDTQVGTYWYHSHDGGQYPDGLRGPFII 120
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 19-132 5.93e-28

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


Pssm-ID: 259925 [Multi-domain]  Cd Length: 125  Bit Score: 109.35  E-value: 5.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  19 VVDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNH-----MDKPTSIHWHGVLvpwQ-----MDGVEH 88
Cdd:cd13856     2 TYTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQltdptMRRSTSIHWHGIF---QhgtnyADGPAF 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1179981522  89 VSQKAIPPGGVFHYRFVL-KQSGTYWYHAHAELQEQQGLYGAFVI 132
Cdd:cd13856    79 VTQCPIAPNHSFTYDFTAgDQAGTFWYHSHLSTQYCDGLRGPLVI 123
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 40-133 2.51e-27

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: 107.56  E-value: 2.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  40 AVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLV--PWQMDGVEHVSQKAIPPGGVFHYRFVLKQSGTYWYHAH 117
Cdd:cd13859    24 AFNGQVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQmgSWKMDGVPGVTQPAIEPGESFTYKFKAERPGTLWYHCH 103

                          90
                  ....*....|....*....
gi 1179981522 118 AELQEQ---QGLYGAFVID 133
Cdd:cd13859   104 VNVNEHvgmRGMWGPLIVD 122
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 21-318 5.70e-26

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


Pssm-ID: 274556 [Multi-domain]  Cd Length: 539  Bit Score: 113.29  E-value: 5.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  21 DLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGV---LVPWQmDGVEHVSQKAIPPG 97
Cdd:TIGR03389   7 TFDVQEKNVTRLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQYNVTIHWHGVrqlRNGWA-DGPAYITQCPIQPG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  98 GVFHYRFVLK-QSGTYWYHAHAeLQEQQGLYGAFVIDPIKAPKYKYMK---DFVVVLSDWSNTKPEQILKNLKKEGdyys 173
Cdd:TIGR03389  86 QSYVYNFTITgQRGTLWWHAHI-SWLRATVYGAIVILPKPGVPYPFPKpdrEVPIILGEWWNADVEAVINQANQTG---- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 174 prfpLQPSlvkfmhdykkgsagerkqlfndykmmqqmrMSiydfsdvayDAFLLNGQPKFKP-------WTALVKKGDVV 246
Cdd:TIGR03389 161 ----GAPN------------------------------VS---------DAYTINGHPGPLYncsskdtFKLTVEPGKTY 197

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1179981522 247 RLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVKIQK--NRPYIIYAESLDTVGA 318
Cdd:TIGR03389 198 LLRIINAALNDELFFAIANHTLTVVEVDATYTKPFKTKTIVIGPGQTTNVLLTADQspGRYFMAARPYMDAPGA 271
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 21-134 1.54e-25

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: 101.95  E-value: 1.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  21 DLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGV---LVPWqMDGVEHVSQKAIPPG 97
Cdd:cd13849     2 TFVVQEKNVTRLCSTKSILTVNGQFPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIrqlRSGW-ADGPAYITQCPIQPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1179981522  98 GVFHYRF-VLKQSGTYWYHAHAELQEQQgLYGAFVIDP 134
Cdd:cd13849    81 QSYTYRFtVTGQEGTLWWHAHISWLRAT-VYGAFIIRP 117
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 22-346 1.76e-24

L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized.


Pssm-ID: 132431 [Multi-domain]  Cd Length: 538  Bit Score: 108.78  E-value: 1.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  22 LVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHM-DKPTSIHWHGV---LVPWQmDGVEHVSQKAIPPG 97
Cdd:TIGR03390  13 LRVTSDNIKIACSSRYSVVVNGTSPGPEIRLQEGQTTWIRVYNDIpDNNVTMHWHGLtqrTAPFS-DGTPLASQWPIPPG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  98 GVFHY--RFVLKQSGTYWYHAHAELQEQQGlYGAFVIDPIKAPKYKYMKDFVVVLSDWSNTKPEQILKNLKKEgdyyspr 175
Cdd:TIGR03390  92 HFFDYeiKPEPGDAGSYFYHSHVGFQAVTA-FGPLIVEDCEPPPYKYDDERILLVSDFFSATDEEIEQGLLST------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 176 fPLQPSlvkfmhdykkgsaGERKqlfndykmmqqmrmsiydfsdvaydAFLLNGQPKFKPWTAL-------------VKK 242
Cdd:TIGR03390 164 -PFTWS-------------GETE-------------------------AVLLNGKSGNKSFYAQinpsgscmlpvidVEP 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 243 GDVVRLRFIGAGGSTIFRVKIPG-SVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVKIQKN--------RPYIIYAESL 313
Cdd:TIGR03390 205 GKTYRLRFIGATALSLISLGIEDhENLTIIEADGSYTKPAKIDHLQLGGGQRYSVLFKAKTEdelcggdkRQYFIQFETR 284

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1179981522 314 D--TVGAAYGALVTSSQHVVDYQKVPPFPePLPVS 346
Cdd:TIGR03390 285 DrpKVYRGYAVLRYRSDKASKLPSVPETP-PLPLP 318
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 40-134 3.46e-24

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: 98.50  E-value: 3.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  40 AVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHVsqkaIPPGGVFHYRFVLKQSGTYWYHAHAE 119
Cdd:cd11024    25 TYNGTVPGPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAMDGTGLGP----IMPGESFTYEFVAEPAGTHLYHCHVQ 100

                          90
                  ....*....|....*...
gi 1179981522 120 LQEQ---QGLYGAFVIDP 134
Cdd:cd11024   101 PLKEhiaMGLYGAFIVDP 118
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 33-132 2.28e-23

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: 96.01  E-value: 2.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  33 GKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHvsqKAIPPGGVFHYRFVLKQ--SG 110
Cdd:cd13855    18 GKPTEFWAYNGSVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDGNPH---DPVAPGNDRVYRFTLPQdsAG 94

                          90       100
                  ....*....|....*....|....*..
gi 1179981522 111 TYWYHAH-----AElQEQQGLYGAFVI 132
Cdd:cd13855    95 TYWYHPHphghtAE-QVYRGLAGAFVV 120
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 586-688 1.62e-21

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: 91.37  E-value: 1.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 586 MDRFIWFINGVP----AYKAHPIRLEPGKRYRFVFTNTS--MMHHPMHIHGHWF-ILRKGNDAYDPLL--------HTID 650
Cdd:cd04207    15 DGTTRWVINGMPfkegDANTDIFSVEAGDVVEIVLINAGnhDMQHPFHLHGHSFwVLGSGGGPFDAPLnltnppwrDTVL 94

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1179981522 651 VPPGATITADVDTDASGQWFFHCHFLYHMMTGMSRVFQ 688
Cdd:cd04207    95 VPPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 48-133 3.33e-21

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: 89.65  E-value: 3.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  48 PTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGveHVSQkAIPPGGVFHYRF-VLKQSGTYWYHAHA-ELQEQQ- 124
Cdd:cd13852    25 PILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDG--HPRY-AIDPGETYVYEFeVLNRAGTYWYHPHPhGLTAKQv 101

                          90
                  ....*....|.
gi 1179981522 125 --GLYGAFVID 133
Cdd:cd13852   102 yrGLAGLFLVT 112
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 31-133 3.89e-21

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: 89.55  E-value: 3.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  31 FAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHvsqKAIPPGGVFHYRFVLKQS- 109
Cdd:cd04232    15 LPGKKTATWGYNGSYLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDGGPH---QPIAPGQTWSPTFTIDQPa 91

                          90       100
                  ....*....|....*....|....*...
gi 1179981522 110 GTYWYHAHAE----LQEQQGLYGAFVID 133
Cdd:cd04232    92 ATLWYHPHTHgktaEQVYRGLAGLFIIE 119
CuRO_1_MCO_like_2 cd13864
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 33-133 8.49e-21

