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Conserved domains on  [gi|50725931|dbj|BAD33459|]
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putative syringolide-induced protein B13-1-1 [Oryza sativa Japonica Group]

Protein Classification

multicopper oxidase( domain architecture ID 11496785)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
25-572 0e+00

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: 1004.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931    25 TRRHDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVAIHWHGIRQIGTPWADGTEGVTQCP 104
Cdd:TIGR03388   1 IRHYKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLHTEGVVIHWHGIRQIGTPWADGTAGVTQCA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   105 ILPGDTFAYTFVVDRPGTYMYHAHYGMQRSAGLNGMIVVEVApgaagDGEREPFRYDGEHTVLLNDWWHRSTYEQAAGLA 184
Cdd:TIGR03388  81 INPGETFIYNFVVDRPGTYFYHGHYGMQRSAGLYGSLIVDVP-----DGEKEPFHYDGEFNLLLSDWWHKSIHEQEVGLS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   185 SVPMVWVGEPQSLLINGRGRFvNCSSSP----ATAASCNVS-HPDCAPAVFAVVPGKTYRFRVASVTSLSALNFEIEGHE 259
Cdd:TIGR03388 156 SKPMRWIGEPQSLLINGRGQF-NCSLAAkfssTNLPQCNLKgNEQCAPQILHVEPGKTYRLRIASTTALAALNFAIEGHK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   260 MTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATPTGTAVLAYYGgrrNSPRARPPTPPP 339
Cdd:TIGR03388 235 LTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQDPSRNYWISVGVRGRKPNTPPGLTVLNYYP---NSPSRLPPTPPP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   340 AGPAWNDTAYRVRQSLATVAHPAHAVPPPpTSDRTILLLNTQNKIGGQIKWALNNVSFTLPHTPYLVAMKRGLLGAFDQR 419
Cdd:TIGR03388 312 VTPAWDDFDRSKAFSLAIKAAMGSPKPPE-TSDRRIVLLNTQNKINGYTKWAINNVSLTLPHTPYLGSLKYNLLNAFDQK 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   420 PPPETYAgaAAFDVYAVQGNPNATTSDAPYRLRFGSVVDVVLQNANMLAANSSETHPWHLHGHDFWVLGHGAGRFDPAVH 499
Cdd:TIGR03388 391 PPPENYP--RDYDIFKPPPNPNTTTGNGIYRLKFNTTVDVILQNANTLNGNNSETHPWHLHGHDFWVLGYGEGKFRPGVD 468
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50725931   500 PAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVFEEGVERVGELPPEIMGCGKT 572
Cdd:TIGR03388 469 EKSYNLKNPPLRNTVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVFAEGVEKVGKLPKEALGCGLT 541
 
Name Accession Description Interval E-value
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
25-572 0e+00

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: 1004.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931    25 TRRHDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVAIHWHGIRQIGTPWADGTEGVTQCP 104
Cdd:TIGR03388   1 IRHYKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLHTEGVVIHWHGIRQIGTPWADGTAGVTQCA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   105 ILPGDTFAYTFVVDRPGTYMYHAHYGMQRSAGLNGMIVVEVApgaagDGEREPFRYDGEHTVLLNDWWHRSTYEQAAGLA 184
Cdd:TIGR03388  81 INPGETFIYNFVVDRPGTYFYHGHYGMQRSAGLYGSLIVDVP-----DGEKEPFHYDGEFNLLLSDWWHKSIHEQEVGLS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   185 SVPMVWVGEPQSLLINGRGRFvNCSSSP----ATAASCNVS-HPDCAPAVFAVVPGKTYRFRVASVTSLSALNFEIEGHE 259
Cdd:TIGR03388 156 SKPMRWIGEPQSLLINGRGQF-NCSLAAkfssTNLPQCNLKgNEQCAPQILHVEPGKTYRLRIASTTALAALNFAIEGHK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   260 MTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATPTGTAVLAYYGgrrNSPRARPPTPPP 339
Cdd:TIGR03388 235 LTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQDPSRNYWISVGVRGRKPNTPPGLTVLNYYP---NSPSRLPPTPPP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   340 AGPAWNDTAYRVRQSLATVAHPAHAVPPPpTSDRTILLLNTQNKIGGQIKWALNNVSFTLPHTPYLVAMKRGLLGAFDQR 419
Cdd:TIGR03388 312 VTPAWDDFDRSKAFSLAIKAAMGSPKPPE-TSDRRIVLLNTQNKINGYTKWAINNVSLTLPHTPYLGSLKYNLLNAFDQK 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   420 PPPETYAgaAAFDVYAVQGNPNATTSDAPYRLRFGSVVDVVLQNANMLAANSSETHPWHLHGHDFWVLGHGAGRFDPAVH 499
Cdd:TIGR03388 391 PPPENYP--RDYDIFKPPPNPNTTTGNGIYRLKFNTTVDVILQNANTLNGNNSETHPWHLHGHDFWVLGYGEGKFRPGVD 468
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50725931   500 PAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVFEEGVERVGELPPEIMGCGKT 572
Cdd:TIGR03388 469 EKSYNLKNPPLRNTVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVFAEGVEKVGKLPKEALGCGLT 541
PLN02604 PLN02604
oxidoreductase
7-574 0e+00

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 889.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931    7 LLCSLFLAAALFGVAAAATRRHDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVAIHWHGI 86
Cdd:PLN02604   6 ALFFLLFSVLNFPAAEARIRRYKWEVKYEYKSPDCFKKLVITINGRSPGPTILAQQGDTVIVELKNSLLTENVAIHWHGI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   87 RQIGTPWADGTEGVTQCPILPGDTFAYTFVVDRPGTYMYHAHYGMQRSAGLNGMIVVEVApgaagDGEREPFRYDGEHTV 166
Cdd:PLN02604  86 RQIGTPWFDGTEGVTQCPILPGETFTYEFVVDRPGTYLYHAHYGMQREAGLYGSIRVSLP-----RGKSEPFSYDYDRSI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  167 LLNDWWHRSTYEQAAGLASVPMVWVGEPQSLLINGRGRFvNCS--SSPATAAS-CNVSHPDCAPAVFAVVPGKTYRFRVA 243
Cdd:PLN02604 161 ILTDWYHKSTYEQALGLSSIPFDWVGEPQSLLIQGKGRY-NCSlvSSPYLKAGvCNATNPECSPYVLTVVPGKTYRLRIS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  244 SVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATPTGTAVLAYY 323
Cdd:PLN02604 240 SLTALSALSFQIEGHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQDPSRNYWVTTSVVSRNNTTPPGLAIFNYY 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  324 ggrRNSPRARPPTPPPAGPAWNDTAYRVRQSLATVAHPAHAVPPPPTSDRTILLLNTQNKIGGQIKWALNNVSFTLPHTP 403
Cdd:PLN02604 320 ---PNHPRRSPPTVPPSGPLWNDVEPRLNQSLAIKARHGYIHPPPLTSDRVIVLLNTQNEVNGYRRWSVNNVSFNLPHTP 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  404 YLVAMKRGLLGAFDQRPPPETYaGAAAFDVYAVQGNPNATTSDAPYRLRFGSVVDVVLQNANMLAANSSETHPWHLHGHD 483
Cdd:PLN02604 397 YLIALKENLTGAFDQTPPPEGY-DFANYDIYAKPNNSNATSSDSIYRLQFNSTVDIILQNANTMNANNSETHPWHLHGHD 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  484 FWVLGHGAGRFDPAVHPAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVFEEGVERVGELP 563
Cdd:PLN02604 476 FWVLGYGEGKFNMSSDPKKYNLVDPIMKNTVPVHPYGWTALRFRADNPGVWAFHCHIESHFFMGMGVVFEEGIERVGKLP 555
                        570
                 ....*....|.
gi 50725931  564 PEIMGCGKTRG 574
Cdd:PLN02604 556 SSIMGCGESKG 566
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
161-322 4.19e-96

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: 290.21  E-value: 4.19e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 161 DGEHTVLLNDWWHRSTYEQAAGLASVPMVWVGEPQSLLINGRGRFvNCSSSPATAAS-----CNVSHPDCAPAVFAVVPG 235
Cdd:cd13871   1 DGELNILLSDWWHKSIYEQETGLSSKPFRWVGEPQSLLIEGRGRY-NCSLAPAYPSSlpspvCNKSNPQCAPFILHVSPG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 236 KTYRFRVASVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATPT 315
Cdd:cd13871  80 KTYRLRIASVTALSSLNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTADQDPSRNYWVSVNVRGRRPNTPP 159

                ....*..
gi 50725931 316 GTAVLAY 322
Cdd:cd13871 160 GLAILNY 166
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
48-553 6.15e-58

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: 199.78  E-value: 6.15e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  48 TINGHTPGPTIRAVQGDTIVVNVKNSlLTENVAIHWHGIRqigTPWA-DgteGVTQCPILPGDTFAYTFVV-DRPGTYMY 125
Cdd:COG2132  37 GYNGQYPGPTIRVREGDRVRVRVTNR-LPEPTTVHWHGLR---VPNAmD---GVPGDPIAPGETFTYEFPVpQPAGTYWY 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 126 HAHY----GMQRSAGLNGMIVVEvapgaaGDGEREPfRYDGEHTVLLNDWwhrsTYEQAAGLASVPMVWVGEP--QSLLI 199
Cdd:COG2132 110 HPHThgstAEQVYRGLAGALIVE------DPEEDLP-RYDRDIPLVLQDW----RLDDDGQLLYPMDAAMGGRlgDTLLV 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 200 NGRgrfvncssspataascnvshpdcAPAVFAVVPGKTYRFRV--ASVTSLSALNFEiEGHEMTVVEADGHYV-KPFVVK 276
Cdd:COG2132 179 NGR-----------------------PNPTLEVRPGERVRLRLlnASNARIYRLALS-DGRPFTVIATDGGLLpAPVEVD 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 277 NLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATptgTAVLAYYGGRRNSPRArpptpppagpawndtayrvrqslA 356
Cdd:COG2132 235 ELLLAPGERADVLVDFSADPGEEVTLANPFEGRSGRA---LLTLRVTGAAASAPLP-----------------------A 288
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 357 TVAHPAHAVPPPPTSDRTILLlntqNKIGGQIKWALNNVsftlphtpylvamkrgllgAFDQRPPPETyagaaafdvyav 436
Cdd:COG2132 289 NLAPLPDLEDREAVRTRELVL----TGGMAGYVWTINGK-------------------AFDPDRPDLT------------ 333
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 437 qgnpnattsdapyrLRFGSVVDVVLQNANMLAanssetHPWHLHGHDFWVLGHGAGRfdpavhpaaynLRDPIMKNTVAV 516
Cdd:COG2132 334 --------------VKLGERERWTLVNDTMMP------HPFHLHGHQFQVLSRNGKP-----------PPEGGWKDTVLV 382
                       490       500       510
                ....*....|....*....|....*....|....*...
gi 50725931 517 HPFGWTALRFRADN-PGVWAFHCHIEAHFFMGMGIVFE 553
Cdd:COG2132 383 PPGETVRILFRFDNyPGDWMFHCHILEHEDAGMMGQFE 420
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
162-325 1.01e-48

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: 165.95  E-value: 1.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   162 GEHTVLLNDWWHRST---YEQAAGLASVPMVWVGEPQSLLINGrgrfvncssspataascnvsHPDCAPAVFAVVPGKTY 238
Cdd:pfam00394   1 EDYVITLSDWYHKDAkdlEKELLASGKAPTDFPPVPDAVLING--------------------KDGASLATLTVTPGKTY 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   239 RFRVASVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPnRNYWLASNVVSRKPATPTGTA 318
Cdd:pfam00394  61 RLRIINVALDDSLNFSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDP-GNYWIVASPNIPAFDNGTAAA 139

                  ....*..
gi 50725931   319 VLAYYGG 325
Cdd:pfam00394 140 ILRYSGA 146
 
Name Accession Description Interval E-value
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
25-572 0e+00

