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Conserved domains on  [gi|15235448|ref|NP_195433|]
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SKU5 similar 15 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02835 super family cl31936
oxidoreductase
4-537 0e+00

oxidoreductase


The actual alignment was detected with superfamily member PLN02835:

Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 767.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448    4 TNLLVCKLFIGALFWLGSV-LVNAEDPYMFYTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEP 82
Cdd:PLN02835   2 GSAVNLHLLLGVLAVLSSVsLVNGEDPYKYYTWTVTYGTISPLGVPQQVILINGQFPGPRLDVVTNDNIILNLINKLDQP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   83 FLITWNGVKQRRTSWQDGVLGTNCPIQPNSNWTYQFQLKDQIGTYTYFASTSLHRASGAFGALNINQRSVITTPYPTPDG 162
Cdd:PLN02835  82 FLLTWNGIKQRKNSWQDGVLGTNCPIPPNSNYTYKFQTKDQIGTFTYFPSTLFHKAAGGFGAINVYERPRIPIPFPLPDG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  163 DFTLLVSDWFSNmTHKDLRKSLDAGSALPLPDALLINGVSKGlIFTGQQGKTYKFRVSNVGIATSINFRIQNHTMSLIEV 242
Cdd:PLN02835 162 DFTLLVGDWYKT-SHKTLQQRLDSGKVLPFPDGVLINGQTQS-TFSGDQGKTYMFRISNVGLSTSLNFRIQGHTMKLVEV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  243 EGAHTLQESYESLDVHVGQSMTVLVTLKASVRDYFIVASTRFTKPVLTTTASLRYQGSKNAAYGPLPIGPTYHIHWSMKQ 322
Cdd:PLN02835 240 EGSHTIQNIYDSLDVHVGQSVAVLVTLNQSPKDYYIVASTRFTRQILTATAVLHYSNSRTPASGPLPALPSGELHWSMRQ 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  323 ARTIRMNLTANAARPNPQGSFHYGTIPINRTLVLANAATLIYGKLRYTVNRISYINPTTPLKLADWYNISGVFDFKTIIS 402
Cdd:PLN02835 320 ARTYRWNLTASAARPNPQGSFHYGKITPTKTIVLANSAPLINGKQRYAVNGVSYVNSDTPLKLADYFGIPGVFSVNSIQS 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  403 TPTTGPAHIGTSVIDVELHEFVEIVFQNDERSIQSWHMDGTSAYAVGYGSGTWNVTMRKRYNLVDAVPRHTFQVYPLSWT 482
Cdd:PLN02835 400 LPSGGPAFVATSVMQTSLHDFLEVVFQNNEKTMQSWHLDGYDFWVVGYGSGQWTPAKRSLYNLVDALTRHTAQVYPKSWT 479
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15235448  483 TILVSLDNKGMWNLRSQIWSRRYLGQELYVRVWNDEKSLYTEAEPPLNVLYCGKA 537
Cdd:PLN02835 480 TILVSLDNQGMWNMRSAIWERQYLGQQFYLRVWNQVHSLANEYDIPDNALLCGKA 534
 
Name Accession Description Interval E-value
PLN02835 PLN02835
oxidoreductase
4-537 0e+00

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 767.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448    4 TNLLVCKLFIGALFWLGSV-LVNAEDPYMFYTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEP 82
Cdd:PLN02835   2 GSAVNLHLLLGVLAVLSSVsLVNGEDPYKYYTWTVTYGTISPLGVPQQVILINGQFPGPRLDVVTNDNIILNLINKLDQP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   83 FLITWNGVKQRRTSWQDGVLGTNCPIQPNSNWTYQFQLKDQIGTYTYFASTSLHRASGAFGALNINQRSVITTPYPTPDG 162
Cdd:PLN02835  82 FLLTWNGIKQRKNSWQDGVLGTNCPIPPNSNYTYKFQTKDQIGTFTYFPSTLFHKAAGGFGAINVYERPRIPIPFPLPDG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  163 DFTLLVSDWFSNmTHKDLRKSLDAGSALPLPDALLINGVSKGlIFTGQQGKTYKFRVSNVGIATSINFRIQNHTMSLIEV 242
Cdd:PLN02835 162 DFTLLVGDWYKT-SHKTLQQRLDSGKVLPFPDGVLINGQTQS-TFSGDQGKTYMFRISNVGLSTSLNFRIQGHTMKLVEV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  243 EGAHTLQESYESLDVHVGQSMTVLVTLKASVRDYFIVASTRFTKPVLTTTASLRYQGSKNAAYGPLPIGPTYHIHWSMKQ 322
Cdd:PLN02835 240 EGSHTIQNIYDSLDVHVGQSVAVLVTLNQSPKDYYIVASTRFTRQILTATAVLHYSNSRTPASGPLPALPSGELHWSMRQ 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  323 ARTIRMNLTANAARPNPQGSFHYGTIPINRTLVLANAATLIYGKLRYTVNRISYINPTTPLKLADWYNISGVFDFKTIIS 402
Cdd:PLN02835 320 ARTYRWNLTASAARPNPQGSFHYGKITPTKTIVLANSAPLINGKQRYAVNGVSYVNSDTPLKLADYFGIPGVFSVNSIQS 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  403 TPTTGPAHIGTSVIDVELHEFVEIVFQNDERSIQSWHMDGTSAYAVGYGSGTWNVTMRKRYNLVDAVPRHTFQVYPLSWT 482
Cdd:PLN02835 400 LPSGGPAFVATSVMQTSLHDFLEVVFQNNEKTMQSWHLDGYDFWVVGYGSGQWTPAKRSLYNLVDALTRHTAQVYPKSWT 479
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15235448  483 TILVSLDNKGMWNLRSQIWSRRYLGQELYVRVWNDEKSLYTEAEPPLNVLYCGKA 537
Cdd:PLN02835 480 TILVSLDNQGMWNMRSAIWERQYLGQQFYLRVWNQVHSLANEYDIPDNALLCGKA 534
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
33-507 6.27e-66

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: 223.09  E-value: 6.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448    33 YTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKL-DEPFLITWNGVKQRRTSWQDGVLG-TNCPIQP 110
Cdd:TIGR03388   4 YKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLhTEGVVIHWHGIRQIGTPWADGTAGvTQCAINP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   111 NSNWTYQFQLkDQIGTYTYFASTSLHRASGAFGALNINQRSVITTPYpTPDGDFTLLVSDWFSNMTHKDlrkslDAG-SA 189
Cdd:TIGR03388  84 GETFIYNFVV-DRPGTYFYHGHYGMQRSAGLYGSLIVDVPDGEKEPF-HYDGEFNLLLSDWWHKSIHEQ-----EVGlSS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   190 LPL-----PDALLING---------------------VSKG-----LIFTGQQGKTYKFRVSNVGIATSINFRIQNHTMS 238
Cdd:TIGR03388 157 KPMrwigePQSLLINGrgqfncslaakfsstnlpqcnLKGNeqcapQILHVEPGKTYRLRIASTTALAALNFAIEGHKLT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   239 LIEVEGAHTLQESYESLDVHVGQSMTVLVTL-KASVRDYFIVASTRFTKPVLTT-TASLRYQGSKNAAYGPL--PIGPTY 314
Cdd:TIGR03388 237 VVEADGNYVEPFTVKDIDIYSGETYSVLLTTdQDPSRNYWISVGVRGRKPNTPPgLTVLNYYPNSPSRLPPTppPVTPAW 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   315 H-IHWSMKQARTIrmnlTANAARPNPQGSFHygtipinRTLVLANAATLIYGKLRYTVNRISYINPTTPLKLADWYNISG 393
Cdd:TIGR03388 317 DdFDRSKAFSLAI----KAAMGSPKPPETSD-------RRIVLLNTQNKINGYTKWAINNVSLTLPHTPYLGSLKYNLLN 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   394 VFDFKT----------IISTPTTGPAHIGTSVIDVELHEFVEIVFQN------DERSIQSWHMDGTSAYAVGYGSGTWNV 457
Cdd:TIGR03388 386 AFDQKPppenyprdydIFKPPPNPNTTTGNGIYRLKFNTTVDVILQNantlngNNSETHPWHLHGHDFWVLGYGEGKFRP 465
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15235448   458 TM-RKRYNLVDAVPRHTFQVYPLSWTTILVSLDNKGMWNLRSQIWSRRYLG 507
Cdd:TIGR03388 466 GVdEKSYNLKNPPLRNTVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMG 516
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
32-148 1.15e-64