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: 89.52  E-value: 8.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  33 GKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHM------------DKPTSIHWHGVLVPW-------QMDGVEHVSQKA 93
Cdd:cd13864    17 GKQIISINGSNDTIGPTIRVKSGDTLNLLVTNHLcneqelskiwqdYCPTSIHFHGLVLENfgkqlanLVDGVPGLTQYP 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1179981522  94 IPPGGVFHYRFVLKQS--GTYWYHAHAELQEQQGLYGAFVID 133
Cdd:cd13864    97 IGVGESYWYNFTIPEDtcGTFWYHSHSSVQYGDGLRGVFIVD 138
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 19-118 3.08e-20

The first 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: 259931 [Multi-domain]  Cd Length: 123  Bit Score: 87.19  E-value: 3.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  19 VVDLVVGYKTVSFA-GKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHVSQKAIPPG 97
Cdd:cd13862     2 DVTLRIAPVTVELApGRTISTLGYNGQVPGPLLRMRQGVSVTVDVFNDTDIPEYVHWHGLPLPADVDGAMEEGTPSVPPH 81

                          90       100
                  ....*....|....*....|.
gi 1179981522  98 GVFHYRFVLKQSGTYWYHAHA 118
Cdd:cd13862    82 GHRRYRMTPRPAGFRWYHTHV 102
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 19-133 4.72e-20

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: 87.31  E-value: 4.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  19 VVDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKP-----------------TSIHWHGVLVP- 80
Cdd:cd13853     3 EVTLTVEYGRVTLAGLPVTLRTYNGSIPGPTLRVRPGDTLRITLKNDLPPEgaaneapapntphcpntTNLHFHGLHVSp 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1179981522  81 -WQMDGVeHVSqkaIPPGGVFHYRFVLKQ---SGTYWYHAHA----ELQEQQGLYGAFVID 133
Cdd:cd13853    83 tGNSDNV-FLT---IAPGESFTYEYDIPAdhpPGTYWYHPHLhgstALQVAGGMAGALVVE 139
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 35-133 3.03e-19

The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal proteins with similarity to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (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: 259916 [Multi-domain]  Cd Length: 117  Bit Score: 84.12  E-value: 3.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  35 PRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKP-TSIHWHGV---LVPWqMDGVEHVSQKAIPPGGVFHYRFVLKQ-- 108
Cdd:cd13847    14 PRPSTLINGSFPGPELRVQEGQHLWVRVYNDLEAGnTTMHFHGLsqyMSPF-SDGTPLASQWPIPPGKFFDYEFPLEAgd 92

                          90       100
                  ....*....|....*....|....*
gi 1179981522 109 SGTYWYHAHAELQEQQGlYGAFVID 133
Cdd:cd13847    93 AGTYYYHSHVGFQSVTA-YGALIVE 116
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
 216-301 5.38e-19

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: 83.54  E-value: 5.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 216 DFSDVAYDAFLLNGQPKFKPWTALVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYD 295
Cdd:cd13870     9 DAGDVRYPYYLINGRPPEDPAVFTARPGDRLRLRLINAAGDTAFRVALAGHRLTVTHTDGFPVEPVEVDALLIGMGERYD 88


                  ....*.
gi 1179981522 296 VLVKIQ 301
Cdd:cd13870    89 AIVTAN 94
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 21-133 1.52e-18

The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of plant pollen multicopper oxidase homologous to 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. This subfamily does not harbor trinuclear copper binding histidines.


Pssm-ID: 259915 [Multi-domain]  Cd Length: 118  Bit Score: 82.07  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  21 DLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVL---VPWQmDGVEHVSQKaIPPG 97
Cdd:cd13846     4 DWNVSYITASPLGVPQQVIAINGQFPGPTINVTTNDNVVVNVFNSLDEPLLLTWNGIQqrrNSWQ-DGVLGTNCP-IPPG 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1179981522  98 GVFHYRFVLK-QSGTYWYHAHAELQEQQGLYGAFVID 133
Cdd:cd13846    82 WNWTYKFQVKdQIGSFFYFPSLHFQRAAGGFGGIRVN 118
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 586-690 5.39e-18

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


Pssm-ID: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 81.15  E-value: 5.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 586 MDRFIWFINGVPAYKAHPIRLEPGKRYRFVFTNTSMMHHPMHIHGHWF--ILRKGND---AYDPLLHTIDVPPGATITAD 660
Cdd:cd04202    25 MDFNYFTINGKSFPATPPLVVKEGDRVRIRLINLSMDHHPMHLHGHFFlvTATDGGPipgSAPWPKDTLNVAPGERYDIE 104

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1179981522 661 VDTDASGQWFFHCHFLYHMMT----GMSRVFQYS 690
Cdd:cd04202   105 FVADNPGDWMFHCHKLHHAMNgmggGMMTLIGYE 138
CopB pfam05275
Copper resistance protein B precursor (CopB); This family consists of several bacterial copper ...
 762-942 3.06e-17

Copper resistance protein B precursor (CopB); This family consists of several bacterial copper resistance proteins. Copper is essential and serves as cofactor for more than 30 enzymes yet a surplus of copper is toxic and leads to radical formation and oxidation of biomolecules. Therefore, copper homeostasis is a key requisite for every organizm. CopB serves to extrude copper when it approaches toxic levels.


Pssm-ID: 428404  Cd Length: 208  Bit Score: 81.42  E-value: 3.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 762 KGLYGPDYNKLELfvnDAE---LLKGKVESADIDIFYWHLISQFWAIKAGANYTNKPANTPYWQpGIGIEGLMPYFIDTN 838
Cdd:pfam05275  26 QAWYGGDYNRLWL---KSEgerSFGGGLEEAELQLLYSRAISPFWDLQAGVRQDFGPGPDRTWA-ALGVQGLAPYWFEVD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 839 LRGYYYN-GSAKLDVELSRDTQITNNLFIRAGIRSILASKTVIQANIGNGLN------QMRY-IVR---PYyrlipglni 907
Cdd:pfam05275 102 ATLYVSEdGDTAARLEAEYELLLTQRLILQPRLELNLYGQDDPERGIGSGLSdleaglRLRYeISRefaPY--------- 172

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1179981522 908 nVEYEHEQDYGAFKNIQISNGEAANQDTITFGLTV 942
Cdd:pfam05275 173 -IGVEWERKFGDTADFARAEGESTSDTRFVAGLRF 206
PLN02792 PLN02792
oxidoreductase
 24-446 3.82e-17

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 85.80  E-value: 3.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  24 VGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLV---PWQmDGVeHVSQKAIPPGGVF 100
Cdd:PLN02792   23 VTYGNISLLTLPRRGILINGQFPGPEIRSLTNDNLVINVHNDLDEPFLLSWNGVHMrknSYQ-DGV-YGTTCPIPPGKNY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 101 HYRFVLK-QSGTYWYHAHAELQEQQGLYGAFVI---DPIKAPKYKYMKDFVVVLSDWSNtKPEQILKNLKKEGDyyspRF 176
Cdd:PLN02792  101 TYDFQVKdQVGSYFYFPSLAVQKAAGGYGSLRIyslPRIPVPFPEPAGDFTFLIGDWYR-RNHTTLKKILDGGR----KL 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 177 PLQPslvkfmhdykkgsagerkqlfndykmmqqmrmsiydfsdvayDAFLLNGQPKFKPWTALVKKGDVVRLRFIGAGGS 256
Cdd:PLN02792  176 PLMP------------------------------------------DGVMINGQGVSYVYSITVDKGKTYRFRISNVGLQ 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 257 TIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVKIqkNRPYIIYAESLDTVGAAYGALVTSSQHVVDYQKV 336
Cdd:PLN02792  214 TSLNFEILGHQLKLIEVEGTHTVQSMYTSLDIHVGQTYSVLVTM--DQPPQNYSIVVSTRFIAAKVLVSSTLHYSNSKGH 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 337 PPFPEPLPVSRDMMAMMMGQMNQGTLPQVIKSSIKKKGVNHSPKMKMS-SMSHEMSHKKLHPMQKNTLsSSMSNMKMDSN 415
Cdd:PLN02792  292 KIIHARQPDPDDLEWSIKQAQSIRTNLTASGPRTNPQGSYHYGKMKISrTLILESSAALVKRKQRYAI-NGVSFVPSDTP 370

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1179981522 416 MKMDSNMKMDSNMKMDS---NMKMDSNMKMDSNM 446
Cdd:PLN02792  371 LKLADHFKIKGVFKVGSipdKPRRGGGMRLDTSV 404
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 580-688 5.28e-17