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: 1004.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931    25 TRRHDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVAIHWHGIRQIGTPWADGTEGVTQCP 104
Cdd:TIGR03388   1 IRHYKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLHTEGVVIHWHGIRQIGTPWADGTAGVTQCA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   105 ILPGDTFAYTFVVDRPGTYMYHAHYGMQRSAGLNGMIVVEVApgaagDGEREPFRYDGEHTVLLNDWWHRSTYEQAAGLA 184
Cdd:TIGR03388  81 INPGETFIYNFVVDRPGTYFYHGHYGMQRSAGLYGSLIVDVP-----DGEKEPFHYDGEFNLLLSDWWHKSIHEQEVGLS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   185 SVPMVWVGEPQSLLINGRGRFvNCSSSP----ATAASCNVS-HPDCAPAVFAVVPGKTYRFRVASVTSLSALNFEIEGHE 259
Cdd:TIGR03388 156 SKPMRWIGEPQSLLINGRGQF-NCSLAAkfssTNLPQCNLKgNEQCAPQILHVEPGKTYRLRIASTTALAALNFAIEGHK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   260 MTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATPTGTAVLAYYGgrrNSPRARPPTPPP 339
Cdd:TIGR03388 235 LTVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQDPSRNYWISVGVRGRKPNTPPGLTVLNYYP---NSPSRLPPTPPP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   340 AGPAWNDTAYRVRQSLATVAHPAHAVPPPpTSDRTILLLNTQNKIGGQIKWALNNVSFTLPHTPYLVAMKRGLLGAFDQR 419
Cdd:TIGR03388 312 VTPAWDDFDRSKAFSLAIKAAMGSPKPPE-TSDRRIVLLNTQNKINGYTKWAINNVSLTLPHTPYLGSLKYNLLNAFDQK 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   420 PPPETYAgaAAFDVYAVQGNPNATTSDAPYRLRFGSVVDVVLQNANMLAANSSETHPWHLHGHDFWVLGHGAGRFDPAVH 499
Cdd:TIGR03388 391 PPPENYP--RDYDIFKPPPNPNTTTGNGIYRLKFNTTVDVILQNANTLNGNNSETHPWHLHGHDFWVLGYGEGKFRPGVD 468
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50725931   500 PAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVFEEGVERVGELPPEIMGCGKT 572
Cdd:TIGR03388 469 EKSYNLKNPPLRNTVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVFAEGVEKVGKLPKEALGCGLT 541
PLN02604 PLN02604
oxidoreductase
7-574 0e+00

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 889.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931    7 LLCSLFLAAALFGVAAAATRRHDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVAIHWHGI 86
Cdd:PLN02604   6 ALFFLLFSVLNFPAAEARIRRYKWEVKYEYKSPDCFKKLVITINGRSPGPTILAQQGDTVIVELKNSLLTENVAIHWHGI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   87 RQIGTPWADGTEGVTQCPILPGDTFAYTFVVDRPGTYMYHAHYGMQRSAGLNGMIVVEVApgaagDGEREPFRYDGEHTV 166
Cdd:PLN02604  86 RQIGTPWFDGTEGVTQCPILPGETFTYEFVVDRPGTYLYHAHYGMQREAGLYGSIRVSLP-----RGKSEPFSYDYDRSI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  167 LLNDWWHRSTYEQAAGLASVPMVWVGEPQSLLINGRGRFvNCS--SSPATAAS-CNVSHPDCAPAVFAVVPGKTYRFRVA 243
Cdd:PLN02604 161 ILTDWYHKSTYEQALGLSSIPFDWVGEPQSLLIQGKGRY-NCSlvSSPYLKAGvCNATNPECSPYVLTVVPGKTYRLRIS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  244 SVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATPTGTAVLAYY 323
Cdd:PLN02604 240 SLTALSALSFQIEGHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQDPSRNYWVTTSVVSRNNTTPPGLAIFNYY 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  324 ggrRNSPRARPPTPPPAGPAWNDTAYRVRQSLATVAHPAHAVPPPPTSDRTILLLNTQNKIGGQIKWALNNVSFTLPHTP 403
Cdd:PLN02604 320 ---PNHPRRSPPTVPPSGPLWNDVEPRLNQSLAIKARHGYIHPPPLTSDRVIVLLNTQNEVNGYRRWSVNNVSFNLPHTP 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  404 YLVAMKRGLLGAFDQRPPPETYaGAAAFDVYAVQGNPNATTSDAPYRLRFGSVVDVVLQNANMLAANSSETHPWHLHGHD 483
Cdd:PLN02604 397 YLIALKENLTGAFDQTPPPEGY-DFANYDIYAKPNNSNATSSDSIYRLQFNSTVDIILQNANTMNANNSETHPWHLHGHD 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  484 FWVLGHGAGRFDPAVHPAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVFEEGVERVGELP 563
Cdd:PLN02604 476 FWVLGYGEGKFNMSSDPKKYNLVDPIMKNTVPVHPYGWTALRFRADNPGVWAFHCHIESHFFMGMGVVFEEGIERVGKLP 555
                        570
                 ....*....|.
gi 50725931  564 PEIMGCGKTRG 574
Cdd:PLN02604 556 SSIMGCGESKG 566
PLN02191 PLN02191
L-ascorbate oxidase
26-573 0e+00

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 653.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   26 RRHDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVAIHWHGIRQIGTPWADGTEGVTQCPI 105
Cdd:PLN02191  24 REYTWEVEYKYWWPDCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLTTEGLVIHWHGIRQKGSPWADGAAGVTQCAI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  106 LPGDTFAYTFVVDRPGTYMYHAHYGMQRSAGLNGMIVVEVApgaagDGEREPFRYDGEHTVLLNDWWHRSTYEQAAGLAS 185
Cdd:PLN02191 104 NPGETFTYKFTVEKPGTHFYHGHYGMQRSAGLYGSLIVDVA-----KGPKERLRYDGEFNLLLSDWWHESIPSQELGLSS 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  186 VPMVWVGEPQSLLINGRGRFvNCS-----SSPATAASCNVSHPD-CAPAVFAVVPGKTYRFRVASVTSLSALNFEIEGHE 259
Cdd:PLN02191 179 KPMRWIGEAQSILINGRGQF-NCSlaaqfSNGTELPMCTFKEGDqCAPQTLRVEPNKTYRIRLASTTALASLNLAVQGHK 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  260 MTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATPTGTAVLAYYGGrrnSPRARPPTPPP 339
Cdd:PLN02191 258 LVVVEADGNYITPFTTDDIDIYSGESYSVLLTTDQDPSQNYYISVGVRGRKPNTTQALTILNYVTA---PASKLPSSPPP 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  340 AGPAWNDTAYRVRQSLATVAHPAHAVPPPPTSDRTILLlNTQNKIGGQIKWALNNVSFTLPHTPYLVAMKRGLLGAFDQR 419
Cdd:PLN02191 335 VTPRWDDFERSKNFSKKIFSAMGSPSPPKKYRKRLILL-NTQNLIDGYTKWAINNVSLVTPATPYLGSVKYNLKLGFNRK 413
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  420 PPPETYAgaAAFDVYAVQGNPNATTSDAPYRLRFGSVVDVVLQNANMLAANSSETHPWHLHGHDFWVLGHGAGRFDPAVH 499
Cdd:PLN02191 414 SPPRSYR--MDYDIMNPPPFPNTTTGNGIYVFPFNVTVDVIIQNANVLKGVVSEIHPWHLHGHDFWVLGYGDGKFKPGID 491
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50725931  500 PAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVFEEGVERVGELPPEIMGCGKTR 573
Cdd:PLN02191 492 EKTYNLKNPPLRNTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEGLNRIGKIPDEALGCGLTK 565
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
25-564 3.69e-114

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: 350.19  E-value: 3.69e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931    25 TRRHDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIRQIGTPWADGTEGVTQCP 104
Cdd:TIGR03389   3 VRHYTFDVQEKNVTRLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNV-QYNVTIHWHGVRQLRNGWADGPAYITQCP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   105 ILPGDTFAYTF-VVDRPGTYMYHAHYGMQRsAGLNGMIVVEVAPGAAgdgerEPF-RYDGEHTVLLNDWWHRST---YEQ 179
Cdd:TIGR03389  82 IQPGQSYVYNFtITGQRGTLWWHAHISWLR-ATVYGAIVILPKPGVP-----YPFpKPDREVPIILGEWWNADVeavINQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   180 AAGLASVPMVwvgePQSLLINGR-GRFVNCSSSPATaascnvshpdcapaVFAVVPGKTYRFRVASVTSLSALNFEIEGH 258
Cdd:TIGR03389 156 ANQTGGAPNV----SDAYTINGHpGPLYNCSSKDTF--------------KLTVEPGKTYLLRIINAALNDELFFAIANH 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   259 EMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRnYWLASNVVSRKPAT---PTGTAVLAYYGGRRNSPRARPP 335
Cdd:TIGR03389 218 TLTVVEVDATYTKPFKTKTIVIGPGQTTNVLLTADQSPGR-YFMAARPYMDAPGAfdnTTTTAILQYKGTSNSAKPILPT 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   336 TPPpagpaWNDTAYRVR--QSLATVAHPAHAVPPPPTSDRTILL-----LNT------QNKIGGQIKWALNNVSFTLPHT 402
Cdd:TIGR03389 297 LPA-----YNDTAAATNfsNKLRSLNSAQYPANVPVTIDRRLFFtiglgLDPcpnntcQGPNGTRFAASMNNISFVMPTT 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   403 PYLVAMKRGLLGA----FDQRPPpetyagaAAFDvYAVQGNPNAT-TSDAP--YRLRFGSVVDVVLQNANMLAansSETH 475
Cdd:TIGR03389 372 ALLQAHYFGISGVfttdFPANPP-------TKFN-YTGTNLPNNLfTTNGTkvVRLKFNSTVELVLQDTSILG---SENH 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   476 PWHLHGHDFWVLGHGAGRFDPAVHPAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVF--E 553
Cdd:TIGR03389 441 PIHLHGYNFFVVGTGFGNFDPKKDPAKFNLVDPPERNTVGVPTGGWAAIRFVADNPGVWFMHCHLEVHTTWGLKMAFlvD 520
                         570
                  ....*....|.
gi 50725931   554 EGVERVGELPP 564
Cdd:TIGR03389 521 NGKGPNQSLLP 531
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
161-322 4.19e-96

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: 290.21  E-value: 4.19e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 161 DGEHTVLLNDWWHRSTYEQAAGLASVPMVWVGEPQSLLINGRGRFvNCSSSPATAAS-----CNVSHPDCAPAVFAVVPG 235
Cdd:cd13871   1 DGELNILLSDWWHKSIYEQETGLSSKPFRWVGEPQSLLIEGRGRY-NCSLAPAYPSSlpspvCNKSNPQCAPFILHVSPG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 236 KTYRFRVASVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATPT 315
Cdd:cd13871  80 KTYRLRIASVTALSSLNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTADQDPSRNYWVSVNVRGRRPNTPP 159

                ....*..
gi 50725931 316 GTAVLAY 322
Cdd:cd13871 160 GLAILNY 166
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
41-555 2.49e-91

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: 290.97  E-value: 2.49e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931    41 CVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVAIHWHGIRQIGTPWADGTEGVTQCPILPGDTFAYTFVVD-- 118
Cdd:TIGR03390  24 CSSRYSVVVNGTSPGPEIRLQEGQTTWIRVYNDIPDNNVTMHWHGLTQRTAPFSDGTPLASQWPIPPGHFFDYEIKPEpg 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   119 RPGTYMYHAHYGMQrSAGLNGMIVVEvapgaagDGEREPFRYDGEHTVLLNDWWHRSTYEQAAGLASVPMVWVGEPQSLL 198
Cdd:TIGR03390 104 DAGSYFYHSHVGFQ-AVTAFGPLIVE-------DCEPPPYKYDDERILLVSDFFSATDEEIEQGLLSTPFTWSGETEAVL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   199 INGRGRfvncssSPATAASCNVSHpDCAPAVFAVVPGKTYRFRVASVTSLSALNFEIEGHE-MTVVEADGHYVKPFVVKN 277
Cdd:TIGR03390 176 LNGKSG------NKSFYAQINPSG-SCMLPVIDVEPGKTYRLRFIGATALSLISLGIEDHEnLTIIEADGSYTKPAKIDH 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   278 LNIYSGETYSVLITA------DQDPNRNYWLASNVVSRkPATPTGTAVLAYYGGRRNSPRARPPTP----PPAGPAWNDT 347
Cdd:TIGR03390 249 LQLGGGQRYSVLFKAktedelCGGDKRQYFIQFETRDR-PKVYRGYAVLRYRSDKASKLPSVPETPplplPNSTYDWLEY 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   348 AYrvrQSLATVAHPAHAVPPPPTsdRTILLLNTQN--KIGGQIKWALNNVSFT--LPHTPYLVAMKRGLLGAFdqrpppE 423
Cdd:TIGR03390 328 EL---EPLSEENNQDFPTLDEVT--RRVVIDAHQNvdPLNGRVAWLQNGLSWTesVRQTPYLVDIYENGLPAT------P 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   424 TYAGAAAFDVYavqgnpnattsDAPYRL---RFGSVVDVVLQNANML--AANSSETHPWHLHGHDFWVLGHGAGRFDPAV 498
Cdd:TIGR03390 397 NYTAALANYGF-----------DPETRAfpaKVGEVLEIVWQNTGSYtgPNGGVDTHPFHAHGRHFYDIGGGDGEYNATA 465
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50725931   499 HPAAYNLRDPIMKNTVAV----------HPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVFEEG 555
Cdd:TIGR03390 466 NEAKLENYTPVLRDTTMLyryavkvvpgAPAGWRAWRIRVTNPGVWMMHCHILQHMVMGMQTVWVFG 532
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
371-563 1.70e-82