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: 206.10  E-value: 1.15e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  32 FYTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQRRTSWQDGVLGTNCPIQPN 111
Cdd:cd13846   2 FFDWNVSYITASPLGVPQQVIAINGQFPGPTINVTTNDNVVVNVFNSLDEPLLLTWNGIQQRRNSWQDGVLGTNCPIPPG 81
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15235448 112 SNWTYQFQLKDQIGTYTYFASTSLHRASGAFGALNIN 148
Cdd:cd13846  82 WNWTYKFQVKDQIGSFFYFPSLHFQRAAGGFGGIRVN 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
36-151 7.22e-42

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: 145.85  E-value: 7.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448    36 TVTYGTRSPLG-VPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQRRTSWQDGVLG-TNCPIQPNSN 113
Cdd:pfam07732   1 TVTYGTVSPLGgTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGvTQCPIPPGQS 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 15235448   114 WTYQFQLKDQIGTYTYFASTSLHRASGAFGALNINQRS 151
Cdd:pfam07732  81 FTYRFQVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDRA 118
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
33-336 3.00e-19

Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis;


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 89.99  E-value: 3.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  33 YTWTVTYGTRSPL-GVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVkqrRTSW-QDGVLGTncPIQP 110
Cdd:COG2132  16 YELTAQPATVELLpGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL---RVPNaMDGVPGD--PIAP 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 111 NSNWTYQFQLKDQIGTYTY----FASTSLHRASGAFGALninqrsVITTP---YPTPDGDFTLLVSDWfSNMTHKDLRKS 183
Cdd:COG2132  91 GETFTYEFPVPQPAGTYWYhphtHGSTAEQVYRGLAGAL------IVEDPeedLPRYDRDIPLVLQDW-RLDDDGQLLYP 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 184 LDAGSALPLPDALLINGVSkGLIFTGQQGKTYKFRVSNVGIATSINFRIQ-NHTMSLIEVEGaHTLQESYE--SLDVHVG 260
Cdd:COG2132 164 MDAAMGGRLGDTLLVNGRP-NPTLEVRPGERVRLRLLNASNARIYRLALSdGRPFTVIATDG-GLLPAPVEvdELLLAPG 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15235448 261 QSMTVLVTLKASVRDYFIVASTRFTKPVLtTTASLRYQGSKNAAYGPLPIGPTYHIHwSMKQARTIRMNLTANAAR 336
Cdd:COG2132 242 ERADVLVDFSADPGEEVTLANPFEGRSGR-ALLTLRVTGAAASAPLPANLAPLPDLE-DREAVRTRELVLTGGMAG 315
 
Name Accession Description Interval E-value
PLN02835 PLN02835
oxidoreductase
4-537 0e+00

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 767.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448    4 TNLLVCKLFIGALFWLGSV-LVNAEDPYMFYTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEP 82
Cdd:PLN02835   2 GSAVNLHLLLGVLAVLSSVsLVNGEDPYKYYTWTVTYGTISPLGVPQQVILINGQFPGPRLDVVTNDNIILNLINKLDQP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   83 FLITWNGVKQRRTSWQDGVLGTNCPIQPNSNWTYQFQLKDQIGTYTYFASTSLHRASGAFGALNINQRSVITTPYPTPDG 162
Cdd:PLN02835  82 FLLTWNGIKQRKNSWQDGVLGTNCPIPPNSNYTYKFQTKDQIGTFTYFPSTLFHKAAGGFGAINVYERPRIPIPFPLPDG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  163 DFTLLVSDWFSNmTHKDLRKSLDAGSALPLPDALLINGVSKGlIFTGQQGKTYKFRVSNVGIATSINFRIQNHTMSLIEV 242
Cdd:PLN02835 162 DFTLLVGDWYKT-SHKTLQQRLDSGKVLPFPDGVLINGQTQS-TFSGDQGKTYMFRISNVGLSTSLNFRIQGHTMKLVEV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  243 EGAHTLQESYESLDVHVGQSMTVLVTLKASVRDYFIVASTRFTKPVLTTTASLRYQGSKNAAYGPLPIGPTYHIHWSMKQ 322
Cdd:PLN02835 240 EGSHTIQNIYDSLDVHVGQSVAVLVTLNQSPKDYYIVASTRFTRQILTATAVLHYSNSRTPASGPLPALPSGELHWSMRQ 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  323 ARTIRMNLTANAARPNPQGSFHYGTIPINRTLVLANAATLIYGKLRYTVNRISYINPTTPLKLADWYNISGVFDFKTIIS 402
Cdd:PLN02835 320 ARTYRWNLTASAARPNPQGSFHYGKITPTKTIVLANSAPLINGKQRYAVNGVSYVNSDTPLKLADYFGIPGVFSVNSIQS 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  403 TPTTGPAHIGTSVIDVELHEFVEIVFQNDERSIQSWHMDGTSAYAVGYGSGTWNVTMRKRYNLVDAVPRHTFQVYPLSWT 482
Cdd:PLN02835 400 LPSGGPAFVATSVMQTSLHDFLEVVFQNNEKTMQSWHLDGYDFWVVGYGSGQWTPAKRSLYNLVDALTRHTAQVYPKSWT 479
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15235448  483 TILVSLDNKGMWNLRSQIWSRRYLGQELYVRVWNDEKSLYTEAEPPLNVLYCGKA 537
Cdd:PLN02835 480 TILVSLDNQGMWNMRSAIWERQYLGQQFYLRVWNQVHSLANEYDIPDNALLCGKA 534
PLN02354 PLN02354
copper ion binding / oxidoreductase
20-538 0e+00

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 675.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   20 GSVLVNAEDPYMFYTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQRRTSWQD 99
Cdd:PLN02354  17 VALVVRAEDPYFFFTWNVTYGTASPLGVPQQVILINGQFPGPNINSTSNNNIVINVFNNLDEPFLLTWSGIQQRKNSWQD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  100 GVLGTNCPIQPNSNWTYQFQLKDQIGTYTYFASTSLHRASGAFGALNINQRSVITTPYPTPDGDFTLLVSDWFSNmTHKD 179
Cdd:PLN02354  97 GVPGTNCPIPPGTNFTYHFQPKDQIGSYFYYPSTGMHRAAGGFGGLRVNSRLLIPVPYADPEDDYTVLIGDWYTK-SHTA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  180 LRKSLDAGSALPLPDALLINGVSKGL------IFTGQQGKTYKFRVSNVGIATSINFRIQNHTMSLIEVEGAHTLQESYE 253
Cdd:PLN02354 176 LKKFLDSGRTLGRPDGVLINGKSGKGdgkdepLFTMKPGKTYRYRICNVGLKSSLNFRIQGHKMKLVEMEGSHVLQNDYD 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  254 SLDVHVGQSMTVLVTLKASVRDYFIVASTRFTKPVLTTTASLRYQGSKNAAYGPLPIGPTYHIhWSMKQARTIRMNLTAN 333
Cdd:PLN02354 256 SLDVHVGQCFSVLVTANQAPKDYYMVASTRFLKKVLTTTGIIRYEGGKGPASPELPEAPVGWA-WSLNQFRSFRWNLTAS 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  334 AARPNPQGSFHYGTIPINRTLVLANAATLIYGKLRYTVNRISYINPTTPLKLADWYNIS-GVFDFKTIISTP--TTGPAH 410
Cdd:PLN02354 335 AARPNPQGSYHYGKINITRTIKLVNSASKVDGKLRYALNGVSHVDPETPLKLAEYFGVAdKVFKYDTIKDNPpaKITKIK 414
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  411 IGTSVIDVELHEFVEIVFQNDERSIQSWHMDGTSAYAVGYGSGTWNVTMRKRYNLVDAVPRHTFQVYPLSWTTILVSLDN 490
Cdd:PLN02354 415 IQPNVLNITFRTFVEIIFENHEKSMQSWHLDGYSFFAVAVEPGTWTPEKRKNYNLLDAVSRHTVQVYPKSWAAILLTFDN 494
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 15235448  491 KGMWNLRSQIWSRRYLGQELYVRVWNDEKSLYTEAEPPLNVLYCGKAK 538
Cdd:PLN02354 495 AGMWNIRSENWERRYLGQQLYASVLSPERSLRDEYNMPENALLCGKVK 542
PLN02991 PLN02991
oxidoreductase
13-537 0e+00