The third 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 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: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 78.58  E-value: 5.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 580 MELFGYMDRFIWFINGVPAYKA------HPI-RLEPGKRYRFVFTNTSMMHHPMHIHGHWF--ILRKGNDAYDPLLH-TI 649
Cdd:cd13906    18 DGGSGVAGGTFWAINGTSWTGGdhshlpPPLaTLKRGRSYVLRLVNETAFLHPMHLHGHFFrvLSRNGRPVPEPFWRdTV 97

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1179981522 650 DVPPGATITADVDTDASGQWFFHCHFLYHMMTGMSRVFQ 688
Cdd:cd13906    98 LLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMGVIR 136
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 219-299 7.83e-17

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: 78.55  E-value: 7.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 219 DVAYDAFLLNGQPKF-----------KPWTALVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFA 287
Cdd:cd04205    28 EPVPDSLLINGRGRFncsmavcnsgcPLPVITVEPGKTYRLRLINAGSFASFNFAIDGHNMTVIEVDGGYVEPLEVDNLD 107

                          90
                  ....*....|..
gi 1179981522 288 IASGETYDVLVK 299
Cdd:cd04205   108 LAPGQRYDVLVK 119
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 591-689 9.20e-16

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: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 74.41  E-value: 9.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 591 WFINGVPAYKAHP-IRLEPGKRYRFVFTNTSMMHHPMHIHGHWFILRK--GNDAYDPLLHTIDVPPGATITADVDTDASG 667
Cdd:cd13908    21 WTINGKSYPDEDPpLVVQQGRRYRLVFRNASDDAHPMHLHRHTFEVTRidGKPTSGLRKDVVMLGGYQRVEVDFVADNPG 100

                          90       100
                  ....*....|....*....|..
gi 1179981522 668 QWFFHCHFLYHMMTGMSRVFQY 689
Cdd:cd13908   101 LTLFHCHQQLHMDYGFMALFKY 122
PLN02354 PLN02354
copper ion binding / oxidoreductase
 24-336 2.08e-14

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 77.14  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  24 VGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLV---PWQmDGVEHvSQKAIPPGGVF 100
Cdd:PLN02354   34 VTYGTASPLGVPQQVILINGQFPGPNINSTSNNNIVINVFNNLDEPFLLTWSGIQQrknSWQ-DGVPG-TNCPIPPGTNF 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 101 HYRFVLK-QSGTYWYHAHAELQEQQGLYGAFVIDP---IKAPKYKYMKDFVVVLSDWSnTKPEQILKNLKKEGdyyspRF 176
Cdd:PLN02354  112 TYHFQPKdQIGSYFYYPSTGMHRAAGGFGGLRVNSrllIPVPYADPEDDYTVLIGDWY-TKSHTALKKFLDSG-----RT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 177 PLQPSLVKFMHDYKKGSaGERKQLFNdykmmqqmrmsiydfsdvaydafllngqpkfkpwtalVKKGDVVRLRFIGAGGS 256
Cdd:PLN02354  186 LGRPDGVLINGKSGKGD-GKDEPLFT-------------------------------------MKPGKTYRYRICNVGLK 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 257 TIFRVKIPGSVMQMVHAQGNDV--NPYtikdfaiasgetydvlvkiqknrpyiiyaESLDT-VGAAYGALVTSSQHVVDY 333
Cdd:PLN02354  228 SSLNFRIQGHKMKLVEMEGSHVlqNDY-----------------------------DSLDVhVGQCFSVLVTANQAPKDY 278


                  ...
gi 1179981522 334 QKV 336
Cdd:PLN02354  279 YMV 281
PLN02168 PLN02168
copper ion binding / pectinesterase
 1-346 2.21e-14

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 76.94  E-value: 2.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522   1 MVLLTSLLVVTNVFSAKRVV--DLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVL 78
Cdd:PLN02168    8 VFVLISLVILELSYAFAPIVsyQWVVSYSQRFILGGNKQVIVINDMFPGPLLNATANDVINVNIFNNLTEPFLMTWNGLQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  79 V---PWQmDGVEHvSQKAIPPGGVFHYRFVLK-QSGTYWYHAHAELQEQQGLYGAFVIDP---IKAPKYKYMKDFVVVLS 151
Cdd:PLN02168   88 LrknSWQ-DGVRG-TNCPILPGTNWTYRFQVKdQIGSYFYFPSLLLQKAAGGYGAIRIYNpelVPVPFPKPDEEYDILIG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 152 DWsntkpeqilknlkkegdYYSPRFPLQPSLvkfmhdykkgSAGERKQlfndykmmqqmrmsiydfsdvAYDAFLLNGQP 231
Cdd:PLN02168  166 DW-----------------FYADHTVMRASL----------DNGHSLP---------------------NPDGILFNGRG 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 232 KFKPWTALvKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVKIQKN-----RPY 306
Cdd:PLN02168  198 PEETFFAF-EPGKTYRLRISNVGLKTCLNFRIQDHDMLLVETEGTYVQKRVYSSLDIHVGQSYSVLVTAKTDpvgiyRSY 276

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1179981522 307 IIYAESLDTVGAAYGAlvtssqHVVDYQKVPPFPE-PLPVS 346
Cdd:PLN02168  277 YIVATARFTDAYLGGV------ALIRYPNSPLDPVgPLPLA 311
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 144-299 3.01e-14

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: 70.81  E-value: 3.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 144 KDFVVVLSDWSNTKPEQILKNLKKEGDYYsPRFPLQPslvkfmhdykkgsagerkqlfndykmmqqmrmsiydfsdvayD 223
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKELLASGKAP-TDFPPVP------------------------------------------D 37

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1179981522 224 AFLLNGQPKFKPWTALVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVK 299
Cdd:pfam00394  38 AVLINGKDGASLATLTVTPGKTYRLRIINVALDDSLNFSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVT 113
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 604-687 3.48e-14

The third cupredoxin domain of the 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 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: 259964 [Multi-domain]  Cd Length: 139  Bit Score: 70.37  E-value: 3.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 604 IRLEPGKRYRFVFTNTSMM---HHPMHIHGH-WFILRKGNDAYD-------------PLLHTIDVPPGATITADVDTDAS 666
Cdd:cd13897    34 KVLEYGSTVEIVLQGTSLLaaeNHPMHLHGFdFYVVGRGFGNFDpstdpatfnlvdpPLRNTVGVPRGGWAAIRFVADNP 113

                          90       100
                  ....*....|....*....|.
gi 1179981522 667 GQWFFHCHFLYHMMTGMSRVF 687
Cdd:cd13897   114 GVWFMHCHFERHTSWGMATVF 134
PRK10965 PRK10965
multicopper oxidase; Provisional
 16-152 6.06e-14

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 75.45  E-value: 6.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  16 AKRVVDLVVGYKTVSFAGKPRIAIA-VNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHVSqkaI 94
Cdd:PRK10965   44 ARGRIQLTIQAGQSSFAGKTATATWgYNGNLLGPAVRLQRGKAVTVDITNQLPEETTLHWHGLEVPGEVDGGPQGI---I 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1179981522  95 PPGGVFHYRFVLKQ-SGTYWYHAHAE----LQEQQGLYGAFVIDPIKA-----PKYKYMKDFVVVLSD 152
Cdd:PRK10965  121 APGGKRTVTFTVDQpAATCWFHPHQHgktgRQVAMGLAGLVLIEDDESlklglPKQWGVDDIPVILQD 188
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 401-529 1.61e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 74.95  E-value: 1.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 401 NTLSSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDS 480
Cdd:NF033609  585 DSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDS 664

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1179981522 481 NMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  665 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 713
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.79e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 74.95  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  594 SASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 673

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  674 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 719
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.85e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 74.95  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  606 SASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 685

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  686 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 731
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 2.00e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 74.56  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  600 SASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 679

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  680 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 725
CuRO_2_MCO_like_2 cd13887
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 216-300 3.17e-13