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: 254.65  E-value: 1.70e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 371 SDRTILLLNTQNKIGGQIKWALNNVSFTLPHTPYLVAMkrgllgafdqrpppetyagaaafdvyavqgnpnattsdAPYR 450
Cdd:cd13893   1 ATRTLLLLNTQNLINGQLRWAINNVSYVPPPTPYLAAL--------------------------------------PVYP 42
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 451 LRFGSVVDVVLQNANMLAANSSETHPWHLHGHDFWVLGHGAGRFDPAVHPAAYNLRDPIMKNTVAVHPFGWTALRFRADN 530
Cdd:cd13893  43 FKGGDVVDVILQNANTNTRNASEQHPWHLHGHDFWVLGYGLGGFDPAADPSSLNLVNPPMRNTVTIFPYGWTALRFKADN 122
                       170       180       190
                ....*....|....*....|....*....|...
gi 50725931 531 PGVWAFHCHIEAHFFMGMGIVFEEGVERVGELP 563
Cdd:cd13893 123 PGVWAFHCHIEWHFHMGMGVVFAEGVERVGRLP 155
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
26-145 2.96e-70

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: 221.55  E-value: 2.96e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  26 RRHDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVAIHWHGIRQIGTPWADGTEGVTQCPI 105
Cdd:cd13845   1 RHYKWKVEYMFWAPDCVEKLVIGINGQFPGPTIRATAGDTIVVELENKLPTEGVAIHWHGIRQRGTPWADGTASVSQCPI 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 50725931 106 LPGDTFAYTFVVDRPGTYMYHAHYGMQRSAGLNGMIVVEV 145
Cdd:cd13845  81 NPGETFTYQFVVDRPGTYFYHGHYGMQRSAGLYGSLIVDP 120
PLN02354 PLN02354
copper ion binding / oxidoreductase
28-547 3.03e-69

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 233.14  E-value: 3.03e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   28 HDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIRQIGTPWADGTEGvTQCPILP 107
Cdd:PLN02354  30 FTWNVTYGTASPLGVPQQVILINGQFPGPNINSTSNNNIVINVFNNL-DEPFLLTWSGIQQRKNSWQDGVPG-TNCPIPP 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  108 GDTFAYTFVV-DRPGTYMYHAHYGMQRSAGLNGMIVVE---VAPGAAGDGErepfrydGEHTVLLNDWWHRSTYEQAAGL 183
Cdd:PLN02354 108 GTNFTYHFQPkDQIGSYFYYPSTGMHRAAGGFGGLRVNsrlLIPVPYADPE-------DDYTVLIGDWYTKSHTALKKFL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  184 ASvpMVWVGEPQSLLINGRGRFVNCSSSPataascnvshpdcapaVFAVVPGKTYRFRVASVTSLSALNFEIEGHEMTVV 263
Cdd:PLN02354 181 DS--GRTLGRPDGVLINGKSGKGDGKDEP----------------LFTMKPGKTYRYRICNVGLKSSLNFRIQGHKMKLV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  264 EADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATPTGtaVLAYYGGRRNSPRARPPTPP----- 338
Cdd:PLN02354 243 EMEGSHVLQNDYDSLDVHVGQCFSVLVTANQAPKDYYMVASTRFLKKVLTTTG--IIRYEGGKGPASPELPEAPVgwaws 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  339 ---PAGPAWNDTAyrvrqSLATVAHPAHAVPPPPTSDRTILLLNTQNKIGGQIKWALNNVSFTLPHTPYLVAmkrgllga 415
Cdd:PLN02354 321 lnqFRSFRWNLTA-----SAARPNPQGSYHYGKINITRTIKLVNSASKVDGKLRYALNGVSHVDPETPLKLA-------- 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  416 fdqrpppeTYAGAA--AFDVYAVQGNPNATTSD---APYRLR--FGSVVDVVLQNanmlaaNSSETHPWHLHGHDFWVLG 488
Cdd:PLN02354 388 --------EYFGVAdkVFKYDTIKDNPPAKITKikiQPNVLNitFRTFVEIIFEN------HEKSMQSWHLDGYSFFAVA 453
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 50725931  489 HGAGRFDPAVHpAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMG 547
Cdd:PLN02354 454 VEPGTWTPEKR-KNYNLLDAVSRHTVQVYPKSWAAILLTFDNAGMWNIRSENWERRYLG 511
PLN02168 PLN02168
copper ion binding / pectinesterase
28-573 4.10e-67

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 227.55  E-value: 4.10e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   28 HDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIRQIGTPWADGTEGvTQCPILP 107
Cdd:PLN02168  29 YQWVVSYSQRFILGGNKQVIVINDMFPGPLLNATANDVINVNIFNNL-TEPFLMTWNGLQLRKNSWQDGVRG-TNCPILP 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  108 GDTFAYTFVV-DRPGTYMYHAHYGMQRSAGLNGMIVV---EVAPgaagdgerEPF-RYDGEHTVLLNDWWH------RST 176
Cdd:PLN02168 107 GTNWTYRFQVkDQIGSYFYFPSLLLQKAAGGYGAIRIynpELVP--------VPFpKPDEEYDILIGDWFYadhtvmRAS 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  177 YEQAAGLASvpmvwvgePQSLLINGRGrfvncssspataascnvshPDcaPAVFAVVPGKTYRFRVASVTSLSALNFEIE 256
Cdd:PLN02168 179 LDNGHSLPN--------PDGILFNGRG-------------------PE--ETFFAFEPGKTYRLRISNVGLKTCLNFRIQ 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  257 GHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDP---NRNYWLASNvvSR-KPATPTGTAVLAYyggrRNSPRA 332
Cdd:PLN02168 230 DHDMLLVETEGTYVQKRVYSSLDIHVGQSYSVLVTAKTDPvgiYRSYYIVAT--ARfTDAYLGGVALIRY----PNSPLD 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  333 RPPTPPPAGPAWnDTAYRVRQSL----------ATVAHPAHAVPPPPTSDRTILLLNTQNKIGGQIKWALNNVSFTLPHT 402
Cdd:PLN02168 304 PVGPLPLAPALH-DYFSSVEQALsirmdlnvgaARSNPQGSYHYGRINVTRTIILHNDVMLSSGKLRYTINGVSFVYPGT 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  403 PylvamkrglLGAFDQRPPPETYAgAAAFDVYAVQGNPNATTS--DAPYRlrfgSVVDVVLQNAnmlaanSSETHPWHLH 480
Cdd:PLN02168 383 P---------LKLVDHFQLNDTII-PGMFPVYPSNKTPTLGTSvvDIHYK----DFYHIVFQNP------LFSLESYHID 442
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  481 GHDFWVLGHGAGRFDPAVHpAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVFEegVERVG 560
Cdd:PLN02168 443 GYNFFVVGYGFGAWSESKK-AGYNLVDAVSRSTVQVYPYSWTAILIAMDNQGMWNVRSQKAEQWYLGQELYMR--VKGEG 519
                        570       580
                 ....*....|....*....|....*.
gi 50725931  561 E-------------LPPEIMGCGKTR 573
Cdd:PLN02168 520 EedpstipvrdenpIPGNVIRCGKVS 545
PLN02835 PLN02835
oxidoreductase
26-576 2.82e-60

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 209.06  E-value: 2.82e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   26 RRHDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIRQIGTPWADGTEGvTQCPI 105
Cdd:PLN02835  30 KYYTWTVTYGTISPLGVPQQVILINGQFPGPRLDVVTNDNIILNLINKL-DQPFLLTWNGIKQRKNSWQDGVLG-TNCPI 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  106 LPGDTFAYTFVV-DRPGTYMYHAHYGMQRSAGLNGMIVVEVAPgaagdgeREPFRY---DGEHTVLLNDWW---HRSTYE 178
Cdd:PLN02835 108 PPNSNYTYKFQTkDQIGTFTYFPSTLFHKAAGGFGAINVYERP-------RIPIPFplpDGDFTLLVGDWYktsHKTLQQ 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  179 QAAGLASVPMvwvgePQSLLINGRgrfvncssspataascnvshpdcAPAVFAVVPGKTYRFRVASVTSLSALNFEIEGH 258
Cdd:PLN02835 181 RLDSGKVLPF-----PDGVLINGQ-----------------------TQSTFSGDQGKTYMFRISNVGLSTSLNFRIQGH 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  259 EMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWLASNVVSRKpaTPTGTAVLAYYGGRR---------NS 329
Cdd:PLN02835 233 TMKLVEVEGSHTIQNIYDSLDVHVGQSVAVLVTLNQSPKDYYIVASTRFTRQ--ILTATAVLHYSNSRTpasgplpalPS 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  330 PRARPPTPPPAGPAWNDTAyrvrqSLATVAHPAHAVPPPPTSDRTILLLNTQNKIGGQIKWALNNVSFTLPHTPYLVAMK 409
Cdd:PLN02835 311 GELHWSMRQARTYRWNLTA-----SAARPNPQGSFHYGKITPTKTIVLANSAPLINGKQRYAVNGVSYVNSDTPLKLADY 385
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  410 RGLLGAFDQRPPPETYAGAAAFdvyavqgnpnATTSDAPYRLRfgSVVDVVLQNanmlaaNSSETHPWHLHGHDFWVLGH 489
Cdd:PLN02835 386 FGIPGVFSVNSIQSLPSGGPAF----------VATSVMQTSLH--DFLEVVFQN------NEKTMQSWHLDGYDFWVVGY 447
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  490 GAGRFDPAVHpAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGI---VFEEGVERVGE--LPP 564
Cdd:PLN02835 448 GSGQWTPAKR-SLYNLVDALTRHTAQVYPKSWTTILVSLDNQGMWNMRSAIWERQYLGQQFylrVWNQVHSLANEydIPD 526
                        570
                 ....*....|..
gi 50725931  565 EIMGCGKTRGGH 576
Cdd:PLN02835 527 NALLCGKAIGRH 538
PLN02991 PLN02991
oxidoreductase
26-576 1.14e-59

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 207.56  E-value: 1.14e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   26 RRHDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIRQIGTPWADGTEGvTQCPI 105
Cdd:PLN02991  29 RFFEWHVTYGNISPLGVAQQGILINGKFPGPDIISVTNDNLIINVFNHL-DEPFLISWSGIRNWRNSYQDGVYG-TTCPI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  106 LPGDTFAYTFVV-DRPGTYMYHAHYGMQRSAGLNGMIVVEVAPgaagdgeREPFRYD---GEHTVLLNDWW---HRSTYE 178
Cdd:PLN02991 107 PPGKNYTYALQVkDQIGSFYYFPSLGFHKAAGGFGAIRISSRP-------LIPVPFPapaDDYTVLIGDWYktnHKDLRA 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  179 QAAGLASVPMvwvgePQSLLINGRGrfvncssspaTAASCNVShpdcapavfavvPGKTYRFRVASVTSLSALNFEIEGH 258
Cdd:PLN02991 180 QLDNGGKLPL-----PDGILINGRG----------SGATLNIE------------PGKTYRLRISNVGLQNSLNFRIQNH 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  259 EMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATPTGtaVLAYyggrRNSPRARP--PT 336
Cdd:PLN02991 233 TMKLVEVEGTHTIQTPFSSLDVHVGQSYSVLITADQPAKDYYIVVSSRFTSKILITTG--VLHY----SNSAGPVSgpIP 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  337 PPPAGPAWN-DTAYRVRQSLATV----AHPAHAVPPPPTSDRTILLLNTQNKIGGQIKWALNNVSFTLPHTPYLVAMKRG 411
Cdd:PLN02991 307 DGPIQLSWSfDQARAIKTNLTASgprpNPQGSYHYGKINITRTIRLANSAGNIEGKQRYAVNSASFYPADTPLKLADYFK 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  412 LLGAFDQRPPPETYAGAAAFdvyavqgnPNATTSDAPYRlrfgSVVDVVLQNANMLaansseTHPWHLHGHDFWVLGHGA 491
Cdd:PLN02991 387 IAGVYNPGSIPDQPTNGAIF--------PVTSVMQTDYK----AFVEIVFENWEDI------VQTWHLDGYSFYVVGMEL 448
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  492 GRFDPAVHpAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGI---VFEEGVERVGE--LPPEI 566
Cdd:PLN02991 449 GKWSAASR-KVYNLNDAVSRCTVQVYPRSWTAIYVSLDNVGMWNLRSELWERQYLGQQFymrVYTTSTSLRDEylIPKNA 527
                        570
                 ....*....|
gi 50725931  567 MGCGKTRGGH 576
Cdd:PLN02991 528 LLCGRATGHH 537
PLN02792 PLN02792
oxidoreductase
28-547 3.27e-58