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 596.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   13 IGALFWLGSvLVNAEDPYMFYTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQ 92
Cdd:PLN02991  12 ILGLLFLIS-FVAAEDPYRFFEWHVTYGNISPLGVAQQGILINGKFPGPDIISVTNDNLIINVFNHLDEPFLISWSGIRN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   93 RRTSWQDGVLGTNCPIQPNSNWTYQFQLKDQIGTYTYFASTSLHRASGAFGALNINQRSVITTPYPTPDGDFTLLVSDWF 172
Cdd:PLN02991  91 WRNSYQDGVYGTTCPIPPGKNYTYALQVKDQIGSFYYFPSLGFHKAAGGFGAIRISSRPLIPVPFPAPADDYTVLIGDWY 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  173 SNmTHKDLRKSLDAGSALPLPDALLINGVSKGLIFTGQQGKTYKFRVSNVGIATSINFRIQNHTMSLIEVEGAHTLQESY 252
Cdd:PLN02991 171 KT-NHKDLRAQLDNGGKLPLPDGILINGRGSGATLNIEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTHTIQTPF 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  253 ESLDVHVGQSMTVLVTLKASVRDYFIVASTRFTKPVLTTTASLRYQGSKNAAYGPLPIGPTyHIHWSMKQARTIRMNLTA 332
Cdd:PLN02991 250 SSLDVHVGQSYSVLITADQPAKDYYIVVSSRFTSKILITTGVLHYSNSAGPVSGPIPDGPI-QLSWSFDQARAIKTNLTA 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  333 NAARPNPQGSFHYGTIPINRTLVLANAATLIYGKLRYTVNRISYINPTTPLKLADWYNISGVFDFKTIISTPTTGPAHIG 412
Cdd:PLN02991 329 SGPRPNPQGSYHYGKINITRTIRLANSAGNIEGKQRYAVNSASFYPADTPLKLADYFKIAGVYNPGSIPDQPTNGAIFPV 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  413 TSVIDVELHEFVEIVFQNDERSIQSWHMDGTSAYAVGYGSGTWNVTMRKRYNLVDAVPRHTFQVYPLSWTTILVSLDNKG 492
Cdd:PLN02991 409 TSVMQTDYKAFVEIVFENWEDIVQTWHLDGYSFYVVGMELGKWSAASRKVYNLNDAVSRCTVQVYPRSWTAIYVSLDNVG 488
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 15235448  493 MWNLRSQIWSRRYLGQELYVRVWNDEKSLYTEAEPPLNVLYCGKA 537
Cdd:PLN02991 489 MWNLRSELWERQYLGQQFYMRVYTTSTSLRDEYLIPKNALLCGRA 533
PLN02168 PLN02168
copper ion binding / pectinesterase
16-536 0e+00

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 578.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   16 LFWLGSvLVNAEDPYMF-----YTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGV 90
Cdd:PLN02168   8 VFVLIS-LVILELSYAFapivsYQWVVSYSQRFILGGNKQVIVINDMFPGPLLNATANDVINVNIFNNLTEPFLMTWNGL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   91 KQRRTSWQDGVLGTNCPIQPNSNWTYQFQLKDQIGTYTYFASTSLHRASGAFGALNINQRSVITTPYPTPDGDFTLLVSD 170
Cdd:PLN02168  87 QLRKNSWQDGVRGTNCPILPGTNWTYRFQVKDQIGSYFYFPSLLLQKAAGGYGAIRIYNPELVPVPFPKPDEEYDILIGD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  171 WFSnMTHKDLRKSLDAGSALPLPDALLINGVS-KGLIFTGQQGKTYKFRVSNVGIATSINFRIQNHTMSLIEVEGAHTLQ 249
Cdd:PLN02168 167 WFY-ADHTVMRASLDNGHSLPNPDGILFNGRGpEETFFAFEPGKTYRLRISNVGLKTCLNFRIQDHDMLLVETEGTYVQK 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  250 ESYESLDVHVGQSMTVLVTLKAS----VRDYFIVASTRFTKPVLTTTASLRYQGSKNAAYGPLPIGPTYHIH-WSMKQAR 324
Cdd:PLN02168 246 RVYSSLDIHVGQSYSVLVTAKTDpvgiYRSYYIVATARFTDAYLGGVALIRYPNSPLDPVGPLPLAPALHDYfSSVEQAL 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  325 TIRMNLTANAARPNPQGSFHYGTIPINRTLVLANAATLIYGKLRYTVNRISYINPTTPLKLADWYNISGVFDFKTIISTP 404
Cdd:PLN02168 326 SIRMDLNVGAARSNPQGSYHYGRINVTRTIILHNDVMLSSGKLRYTINGVSFVYPGTPLKLVDHFQLNDTIIPGMFPVYP 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  405 TTGPAHIGTSVIDVELHEFVEIVFQNDERSIQSWHMDGTSAYAVGYGSGTWNVTMRKRYNLVDAVPRHTFQVYPLSWTTI 484
Cdd:PLN02168 406 SNKTPTLGTSVVDIHYKDFYHIVFQNPLFSLESYHIDGYNFFVVGYGFGAWSESKKAGYNLVDAVSRSTVQVYPYSWTAI 485
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15235448  485 LVSLDNKGMWNLRSQIWSRRYLGQELYVRV----WNDEKSLYTEAEPPL--NVLYCGK 536
Cdd:PLN02168 486 LIAMDNQGMWNVRSQKAEQWYLGQELYMRVkgegEEDPSTIPVRDENPIpgNVIRCGK 543
PLN02792 PLN02792
oxidoreductase
23-537 0e+00

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 573.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   23 LVNAEDPYmFYTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQRRTSWQDGVL 102
Cdd:PLN02792  10 FVKADDTL-FYNWRVTYGNISLLTLPRRGILINGQFPGPEIRSLTNDNLVINVHNDLDEPFLLSWNGVHMRKNSYQDGVY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  103 GTNCPIQPNSNWTYQFQLKDQIGTYTYFASTSLHRASGAFGALNINQRSVITTPYPTPDGDFTLLVSDWFSNmTHKDLRK 182
Cdd:PLN02792  89 GTTCPIPPGKNYTYDFQVKDQVGSYFYFPSLAVQKAAGGYGSLRIYSLPRIPVPFPEPAGDFTFLIGDWYRR-NHTTLKK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  183 SLDAGSALP-LPDALLIN--GVSKGLIFTGQQGKTYKFRVSNVGIATSINFRIQNHTMSLIEVEGAHTLQESYESLDVHV 259
Cdd:PLN02792 168 ILDGGRKLPlMPDGVMINgqGVSYVYSITVDKGKTYRFRISNVGLQTSLNFEILGHQLKLIEVEGTHTVQSMYTSLDIHV 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  260 GQSMTVLVTLKASVRDYFIVASTRFTKPVLTTTASLRYQGSKNAAYGPLPIGPTYHIHWSMKQARTIRMNLTANAARPNP 339
Cdd:PLN02792 248 GQTYSVLVTMDQPPQNYSIVVSTRFIAAKVLVSSTLHYSNSKGHKIIHARQPDPDDLEWSIKQAQSIRTNLTASGPRTNP 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  340 QGSFHYGTIPINRTLVLANAATLIYGKLRYTVNRISYINPTTPLKLADWYNISGVFDFKTIISTPTTGPA-HIGTSVIDV 418
Cdd:PLN02792 328 QGSYHYGKMKISRTLILESSAALVKRKQRYAINGVSFVPSDTPLKLADHFKIKGVFKVGSIPDKPRRGGGmRLDTSVMGA 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  419 ELHEFVEIVFQNDERSIQSWHMDGTSAYAVGYGSGTWNVTMRKRYNLVDAVPRHTFQVYPLSWTTILVSLDNKGMWNLRS 498
Cdd:PLN02792 408 HHNAFLEIIFQNREKIVQSYHLDGYNFWVVGINKGIWSRASRREYNLKDAISRSTTQVYPESWTAVYVALDNVGMWNLRS 487
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 15235448  499 QIWSRRYLGQELYVRVWNDEKSLYTEAEPPLNVLYCGKA 537
Cdd:PLN02792 488 QFWARQYLGQQFYLRVYSPTHSLKDEYPLPKNALLCGRA 526
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
11-535 3.07e-172