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 oxidise 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 family of MCOs 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: 259954 [Multi-domain]  Cd Length: 114  Bit Score: 66.96  E-value: 3.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 216 DFSDVAYDAFLLNGQPKFKPWTALVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYD 295
Cdd:cd13887     4 DLNDVDYDAFLANDRTLDDPEVVRVEPGGRVRLRVINGSTATNFHIDLGDLKGTLIAVDGNPVQPVEGRRFPLATAQRLD 83


                  ....*
gi 1179981522 296 VLVKI 300
Cdd:cd13887    84 LLVTI 88
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-573 6.05e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 73.02  E-value: 6.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  718 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 797

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMPTEPTIIGDKMGPPTSSYKTSMGTKYQPmia 563
Cdd:NF033609  798 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVP--- 874

                         170
                  ....*....|
gi 1179981522 564 avktndPNTP 573
Cdd:NF033609  875 ------PNSP 878
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
 38-303 7.15e-13

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 72.39  E-value: 7.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  38 AIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVL---VPWQmDGVEHvSQKAIPPGGVFHYRFVLK-QSGTYW 113
Cdd:PLN00044   50 AIGINGQFPGPALNVTTNWNLVVNVRNALDEPLLLTWHGVQqrkSAWQ-DGVGG-TNCAIPAGWNWTYQFQVKdQVGSFF 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 114 YHAHAELQEQQGLYGAFVID-----PIKAPkYKYMKDFVVVLSDWSNTKPeqilKNLKKEGDYYSPRFPLQPSLVKFMHD 188
Cdd:PLN00044  128 YAPSTALHRAAGGYGAITINnrdviPIPFG-FPDGGDITLFIADWYARDH----RALRRALDAGDLLGAPDGVLINAFGP 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 189 YKkgsagerkqlFNDYKMMqqmrmsiydfSDVAYDAflLNGQPkfkpwtalvkkGDVVRLRFIGAGGSTIFRVKIPGSVM 268
Cdd:PLN00044  203 YQ----------YNDSLVP----------PGITYER--INVDP-----------GKTYRFRVHNVGVATSLNFRIQGHNL 249

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1179981522 269 QMVHAQGNDVNPYTIKDFAIASGETYDVLVKIQKN 303
Cdd:PLN00044  250 LLVEAEGSYTSQQNYTNLDIHVGQSYSFLLTMDQN 284
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 7.18e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 73.02  E-value: 7.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  582 SGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSD 661

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  662 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 707
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 8.88e-13

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 72.63  E-value: 8.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  576 SDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSD 655

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  656 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 701
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.23e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 72.25  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  688 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 767

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  768 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 813
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.56e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.86  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  694 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 773

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  774 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 819
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.70e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.48  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  700 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 779

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  780 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 825
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.76e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.48  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  682 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 761

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  762 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 807
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.90e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.48  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  618 SASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 697

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMkmDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  698 SDSDSDSDSDS--DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 741
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 2.39e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.09  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  676 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 755

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  756 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 801
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 2.41e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.09  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  706 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 785

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  786 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 831
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 2.67e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.09  E-value: 2.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  612 SASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 691

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMkmDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  692 SDSDSDSDSDSDSDSDS--DSDSDSDSDSDSDSDSDSDSDSDSDSD 735
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 405-529 2.83e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 71.09  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 405 SSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMKM 484
Cdd:NF033609  571 SDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDS 650

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1179981522 485 DSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  651 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 695
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 2.98e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 70.71  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  624 SASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 703

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMkmDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  704 SDSDS--DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 747
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 42-134 3.01e-12

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 64.15  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  42 NNQIPAPTLRFKEGDEITINVSNHMDK--PTSIHWHGVLVPWqmdGVEHVSqkaIPPGGVFHYRFVLKQSGTYWYH---A 116
Cdd:cd11020    27 NGQVPGPVIRVREGDTVELTLTNPGTNtmPHSIDFHAATGPG---GGEFTT---IAPGETKTFSFKALYPGVFMYHcatA 100

                          90
                  ....*....|....*...
gi 1179981522 117 HAELQEQQGLYGAFVIDP 134
Cdd:cd11020   101 PVLMHIANGMYGAIIVEP 118
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 3.11e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 70.71  E-value: 3.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  712 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 791

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  792 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 837
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 3.53e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 70.71  E-value: 3.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  670 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 749

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  750 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 795
PLN02835 PLN02835
oxidoreductase
 4-340 3.81e-12

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 70.00  E-value: 3.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522   4 LTSLLVVTNVFSAKRVVDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLV---P 80
Cdd:PLN02835   16 VLSSVSLVNGEDPYKYYTWTVTYGTISPLGVPQQVILINGQFPGPRLDVVTNDNIILNLINKLDQPFLLTWNGIKQrknS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  81 WQmDGVEHvSQKAIPPGGVFHYRFVLK-QSGTYWYHAHAELQEQQGLYGAFVID-----PIKAPKYKymKDFVVVLSDWS 154
Cdd:PLN02835   96 WQ-DGVLG-TNCPIPPNSNYTYKFQTKdQIGTFTYFPSTLFHKAAGGFGAINVYerpriPIPFPLPD--GDFTLLVGDWY 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 155 NTKPEQILKNLKKEGdyySPRFPlqpslvkfmhdykkgsagerkqlfndykmmqqmrmsiydfsdvayDAFLLNGQPKFk 234
Cdd:PLN02835  172 KTSHKTLQQRLDSGK---VLPFP---------------------------------------------DGVLINGQTQS- 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 235 pwTALVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVKI-QKNRPYIIYAES- 312
Cdd:PLN02835  203 --TFSGDQGKTYMFRISNVGLSTSLNFRIQGHTMKLVEVEGSHTIQNIYDSLDVHVGQSVAVLVTLnQSPKDYYIVASTr 280

                         330       340
                  ....*....|....*....|....*....
gi 1179981522 313 -LDTVGAAYGALVTSSQHVVDYQKVPPFP 340
Cdd:PLN02835  281 fTRQILTATAVLHYSNSRTPASGPLPALP 309
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 4.02e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 70.32  E-value: 4.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  664 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 743

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  744 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 789
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 590-683 5.58e-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: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 64.08  E-value: 5.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 590 IWFINGVPAYKAHP-IRLEPGKRYRFVFTNTSMMHHPMHIHGHWFILRKGNDAYDPLLHTIDVPPGATITADVDTDASGQ 668
Cdd:cd13909    36 FWAFNGVAGRPDDPlLEARRGETVRIEMVNNTGFPHGMHLHGHHFRAILPNGALGPWRDTLLMDRGETREIAFVADNPGD 115

                          90
                  ....*....|....*
gi 1179981522 669 WFFHCHFLYHMMTGM 683
Cdd:cd13909   116 WLLHCHMLEHAAAGM 130
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 5.60e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 69.94  E-value: 5.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  658 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 737

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  738 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 783
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 6.31e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 69.94  E-value: 6.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMk 483
Cdd:NF033609  630 SASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS- 708

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 mDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  709 -DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 753
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 8.22e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 69.55  E-value: 8.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMk 483
Cdd:NF033609  648 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS- 726

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 mDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  727 -DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 771
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 8.22e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 69.55  E-value: 8.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMKMDSNMK 483
Cdd:NF033609  652 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 731

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  732 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 777
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 9.58e-12

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 69.17  E-value: 9.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMKMDSNMkmDSNMK 483
Cdd:NF033609  636 SASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS--DSDSD 713

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  714 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 759
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 404-529 1.18e-11

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 68.78  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 404 SSSMSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSSMKMDSSMkmDSNMKMDSNMK 483
Cdd:NF033609  642 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS--DSDSDSDSDSD 719

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1179981522 484 MDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSNMKMDSN 529
Cdd:NF033609  720 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 765
PLN02991 PLN02991
oxidoreductase
 2-344 4.82e-11