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 203.29  E-value: 3.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   28 HDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIRQIGTPWADGTEGvTQCPILP 107
Cdd:PLN02792  19 YNWRVTYGNISLLTLPRRGILINGQFPGPEIRSLTNDNLVINVHNDL-DEPFLLSWNGVHMRKNSYQDGVYG-TTCPIPP 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  108 GDTFAYTFVV-DRPGTYMYHAHYGMQRSAGLNGMIVVEVAPgaagdgeREPFRYD---GEHTVLLNDWW---HRSTYEQA 180
Cdd:PLN02792  97 GKNYTYDFQVkDQVGSYFYFPSLAVQKAAGGYGSLRIYSLP-------RIPVPFPepaGDFTFLIGDWYrrnHTTLKKIL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  181 AGLASVPMVwvgePQSLLINGRGrfVNCSSSpataascnvshpdcapavFAVVPGKTYRFRVASVTSLSALNFEIEGHEM 260
Cdd:PLN02792 170 DGGRKLPLM----PDGVMINGQG--VSYVYS------------------ITVDKGKTYRFRISNVGLQTSLNFEILGHQL 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  261 TVVEADGHYVKPFVVKNLNIYSGETYSVLITADQdPNRNYwlaSNVVSRK-PATPTGTAVLAYYGGRRNSPRARPPTPPP 339
Cdd:PLN02792 226 KLIEVEGTHTVQSMYTSLDIHVGQTYSVLVTMDQ-PPQNY---SIVVSTRfIAAKVLVSSTLHYSNSKGHKIIHARQPDP 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  340 AGPAWN-DTAYRVRQSLATVAHPAHAVPPPPTS----DRTILLLNTQNKIGGQIKWALNNVSFTLPHTPYLVAMKRGLLG 414
Cdd:PLN02792 302 DDLEWSiKQAQSIRTNLTASGPRTNPQGSYHYGkmkiSRTLILESSAALVKRKQRYAINGVSFVPSDTPLKLADHFKIKG 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  415 AFDQRPPPET--YAGAAAFDVYAVQGNPNAttsdapyrlrfgsVVDVVLQNANMLAANssethpWHLHGHDFWVLGHGAG 492
Cdd:PLN02792 382 VFKVGSIPDKprRGGGMRLDTSVMGAHHNA-------------FLEIIFQNREKIVQS------YHLDGYNFWVVGINKG 442
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 50725931  493 RFDPAVHpAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMG 547
Cdd:PLN02792 443 IWSRASR-REYNLKDAISRSTTQVYPESWTAVYVALDNVGMWNLRSQFWARQYLG 496
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
48-553 6.15e-58

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: 199.78  E-value: 6.15e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  48 TINGHTPGPTIRAVQGDTIVVNVKNSlLTENVAIHWHGIRqigTPWA-DgteGVTQCPILPGDTFAYTFVV-DRPGTYMY 125
Cdd:COG2132  37 GYNGQYPGPTIRVREGDRVRVRVTNR-LPEPTTVHWHGLR---VPNAmD---GVPGDPIAPGETFTYEFPVpQPAGTYWY 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 126 HAHY----GMQRSAGLNGMIVVEvapgaaGDGEREPfRYDGEHTVLLNDWwhrsTYEQAAGLASVPMVWVGEP--QSLLI 199
Cdd:COG2132 110 HPHThgstAEQVYRGLAGALIVE------DPEEDLP-RYDRDIPLVLQDW----RLDDDGQLLYPMDAAMGGRlgDTLLV 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 200 NGRgrfvncssspataascnvshpdcAPAVFAVVPGKTYRFRV--ASVTSLSALNFEiEGHEMTVVEADGHYV-KPFVVK 276
Cdd:COG2132 179 NGR-----------------------PNPTLEVRPGERVRLRLlnASNARIYRLALS-DGRPFTVIATDGGLLpAPVEVD 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 277 NLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATptgTAVLAYYGGRRNSPRArpptpppagpawndtayrvrqslA 356
Cdd:COG2132 235 ELLLAPGERADVLVDFSADPGEEVTLANPFEGRSGRA---LLTLRVTGAAASAPLP-----------------------A 288
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 357 TVAHPAHAVPPPPTSDRTILLlntqNKIGGQIKWALNNVsftlphtpylvamkrgllgAFDQRPPPETyagaaafdvyav 436
Cdd:COG2132 289 NLAPLPDLEDREAVRTRELVL----TGGMAGYVWTINGK-------------------AFDPDRPDLT------------ 333
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 437 qgnpnattsdapyrLRFGSVVDVVLQNANMLAanssetHPWHLHGHDFWVLGHGAGRfdpavhpaaynLRDPIMKNTVAV 516
Cdd:COG2132 334 --------------VKLGERERWTLVNDTMMP------HPFHLHGHQFQVLSRNGKP-----------PPEGGWKDTVLV 382
                       490       500       510
                ....*....|....*....|....*....|....*...
gi 50725931 517 HPFGWTALRFRADN-PGVWAFHCHIEAHFFMGMGIVFE 553
Cdd:COG2132 383 PPGETVRILFRFDNyPGDWMFHCHILEHEDAGMMGQFE 420
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
28-534 3.26e-53

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 191.03  E-value: 3.26e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   28 HDWDISYQFTSP--DCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIRQIGTPWADGTEGvTQCPI 105
Cdd:PLN00044  30 YDWEVSYVSAAPlgGVKKQEAIGINGQFPGPALNVTTNWNLVVNVRNAL-DEPLLLTWHGVQQRKSAWQDGVGG-TNCAI 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  106 LPGDTFAYTFVV-DRPGTYMYHAHYGMQRSAGLNGMIVV---EVAPGAAgdgerePFRYDGEHTVLLNDWWHRSTYEQAA 181
Cdd:PLN00044 108 PAGWNWTYQFQVkDQVGSFFYAPSTALHRAAGGYGAITInnrDVIPIPF------GFPDGGDITLFIADWYARDHRALRR 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  182 GL-ASVPMvwvGEPQSLLINGRGRF-VNCSSSPataascnvshPDCAPAVFAVVPGKTYRFRVASVTSLSALNFEIEGHE 259
Cdd:PLN00044 182 ALdAGDLL---GAPDGVLINAFGPYqYNDSLVP----------PGITYERINVDPGKTYRFRVHNVGVATSLNFRIQGHN 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  260 MTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATP---TGTAVLAYyggrRNSPRARPPT 336
Cdd:PLN00044 249 LLLVEAEGSYTSQQNYTNLDIHVGQSYSFLLTMDQNASTDYYVVASARFVDAAVVdklTGVAILHY----SNSQGPASGP 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  337 PPPAGPAWNDTAYRVRQSLATVAHPAHAVPP-----------PPTSDRTILLLNTQNKIGGQIKWALNNVSFTLPHTPYL 405
Cdd:PLN00044 325 LPDAPDDQYDTAFSINQARSIRWNVTASGARpnpqgsfhygdITVTDVYLLQSMAPELIDGKLRATLNEISYIAPSTPLM 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  406 VAMKRGLLGAFDQRPPPETYAGAAAFDVYAVQGNpnattsdapyrlrFGSVVDVVLQNanmlaaNSSETHPWHLHGHDFW 485
Cdd:PLN00044 405 LAQIFNVPGVFKLDFPNHPMNRLPKLDTSIINGT-------------YKGFMEIIFQN------NATNVQSYHLDGYAFF 465
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 50725931  486 VLGHGAGRFDPAVHpAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVW 534
Cdd:PLN00044 466 VVGMDYGLWTDNSR-GTYNKWDGVARSTIQVFPGAWTAILVFLDNAGIW 513
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
26-144 2.53e-49

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: 166.69  E-value: 2.53e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  26 RRHDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVAIHWHGIRQIGTPWADGTEGVTQCPI 105
Cdd:cd04206   1 REYELTITETTVNPDGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNLPNEPTSIHWHGLRQPGTNDGDGVAGLTQCPI 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 50725931 106 LPGDTFAYTFVVD-RPGTYMYHAHYGMQRSAGLNGMIVVE 144
Cdd:cd04206  81 PPGESFTYRFTVDdQAGTFWYHSHVGGQRADGLYGPLIVE 120
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
162-325 1.01e-48

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: 165.95  E-value: 1.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   162 GEHTVLLNDWWHRST---YEQAAGLASVPMVWVGEPQSLLINGrgrfvncssspataascnvsHPDCAPAVFAVVPGKTY 238
Cdd:pfam00394   1 EDYVITLSDWYHKDAkdlEKELLASGKAPTDFPPVPDAVLING--------------------KDGASLATLTVTPGKTY 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   239 RFRVASVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPnRNYWLASNVVSRKPATPTGTA 318
Cdd:pfam00394  61 RLRIINVALDDSLNFSIEGHKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDP-GNYWIVASPNIPAFDNGTAAA 139

                  ....*..
gi 50725931   319 VLAYYGG 325
Cdd:pfam00394 140 ILRYSGA 146
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
40-143 2.48e-48

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: 163.48  E-value: 2.48e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  40 DCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVAIHWHGIRQIGTPWADGTEGVTQCPILPGDTFAYTFVVDR 119
Cdd:cd13858   1 DGVERPVITVNGQLPGPSIEVCEGDTVVVDVKNRLPGESTTIHWHGIHQRGTPYMDGVPMVTQCPILPGQTFRYKFKADP 80
                        90       100
                ....*....|....*....|....
gi 50725931 120 PGTYMYHAHYGMQRSAGLNGMIVV 143
Cdd:cd13858  81 AGTHWYHSHSGTQRADGLFGALIV 104
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
416-552 1.16e-47

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: 162.81  E-value: 1.16e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 416 FDQRPPPetyagaaAFDVYAVQGNPNATTSDAP--YRLRFGSVVDVVLQNANMLAAnssETHPWHLHGHDFWVLGHGAGR 493
Cdd:cd13897   6 FPDRPPV-------PFDYTGNAPNENTPTSRGTkvKVLEYGSTVEIVLQGTSLLAA---ENHPMHLHGFDFYVVGRGFGN 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 50725931 494 FDPAVHPAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVF 552
Cdd:cd13897  76 FDPSTDPATFNLVDPPLRNTVGVPRGGWAAIRFVADNPGVWFMHCHFERHTSWGMATVF 134
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
31-144 2.04e-44

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: 153.56  E-value: 2.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931    31 DISYQFTSPDC-VRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIRQIGTPWADGTEGVTQCPILPGD 109
Cdd:pfam07732   1 TVTYGTVSPLGgTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNL-DEPTSIHWHGLQQRGTPWMDGVPGVTQCPIPPGQ 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 50725931   110 TFAYTF-VVDRPGTYMYHAHYGMQRSAGLNGMIVVE 144
Cdd:pfam07732  80 SFTYRFqVKQQAGTYWYHSHTSGQQAAGLAGAIIIE 115
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
26-143 2.48e-44

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: 153.18  E-value: 2.48e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  26 RRHDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNsLLTENVAIHWHGIRQIGTPWADGTEGVTQCPI 105
Cdd:cd13857   1 REYNFTISEITGAPDGFVRPMLVINGQFPGPLIEANQGDRIVVHVTN-ELDEPTSIHWHGLFQNGTNWMDGTAGITQCPI 79
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 50725931 106 LPGDTFAYTFVVDRP-GTYMYHAHYGMQRSAGLNGMIVV 143
Cdd:cd13857  80 PPGGSFTYNFTVDGQyGTYWYHSHYSTQYADGLVGPLIV 118
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
164-322 3.52e-44

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: 154.05  E-value: 3.52e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 164 HTVLLNDWWHRSTYEQAAGLASVPMVWVGEPQSLLINGRGRFvNCSSspataASCNVShpdCAPAVFAVVPGKTYRFRVA 243
Cdd:cd04205   1 RVLLLSDWYHDSAEDVLAGYMPNSFGNEPVPDSLLINGRGRF-NCSM-----AVCNSG---CPLPVITVEPGKTYRLRLI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 244 SVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPnRNYWLASNVVSR---KPATPTGTAVL 320
Cdd:cd04205  72 NAGSFASFNFAIDGHNMTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKADQPP-GNYWIRASADGRtfdEGGNPNGTAIL 150

                ..
gi 50725931 321 AY 322
Cdd:cd04205 151 RY 152
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
25-143 5.01e-44

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: 152.40  E-value: 5.01e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  25 TRRHDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVAIHWHGIRQIGTPWADGTEGVTQCP 104
Cdd:cd13854   3 TRKYTLTITNSTLAPDGVEKEVMLINGQYPGPLIEANWGDTIEVTVINKLQDNGTSIHWHGIRQLNTNWQDGVPGVTECP 82
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 50725931 105 ILPGDTFAYTFVVDRPGTYMYHAHYGMQRSAGLNGMIVV 143
Cdd:cd13854  83 IAPGDTRTYRFRATQYGTSWYHSHYSAQYGDGVVGPIVI 121
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
416-557 2.47e-38