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 499.96  E-value: 3.07e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   11 LFIGALFWLGSVLVNAEDPYMFYTWTVTYGTRSPLG--VPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWN 88
Cdd:PLN00044   8 LLLAAALALAPAPAGAGDPYAYYDWEVSYVSAAPLGgvKKQEAIGINGQFPGPALNVTTNWNLVVNVRNALDEPLLLTWH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   89 GVKQRRTSWQDGVLGTNCPIQPNSNWTYQFQLKDQIGTYTYFASTSLHRASGAFGALNINQRSVITTPYPTPD-GDFTLL 167
Cdd:PLN00044  88 GVQQRKSAWQDGVGGTNCAIPAGWNWTYQFQVKDQVGSFFYAPSTALHRAAGGYGAITINNRDVIPIPFGFPDgGDITLF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  168 VSDWFsNMTHKDLRKSLDAGSALPLPDALLING----------VSKGLIFTG---QQGKTYKFRVSNVGIATSINFRIQN 234
Cdd:PLN00044 168 IADWY-ARDHRALRRALDAGDLLGAPDGVLINAfgpyqyndslVPPGITYERinvDPGKTYRFRVHNVGVATSLNFRIQG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  235 HTMSLIEVEGAHTLQESYESLDVHVGQSMTVLVTLKASVR-DYFIVASTRFTKPV----LTTTASLRYQGSKNAAYGPLP 309
Cdd:PLN00044 247 HNLLLVEAEGSYTSQQNYTNLDIHVGQSYSFLLTMDQNAStDYYVVASARFVDAAvvdkLTGVAILHYSNSQGPASGPLP 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  310 IGPT--YHIHWSMKQARTIRMNLTANAARPNPQGSFHYGTIPINRTLVL-ANAATLIYGKLRYTVNRISYINPTTPLKLA 386
Cdd:PLN00044 327 DAPDdqYDTAFSINQARSIRWNVTASGARPNPQGSFHYGDITVTDVYLLqSMAPELIDGKLRATLNEISYIAPSTPLMLA 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  387 DWYNISGVF--DFKtiiSTPTTGPAHIGTSVIDVELHEFVEIVFQNDERSIQSWHMDGTSAYAVGYGSGTWNVTMRKRYN 464
Cdd:PLN00044 407 QIFNVPGVFklDFP---NHPMNRLPKLDTSIINGTYKGFMEIIFQNNATNVQSYHLDGYAFFVVGMDYGLWTDNSRGTYN 483
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15235448  465 LVDAVPRHTFQVYPLSWTTILVSLDNKGMWNLRSQIWSRRYLGQELYVRVWNDEKSLYTEAEP-PLNVLYCG 535
Cdd:PLN00044 484 KWDGVARSTIQVFPGAWTAILVFLDNAGIWNLRVENLDAWYLGQEVYINVVNPEDNSNKTVLPiPDNAIFCG 555
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
33-507 6.27e-66

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: 223.09  E-value: 6.27e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448    33 YTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKL-DEPFLITWNGVKQRRTSWQDGVLG-TNCPIQP 110
Cdd:TIGR03388   4 YKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLhTEGVVIHWHGIRQIGTPWADGTAGvTQCAINP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   111 NSNWTYQFQLkDQIGTYTYFASTSLHRASGAFGALNINQRSVITTPYpTPDGDFTLLVSDWFSNMTHKDlrkslDAG-SA 189
Cdd:TIGR03388  84 GETFIYNFVV-DRPGTYFYHGHYGMQRSAGLYGSLIVDVPDGEKEPF-HYDGEFNLLLSDWWHKSIHEQ-----EVGlSS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   190 LPL-----PDALLING---------------------VSKG-----LIFTGQQGKTYKFRVSNVGIATSINFRIQNHTMS 238
Cdd:TIGR03388 157 KPMrwigePQSLLINGrgqfncslaakfsstnlpqcnLKGNeqcapQILHVEPGKTYRLRIASTTALAALNFAIEGHKLT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   239 LIEVEGAHTLQESYESLDVHVGQSMTVLVTL-KASVRDYFIVASTRFTKPVLTT-TASLRYQGSKNAAYGPL--PIGPTY 314
Cdd:TIGR03388 237 VVEADGNYVEPFTVKDIDIYSGETYSVLLTTdQDPSRNYWISVGVRGRKPNTPPgLTVLNYYPNSPSRLPPTppPVTPAW 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   315 H-IHWSMKQARTIrmnlTANAARPNPQGSFHygtipinRTLVLANAATLIYGKLRYTVNRISYINPTTPLKLADWYNISG 393
Cdd:TIGR03388 317 DdFDRSKAFSLAI----KAAMGSPKPPETSD-------RRIVLLNTQNKINGYTKWAINNVSLTLPHTPYLGSLKYNLLN 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   394 VFDFKT----------IISTPTTGPAHIGTSVIDVELHEFVEIVFQN------DERSIQSWHMDGTSAYAVGYGSGTWNV 457
Cdd:TIGR03388 386 AFDQKPppenyprdydIFKPPPNPNTTTGNGIYRLKFNTTVDVILQNantlngNNSETHPWHLHGHDFWVLGYGEGKFRP 465
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15235448   458 TM-RKRYNLVDAVPRHTFQVYPLSWTTILVSLDNKGMWNLRSQIWSRRYLG 507
Cdd:TIGR03388 466 GVdEKSYNLKNPPLRNTVVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMG 516
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
32-148 1.15e-64

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: 206.10  E-value: 1.15e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  32 FYTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQRRTSWQDGVLGTNCPIQPN 111
Cdd:cd13846   2 FFDWNVSYITASPLGVPQQVIAINGQFPGPTINVTTNDNVVVNVFNSLDEPLLLTWNGIQQRRNSWQDGVLGTNCPIPPG 81
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15235448 112 SNWTYQFQLKDQIGTYTYFASTSLHRASGAFGALNIN 148
Cdd:cd13846  82 WNWTYKFQVKDQIGSFFYFPSLHFQRAAGGFGGIRVN 118
CuRO_2_AAO_like_1 cd13872
The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate ...
162-297 6.94e-60

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: 194.54  E-value: 6.94e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 162 GDFTLLVSDWFsNMTHKDLRKSLDAGSALPLPDALLINGVS------KGLIFTGQQGKTYKFRVSNVGIATSINFRIQNH 235
Cdd:cd13872   1 DEYTVLIGDWY-KTDHKTLRQSLDKGRTLGRPDGILINGKGpygygaNETSFTVEPGKTYRLRISNVGLRTSLNFRIQGH 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15235448 236 TMSLIEVEGAHTLQESYESLDVHVGQSMTVLVTLKASVRDYFIVASTRFTKPVLTTTASLRY 297
Cdd:cd13872  80 KMLLVETEGSYTAQNTYDSLDVHVGQSYSVLVTADQSPKDYYIVASSRFLSPELTGVAILHY 141
PLN02191 PLN02191
L-ascorbate oxidase
16-507 2.23e-58