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 66.58  E-value: 4.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522   2 VLLTSLLVVTNVFSAK--RVVDLVVGYKTVSFAGKPRIAIAVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLv 79
Cdd:PLN02991   11 MILGLLFLISFVAAEDpyRFFEWHVTYGNISPLGVAQQGILINGKFPGPDIISVTNDNLIINVFNHLDEPFLISWSGIR- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  80 PWQ---MDGVeHVSQKAIPPGGVFHYRFVLK-QSGTYWYHAHAELQEQQGLYGAFVID-------PIKAPKykymKDFVV 148
Cdd:PLN02991   90 NWRnsyQDGV-YGTTCPIPPGKNYTYALQVKdQIGSFYYFPSLGFHKAAGGFGAIRISsrplipvPFPAPA----DDYTV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 149 VLSDWSNTKPEQILKNLKKEGdyyspRFPLQpslvkfmhdykkgsagerkqlfndykmmqqmrmsiydfsdvayDAFLLN 228
Cdd:PLN02991  165 LIGDWYKTNHKDLRAQLDNGG-----KLPLP-------------------------------------------DGILIN 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 229 GQPKFKpwTALVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDV--NPYTIKDFAIasGETYDVLVKI-QKNRP 305
Cdd:PLN02991  197 GRGSGA--TLNIEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTHTiqTPFSSLDVHV--GQSYSVLITAdQPAKD 272

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1179981522 306 YIIyaesldTVGAAYGALVTSSQHVVDY-QKVPPFPEPLP 344
Cdd:PLN02991  273 YYI------VVSSRFTSKILITTGVLHYsNSAGPVSGPIP 306
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 602-688 5.21e-11

The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi, plants and insects. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 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: 259972 [Multi-domain]  Cd Length: 174  Bit Score: 62.31  E-value: 5.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 602 HPIRLEPGKRYRFVFTNTSM---MHHPMHIHGHWFI------------------------------LRKGNDAYDPLLHT 648
Cdd:cd13905    45 HVIKLPLNSVVEIVLINEGPgpgLSHPFHLHGHSFYvlgmgfpgynsttgeilsqnwnnklldrggLPGRNLVNPPLKDT 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1179981522 649 IDVPPGATITADVDTDASGQWFFHCHFLYHMMTGMSRVFQ 688
Cdd:cd13905   125 VVVPNGGYVVIRFRADNPGYWLLHCHIEFHLLEGMALVLK 164
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 586-688 1.59e-10

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: 59.72  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 586 MDRFIWFINGVP-AYKAHPIRLEPGKRYRFVFTNTSMMHHPMHIHGHWF--ILRKGNDAYDPLL---HTIDVPPGATITA 659
Cdd:cd13902    16 AGGMMFLINGKTfDMNRIDFVAKVGEVEVWEVTNTSHMDHPFHLHGTQFqvLEIDGNPQKPEYRawkDTVNLPPGEAVRI 95

                          90       100
                  ....*....|....*....|....*....
gi 1179981522 660 DVDTDASGQWFFHCHFLYHMMTGMSRVFQ 688
Cdd:cd13902    96 ATRQDDPGMWMYHCHILEHEDAGMMGMLH 124
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 602-694 2.46e-10

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


Pssm-ID: 259966 [Multi-domain]  Cd Length: 160  Bit Score: 59.96  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 602 HPIRLEPGKRYRFVFTNTSMMHHPMHIHGHWF-ILRKGNDAYDPLLH--------------TIDVPPGATITADVDTDAS 666
Cdd:cd13899    56 NAFVLNHGEVVELVVNNWDAGKHPFHLHGHKFqVVQRSPDVASDDPNppinefpenpmrrdTVMVPPGGSVVIRFRADNP 135

                          90       100
                  ....*....|....*....|....*...
gi 1179981522 667 GQWFFHCHFLYHMMTGMSrvfqySTLIE 694
Cdd:cd13899   136 GVWFFHCHIEWHLEAGLA-----ATFIE 158
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 588-683 7.08e-10

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 57.24  E-value: 7.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 588 RFIWFINGVPAYKAHPIRLEPGKRYRFVFTNTSMMHHPMHIHGH--WFILRKGNdAYDPLLHTIDVPPGATITADVDTDA 665
Cdd:cd00920     9 GWSFTYNGVLLFGPPVLVVPVGDTVRVQFVNKLGENHSVTIAGFgvPVVAMAGG-ANPGLVNTLVIGPGESAEVTFTTDQ 87

                          90
                  ....*....|....*...
gi 1179981522 666 SGQWFFHCHFLYHMMTGM 683
Cdd:cd00920    88 AGVYWFYCTIPGHNHAGM 105
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 42-134 8.09e-10

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 57.50  E-value: 8.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  42 NNQIPAPTLRFKEGDEITINVSNHMDK--PTSIHWHGVLVPwQMDGvehvSQKAIPPGGVFHYRFVLKQSGTYWYHAHAE 119
Cdd:cd04201    27 DGDIPGPMLRVREGDTVELHFSNNPSStmPHNIDFHAATGA-GGGA----GATFIAPGETSTFSFKATQPGLYVYHCAVA 101

                          90
                  ....*....|....*...
gi 1179981522 120 ---LQEQQGLYGAFVIDP 134
Cdd:cd04201   102 pvpMHIANGMYGLILVEP 119
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 624-687 1.01e-09

The third 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. 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: 259970 [Multi-domain]  Cd Length: 147  Bit Score: 57.67  E-value: 1.01e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1179981522 624 HPMHIHGHWF--ILRKGNDAY---DPLLHtiDV----PPGATITADVDTDASGQWFFHCHFLYHMMTGMSRVF 687
Cdd:cd13903    73 HPFHLHGHAFsvVRSAGSNTYnyvNPVRR--DVvsvgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVF 143
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 583-680 1.85e-09

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: 56.48  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 583 FGYMDRFIWFINGVP-AYKAHPIRLEPGKRYRFVFTNTSMMHHPMHIHGHWF-ILRKGNDAYDP--LLHTIDVPPGATIT 658
Cdd:cd13900    12 MSPGGGGAFTINGKPfDPDRPDRTVRLGTVEEWTLINTSGEDHPFHIHVNPFqVVSINGKPGLPpvWRDTVNVPAGGSVT 91

                          90       100
                  ....*....|....*....|....*..
gi 1179981522 659 ADVD-TDASGQWFFHCHFLYH----MM 680
Cdd:cd13900    92 IRTRfRDFTGEFVLHCHILDHedqgMM 118
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 614-688 1.10e-08

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: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 55.38  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 614 FVFTNTSMMHHPMHIHGHWF-ILRKGNDAYDPLLHTidVPPGATI---------TADVD----------TDASGQWFFHC 673
Cdd:cd13910    73 LVINNLDDGDHPFHLHGHKFwVLGSGDGRYGGGGYT--APDGTSLnttnplrrdTVSVPgfgwavlrfvADNPGLWAFHC 150

                          90
                  ....*....|....*
gi 1179981522 674 HFLYHMMTGMSRVFQ 688
Cdd:cd13910   151 HILWHMAAGMLMQFA 165
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 588-684 6.36e-08

The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces; The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 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: 259968 [Multi-domain]  Cd Length: 157  Bit Score: 53.00  E-value: 6.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 588 RFIWFINGVPAY--KAHPIRL--------------------EPGKRYRFVFTNTSMMHHPMHIHGH-WFILRKGNDAYDP 644
Cdd:cd13901    23 VFLWTLNGSSFRvdWNDPTLLlvadgntstfppewnvielpKANKWVYIVIQNNSPLPHPIHLHGHdFYILAQGTGTFDD 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1179981522 645 LLHTI--------DV---PPGATITADVDTDASGQWFFHCHFLYHMMTGMS 684
Cdd:cd13901   103 DGTILnlnnpprrDVamlPAGGYLVIAFKTDNPGAWLMHCHIAWHASGGLA 153
CuRO_3_MCO_like_5 cd13911
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 591-688 3.13e-07

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: 49.85  E-value: 3.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 591 WFINGVPAYKAHP-IRLEPGKRYRFVFTntSMMHHPMHIHG-HWFILRKGNDAYDPLLH----TIDVPPGATITADVDTD 664
Cdd:cd13911    17 WTVNGKVFDPDHIaARPRLGTTEIWVFS--SDGRHPVHLHGaHFQVVSRTGGRPGEWDAgwkdTVLLRPRESVTVIIRFD 94