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: 137.57  E-value: 2.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   416 FDQRPPPETYAGAAAFDVYAVQGNPNATTSDA-PYRLRFGSVVDVVLQNANMLaansseTHPWHLHGHDFWVLGHGAGrF 494
Cdd:pfam07731   2 TPPKLPTLLQITSGNFRRNDWAINGLLFPPNTnVITLPYGTVVEWVLQNTTTG------VHPFHLHGHSFQVLGRGGG-P 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50725931   495 DPAVHPAAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVFEEGVE 557
Cdd:pfam07731  75 WPEEDPKTYNLVDPVRRDTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPG 137
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
162-322 2.26e-37

The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant laccases similar 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 couples 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: 259941 [Multi-domain]  Cd Length: 161  Bit Score: 135.88  E-value: 2.26e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 162 GEHTVLLNDWWHRSTYEQAAGLASVPMVWVGEPQSLLINGRGrfvNCSSSPATAASCNVShpdCAPAVFAVVPGKTYRFR 241
Cdd:cd13873   1 EERILLFSDYFPKTDSTIETGLTATPFVWPGEPNALLVNGKS---GGTCNKSATEGCTTS---CHPPVIDVEPGKTYRFR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 242 VASVTSLSALNFEIEGH-EMTVVEADGHYVKPFVVKNLNIYSGETYSVLITAD-----QDPNRN-YWLasNVVSR-KPAT 313
Cdd:cd13873  75 FIGATALSFVSLGIEGHdNLTIIEADGSYTKPAETDHLQLGSGQRYSFLLKTKsleelAALNKTtFWI--QIETRwRPTN 152

                ....*....
gi 50725931 314 PTGTAVLAY 322
Cdd:cd13873 153 DTGYAVLRY 161
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
373-552 3.05e-35

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: 130.90  E-value: 3.05e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 373 RTILLLNTQNKIGGQIKWALNNVSF--TLPHTPYLVAMKRGLLGAFdqrPPPETYAGAAAFDvyavqgnpnATTSDAPYR 450
Cdd:cd13895   4 RRIIITIQQLNADGGVLWAQNGLTWteTLPSVPYLVQLYEYGTSLL---PDYEAALANGGFD---------PETNTFPAK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 451 LrfGSVVDVVLQNANMlAANSSETHPWHLHGHDFWVLGHGAGRFDPAVHPAAYNLR--DPIMKNTVAVHPF--------- 519
Cdd:cd13895  72 L--GEVLDIVWQNTAS-PTGGLDAHPWHAHGAHYYDLGSGLGTYSATALANEEKLRgyNPIRRDTTMLYRYggkgyyppp 148
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 50725931 520 ----GWTALRFRADNPGVWAFHCHIEAHFFMGMGIVF 552
Cdd:cd13895 149 gtgsGWRAWRLRVDDPGVWMLHCHILQHMIMGMQTVW 185
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
447-553 1.07e-34

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: 127.58  E-value: 1.07e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 447 APYRLRFGSVVDVVLQNANmlaaNSSETHPWHLHGHDFWVLGHGAGRFDpavhpAAYNLRDPIMKNTVAVHPFGWTALRF 526
Cdd:cd04207  35 DIFSVEAGDVVEIVLINAG----NHDMQHPFHLHGHSFWVLGSGGGPFD-----APLNLTNPPWRDTVLVPPGGWVVIRF 105
                        90       100
                ....*....|....*....|....*..
gi 50725931 527 RADNPGVWAFHCHIEAHFFMGMGIVFE 553
Cdd:cd04207 106 KADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
32-143 1.69e-34

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: 126.26  E-value: 1.69e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  32 ISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIRQIGTPWADGTEGVTQCPILPGDTF 111
Cdd:cd13850   5 VTEGSPDGDGGEREVILINGQFPGPPIILDEGDEVEILVTNNL-PVNTTIHFHGILQRGTPWSDGVPGVTQWPIQPGGSF 83
                        90       100       110
                ....*....|....*....|....*....|...
gi 50725931 112 AYTF-VVDRPGTYMYHAHYGMQRSAGLNGMIVV 143
Cdd:cd13850  84 TYRWkAEDQYGLYWYHSHYRGYYMDGLYGPIYI 116
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
28-143 2.82e-34

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: 125.91  E-value: 2.82e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  28 HDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTEN----VAIHWHGIRQIGTPWADGTEGVTQC 103
Cdd:cd13856   3 YTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTmrrsTSIHWHGIFQHGTNYADGPAFVTQC 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 50725931 104 PILPGDTFAYTF-VVDRPGTYMYHAHYGMQRSAGLNGMIVV 143
Cdd:cd13856  83 PIAPNHSFTYDFtAGDQAGTFWYHSHLSTQYCDGLRGPLVI 123
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
26-143 2.10e-33

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: 123.53  E-value: 2.10e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  26 RRHDWDISYQFTSPDCV-RKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVAIHWHGIRQIGTPWADGTEGVTQCP 104
Cdd:cd13851   1 VEFDWNITWVTANPDGLfERRVIGINGQWPPPPIEVNKGDTVVIHATNSLGDQPTSLHFHGLFQNGTNYMDGPVGVTQCP 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 50725931 105 ILPGDTFAYTFVVDRP-GTYMYHAHYGMQRSAGLNGMIVV 143
Cdd:cd13851  81 IPPGQSFTYEFTVDTQvGTYWYHSHDGGQYPDGLRGPFII 120
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
163-302 7.70e-32

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: 120.03  E-value: 7.70e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 163 EHTVLLNDWWHRSTYEQAAGLASVPMVWVgePQSLLINGRGRFVNCSSSPATAAScnvshpdcaPAVFAVVPGKTYRFRV 242
Cdd:cd13884   1 EHVILIQDWTHELSSERFVGRGHNGGGQP--PDSILINGKGRYYDPKTGNTNNTP---------LEVFTVEQGKRYRFRL 69
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50725931 243 ASVTSLS-ALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNrNYWL 302
Cdd:cd13884  70 INAGATNcPFRVSIDGHTLTVIASDGNDVEPVEVDSIIIYPGERYDFVLNANQPIG-NYWI 129
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
455-552 8.89e-31

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: 117.78  E-value: 8.89e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 455 SVVDVVLQNANMLAanssetHPWHLHGHDFWVLGHGAGRFDPAVHPAA----YNLRDPIMKNTVAVHPFGWTALRFRADN 530
Cdd:cd13910  69 KVVDLVINNLDDGD------HPFHLHGHKFWVLGSGDGRYGGGGYTAPdgtsLNTTNPLRRDTVSVPGFGWAVLRFVADN 142
                        90       100
                ....*....|....*....|..
gi 50725931 531 PGVWAFHCHIEAHFFMGMGIVF 552
Cdd:cd13910 143 PGLWAFHCHILWHMAAGMLMQF 164
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
165-322 9.73e-31

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: 117.51  E-value: 9.73e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 165 TVL-LNDWWHRSTYEQAAGLASVPMVwvgePQSLLINGRGRFVNCSSSPAtaascnvshpdcapAVFAVVPGKTYRFRVA 243
Cdd:cd13882   1 TVItLGDWYHTAAPDLLATTAGVPPV----PDSGTINGKGRFDGGPTSPL--------------AVINVKRGKRYRFRVI 62
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50725931 244 SVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNrNYWLASNVVSRKPATPTGTAVLAY 322
Cdd:cd13882  63 NISCIPSFTFSIDGHNLTVIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVD-NYWIRAPPTGGTPANNGGQLNRAI 140
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
28-143 2.85e-30

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: 114.66  E-value: 2.85e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  28 HDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLtENVAIHWHGIRQIGTPWADGTEGVTQCPILP 107
Cdd:cd13849   1 YTFVVQEKNVTRLCSTKSILTVNGQFPGPTIRVHEGDTVVVNVTNRSP-YNITIHWHGIRQLRSGWADGPAYITQCPIQP 79
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 50725931 108 GDTFAYTF-VVDRPGTYMYHAHYGMQRsAGLNGMIVV 143
Cdd:cd13849  80 GQSYTYRFtVTGQEGTLWWHAHISWLR-ATVYGAFII 115
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
165-302 3.57e-30

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: 115.83  E-value: 3.57e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 165 TVLLNDWWHR--STYeqaagLASVPMVWVGE----PQSLLINGRGRFvNCSSSPAtAASCNVSHPDCApaVFAVVPGKTY 238
Cdd:cd13886   2 VVMVNDYYHDpsSVL-----LARYLAPGNEGdepvPDNGLINGIGQF-DCASATY-KIYCCASNGTYY--NFTLEPNKTY 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50725931 239 RFRVASVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWL 302
Cdd:cd13886  73 RLRLINAGSFADFTFSVDGHPLTVIEADGTLVEPVEVHSITISVAQRYSVILTTNQPTGGNFWM 136
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
50-144 1.24e-28

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: 110.02  E-value: 1.24e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  50 NGHTPGPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIRqigTPWA-DGTEGVTQCPILPGDTFAYTFVVDRPGTYMYHAH 128
Cdd:cd13861  26 NGQVPGPELRVRQGDTLRVRLTNRL-PEPTTIHWHGLR---LPNAmDGVPGLTQPPVPPGESFTYEFTPPDAGTYWYHPH 101
                        90
                ....*....|....*...
gi 50725931 129 YGM--QRSAGLNGMIVVE 144
Cdd:cd13861 102 VGSqeQLDRGLYGPLIVE 119
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
46-144 2.70e-28

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: 109.21  E-value: 2.70e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  46 AVTINGHTPGPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIR-QIGTpwaDGTEGVTQCPILPGDTFAYTFVVDRPGTYM 124
Cdd:cd13860  22 AWGYNGSVPGPTIEVTEGDRVRILVTNEL-PEPTTVHWHGLPvPNGM---DGVPGITQPPIQPGETFTYEFTAKQAGTYM 97
                        90       100
                ....*....|....*....|..
gi 50725931 125 YHAHYGM--QRSAGLNGMIVVE 144
Cdd:cd13860  98 YHSHVDEakQEDMGLYGAFIVH 119
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
46-144 5.13e-28

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: 108.14  E-value: 5.13e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  46 AVTINGHTPGPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIRqigTPWA-DGTEGVTQCPILPGDTFAYTFVVDRPGTYM 124
Cdd:cd13848  21 AITVNGQVPGPLLRFKEGDDATIRVHNRL-DEDTSIHWHGLL---LPNDmDGVPGLSFPGIKPGETFTYRFPVRQSGTYW 96
                        90       100
                ....*....|....*....|
gi 50725931 125 YHAHYGMQRSAGLNGMIVVE 144
Cdd:cd13848  97 YHSHSGLQEQTGLYGPIIID 116
CuRO_2_AAO_like_1 cd13872
The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate ...
162-322 5.82e-28

The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate oxidase; The proteins in this subfamily are expressed in plant pollen. They share homology to ascorbate oxidase and other members of the blue copper oxidase family. The expression of the protein is detected during germination and pollen tube growth. Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. It is a member of the multicopper oxidase (MCO) family that couples 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: 259940 [Multi-domain]  Cd Length: 141  Bit Score: 109.03  E-value: 5.82e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 162 GEHTVLLNDWWHRSTYEQAAGLASVPMVwvGEPQSLLINGRGRFVNCSSSPAtaascnvshpdcapavFAVVPGKTYRFR 241
Cdd:cd13872   1 DEYTVLIGDWYKTDHKTLRQSLDKGRTL--GRPDGILINGKGPYGYGANETS----------------FTVEPGKTYRLR 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 242 VASVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPnRNYWLasnVVSRKPATP--TGTAV 319
Cdd:cd13872  63 ISNVGLRTSLNFRIQGHKMLLVETEGSYTAQNTYDSLDVHVGQSYSVLVTADQSP-KDYYI---VASSRFLSPelTGVAI 138

                ...
gi 50725931 320 LAY 322
Cdd:cd13872 139 LHY 141
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
450-555 1.91e-26

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: 105.84  E-value: 1.91e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 450 RLRFGSVVDVVLQNANMLAANSsetHPWHLHGHDFWVLGHGAGRFDPAV----HPAAY------------NLRDPIMKNT 513
Cdd:cd13905  48 KLPLNSVVEIVLINEGPGPGLS---HPFHLHGHSFYVLGMGFPGYNSTTgeilSQNWNnklldrgglpgrNLVNPPLKDT 124
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 50725931 514 VAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVFEEG 555
Cdd:cd13905 125 VVVPNGGYVVIRFRADNPGYWLLHCHIEFHLLEGMALVLKVG 166
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
391-554 9.70e-26