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 203.71  E-value: 2.23e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   16 LFWLGSVLV----NAEDPYMFYTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLD-EPFLITWNGV 90
Cdd:PLN02191   5 VWWIVTVVAvlthTASAAVREYTWEVEYKYWWPDCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLTtEGLVIHWHGI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   91 KQRRTSWQDGVLG-TNCPIQPNSNWTYQFQLkDQIGTYTYFASTSLHRASGAFGALninqrsvITTPYPTP------DGD 163
Cdd:PLN02191  85 RQKGSPWADGAAGvTQCAINPGETFTYKFTV-EKPGTHFYHGHYGMQRSAGLYGSL-------IVDVAKGPkerlryDGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  164 FTLLVSDWFsnmtHKDLRKSLDAGSALPL-----PDALLING-----VSKGLIFT------------GQQ---------- 211
Cdd:PLN02191 157 FNLLLSDWW----HESIPSQELGLSSKPMrwigeAQSILINGrgqfnCSLAAQFSngtelpmctfkeGDQcapqtlrvep 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  212 GKTYKFRVSNVGIATSINFRIQNHTMSLIEVEGAHTLQESYESLDVHVGQSMTVLVTLKA-SVRDYFIVASTRFTKP--- 287
Cdd:PLN02191 233 NKTYRIRLASTTALASLNLAVQGHKLVVVEADGNYITPFTTDDIDIYSGESYSVLLTTDQdPSQNYYISVGVRGRKPntt 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  288 -VLTTTASLRYQGSKNAAYGPlPIGPTYHihwSMKQARTIRMNLTANAARPNPQGSFHygtipinRTLVLANAATLIYGK 366
Cdd:PLN02191 313 qALTILNYVTAPASKLPSSPP-PVTPRWD---DFERSKNFSKKIFSAMGSPSPPKKYR-------KRLILLNTQNLIDGY 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  367 LRYTVNRISYINPTTPLKLADWYNISGVFDFKT----------IISTPTTGPAHIGTSVIDVELHEFVEIVFQNDE---- 432
Cdd:PLN02191 382 TKWAINNVSLVTPATPYLGSVKYNLKLGFNRKSpprsyrmdydIMNPPPFPNTTTGNGIYVFPFNVTVDVIIQNANvlkg 461
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15235448  433 --RSIQSWHMDGTSAYAVGYGSGTWNVTM-RKRYNLVDAVPRHTFQVYPLSWTTILVSLDNKGMWNLRSQIWSRRYLG 507
Cdd:PLN02191 462 vvSEIHPWHLHGHDFWVLGYGDGKFKPGIdEKTYNLKNPPLRNTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMG 539
PLN02604 PLN02604
oxidoreductase
33-539 4.02e-56

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 197.39  E-value: 4.02e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   33 YTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKL-DEPFLITWNGVKQRRTSWQDGVLG-TNCPIQP 110
Cdd:PLN02604  27 YKWEVKYEYKSPDCFKKLVITINGRSPGPTILAQQGDTVIVELKNSLlTENVAIHWHGIRQIGTPWFDGTEGvTQCPILP 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  111 NSNWTYQFQLkDQIGTYTYFASTSLHRASGAFGALNINQRSVITTPYpTPDGDFTLLVSDWFsnmtHKDLRKSLDAGSAL 190
Cdd:PLN02604 107 GETFTYEFVV-DRPGTYLYHAHYGMQREAGLYGSIRVSLPRGKSEPF-SYDYDRSIILTDWY----HKSTYEQALGLSSI 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  191 PL-----PDALLINGvsKG--------------------------LIFTGQQGKTYKFRVSNVGIATSINFRIQNHTMSL 239
Cdd:PLN02604 181 PFdwvgePQSLLIQG--KGryncslvsspylkagvcnatnpecspYVLTVVPGKTYRLRISSLTALSALSFQIEGHNMTV 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  240 IEVEGAHTLQESYESLDVHVGQSMTVLVTL-KASVRDYFI---VASTRFTKPvlTTTASLRYQgsKNAAYGPLPIGPTYH 315
Cdd:PLN02604 259 VEADGHYVEPFVVKNLFIYSGETYSVLVKAdQDPSRNYWVttsVVSRNNTTP--PGLAIFNYY--PNHPRRSPPTVPPSG 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  316 IHWSMKQARtirmnLTANAARPNPQGSFHYGTIPINRTLVLANAATLIYGKLRYTVNRISYINPTTPLKLADWYNISGVF 395
Cdd:PLN02604 335 PLWNDVEPR-----LNQSLAIKARHGYIHPPPLTSDRVIVLLNTQNEVNGYRRWSVNNVSFNLPHTPYLIALKENLTGAF 409
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  396 ---------DFKT--IISTPTTGPAHIGTSVIDVELHEFVEIVFQN------DERSIQSWHMDGTSAYAVGYGSGTWNVT 458
Cdd:PLN02604 410 dqtpppegyDFANydIYAKPNNSNATSSDSIYRLQFNSTVDIILQNantmnaNNSETHPWHLHGHDFWVLGYGEGKFNMS 489
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  459 MR-KRYNLVDAVPRHTFQVYPLSWTTILVSLDNKGMWNLRSQIWSRRYLGQELYVrvwndEKSLYTEAEPPLNVLYCGKA 537
Cdd:PLN02604 490 SDpKKYNLVDPIMKNTVPVHPYGWTALRFRADNPGVWAFHCHIESHFFMGMGVVF-----EEGIERVGKLPSSIMGCGES 564

                 ..
gi 15235448  538 KR 539
Cdd:PLN02604 565 KG 566
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
33-494 1.18e-53

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: 190.33  E-value: 1.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448    33 YTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQRRTSWQDG-VLGTNCPIQPN 111
Cdd:TIGR03389   6 YTFDVQEKNVTRLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQYNVTIHWHGVRQLRNGWADGpAYITQCPIQPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   112 SNWTYQFQLKDQIGTYTYFASTSLHRASgAFGALNINQRSVITTPYPTPDGDFTLLVSDWFSNMTHKDLRKSLDAGSALP 191
Cdd:TIGR03389  86 QSYVYNFTITGQRGTLWWHAHISWLRAT-VYGAIVILPKPGVPYPFPKPDREVPIILGEWWNADVEAVINQANQTGGAPN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   192 LPDALLING---------VSKGLIFTGQQGKTYKFRVSNVGIATSINFRIQNHTMSLIEVEGAHTLQESYESLDVHVGQS 262
Cdd:TIGR03389 165 VSDAYTINGhpgplyncsSKDTFKLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEVDATYTKPFKTKTIVIGPGQT 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   263 MTVLVTLKASVRDYFIVASTRFTKPV----LTTTASLRYQGSKNAAYGPLPIGPTYH-IHWSMKQARTIRMNLTANAARP 337
Cdd:TIGR03389 245 TNVLLTADQSPGRYFMAARPYMDAPGafdnTTTTAILQYKGTSNSAKPILPTLPAYNdTAAATNFSNKLRSLNSAQYPAN 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   338 NPQGSFH--YGTIPINRTLVLANAATLIYG-KLRYTVNRISYINPTTPLKLADWYNISGVF--DFK---------TIIST 403
Cdd:TIGR03389 325 VPVTIDRrlFFTIGLGLDPCPNNTCQGPNGtRFAASMNNISFVMPTTALLQAHYFGISGVFttDFPanpptkfnyTGTNL 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   404 PTTGPAHIGTSVIDVELHEFVEIVFQNDerSI-----QSWHMDGTSAYAVGYGSGTWNVTMR-KRYNLVDAVPRHTFQVY 477
Cdd:TIGR03389 405 PNNLFTTNGTKVVRLKFNSTVELVLQDT--SIlgsenHPIHLHGYNFFVVGTGFGNFDPKKDpAKFNLVDPPERNTVGVP 482
                         490
                  ....*....|....*..
gi 15235448   478 PLSWTTILVSLDNKGMW 494
Cdd:TIGR03389 483 TGGWAAIRFVADNPGVW 499
CuRO_3_AAO_like_1 cd13894
The third cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
378-499 3.17e-52