                          90       100
                  ....*....|....*....|....*
gi 1179981522 665 A-SGQWFFHCHFLYHMMTGMSRVFQ 688
Cdd:cd13911    95 GyRGRYVFHCHNLEHEDMGMMANFQ 119
CuRO_3_CueO_FtsP cd13890
The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 617-683 3.22e-07

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: 49.94  E-value: 3.22e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1179981522 617 TNTSMMHHPMHIHGHWF-IL-RKGNDAYDPLL---HTIDVPPGAT----ITADVDTDASGQWFFHCHFLYHMMTGM 683
Cdd:cd13890    43 TNTDGMPHPFHIHGVQFrILsRNGQPPPPNEAgwkDTVWVPPGETvrilVKFDHYADPTGPFMYHCHILEHEDNGM 118
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 45-134 5.12e-07

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: 49.96  E-value: 5.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  45 IPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEhVSQKAIPPGG--VFHYR-----------FVLKQSGT 111
Cdd:cd14449    27 VPGPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTG-MNASIVAPGDtrIYTWRthggyrradgsWAEGTAGY 105

                          90       100
                  ....*....|....*....|....*....
gi 1179981522 112 YWYHAHAELQEQ------QGLYGAFVIDP 134
Cdd:cd14449   106 WHYHDHVFGTEHgteglsRGLYGALIVRR 134
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
 217-314 5.70e-07

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: 49.92  E-value: 5.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 217 FSDVAYDAFLLNGQ-----PKFKPWTAL------VKKGDVVRLRFIGAGGSTI-FRVKIPGSVMQMVHAQGNDVNPYTIK 284
Cdd:cd13884    25 GGGQPPDSILINGKgryydPKTGNTNNTplevftVEQGKRYRFRLINAGATNCpFRVSIDGHTLTVIASDGNDVEPVEVD 104

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1179981522 285 DFAIASGETYDVLVKiqKNRP---YIIYAESLD 314
Cdd:cd13884   105 SIIIYPGERYDFVLN--ANQPignYWIRARGLE 135
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 227-317 7.01e-07

The second 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. MCOs couple oxidation of substrates with reduction of dioxygen 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: 259939 [Multi-domain]  Cd Length: 166  Bit Score: 50.23  E-value: 7.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 227 LNGQPKFKPWTALVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVKIQKNrPY 306
Cdd:cd13871    63 NKSNPQCAPFILHVSPGKTYRLRIASVTALSSLNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTADQD-PS 141

                          90
                  ....*....|.
gi 1179981522 307 IIYAESLDTVG 317
Cdd:cd13871   142 RNYWVSVNVRG 152
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 591-687 8.24e-07

The third 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 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: 259960 [Multi-domain]  Cd Length: 155  Bit Score: 49.73  E-value: 8.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 591 WFINGVPAYKAHPIRLEPGKRYRFVF--------------TNTSMMHHPMHIHGHWF-ILRKGNDAYDPLLH-------- 647
Cdd:cd13893    20 WAINNVSYVPPPTPYLAALPVYPFKGgdvvdvilqnantnTRNASEQHPWHLHGHDFwVLGYGLGGFDPAADpsslnlvn 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1179981522 648 -----TIDVPPGATITADVDTDASGQWFFHCHFLYHMMTGMSRVF 687
Cdd:cd13893   100 ppmrnTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGMGVVF 144
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 609-688 1.03e-06

cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin homologous proteins. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. Ceruloplasmin also functions in copper transport, amine oxidase and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first domain of the triplicated units.


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 48.37  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 609 GKRYRFVFT--NTSMMHHPMHIHGHwfILRKGNDAYDPLLHTIdvpPGATITADVDTDASGQWFFHCHFLYHMMTGMSRV 686
Cdd:cd11023    41 GKRVRWHLVayGNEVDFHTPHWHGQ--TVEADKSRRTDVAELM---PASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQ 115


                  ..
gi 1179981522 687 FQ 688
Cdd:cd11023   116 FA 117
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 48-117 1.72e-06

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 47.61  E-value: 1.72e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1179981522  48 PTLRFKEGDEITINVSNHMDKPTSIHWHGVLVP-WQMDGVEH---VSQKAIPPGGVFHYRFVLKQSGTYWYHAH 117
Cdd:cd00920    23 PVLVVPVGDTVRVQFVNKLGENHSVTIAGFGVPvVAMAGGANpglVNTLVIGPGESAEVTFTTDQAGVYWFYCT 96
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 48-132 3.93e-06

The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 1 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259888 [Multi-domain]  Cd Length: 165  Bit Score: 47.93  E-value: 3.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  48 PTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQ------MDGVEHVSQK--AIPPGGVFHYRF-VLKQSG-------- 110
Cdd:cd04226    57 PTLRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKsegslySDNTSPVEKLddAVQPGQEYTYVWdITEEVGpteadppc 136

                          90       100
                  ....*....|....*....|....*
gi 1179981522 111 -TYWYHAHAELQE--QQGLYGAFVI 132
Cdd:cd04226   137 lTYIYYSHVNMVRdfNSGLIGALLI 161
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 240-299 4.71e-06

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 oxidise 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 family of MCOs 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: 259953 [Multi-domain]  Cd Length: 163  Bit Score: 47.65  E-value: 4.71e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 240 VKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVK 299
Cdd:cd13886    66 LEPNKTYRLRLINAGSFADFTFSVDGHPLTVIEADGTLVEPVEVHSITISVAQRYSVILT 125
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 48-132 5.44e-06

cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin homologous proteins. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. Ceruloplasmin also functions in copper transport, amine oxidase and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first domain of the triplicated units.


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 47.80  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  48 PTLRFKEGDEITINVSNHMDK-PTSIHWHGVLVPWQMDGVEHVSQKAIPPGGVFHYRFVLKQ----------SGTYWYHA 116
Cdd:cd04229    74 PVIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGAGDVVAPGETYTYRWIVPEdagpgpgdpsSRLWLYHS 153

                          90
                  ....*....|....*...
gi 1179981522 117 HAELQEQQ--GLYGAFVI 132
Cdd:cd04229   154 HVDVFAHTnaGLVGPIIV 171
CuRO_3_McoP_like cd13888
The third cupredoxin domain of multicopper oxidase McoP and similar proteins; This subfamily ...
 586-683 6.29e-06

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: 46.79  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 586 MDRFIWFING---VPAYKAHPIRLEPGKRYRFVFTN-TSMMHHPMHIHGH--WFILRKGN------DAYDP--------- 644
Cdd:cd13888    10 MGRMQWTINGetwADDPDAFPVERVGGTVEIWELVNdAASMPHPMHIHGFqfQVLERSDSppqvaeLAVAPsgrtatdlg 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1179981522 645 LLHTIDVPPGATITADVDTDAS---GQWF-FHCHFLYHMMTGM 683
Cdd:cd13888    90 WKDTVLVWPGETVRIAVDFTHDypgDQLYlLHCHNLEHEDDGM 132
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 591-693 8.32e-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: 45.72  E-value: 8.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 591 WFING-VPAykahP-IRLEPGKRYRFVFTNTSMMHHPMHIHGHwfilrkgNDAYDPLLHTIDVPPGATITADVDTDASGQ 668
Cdd:cd11024    24 WTYNGtVPG----PtLRATEGDLVRIHFINTGDHPHTIHFHGI-------HDAAMDGTGLGPIMPGESFTYEFVAEPAGT 92

                          90       100
                  ....*....|....*....|....*...
gi 1179981522 669 WFFHCHF---LYHMMTGMsrvfqYSTLI 693
Cdd:cd11024    93 HLYHCHVqplKEHIAMGL-----YGAFI 115
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 147-305 1.50e-05

The second 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 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: 259950 [Multi-domain]  Cd Length: 164  Bit Score: 46.18  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 147 VVVLSDWSNTKPEQILKNLKKEGDYYSPRFPLQPslvkfmhdykkgsagerkqlfndykmmqqmrmsiydfsdvayDAFL 226
Cdd:cd13883     2 VLFISDWYHDQSEVIVAGLLSPQGYKGSPAAPSP------------------------------------------DSAL 39

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 227 LNGQPKF--------------KPWTALVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVN-PYTIKDFAIASG 291
Cdd:cd13883    40 INGIGQFncsaadpgtcctqtSPPEIQVEAGKRTRFRLINAGSHAMFRFSVDNHTLNVVEADDTPVYgPTVVHRIPIHNG 119