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: 103.49  E-value: 9.70e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 391 ALNNVSFTLPHTPYL-VAMKRGLLGAfdqrpPPETYAGaaafdvyavqgNPNattsdaPYRLRFGSVVDVVLQNanmlaa 469
Cdd:cd13899  21 AFNNITYVSPKVPTLyTALSMGDDAL-----DPAIYGP-----------QTN------AFVLNHGEVVELVVNN------ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 470 NSSETHPWHLHGHDFWVLGHGAGRFDPAVHPAAYNLRD-PIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGM 548
Cdd:cd13899  73 WDAGKHPFHLHGHKFQVVQRSPDVASDDPNPPINEFPEnPMRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGL 152

                ....*.
gi 50725931 549 GIVFEE 554
Cdd:cd13899 153 AATFIE 158
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
28-143 1.57e-25

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: 101.33  E-value: 1.57e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  28 HDWDISYQFTSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSlLTENVAIHWHGIRQIGTPWADGTEGvTQCPILP 107
Cdd:cd13846   3 FDWNVSYITASPLGVPQQVIAINGQFPGPTINVTTNDNVVVNVFNS-LDEPLLLTWNGIQQRRNSWQDGVLG-TNCPIPP 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 50725931 108 GDTFAYTFVV-DRPGTYMYHAHYGMQRSAGLNGMIVV 143
Cdd:cd13846  81 GWNWTYKFQVkDQIGSFFYFPSLHFQRAAGGFGGIRV 117
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
166-322 2.48e-25

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: 102.42  E-value: 2.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 166 VLLNDWWHRSTYEQAAGLASVP----MVWVGEPQSLLINGRGRFvNCSsspatAASCNVSHPDCAPAVFAVVPGKTYRFR 241
Cdd:cd13883   3 LFISDWYHDQSEVIVAGLLSPQgykgSPAAPSPDSALINGIGQF-NCS-----AADPGTCCTQTSPPEIQVEAGKRTRFR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 242 VASVTSLSALNFEIEGHEMTVVEADGHYV-KPFVVKNLNIYSGETYSVLITADQD-PNRNYWL----ASNVVSRKPATPT 315
Cdd:cd13883  77 LINAGSHAMFRFSVDNHTLNVVEADDTPVyGPTVVHRIPIHNGQRYSVIIDTTSGkAGDSFWLrarmATDCFAWDLQQQT 156

                ....*..
gi 50725931 316 GTAVLAY 322
Cdd:cd13883 157 GKAILRY 163
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
50-140 2.25e-24

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: 98.32  E-value: 2.25e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  50 NGHTPGPTIRAVQGDTIVVNVKNsLLTENVAIHWHGIRQIGTPWADGTEGVTQCPILPGDTFAYTFVVDRPGTYMYHAHY 129
Cdd:cd13859  26 NGQVPGPLIHVKEGDDLVVHVTN-NTTLPHTIHWHGVLQMGSWKMDGVPGVTQPAIEPGESFTYKFKAERPGTLWYHCHV 104
                        90
                ....*....|.
gi 50725931 130 GMQRSAGLNGM 140
Cdd:cd13859 105 NVNEHVGMRGM 115
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
372-555 3.39e-24

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: 99.25  E-value: 3.39e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 372 DRTILLlnTQNKIGGQIKWALNNVSFtlphtpYLVAMKrgllgafDQRPPPETYAGAAAFDvyavqgnPNATTSdapyrL 451
Cdd:cd13898   1 DQTLIL--TLGRVGSAYSWTLNGTEL------YPLDEE-------AYPPLLFLPDPATALD-------SALTIS-----T 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 452 RFGSVVDVVLQNAnmlaANSSETHPWHLHGHDFWVLGHGAGRFD-----PAVH--PAAYNLRDPIMKNTV----AVHPFG 520
Cdd:cd13898  54 KNGTWVDLIFQVT----GPPQPPHPIHKHGNKAFVIGTGTGPFNwssvaEAAEaaPENFNLVNPPLRDTFttppSTEGPS 129
                       170       180       190
                ....*....|....*....|....*....|....*
gi 50725931 521 WTALRFRADNPGVWAFHCHIEAHFFMGMGIVFEEG 555
Cdd:cd13898 130 WLVIRYHVVNPGAWLLHCHIQSHLAGGMAVVLLDG 164
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
163-300 1.64e-23

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: 96.85  E-value: 1.64e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 163 EHTVLLNDWWHRSTYEqaagLASVPMVWVGE------PQSLLINgrgrfvncssspataascnvshpDCAPAVFAVVPGK 236
Cdd:cd13877   2 EVTLTLSDWYHDQSPD----LLRDFLSPYNPtgaepiPDSSLFN-----------------------DTQNATINFEPGK 54
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50725931 237 TYRFRVASVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNY 300
Cdd:cd13877  55 TYLLRIINMGAFASQYFHIEGHDMTIIEVDGVYVKPYPVDTLYIAVGQRYSVLVKAKNDTDRNY 118
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
37-144 2.35e-23

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: 95.29  E-value: 2.35e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  37 TSPDCVRKLAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVAIHWHGIRQIGTPWADGTEGVTQCPILPGDTFAYTFV 116
Cdd:cd13847   8 SCDPFGPRPSTLINGSFPGPELRVQEGQHLWVRVYNDLEAGNTTMHFHGLSQYMSPFSDGTPLASQWPIPPGKFFDYEFP 87
                        90       100       110
                ....*....|....*....|....*....|
gi 50725931 117 VDR--PGTYMYHAHYGMQrSAGLNGMIVVE 144
Cdd:cd13847  88 LEAgdAGTYYYHSHVGFQ-SVTAYGALIVE 116
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
164-322 5.99e-23

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: 94.97  E-value: 5.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 164 HTVLLNDWWHRST---YEQAAGLASVPMVwvgePQSLLINGR-GRFVNCSSSPAtaascnvshpdcapAVFAVVPGKTYR 239
Cdd:cd13875   1 VPIILGEWWNRDVndvEDQALLTGGGPNI----SDAYTINGQpGDLYNCSSKDT--------------FVLTVEPGKTYL 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 240 FRVASvtslSALN----FEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRnYWLASNVVSRKPATP- 314
Cdd:cd13875  63 LRIIN----AALNeelfFKIANHTLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTADQPPGR-YYMAARPYQSAPPVPf 137
                       170
                ....*....|.
gi 50725931 315 ---TGTAVLAY 322
Cdd:cd13875 138 dntTATAILEY 148
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
434-550 4.52e-22

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: 93.06  E-value: 4.52e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 434 YAVQGNPNA-TTSDAPYRL-RFGSVVDVVLQNanmlaaNSSETHPWHLHGHDFWVLGHGAGRFDPAvhPAAYNLRDPIMK 511
Cdd:cd13901  44 LVADGNTSTfPPEWNVIELpKANKWVYIVIQN------NSPLPHPIHLHGHDFYILAQGTGTFDDD--GTILNLNNPPRR 115
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 50725931 512 NTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGI 550
Cdd:cd13901 116 DVAMLPAGGYLVIAFKTDNPGAWLMHCHIAWHASGGLAL 154
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
165-302 1.01e-21

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: 92.31  E-value: 1.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 165 TVLLNDWWHRSTYE--QAAGLASVPMVwvgePQSLLINGRGRFvNCSSSPAtaascnvshpdcAPAVFAVVPGKTYRFRV 242
Cdd:cd13880   3 PVLLTDWYHRSAFElfSEELPTGGPPP----MDNILINGKGKF-PCSTGAG------------SYFETTFTPGKKYRLRL 65
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 243 ASVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNRNYWL 302
Cdd:cd13880  66 INTGVDTTFRFSIDGHNLTVIAADFVPIVPYTTDSLNIGIGQRYDVIVEANQDPVGNYWI 125
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
372-556 1.18e-21

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: 91.19  E-value: 1.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 372 DRTILLLNTQNKIGGQikWALNNVSFTLPHTPYLVAMkrgLLGAfdqrpppetyagAAAFDVyavqgNPNATTsdapYRL 451
Cdd:cd13903   1 DVNITLTFGLNGTTGL--FTINGVSYVSPTVPVLLQI---LSGA------------TSAEDL-----LPTEST----IIL 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 452 RFGSVVDVVLQnanmlAANSSETHPWHLHGHDFWVLgHGAGRfdpavhpAAYNLRDPIMKNTVAVHPFG-WTALRFRADN 530
Cdd:cd13903  55 PRNKVVEITIP-----GGAIGGPHPFHLHGHAFSVV-RSAGS-------NTYNYVNPVRRDVVSVGTPGdGVTIRFVTDN 121
                       170       180
                ....*....|....*....|....*.
gi 50725931 531 PGVWAFHCHIEAHFFMGMGIVFEEGV 556
Cdd:cd13903 122 PGPWFLHCHIDWHLEAGLAVVFAEDP 147
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
456-551 1.99e-21

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: 91.20  E-value: 1.99e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 456 VVDVVLQNANmlaanSSETHPWHLHGHDFWVLGHGAGRFDPAVHP-AAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVW 534
Cdd:cd13904  64 WYDIVINNLD-----PAIDHPYHLHGVDFHIVARGSGTLTLEQLAnVQYNTTNPLRRDTIVIPGGSWAVLRIPADNPGVW 138
                        90       100
                ....*....|....*....|
gi 50725931 535 AFHCHIEAHF---FMGMGIV 551
Cdd:cd13904 139 ALHCHIGWHLaagFAGVVVV 158
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
164-322 4.19e-21

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: 89.57  E-value: 4.19e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 164 HTVLLNDWWHRST-----YEQAAGLASVPMvwvgepQSLLINGRGRfVNCssspataascnvshpdcapAVFAVVPGKTY 238
Cdd:cd13876   1 QPIILSDWRHLTSeeywkIMRASGIEPFCY------DSILINGKGR-VYC-------------------LIVIVDPGERW 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 239 R-FRVASVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQDPNrNYW--LASNvvsRKPATPT 315
Cdd:cd13876  55 VsLNFINAGGFHTLAFSIDEHPMWVYAVDGGYIEPQLVDAISITNGERYSVLVKLDKPPG-DYTirVAST---GAPQVIS 130

                ....*..
gi 50725931 316 GTAVLAY 322
Cdd:cd13876 131 GYAILRY 137
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
444-553 1.46e-18

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: 81.53  E-value: 1.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 444 TSDAPYRLRFGSVVDVVLQNANMLAanssetHPWHLHGHDFWVLGhGAGRFDPavhpaaynlrdpiMKNTVAVHPFGWTA 523
Cdd:cd13896  25 PDADPLRVREGERVRIVFVNDTMMA------HPMHLHGHFFQVEN-GNGEYGP-------------RKDTVLVPPGETVS 84
                        90       100       110
                ....*....|....*....|....*....|
gi 50725931 524 LRFRADNPGVWAFHCHIEAHFFMGMGIVFE 553
Cdd:cd13896  85 VDFDADNPGRWAFHCHNLYHMEAGMMRVVE 114
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
446-557 8.79e-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: 79.99  E-value: 8.79e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 446 DAPYRLRFGSVVDVVLQNANMLAanssetHPWHLHGHDFWVLGHGAGRFDPAvhpaaynlrDPIMKNTVAVHPFGWTALR 525
Cdd:cd04202  40 TPPLVVKEGDRVRIRLINLSMDH------HPMHLHGHFFLVTATDGGPIPGS---------APWPKDTLNVAPGERYDIE 104
                        90       100       110
                ....*....|....*....|....*....|....
gi 50725931 526 FRADNPGVWAFHCHIEAH--FFMGMGIVFEEGVE 557
Cdd:cd04202 105 FVADNPGDWMFHCHKLHHamNGMGGGMMTLIGYE 138
CuRO_1_MCO_like_2 cd13864
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
44-144 1.68e-16

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: 76.42  E-value: 1.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  44 KLAVTINGH--TPGPTIRAVQGDTIVVNVKNSLLTEN-----------VAIHWHGI------RQIGTPwADGTEGVTQCP 104
Cdd:cd13864  18 KQIISINGSndTIGPTIRVKSGDTLNLLVTNHLCNEQelskiwqdycpTSIHFHGLvlenfgKQLANL-VDGVPGLTQYP 96
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 50725931 105 ILPGDTFAYTFVVDRP--GTYMYHAHYGMQRSAGLNGMIVVE 144
Cdd:cd13864  97 IGVGESYWYNFTIPEDtcGTFWYHSHSSVQYGDGLRGVFIVD 138
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
49-144 2.51e-16

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: 75.30  E-value: 2.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  49 INGHTPGPTIRAVQGDTIVVNVKNSlLTENVAIHWHGIRQIGTpwADGteGVTQcPILPGDTFAYTFVVDRP-GTYMYHA 127
Cdd:cd04232  25 YNGSYLGPTIRVKKGDTVRINVTNN-LDEETTVHWHGLHVPGE--MDG--GPHQ-PIAPGQTWSPTFTIDQPaATLWYHP 98
                        90       100
                ....*....|....*....|..
gi 50725931 128 HYgMQRSA-----GLNGMIVVE 144
Cdd:cd04232  99 HT-HGKTAeqvyrGLAGLFIIE 119
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
48-144 8.17e-16