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: 173.77  E-value: 3.17e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 378 NPTTPLKLADWYNISGVFDFKTIISTPTTGPAHIGTSVIDVELHEFVEIVFQNDERSIQSWHMDGTSAYAVGYGSGTWNV 457
Cdd:cd13894   1 NPDTPLKLADYFKIKGVFQLDSIPDPPTRKTPYLGTSVINGTYRGFIEIVFQNNEDTVQSWHLDGYSFFVVGMGFGDWTP 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15235448 458 TMRKRYNLVDAVPRHTFQVYPLSWTTILVSLDNKGMWNLRSQ 499
Cdd:cd13894  81 EKRKSYNLLDAVSRSTTQVYPGSWTAILLELDNVGMWNVRSQ 122
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
36-151 7.22e-42

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: 145.85  E-value: 7.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448    36 TVTYGTRSPLG-VPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQRRTSWQDGVLG-TNCPIQPNSN 113
Cdd:pfam07732   1 TVTYGTVSPLGgTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGvTQCPIPPGQS 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 15235448   114 WTYQFQLKDQIGTYTYFASTSLHRASGAFGALNINQRS 151
Cdd:pfam07732  81 FTYRFQVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDRA 118
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
162-300 3.25e-41

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: 145.15  E-value: 3.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   162 GDFTLLVSDWFsNMTHKDLRKSLDAGSAL-----PLPDALLINGVSKGL--IFTGQQGKTYKFRVSNVGIATSINFRIQN 234
Cdd:pfam00394   1 EDYVITLSDWY-HKDAKDLEKELLASGKAptdfpPVPDAVLINGKDGASlaTLTVTPGKTYRLRIINVALDDSLNFSIEG 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235448   235 HTMSLIEVEGAHTLQESYESLDVHVGQSMTVLVTLKASVRDYFIVASTRFTKPVL-TTTASLRYQGS 300
Cdd:pfam00394  80 HKMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPNIPAFDNgTAAAILRYSGA 146
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
381-520 8.62e-35

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: 127.55  E-value: 8.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   381 TPLKLADWYNI-SGVFDFKTIISTPTTGPahIGTSVIDVELHEFVEIVFQNDERSIQSWHMDGTSAYAVGYGSGTWNVTM 459
Cdd:pfam07731   2 TPPKLPTLLQItSGNFRRNDWAINGLLFP--PNTNVITLPYGTVVEWVLQNTTTGVHPFHLHGHSFQVLGRGGGPWPEED 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15235448   460 RKRYNLVDAVPRHTFQVYPLSWTTILVSLDNKGMWNLRSQIWsrRYLGQELYVRVWNDEKS 520
Cdd:pfam07731  80 PKTYNLVDPVRRDTVQVPPGGWVAIRFRADNPGVWLFHCHIL--WHLDQGMMGQFVVRPGD 138
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
33-148 2.39e-28

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: 109.27  E-value: 2.39e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  33 YTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQRRTSWQDGVLG-TNCPIQPN 111
Cdd:cd13857   3 YNFTISEITGAPDGFVRPMLVINGQFPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTNWMDGTAGiTQCPIPPG 82
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15235448 112 SNWTYQFQLKDQIGTYTYFASTSLHRASGAFGALNIN 148
Cdd:cd13857  83 GSFTYNFTVDGQYGTYWYHSHYSTQYADGLVGPLIVH 119
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
33-145 2.09e-27

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: 106.60  E-value: 2.09e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  33 YTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLD-EPFLITWNGVKQRRTSWQDGVLG-TNCPIQP 110
Cdd:cd04206   3 YELTITETTVNPDGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNLPnEPTSIHWHGLRQPGTNDGDGVAGlTQCPIPP 82
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15235448 111 NSNWTYQFQLKDQIGTYTYFASTSLHRASGAFGAL 145
Cdd:cd04206  83 GESFTYRFTVDDQAGTFWYHSHVGGQRADGLYGPL 117
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
33-148 1.30e-22

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: 93.08  E-value: 1.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  33 YTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKL-DEPFLITWNGVKQRRTSWQDGVLG-TNCPIQP 110
Cdd:cd13854   6 YTLTITNSTLAPDGVEKEVMLINGQYPGPLIEANWGDTIEVTVINKLqDNGTSIHWHGIRQLNTNWQDGVPGvTECPIAP 85
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15235448 111 NSNWTYQFQLkDQIGTYTYFASTSLHRASGAFGALNIN 148
Cdd:cd13854  86 GDTRTYRFRA-TQYGTSWYHSHYSAQYGDGVVGPIVIH 122
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
47-509 3.85e-21

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: 96.83  E-value: 3.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448    47 VPQQVILINGQFPGPAIEAVTNNNIVVNLINKL-DEPFLITWNGVKQRRTSWQDGV-LGTNCPIQPNSNWTYQFQLK-DQ 123
Cdd:TIGR03390  25 SSRYSVVVNGTSPGPEIRLQEGQTTWIRVYNDIpDNNVTMHWHGLTQRTAPFSDGTpLASQWPIPPGHFFDYEIKPEpGD 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   124 IGTYTYFASTSLhRASGAFGALNInqRSVITTPYPTpDGDFTLLVSDWFSNmTHKDLRKSLdagSALPL-----PDALLI 198
Cdd:TIGR03390 105 AGSYFYHSHVGF-QAVTAFGPLIV--EDCEPPPYKY-DDERILLVSDFFSA-TDEEIEQGL---LSTPFtwsgeTEAVLL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   199 NGVSKGLIFTGQQ---------------GKTYKFRVSNVGIATSINFRIQNH-TMSLIEVEGAHTLQESYESLDVHVGQS 262
Cdd:TIGR03390 177 NGKSGNKSFYAQInpsgscmlpvidvepGKTYRLRFIGATALSLISLGIEDHeNLTIIEADGSYTKPAKIDHLQLGGGQR 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   263 MTVLVTLKASV-------RDYFIVASTRFTKPVLTTTASLRYQGSKNAAYGPLPIGPTYHI-----HWSMKQARTirMNL 330
Cdd:TIGR03390 257 YSVLFKAKTEDelcggdkRQYFIQFETRDRPKVYRGYAVLRYRSDKASKLPSVPETPPLPLpnstyDWLEYELEP--LSE 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   331 TANAARPNPQGSFHYGTIPINRTLVLANaatliyGKLRYTVNRISYIN--PTTPLkLADWYNisgvfDFKTIISTPTTGP 408
Cdd:TIGR03390 335 ENNQDFPTLDEVTRRVVIDAHQNVDPLN------GRVAWLQNGLSWTEsvRQTPY-LVDIYE-----NGLPATPNYTAAL 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448   409 AHIG----TSVIDVELHEFVEIVFQNDERS--------IQSWHMDGTSAYAVGYGSGTWNVTM-RKRYNLVDAVPRHTFQ 475
Cdd:TIGR03390 403 ANYGfdpeTRAFPAKVGEVLEIVWQNTGSYtgpnggvdTHPFHAHGRHFYDIGGGDGEYNATAnEAKLENYTPVLRDTTM 482
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 15235448   476 VY----------PLSWTTILVSLDNKGMWNLRSQIWSRRYLGQE 509
Cdd:TIGR03390 483 LYryavkvvpgaPAGWRAWRIRVTNPGVWMMHCHILQHMVMGMQ 526
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
33-148 7.35e-21

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: 88.27  E-value: 7.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  33 YTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKL-DEPFLITWNGVKQRRTSWQDGVLG-TNCPIQP 110
Cdd:cd13845   3 YKWKVEYMFWAPDCVEKLVIGINGQFPGPTIRATAGDTIVVELENKLpTEGVAIHWHGIRQRGTPWADGTASvSQCPINP 82
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15235448 111 NSNWTYQFqLKDQIGTYTYFASTSLHRASGAFGALNIN 148
Cdd:cd13845  83 GETFTYQF-VVDRPGTYFYHGHYGMQRSAGLYGSLIVD 119
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
165-297 1.34e-20