                         170
                  ....*....|....
gi 1179981522 292 ETYDVLVKIQKNRP 305
Cdd:cd13883   120 QRYSVIIDTTSGKA 133
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 223-315 1.61e-05

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: 45.62  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 223 DAFLLNGQ--PKFKpwtalVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDVLVKI 300
Cdd:cd13877    36 DSSLFNDTqnATIN-----FEPGKTYLLRIINMGAFASQYFHIEGHDMTIIEVDGVYVKPYPVDTLYIAVGQRYSVLVKA 110

                          90
                  ....*....|....*..
gi 1179981522 301 QKN--RPYIIYAeSLDT 315
Cdd:cd13877   111 KNDtdRNYAIIN-GMDK 126
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 593-676 2.75e-05

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: 45.00  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 593 INGVPAYKAHPIRLEPGKRYRFVFTNTSMM-HHPMHIHGH--WFILRKGNdAYDPL-LHTIDVPPGATITADVDTD-ASG 667
Cdd:pfam00394  41 INGKDGASLATLTVTPGKTYRLRIINVALDdSLNFSIEGHkmTVVEVDGV-YVNPFtVDSLDIFPGQRYSVLVTANqDPG 119


                  ....*....
gi 1179981522 668 QWFFHCHFL 676
Cdd:pfam00394 120 NYWIVASPN 128
DUF6612 pfam20316
Family of unknown function (DUF6612); This family of proteins is functionally uncharacterized. ...
 361-529 3.15e-05

Family of unknown function (DUF6612); This family of proteins is functionally uncharacterized. However, based on similarity to other families it is likely to be involved in lipoprotein biosynthesis. This family of proteins is found in bacteria. Proteins in this family are typically between 263 and 293 amino acids in length.


Pssm-ID: 466466  Cd Length: 237  Bit Score: 46.51  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 361 TLPQVIKSSIKKkgvnhSPKMKMSSMSHEMShkklhpmQKNTLSSSMSNMKMDSNMKMD-----SNMKMDSNMKMDSNMK 435
Cdd:pfam20316   1 TAEEVITKATEA-----SKKLKSFSMDMEMK-------QNITSSQGKQEQKTDSTMKMDfitepLAMHQKMTMSMPGQGE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 436 MDSNMKMDSN------------MKMDSNMKMDSNMKMDSSMKMDSSMKM-------------------------DSNMKM 478
Cdd:pfam20316  69 QEIEQYITKDgiymydqtqgqwMKLPDEMSEQLLKASKQQANPEKQLKQlksiakdfkvteegdnyvltasgsgDKVKEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1179981522 479 DSN-MKMDSNMKMDSNMKMDSNMKMDS---------------NMKMDSNMKMDSN-MKMDSNMKMDSN 529
Cdd:pfam20316 149 AKElMKSQSPAGAAEQTAMLKQMKIKKvdytytvdkktylptKMDVDMDMEMEEEgQKVSMDQKMKST 216
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 615-688 6.02e-05

The third 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 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: 259965 [Multi-domain]  Cd Length: 164  Bit Score: 44.56  E-value: 6.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 615 VFTNTSMMH--HPMHIHG-HWFILRKGNDAYD--------------------PLLHTIDVPPGATITADV----DTDASG 667
Cdd:cd13898    62 IFQVTGPPQppHPIHKHGnKAFVIGTGTGPFNwssvaeaaeaapenfnlvnpPLRDTFTTPPSTEGPSWLviryHVVNPG 141

                          90       100
                  ....*....|....*....|.
gi 1179981522 668 QWFFHCHFLYHMMTGMSRVFQ 688
Cdd:cd13898   142 AWLLHCHIQSHLAGGMAVVLL 162
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 223-298 7.75e-05

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: 43.94  E-value: 7.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 223 DAFLLNGQPKFK--PWTAL----VKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGETYDV 296
Cdd:cd13882    28 DSGTINGKGRFDggPTSPLavinVKRGKRYRFRVINISCIPSFTFSIDGHNLTVIEADGVETKPLTVDSVQIYAGQRYSV 107


                  ..
gi 1179981522 297 LV 298
Cdd:cd13882   108 VV 109
PRK10883 PRK10883
FtsI repressor; Provisional
 30-152 8.88e-05

FtsI repressor; Provisional


Pssm-ID: 182808 [Multi-domain]  Cd Length: 471  Bit Score: 46.24  E-value: 8.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  30 SFAGKPRIAI-AVNNQIPAPTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPW-QMDGvehvSQKAIPPGG----VFHYR 103
Cdd:PRK10883   58 SFTGGTKASVwGINGRYLGPTIRVWKGDDVKLIYSNRLTEPVSMTVSGLQVPGpLMGG----PARMMSPNAdwapVLPIR 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 104 fvlKQSGTYWYHAHAELQEQQ----GLYGAFVID-------PIkaPKYKYMKDFVVVLSD 152
Cdd:PRK10883  134 ---QNAATCWYHANTPNRMAQhvynGLAGMWLVEdevskslPI--PNHYGVDDFPVIIQD 188
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
 223-299 1.21e-04

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: 43.36  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 223 DAFLLNGQP----------KFKpwtALVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFAIASGE 292
Cdd:cd13875    31 DAYTINGQPgdlyncsskdTFV---LTVEPGKTYLLRIINAALNEELFFKIANHTLTVVAVDASYTKPFTTDYILIAPGQ 107


                  ....*..
gi 1179981522 293 TYDVLVK 299
Cdd:cd13875   108 TTDVLLT 114
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 45-134 2.11e-04

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: 42.42  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  45 IPAPTLRFKEGDEITINVSNHMDKPTSIHWHGV---LV-----PWQMDGVEHVSQK--------AIPPGGVFHYRFVLKQ 108
Cdd:pfam07731  31 PNTNVITLPYGTVVEWVLQNTTTGVHPFHLHGHsfqVLgrgggPWPEEDPKTYNLVdpvrrdtvQVPPGGWVAIRFRADN 110

                          90       100
                  ....*....|....*....|....*.
gi 1179981522 109 SGTYWYHAHAELQEQQGLYGAFVIDP 134
Cdd:pfam07731 111 PGVWLFHCHILWHLDQGMMGQFVVRP 136
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 48-132 2.42e-04

The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the first cupredoxin domain of ceruloplasmin.


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 43.18  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  48 PTLRFKEGDEITINVSNHMDKPTSIHWHGV---------LVPWQMDGVEHvSQKAIPPGGVFHYRFVLKQSG-------- 110
Cdd:cd04222    76 PILKAEVGDVIVVHLKNFASRPYSLHPHGVfynkenegaLYPDNTSGFEK-ADDAVPPGGSYTYTWTVPEEQaptkadan 154

                          90       100
                  ....*....|....*....|....*.
gi 1179981522 111 --TYWYHAH--AELQEQQGLYGAFVI 132
Cdd:cd04222   155 clTRIYHSHidAPKDIASGLIGPLII 180
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 48-132 5.92e-04

Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the first, third, and fifth cupredoxin domains of ceruloplasmin and similar proteins including the first, third and fifth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. It functions in copper transport, amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. Human Factor VIII facilitates blood clotting by acting as a cofactor for factor IXa. Factor VIII and IXa forms a complex in the presence of Ca+2 and phospholipids that converts factor X to the activated form Xa.