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: 73.84  E-value: 8.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  48 TINGHTPGPTIRAVQGDTIVVNVKNSLLTENvAIHWHGIRqigTPWADGTEGVtqcPILPGDTFAYTFVVDRPGTYMYHA 127
Cdd:cd11024  25 TYNGTVPGPTLRATEGDLVRIHFINTGDHPH-TIHFHGIH---DAAMDGTGLG---PIMPGESFTYEFVAEPAGTHLYHC 97
                        90       100
                ....*....|....*....|
gi 50725931 128 HY---GMQRSAGLNGMIVVE 144
Cdd:cd11024  98 HVqplKEHIAMGLYGAFIVD 117
CuRO_1_LCC_like_3 cd13865
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
48-144 4.48e-15

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: 71.57  E-value: 4.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  48 TINGHTPGPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIRqigTPWA-DGTEGVTQCPILPGDTFAYTFVVDRPGTYMYH 126
Cdd:cd13865  21 GIRQPDGTEGLRLTEGDRFDVELENRL-DEPTTIHWHGLI---PPNLqDGVPDVTQPPIPPGQSQRYDFPLVQPGTFWMH 96
                        90
                ....*....|....*...
gi 50725931 127 AHYGMQRSAGLNGMIVVE 144
Cdd:cd13865  97 SHYGLQEQKLLAAPLIIR 114
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
55-144 1.24e-14

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: 70.39  E-value: 1.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  55 GPTIRAVQGDTIVVNVKNSLlTENVAIHWHGIRqigTPWA-DGTEGVTqcpILPGDTFAYTF-VVDRPGTYMYHAH---- 128
Cdd:cd13852  24 GPILRLRKGQKVRITFKNNL-PEPTIIHWHGLH---VPAAmDGHPRYA---IDPGETYVYEFeVLNRAGTYWYHPHphgl 96
                        90
                ....*....|....*.
gi 50725931 129 YGMQRSAGLNGMIVVE 144
Cdd:cd13852  97 TAKQVYRGLAGLFLVT 112
CuRO_3_AAO_like_1 cd13894
The third cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
431-534 2.14e-14

The third 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 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. This subfamily does not harbor T1 copper or trinuclear copper binding sites.


Pssm-ID: 259961 [Multi-domain]  Cd Length: 123  Bit Score: 69.77  E-value: 2.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 431 FDVYAVQGNPNATTS--DAPYRlrfgSVVDVVLQNanmlaaNSSETHPWHLHGHDFWVLGHGAGRFDPAVHpAAYNLRDP 508
Cdd:cd13894  23 IPDPPTRKTPYLGTSviNGTYR----GFIEIVFQN------NEDTVQSWHLDGYSFFVVGMGFGDWTPEKR-KSYNLLDA 91
                        90       100
                ....*....|....*....|....*.
gi 50725931 509 IMKNTVAVHPFGWTALRFRADNPGVW 534
Cdd:cd13894  92 VSRSTTQVYPGSWTAILLELDNVGMW 117
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
46-144 1.47e-13

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: 67.24  E-value: 1.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  46 AVTINGHTPGPTIRAVQGDTIVVNVKNslLTENVAIH---WHGIRqigtpwADGTEGVTQcpILPGDTFAYTFVVDRPGT 122
Cdd:cd11020  23 AWTFNGQVPGPVIRVREGDTVELTLTN--PGTNTMPHsidFHAAT------GPGGGEFTT--IAPGETKTFSFKALYPGV 92
                        90       100
                ....*....|....*....|....*
gi 50725931 123 YMYH---AHYGMQRSAGLNGMIVVE 144
Cdd:cd11020  93 FMYHcatAPVLMHIANGMYGAIIVE 117
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
48-144 9.60e-13

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: 65.74  E-value: 9.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  48 TINGHTPGPTIRAVQGDTIVVNVKNSLLTENVA----------------IHWHGirqigtPWADGTEG-----VTqcpIL 106
Cdd:cd13853  24 TYNGSIPGPTLRVRPGDTLRITLKNDLPPEGAAneapapntphcpnttnLHFHG------LHVSPTGNsdnvfLT---IA 94
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 50725931 107 PGDTFAYTFVVDR---PGTYMYHAHY----GMQRSAGLNGMIVVE 144
Cdd:cd13853  95 PGESFTYEYDIPAdhpPGTYWYHPHLhgstALQVAGGMAGALVVE 139
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
55-143 1.34e-12

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: 66.29  E-value: 1.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  55 GPTIRAVQGDTIVVNVKNSLLTENVAIHWHGIRQigTPWADGTEGVTQCPILPGDTFAYTFVVDR---PGT-------YM 124
Cdd:cd04229  73 GPVIRAEVGDTIKVVFKNNLDEFPVNMHPHGGLY--SKDNEGTTDGAGDVVAPGETYTYRWIVPEdagPGPgdpssrlWL 150
                        90       100
                ....*....|....*....|.
gi 50725931 125 YHAHYGMQR--SAGLNGMIVV 143
Cdd:cd04229 151 YHSHVDVFAhtNAGLVGPIIV 171
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
416-553 4.93e-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: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 63.24  E-value: 4.93e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 416 FDQRPPpetyaGAAAFDVYAVQGNPNATtSDAPYRLRFGSVVDVVLQNAnmlaanSSETHPWHLHGHDFWVLghgagRFD 495
Cdd:cd13908   8 FEKRNA-----GDGGFNLWTINGKSYPD-EDPPLVVQQGRRYRLVFRNA------SDDAHPMHLHRHTFEVT-----RID 70
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 50725931 496 PAVHPAaynlrdpIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVFE 553
Cdd:cd13908  71 GKPTSG-------LRKDVVMLGGYQRVEVDFVADNPGLTLFHCHQQLHMDYGFMALFK 121
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
48-143 5.06e-12

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: 62.88  E-value: 5.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  48 TINGHTPGPTIRAVQGDTIVVNVKNSlLTENVAIHWHGIrqigtPWADGTEGVTQCPILPGDTFAYTFVV--DRPGTYMY 125
Cdd:cd13855  25 AYNGSVPGPLIEVFEGDTVEITFRNR-LPEPTTVHWHGL-----PVPPDQDGNPHDPVAPGNDRVYRFTLpqDSAGTYWY 98
                        90       100
                ....*....|....*....|..
gi 50725931 126 HAH-YGM---QRSAGLNGMIVV 143
Cdd:cd13855  99 HPHpHGHtaeQVYRGLAGAFVV 120
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
48-144 1.77e-11

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: 61.35  E-value: 1.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  48 TINGHTPGPTIRAVQGDTIVVNVKN---SLLTENvaIHWHGIRQIGtpwadGTEGVTQcpILPGDTFAYTFVVDRPGTYM 124
Cdd:cd04201  25 TFDGDIPGPMLRVREGDTVELHFSNnpsSTMPHN--IDFHAATGAG-----GGAGATF--IAPGETSTFSFKATQPGLYV 95
                        90       100
                ....*....|....*....|...
gi 50725931 125 YHAHYG---MQRSAGLNGMIVVE 144
Cdd:cd04201  96 YHCAVApvpMHIANGMYGLILVE 118
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
475-548 2.12e-11

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: 61.26  E-value: 2.12e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50725931 475 HPWHLHGHDFWVLGHGAGRFDPAVhpaaynlrdPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGM 548
Cdd:cd13902  55 HPFHLHGTQFQVLEIDGNPQKPEY---------RAWKDTVNLPPGEAVRIATRQDDPGMWMYHCHILEHEDAGM 119
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
475-548 8.31e-10

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: 57.01  E-value: 8.31e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50725931 475 HPWHLHGHDFWVLGHGaGRfdPAVHPaayNLRDpimknTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGM 548
Cdd:cd13906  69 HPMHLHGHFFRVLSRN-GR--PVPEP---FWRD-----TVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGM 131
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
197-294 1.81e-09

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: 55.42  E-value: 1.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 197 LLINGRgrfvncssspataascnvshPDCAPAVFAVVPGKTYRFRVASVTSLSALNFEIEGHEMTVVEADGHYVKPFVVK 276
Cdd:cd13870  18 YLINGR--------------------PPEDPAVFTARPGDRLRLRLINAAGDTAFRVALAGHRLTVTHTDGFPVEPVEVD 77
                        90
                ....*....|....*...
gi 50725931 277 NLNIYSGETYSVLITADQ 294
Cdd:cd13870  78 ALLIGMGERYDAIVTANN 95
PRK10965 PRK10965
multicopper oxidase; Provisional
49-144 2.48e-09

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 59.65  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   49 INGHTPGPTIRAVQGDTIVVNVKNSlLTENVAIHWHGIRQIGTpwADGTegvTQCPILPGDTFAYTFVVDRP-GTYMYHA 127
Cdd:PRK10965  70 YNGNLLGPAVRLQRGKAVTVDITNQ-LPEETTLHWHGLEVPGE--VDGG---PQGIIAPGGKRTVTFTVDQPaATCWFHP 143
                         90       100
                 ....*....|....*....|.
gi 50725931  128 HY----GMQRSAGLNGMIVVE 144
Cdd:PRK10965 144 HQhgktGRQVAMGLAGLVLIE 164
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
436-553 3.01e-09

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: 54.93  E-value: 3.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 436 VQGNPNATTSDAPYRLRF--GSVVDVVLQNANmlaansSETHPWHLHGHDFWVLGHGAGRFdpavhpaaynlrdPIMKNT 513
Cdd:cd00920  10 WSFTYNGVLLFGPPVLVVpvGDTVRVQFVNKL------GENHSVTIAGFGVPVVAMAGGAN-------------PGLVNT 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 50725931 514 VAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVFE 553
Cdd:cd00920  71 LVIGPGESAEVTFTTDQAGVYWFYCTIPGHNHAGMVGTIN 110
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
448-548 5.02e-08

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: 51.48  E-value: 5.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 448 PYRLRFGSVVDVVLQNAnmlaanSSETHPWHLHGHDFWVLGhgagRFDPAVhpaaynlRDPIMKNTVAVHPFGWTALRFR 527
Cdd:cd13900  33 DRTVRLGTVEEWTLINT------SGEDHPFHIHVNPFQVVS----INGKPG-------LPPVWRDTVNVPAGGSVTIRTR 95
                        90       100
                ....*....|....*....|..
gi 50725931 528 ADNP-GVWAFHCHIEAHFFMGM 548
Cdd:cd13900  96 FRDFtGEFVLHCHILDHEDQGM 117
CuRO_2_CopA cd13874
The second cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
234-295 1.48e-07

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: 49.98  E-value: 1.48e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50725931 234 PGKTYRFRVASVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLITADQD 295
Cdd:cd13874  31 PGERVRLRFINAAASTYFDVRIPGGKMTVVAADGQDVRPVEVDEFRIGVAETYDVIVTIPEN 92
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
45-128 3.85e-07

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: 49.05  E-value: 3.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  45 LAVTINGHTPGPTIRAVQGDTIVVNVKNSLLTENVaIHWHGIrQIGTPwADGTEGVTQCPILPGDTFAYTFVVDRPGTYM 124
Cdd:cd13862  21 STLGYNGQVPGPLLRMRQGVSVTVDVFNDTDIPEY-VHWHGL-PLPAD-VDGAMEEGTPSVPPHGHRRYRMTPRPAGFRW 97

                ....
gi 50725931 125 YHAH 128
Cdd:cd13862  98 YHTH 101
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
55-141 5.05e-07

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 48.38  E-value: 5.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  55 GPTIRAVQGDTIVVNVKNSL-LTENVAIHWHGIRQIGTPWADGTEGVTQCPILPGDTFAYTFVVDRPGTYMYHAHYGMQR 133
Cdd:cd00920  22 PPVLVVPVGDTVRVQFVNKLgENHSVTIAGFGVPVVAMAGGANPGLVNTLVIGPGESAEVTFTTDQAGVYWFYCTIPGHN 101

                ....*...
gi 50725931 134 SAGLNGMI 141
Cdd:cd00920 102 HAGMVGTI 109
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
475-553 5.26e-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: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 49.05  E-value: 5.26e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50725931 475 HPWHLHGHDFWVLGHGaGRFDPavhpaaynLRDpimknTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMGIVFE 553
Cdd:cd13909  71 HGMHLHGHHFRAILPN-GALGP--------WRD-----TLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGMMSWFR 135
CuRO_3_MCO_like_5 cd13911
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
471-553 8.76e-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: 47.93  E-value: 8.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 471 SSETHPWHLHGHDFWVLGHGAGRfdpavhPAAYnlrDPIMKNTVAVHPFGWTALRFRADN-PGVWAFHCHIEAHFFMGMG 549
Cdd:cd13911  45 SDGRHPVHLHGAHFQVVSRTGGR------PGEW---DAGWKDTVLLRPRESVTVIIRFDGyRGRYVFHCHNLEHEDMGMM 115