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: 88.57  E-value: 1.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 165 TLLVSDWFsNMTHKDLRKSLDAGS--ALPLPDALLINGVSKGL-------------IFTGQQGKTYKFRVSNVGIATSIN 229
Cdd:cd04205   2 VLLLSDWY-HDSAEDVLAGYMPNSfgNEPVPDSLLINGRGRFNcsmavcnsgcplpVITVEPGKTYRLRLINAGSFASFN 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15235448 230 FRIQNHTMSLIEVEGAHTLQESYESLDVHVGQSMTVLVTLKASVRDYFIVASTRFT----KPVLTTTASLRY 297
Cdd:cd04205  81 FAIDGHNMTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKADQPPGNYWIRASADGRtfdeGGNPNGTAILRY 152
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
33-131 1.55e-19

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: 84.27  E-value: 1.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  33 YTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQRRTSWQDGVLG-TNCPIQPN 111
Cdd:cd13850   1 FTLTVTEGSPDGDGGEREVILINGQFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTPWSDGVPGvTQWPIQPG 80
                        90       100
                ....*....|....*....|
gi 15235448 112 SNWTYQFQLKDQIGTYTYFA 131
Cdd:cd13850  81 GSFTYRWKAEDQYGLYWYHS 100
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
163-297 1.57e-19

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: 85.30  E-value: 1.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 163 DFTLLVSDWFSN----MTHKDLRKSLDAGsALPLPDALLINGvSKGLIFTGQQGKTYKFRVSNVGIATSINFRIQNHTMS 238
Cdd:cd13877   2 EVTLTLSDWYHDqspdLLRDFLSPYNPTG-AEPIPDSSLFND-TQNATINFEPGKTYLLRIINMGAFASQYFHIEGHDMT 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235448 239 LIEVEGAHTLQESYESLDVHVGQSMTVLVTLKASV-RDYFIVAS----TRFTKP---VLTTTASLRY 297
Cdd:cd13877  80 IIEVDGVYVKPYPVDTLYIAVGQRYSVLVKAKNDTdRNYAIINGmdkdMLDTVPddlYLNKTNWLVY 146
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
33-336 3.00e-19

Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis;


Pssm-ID: 441735 [Multi-domain]  Cd Length: 423  Bit Score: 89.99  E-value: 3.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  33 YTWTVTYGTRSPL-GVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVkqrRTSW-QDGVLGTncPIQP 110
Cdd:COG2132  16 YELTAQPATVELLpGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL---RVPNaMDGVPGD--PIAP 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 111 NSNWTYQFQLKDQIGTYTY----FASTSLHRASGAFGALninqrsVITTP---YPTPDGDFTLLVSDWfSNMTHKDLRKS 183
Cdd:COG2132  91 GETFTYEFPVPQPAGTYWYhphtHGSTAEQVYRGLAGAL------IVEDPeedLPRYDRDIPLVLQDW-RLDDDGQLLYP 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 184 LDAGSALPLPDALLINGVSkGLIFTGQQGKTYKFRVSNVGIATSINFRIQ-NHTMSLIEVEGaHTLQESYE--SLDVHVG 260
Cdd:COG2132 164 MDAAMGGRLGDTLLVNGRP-NPTLEVRPGERVRLRLLNASNARIYRLALSdGRPFTVIATDG-GLLPAPVEvdELLLAPG 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15235448 261 QSMTVLVTLKASVRDYFIVASTRFTKPVLtTTASLRYQGSKNAAYGPLPIGPTYHIHwSMKQARTIRMNLTANAAR 336
Cdd:COG2132 242 ERADVLVDFSADPGEEVTLANPFEGRSGR-ALLTLRVTGAAASAPLPANLAPLPDLE-DREAVRTRELVLTGGMAG 315
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
33-147 8.10e-19

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: 82.39  E-value: 8.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  33 YTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFL-----ITWNGVKQRRTSWQDGVLG-TNC 106
Cdd:cd13856   3 YTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTMrrstsIHWHGIFQHGTNYADGPAFvTQC 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15235448 107 PIQPNSNWTYQFQLKDQIGTYTYFASTSLHRASGAFGALNI 147
Cdd:cd13856  83 PIAPNHSFTYDFTAGDQAGTFWYHSHLSTQYCDGLRGPLVI 123
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
46-145 8.46e-18

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: 78.73  E-value: 8.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  46 GVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLD-EPFLITWNGVKQRRTSWQDGVLG-TNCPIQPNSNWTYQFQlKDQ 123
Cdd:cd13858   2 GVERPVITVNGQLPGPSIEVCEGDTVVVDVKNRLPgESTTIHWHGIHQRGTPYMDGVPMvTQCPILPGQTFRYKFK-ADP 80
                        90       100
                ....*....|....*....|..
gi 15235448 124 IGTYTYFASTSLHRASGAFGAL 145
Cdd:cd13858  81 AGTHWYHSHSGTQRADGLFGAL 102
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
33-142 6.85e-17

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: 76.53  E-value: 6.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  33 YTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQRRTSWQDGV-LGTNCPIQPN 111
Cdd:cd13849   1 YTFVVQEKNVTRLCSTKSILTVNGQFPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLRSGWADGPaYITQCPIQPG 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 15235448 112 SNWTYQFQLKDQIGTYTYFASTSLHRAS--GAF 142
Cdd:cd13849  81 QSYTYRFTVTGQEGTLWWHAHISWLRATvyGAF 113
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
33-129 3.84e-16

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: 74.61  E-value: 3.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  33 YTWTVTYGTRSPLGV-PQQVILINGQFPGPAIEAVTNNNIVVNLINKL-DEPFLITWNGVKQRRTSWQDGVLG-TNCPIQ 109
Cdd:cd13851   3 FDWNITWVTANPDGLfERRVIGINGQWPPPPIEVNKGDTVVIHATNSLgDQPTSLHFHGLFQNGTNYMDGPVGvTQCPIP 82
                        90       100
                ....*....|....*....|
gi 15235448 110 PNSNWTYQFQLKDQIGTYTY 129
Cdd:cd13851  83 PGQSFTYEFTVDTQVGTYWY 102
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
166-303 5.27e-16

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: 75.52  E-value: 5.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 166 LLVSDWFsnmtHkDLRKSLDAGSA--LPLPDALLINGV--------SKGLIFTGQQGKTYKFRVSNVGIATSINFRIQNH 235
Cdd:cd13882   3 ITLGDWY----H-TAAPDLLATTAgvPPVPDSGTINGKgrfdggptSPLAVINVKRGKRYRFRVINISCIPSFTFSIDGH 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15235448 236 TMSLIEVEGAHTLQESYESLDVHVGQSMTVLVTLKASVRDYFIVASTRFTKPV----LTTTASLRYQGSKNA 303
Cdd:cd13882  78 NLTVIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWIRAPPTGGTPAnnggQLNRAILRYKGAPEV 149
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
351-511 2.95e-14

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: 70.53  E-value: 2.95e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 351 NRTLVLANAATLIYGKLRYTVNRISYINPTTPLKLAdwyniSGVFDFKtiistpttgpahiGTSVIDVELHEFVEIVFQN 430
Cdd:cd13893   2 TRTLLLLNTQNLINGQLRWAINNVSYVPPPTPYLAA-----LPVYPFK-------------GGDVVDVILQNANTNTRNA 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 431 DErsIQSWHMDGTSAYAVGYGSGTWN-VTMRKRYNLVDAVPRHTFQVYPLSWTTILVSLDNKGMWNLRSQIWSRRYLGQE 509
Cdd:cd13893  64 SE--QHPWHLHGHDFWVLGYGLGGFDpAADPSSLNLVNPPMRNTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGMG 141

                ..
gi 15235448 510 LY 511
Cdd:cd13893 142 VV 143
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
161-297 2.31e-13