Pssm-ID: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 41.62  E-value: 5.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522  48 PTLRFKEGDEITINVSNHMDKPTSIHWHGVLVPWQMDGVEHVSQK--------AIPPGGVFHYRF-VLKQSG-------- 110
Cdd:cd04199    70 PTIRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTgpdekkddAVAPGETYTYVWiVTEESGptkgdpac 149

                          90       100
                  ....*....|....*....|....*
gi 1179981522 111 -TYWYHAHAELQEQ--QGLYGAFVI 132
Cdd:cd04199   150 lTWAYYSHVDLEKDinSGLIGPLLI 174
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 624-687 6.81e-04

The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal proteins with similarity to ascorbate oxidase. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to multicopper oxidase (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 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: 259962 [Multi-domain]  Cd Length: 188  Bit Score: 41.92  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 624 HPMHIHG-HWFILRKGNDAYDPLLH---------------TIDVPPGATITADVDTDAS-------------GQWFFHCH 674
Cdd:cd13895    93 HPWHAHGaHYYDLGSGLGTYSATALaneeklrgynpirrdTTMLYRYGGKGYYPPPGTGsgwrawrlrvddpGVWMLHCH 172

                          90
                  ....*....|...
gi 1179981522 675 FLYHMMTGMSRVF 687
Cdd:cd13895   173 ILQHMIMGMQTVW 185
CuRO_3_PHS cd13892
The third Cupredoxin domain of phenoxazinone synthase (PHS); Phenoxazinone synthase (PHS, ...
 609-687 7.34e-04

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: 41.75  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 609 GKRYRFVFTNTSMMH-HPMHIH-GHWFILRKgnDAYD---------------------PLLH-------TIDVPPGATIT 658
Cdd:cd13892    71 GSWERWTFVNLGEGHpHPMHIHlAEFQVLER--QPYDvtgfdttvggtdrpitpgeaaPLEPvelgwkdTVVVGPGELVT 148

                          90       100       110
                  ....*....|....*....|....*....|
gi 1179981522 659 ADVDTD-ASGQWFFHCHFLYHMMTGMSRVF 687
Cdd:cd13892   149 VLVQFDgATGRFMYHCHILEHEDHDMMRPF 178
CuRO_3_CotA_like cd13891
The third Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat ...
 616-680 8.02e-04

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: 40.74  E-value: 8.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 616 FTNTSMMHHPMHIH------------------GHWFILRKGnDAYDPLLH------TIDVPPGATITADVD-TDASGQWF 670
Cdd:cd13891    46 IINLTPDAHPIHLHlvqfqvldrqpfdvdeynATGEIYYTG-PPRPPAPNergwkdTVRAYPGEVTRIIVRfDGPEGGYV 124

                          90
                  ....*....|....
gi 1179981522 671 FHCHFLYH----MM 680
Cdd:cd13891   125 WHCHILEHedneMM 138
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 624-682 1.04e-03

The third 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 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: 259971 [Multi-domain]  Cd Length: 158  Bit Score: 40.74  E-value: 1.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1179981522 624 HPMHIHGH-WFILRKGNDAYD-------------PLLH-TIDVPPGATITADVDTDASGQWFFHCHFLYHMMTG 682
Cdd:cd13904    78 HPYHLHGVdFHIVARGSGTLTleqlanvqynttnPLRRdTIVIPGGSWAVLRIPADNPGVWALHCHIGWHLAAG 151
CuRO_2_CumA_like cd13885
The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 226-300 1.16e-03

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: 40.00  E-value: 1.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1179981522 226 LLNG--QPKFKpwtalVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIKDFA--IASGETYDVLVKI 300
Cdd:cd13885    39 TINGrvQPDFT-----VRAGERVRLRLINAANARVFALKFPGHEARVIALDGQPAEPFVARNGAvvLAPGMRIDLVIDA 112
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 223-299 1.25e-03

The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces; The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. 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: 259947 [Multi-domain]  Cd Length: 167  Bit Score: 40.70  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 223 DAFLLNGQPKFKP-------WTALVKKGDVVRLRFIGAGGSTIFRVKIPGSVMQMVhaqGND---VNPYTIKDFAIASGE 292
Cdd:cd13880    31 DNILINGKGKFPCstgagsyFETTFTPGKKYRLRLINTGVDTTFRFSIDGHNLTVI---AADfvpIVPYTTDSLNIGIGQ 107


                  ....*..
gi 1179981522 293 TYDVLVK 299
Cdd:cd13880   108 RYDVIVE 114
CuRO_3_BOD cd13889
The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the ...
 590-681 1.33e-03

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: 39.60  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 590 IWFINGVPAYKAHPIRLEPGK----RYRFVfTNTSMMHHPMHIH--GHWFILRKGND----AYDPLLH-TIDVPPGATIT 658
Cdd:cd13889    14 MWTINGKTWADPNRIDAAPQLgtveIWTLI-NGGGGWSHPIHIHleDFQILSRNGGSravpPYERGRKdVVYLGPGEEVR 92

                          90       100
                  ....*....|....*....|....*...
gi 1179981522 659 ADVD-TDASGQWFFHCHFLYH----MMT 681
Cdd:cd13889    93 VLMRfRPFRGKYMMHCHNLVHedhdMML 120
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 624-688 3.13e-03

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 38.93  E-value: 3.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1179981522 624 HPMHIHGHWFILRKGNDAydpllhTIDVPPGATITADVDTDASGQWFFHCHFLYHMMTGMSRVFQ 688
Cdd:cd04200    82 HSIHFHGQTFLYKGYRID------TLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFL 140
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 206-304 3.65e-03

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


Pssm-ID: 259944 [Multi-domain]  Cd Length: 138  Bit Score: 38.72  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 206 MMQQMRMSIYDFSdvAYDAFLLNGQPKFKPWTALVKKGDV-VRLRFIGAGGSTIFRVKIPGSVMQMVHAQGNDVNPYTIK 284
Cdd:cd13876    16 YWKIMRASGIEPF--CYDSILINGKGRVYCLIVIVDPGERwVSLNFINAGGFHTLAFSIDEHPMWVYAVDGGYIEPQLVD 93

                          90       100
                  ....*....|....*....|
gi 1179981522 285 DFAIASGETYDVLVKIQKNR 304
Cdd:cd13876    94 AISITNGERYSVLVKLDKPP 113
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 624-683 4.36e-03

The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasis and copper transport in blood. It also functions in amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains with six copper centers; three mononuclear sites in domain 2, 4 and 6 and three in the form of trinuclear clusters at the interface of domains 1 and 6. Ceruloplasmin exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. This model represents the sixth cupredoxin domain of ceruloplasmin.


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 38.70  E-value: 4.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1179981522 624 HPMHIHGHWFILRKG----NDAYDpllhtidVPPGATITADVDTDASGQWFFHCHFLYHMMTGM 683
Cdd:cd11012    82 HTAHFHGHSFDYKHRgvyrSDVFD-------LFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGM 138
CuRO_1_BOD_CotA_like cd13844
The first Cupredoxin domain of Bilirubin oxidase (BOD), the bacterial endospore coat component ...
 69-118 4.55e-03

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: 38.81  E-value: 4.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1179981522  69 PTSIHWHGVLVPWQMDGVEHVSqkaIPPGGVFH-------YRFVLKQSG-TYWYHAHA 118
Cdd:cd13844    86 PTVVHLHGGEVPPESDGYPEAW---FTPGGEEGpgfgsatYYYPNDQSAaTLWYHDHA 140
CuRO_3_MCO_like_1 cd13907
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 586-687 4.56e-03

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: 38.62  E-value: 4.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 586 MDRFIWFINGVP-----AYKAHPIRLEPGKRYRFVFTNTSM-------------------MHHPMHIHGHWF--ILRKGN 639
Cdd:cd13907    10 MQHMEWTINGRSfemddVTPDETVKLNTTEVWEIINDLGGMgggggmmggggmmmggmmaMPHPIHLHGVQFqvLERSVG 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1179981522 640 DAYDPLLHTID-------------VPPGATITADVD-TDASGQWFFHCHFLYHMMTGMSRVF 687
Cdd:cd13907    90 PKDRAYWATVKdgfidegwkdtvlVMPGERVRIIKPfDDYKGLFLYHCHNLEHEDMGMMRNF 151
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 222-309 4.94e-03

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 37.60  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179981522 222 YDAFLLNGQPKFKPWTALVKKGDVVRLRFIgAGGSTIFRVKIPGSVMQMVHAQGNDvNPYTIKDFAIASGETYDVLVKIQ 301
Cdd:cd00920     9 GWSFTYNGVLLFGPPVLVVPVGDTVRVQFV-NKLGENHSVTIAGFGVPVVAMAGGA-NPGLVNTLVIGPGESAEVTFTTD 86


                  ....*...
gi 1179981522 302 KNRPYIIY 309
Cdd:cd00920    87 QAGVYWFY 94
 
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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