                ....
gi 50725931 550 IVFE 553
Cdd:cd13911 116 ANFQ 119
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
55-143 8.88e-07

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: 49.33  E-value: 8.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  55 GPTIRAVQGDTIVVNVKNsLLTENVAIHWHGIR----QIGTPWADGTEGV--TQCPILPGDTFAYTFVVDR---PG---- 121
Cdd:cd04199  69 GPTIRAEVGDTIKVHFKN-KASRPYSIHPHGVSyekdSEGASYSDQTGPDekKDDAVAPGETYTYVWIVTEesgPTkgdp 147
                        90       100
                ....*....|....*....|....*..
gi 50725931 122 ---TYMYHAHYGMQR--SAGLNGMIVV 143
Cdd:cd04199 148 aclTWAYYSHVDLEKdiNSGLIGPLLI 174
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
55-143 1.10e-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: 48.70  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  55 GPTIRAVQGDTIVVNVKNsLLTENVAIHWHGI----RQIGTPWADGTEGVTQC--PILPGDTFAYTFVV---------DR 119
Cdd:cd04226  56 GPTLRAEVGDTLIVHFKN-MADKPLSIHPQGIaygkKSEGSLYSDNTSPVEKLddAVQPGQEYTYVWDIteevgpteaDP 134
                        90       100
                ....*....|....*....|....*..
gi 50725931 120 PG-TYMYHAHYGMQR--SAGLNGMIVV 143
Cdd:cd04226 135 PClTYIYYSHVNMVRdfNSGLIGALLI 161
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
55-143 5.67e-06

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: 47.03  E-value: 5.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  55 GPTIRAVQGDTIVVNVKNsLLTENVAIHWHGIR----QIGTPWADGTEGVTQC--PILPGDTFAYTFVVDR---PG---- 121
Cdd:cd04222  75 GPILKAEVGDVIVVHLKN-FASRPYSLHPHGVFynkeNEGALYPDNTSGFEKAddAVPPGGSYTYTWTVPEeqaPTkada 153
                        90       100
                ....*....|....*....|....*..
gi 50725931 122 ---TYMYHAHYGMQR--SAGLNGMIVV 143
Cdd:cd04222 154 nclTRIYHSHIDAPKdiASGLIGPLII 180
CuRO_3_McoP_like cd13888
The third cupredoxin domain of multicopper oxidase McoP and similar proteins; This subfamily ...
475-550 9.20e-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: 45.63  E-value: 9.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 475 HPWHLHGHDFWVL---GHGAGRFDPAVHPAAYNLRDPIMKNTVAVHPfGWT---ALRFRADNPG--VWAFHCHIEAHFFM 546
Cdd:cd13888  52 HPMHIHGFQFQVLersDSPPQVAELAVAPSGRTATDLGWKDTVLVWP-GETvriAVDFTHDYPGdqLYLLHCHNLEHEDD 130

                ....
gi 50725931 547 GMGI 550
Cdd:cd13888 131 GMMV 134
CuRO_3_CueO_FtsP cd13890
The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
467-548 1.71e-05

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: 44.55  E-value: 1.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 467 LAANSSETHPWHLHGHDFWVLGHGAGRfdPAVHPAAYnlrdpimKNTVAVHPFGWT--ALRFR--ADNPGVWAFHCHIEA 542
Cdd:cd13890  42 VTNTDGMPHPFHIHGVQFRILSRNGQP--PPPNEAGW-------KDTVWVPPGETVriLVKFDhyADPTGPFMYHCHILE 112

                ....*.
gi 50725931 543 HFFMGM 548
Cdd:cd13890 113 HEDNGM 118
CuRO_3_MCO_like_1 cd13907
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
475-548 2.70e-04

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: 41.70  E-value: 2.70e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50725931 475 HPWHLHGHDFWVLGHGAGRFDPAVHPAA-YNLRDPIMKNTVAVHPFGWTAL--RFRaDNPGVWAFHCHIEAHFFMGM 548
Cdd:cd13907  72 HPIHLHGVQFQVLERSVGPKDRAYWATVkDGFIDEGWKDTVLVMPGERVRIikPFD-DYKGLFLYHCHNLEHEDMGM 147
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
55-125 2.84e-04

The third 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 third cupredoxin domain of ceruloplasmin.


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 42.07  E-value: 2.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  55 GPTIRAVQGDTIVVNVKNSlLTENVAIHWHGIR----QIGTPWADGTeGVTQCPILPGDTFAYTF-VVDRPG-------- 121
Cdd:cd04224  82 GPVIRAEVGDTIKVTFRNK-ASRPFSIQPHGVFyeknYEGAMYRDGD-PSPGSHVSPGETFTYEWtVPEGVGptnqdppc 159

                ....*
gi 50725931 122 -TYMY 125
Cdd:cd04224 160 lTYLY 164
CuRO_2_CumA_like cd13885
The second cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
227-298 5.12e-04

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: 40.39  E-value: 5.12e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50725931 227 PAVFAVVPGKTYRFRV--ASVTSLSALNFEieGHEMTVVEADGHYVKPFVVKNLNIY--SGETYSVLITADQDPNR 298
Cdd:cd13885  45 QPDFTVRAGERVRLRLinAANARVFALKFP--GHEARVIALDGQPAEPFVARNGAVVlaPGMRIDLVIDAPQAAGT 118
PetE COG3794
Plastocyanin [Energy production and conversion];
56-144 8.50e-04

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 38.44  E-value: 8.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  56 PTIRAVQGDTIV-VNvknsllTENVAIHWHGIRQIGTPWADGTegvtqcpILPGDTFAYTFvvDRPGTYMYH--AHYGMQ 132
Cdd:COG3794   6 ATLTVKPGDTVTwVN------TDSVPHNVTSDDGPDGAFDSGL-------LAPGETFSVTF--DEPGTYDYYctPHPWMV 70
                        90
                ....*....|..
gi 50725931 133 rsaglnGMIVVE 144
Cdd:COG3794  71 ------GTIVVG 76
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
56-144 1.11e-03

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


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 38.37  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931  56 PTIRAVQGDTIVVNVKN----SLLTENVAIHWHGIRQIgtpwadgtegvtqcpILPGDTFAYTFVVDRPGTYMY------ 125
Cdd:cd04223  16 DIIEVKEGDEVTVHLTNleqdEDITHGFAIPGYNVNLS---------------LEPGETATVTFVADKPGVYPYyctefc 80
                        90       100
                ....*....|....*....|
gi 50725931 126 HA-HYGMQrsaglnGMIVVE 144
Cdd:cd04223  81 SAlHLEMQ------GYLIVE 94
CuRO_3_BOD cd13889
The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the ...
475-553 1.22e-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: 39.22  E-value: 1.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 475 HPWHLHGHDFWVLGHGAGrfDPAVHPAAYNLRDpimknTVAVHPFGWT--ALRFRaDNPGVWAFHCHIEAHFFMGMGIVF 552
Cdd:cd13889  51 HPIHIHLEDFQILSRNGG--SRAVPPYERGRKD-----VVYLGPGEEVrvLMRFR-PFRGKYMMHCHNLVHEDHDMMLRF 122

                .
gi 50725931 553 E 553
Cdd:cd13889 123 E 123
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
470-552 1.38e-03

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: 38.74  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 470 NSSETHPWHLHGHDfwVLGHGAGRFDpavhpaaynlrdpimknTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFFMGMG 549
Cdd:cd11023  53 NEVDFHTPHWHGQT--VEADKSRRTD-----------------VAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMM 113

                ...
gi 50725931 550 IVF 552
Cdd:cd11023 114 TQF 116
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
470-548 1.40e-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: 39.32  E-value: 1.40e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50725931 470 NSSETHPWHLHGHDFWVLGHgagrfdpavHPAAYNLrdpimkntvavHPFGWTALRFRADNPGVWAFHCHIEAHFFMGM 548
Cdd:cd04200  77 NEVDVHSIHFHGQTFLYKGY---------RIDTLTL-----------FPATFETVEMVPSNPGTWLLHCHNSDHRHAGM 135
CuRO_2_MCO_like_2 cd13887
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
226-291 2.17e-03

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: 38.07  E-value: 2.17e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50725931 226 APAVFAVVPGKTYRFRVASVTSLSALNFEIEGHEMTVVEADGHYVKPFVVKNLNIYSGETYSVLIT 291
Cdd:cd13887  22 DPEVVRVEPGGRVRLRVINGSTATNFHIDLGDLKGTLIAVDGNPVQPVEGRRFPLATAQRLDLLVT 87
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
466-548 2.87e-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: 38.31  E-value: 2.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 466 MLAANSSETHPWHLHGHDFwvlghgagrfdpavhpaAYNLRDPIMKNTVAVHPFGWTALRFRADNPGVWAFHCHIEAHFF 545
Cdd:cd11012  73 MGMGNEIDIHTAHFHGHSF-----------------DYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIH 135

                ...
gi 50725931 546 MGM 548
Cdd:cd11012 136 AGM 138
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
225-294 4.71e-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: 37.21  E-value: 4.71e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 225 CAPAVFAVVPGKTYRFRVASvTSLSALNFEIEGHEMTVVEADGHYVKPFVVKnLNIYSGETYSVLITADQ 294
Cdd:cd00920  20 FGPPVLVVPVGDTVRVQFVN-KLGENHSVTIAGFGVPVVAMAGGANPGLVNT-LVIGPGESAEVTFTTDQ 87
CuRO_2_McoC_like cd13881
The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
193-298 4.83e-03

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


Pssm-ID: 259948 [Multi-domain]  Cd Length: 142  Bit Score: 37.59  E-value: 4.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 193 EPQSLLINGRgrfvncssspataascnvSHPdcapaVFAVVPGKTYRFRVASVTSLSALNFEIEGHEMTVVEADG-HYVK 271
Cdd:cd13881  30 EGDLVLVNGQ------------------LNP-----TITVRPGEVQRWRIVNAASARYFRLALDGHKFRLIGTDGgLLEA 86
                        90       100
                ....*....|....*....|....*..
gi 50725931 272 PFVVKNLNIYSGETYSVLITADQDPNR 298
Cdd:cd13881  87 PREVDELLLAPGERAEVLVTAGEPGGR 113
PRK10883 PRK10883
FtsI repressor; Provisional
43-144 7.04e-03

FtsI repressor; Provisional


Pssm-ID: 182808 [Multi-domain]  Cd Length: 471  Bit Score: 39.30  E-value: 7.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931   43 RKLAV-TINGHTPGPTIRAVQGDTIVVNVKNSlLTENVAIHWHGIrQIGTPWADG-----TEGVTQCPILPgdtfaytfV 116
Cdd:PRK10883  63 TKASVwGINGRYLGPTIRVWKGDDVKLIYSNR-LTEPVSMTVSGL-QVPGPLMGGparmmSPNADWAPVLP--------I 132
                         90       100       110
                 ....*....|....*....|....*....|..
gi 50725931  117 VDRPGTYMYHA----HYGMQRSAGLNGMIVVE 144
Cdd:PRK10883 133 RQNAATCWYHAntpnRMAQHVYNGLAGMWLVE 164
CuRO_2_BOD_CotA_like cd14448
Cupredoxin domain 2 of Bilirubin oxidase (BOD), the bacterial endospore coat component CotA, ...
198-317 8.57e-03

Cupredoxin domain 2 of Bilirubin oxidase (BOD), the bacterial endospore coat component CotA, and similar proteins; Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and is required for spore resistance against hydrogen peroxide and UV light. Also included in this subfamily are phenoxazinone synthase (PHS), which catalyzes the oxidative coupling of substituted o-aminophenols to produce phenoxazinones, and FtsP (also named SufI), which is a component of the cell division apparatus. These proteins are laccase-like multicopper oxidases (MCOs) that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259990 [Multi-domain]  Cd Length: 144  Bit Score: 36.90  E-value: 8.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50725931 198 LINGRGRFVNCS---SSPATAASC-NVSHPDCAPAVFAVVPGKTYRFRVASVTSLSALNFEI-EGHEMTVVEADGHYV-K 271
Cdd:cd14448  10 QFNADGTLYYPSpptNMEWVPGFFgDVILVNGKIWPYLEVEPGWYRLRLLNASNARHYNLALsDGLPFHVIGSDGGLLeA 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 50725931 272 PFVVKNLNIYSGETYSVLITADQDPNRNYWLASNVVSRKPATPTGT 317
Cdd:cd14448  90 PVKVKELVLAPAERIDVVVDFSQYAGEEVELVNLGGASMAILPTDY 135
 
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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