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: 67.95  E-value: 2.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 161 DGDFTLLVSDWFsnmtHKDLRKSLDAGSALPL-----PDALLINGVSK--------------------------GLIFTG 209
Cdd:cd13871   1 DGELNILLSDWW----HKSIYEQETGLSSKPFrwvgePQSLLIEGRGRyncslapaypsslpspvcnksnpqcaPFILHV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 210 QQGKTYKFRVSNVGIATSINFRIQNHTMSLIEVEGAHTLQESYESLDVHVGQSMTVLVTL-KASVRDYFIVASTRFTKPV 288
Cdd:cd13871  77 SPGKTYRLRIASVTALSSLNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTAdQDPSRNYWVSVNVRGRRPN 156
                       170
                ....*....|
gi 15235448 289 LTT-TASLRY 297
Cdd:cd13871 157 TPPgLAILNY 166
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
164-297 3.77e-13

The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259953 [Multi-domain]  Cd Length: 163  Bit Score: 67.30  E-value: 3.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 164 FTLLVSDWFSNMTHKDLRKSLDAGS--ALPLPDALLINGVSK------------GLI------FTGQQGKTYKFRVSNVG 223
Cdd:cd13886   1 VVVMVNDYYHDPSSVLLARYLAPGNegDEPVPDNGLINGIGQfdcasatykiycCASngtyynFTLEPNKTYRLRLINAG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 224 IATSINFRIQNHTMSLIEVEGahTLQESYE--SLDVHVGQSMTVLVTLKAS------VRDYFIVASTRFTKPVLTTT--A 293
Cdd:cd13886  81 SFADFTFSVDGHPLTVIEADG--TLVEPVEvhSITISVAQRYSVILTTNQPtggnfwMRAELNTDCFTYDNPNLDPDvrA 158

                ....
gi 15235448 294 SLRY 297
Cdd:cd13886 159 IVSY 162
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
164-297 5.44e-13

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: 66.47  E-value: 5.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 164 FTLLVSDWFSNMTHKDLRKSLDAGSALPLPDALLINGV-------SKGLIF--TGQQGKTYKFRVSNVGIATSINFRIQN 234
Cdd:cd13875   1 VPIILGEWWNRDVNDVEDQALLTGGGPNISDAYTINGQpgdlyncSSKDTFvlTVEPGKTYLLRIINAALNEELFFKIAN 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15235448 235 HTMSLIEVEGAHTLQESYESLDVHVGQSMTVLVTLKASVRDYFIVASTRFTKPVL-----TTTASLRY 297
Cdd:cd13875  81 HTLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTADQPPGRYYMAARPYQSAPPVpfdntTATAILEY 148
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
395-494 5.39e-11

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: 60.35  E-value: 5.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 395 FDFkTIISTPTTGPAHIGTSVIDVELHEFVEIVFQNDerSIQS-----WHMDGTSAYAVGYGSGTWN-VTMRKRYNLVDA 468
Cdd:cd13897  14 FDY-TGNAPNENTPTSRGTKVKVLEYGSTVEIVLQGT--SLLAaenhpMHLHGFDFYVVGRGFGNFDpSTDPATFNLVDP 90
                        90       100
                ....*....|....*....|....*.
gi 15235448 469 VPRHTFQVYPLSWTTILVSLDNKGMW 494
Cdd:cd13897  91 PLRNTVGVPRGGWAAIRFVADNPGVW 116
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
163-297 5.74e-11

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: 60.71  E-value: 5.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 163 DFTLLVSDWFSNMTHKDLRKSlDAGSALPLPDALLINGvsKG---------------LIFTGQQGKTYKFRVSNVGIAT- 226
Cdd:cd13884   1 EHVILIQDWTHELSSERFVGR-GHNGGGQPPDSILING--KGryydpktgntnntplEVFTVEQGKRYRFRLINAGATNc 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15235448 227 SINFRIQNHTMSLIEVEGAHTLQESYESLDVHVGQSMTVLVTLKASVRDYFIVAST--RFTKPVLTTTASLRY 297
Cdd:cd13884  78 PFRVSIDGHTLTVIASDGNDVEPVEVDSIIIYPGERYDFVLNANQPIGNYWIRARGleDCDNRRLQQLAILRY 150
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
378-494 1.74e-10

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


Pssm-ID: 259870 [Multi-domain]  Cd Length: 132  Bit Score: 59.01  E-value: 1.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 378 NPTTPLKLADWYNISGVFDFkTIISTPTTGPAHiGTSVIDVELHEFVEIVFQNDERS--IQSWHMDGTSAYAVGYGSGTW 455
Cdd:cd04207   1 DRTRRLVLSQTGAPDGTTRW-VINGMPFKEGDA-NTDIFSVEAGDVVEIVLINAGNHdmQHPFHLHGHSFWVLGSGGGPF 78
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15235448 456 NVtmrkRYNLVDAVPRHTFQVYPLSWTTILVSLDNKGMW 494
Cdd:cd04207  79 DA----PLNLTNPPWRDTVLVPPGGWVVIRFKADNPGVW 113
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
33-147 3.83e-09

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: 54.59  E-value: 3.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  33 YTWTVTYGTRSPLGVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQRRTswQDGVLGTNCP-IQPN 111
Cdd:cd13848   3 YDLVIAETPVNIGGKEGEAITVNGQVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPND--MDGVPGLSFPgIKPG 80
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15235448 112 SNWTYQFQLKdQIGTYTYFASTSLHRASGAFGALNI 147
Cdd:cd13848  81 ETFTYRFPVR-QSGTYWYHSHSGLQEQTGLYGPIII 115
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
166-298 6.77e-09

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: 54.52  E-value: 6.77e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 166 LLVSDWfSNMTHKD-LRKSLDAGSALPLPDALLINGvsKG----LIFTGQQGKTY-KFRVSNVGIATSINFRIQNHTMSL 239
Cdd:cd13876   3 IILSDW-RHLTSEEyWKIMRASGIEPFCYDSILING--KGrvycLIVIVDPGERWvSLNFINAGGFHTLAFSIDEHPMWV 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 240 IEVEGAHTLQESYESLDVHVGQSMTVLVTLKASVRDYFI-VASTRFTKpVLTTTASLRYQ 298
Cdd:cd13876  80 YAVDGGYIEPQLVDAISITNGERYSVLVKLDKPPGDYTIrVASTGAPQ-VISGYAILRYK 138
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
166-297 1.32e-08

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: 54.27  E-value: 1.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 166 LLVSDWFSNM-----THKDLRKSLDAGSALPLPDALLINGV--------SKG--------LIFTGQQGKTYKFRVSNVGI 224
Cdd:cd13883   3 LFISDWYHDQsevivAGLLSPQGYKGSPAAPSPDSALINGIgqfncsaaDPGtcctqtspPEIQVEAGKRTRFRLINAGS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 225 ATSINFRIQNHTMSLIE-----VEGAHTLQEsyesLDVHVGQSMTVLVTLKA-SVRDYFIVASTRFTKPV------LTTT 292
Cdd:cd13883  83 HAMFRFSVDNHTLNVVEaddtpVYGPTVVHR----IPIHNGQRYSVIIDTTSgKAGDSFWLRARMATDCFawdlqqQTGK 158

                ....*
gi 15235448 293 ASLRY 297
Cdd:cd13883 159 AILRY 163
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
165-300 2.36e-07

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: 50.71  E-value: 2.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 165 TLLVSDWFSNMTHKDLRKSLDAGsALPLPDALLING-------VSKGL--IFTGQQGKTYKFRVSNVGIATSINFRIQNH 235
Cdd:cd13880   3 PVLLTDWYHRSAFELFSEELPTG-GPPPMDNILINGkgkfpcsTGAGSyfETTFTPGKKYRLRLINTGVDTTFRFSIDGH 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15235448 236 TMSLIE-----VEGAHTlqesyESLDVHVGQSMTVLVTLKAS-VRDYFIVA-----STRFTKPVLTTTASLRYQGS 300
Cdd:cd13880  82 NLTVIAadfvpIVPYTT-----DSLNIGIGQRYDVIVEANQDpVGNYWIRAepatgCSGTNNNPDNRTGILRYDGA 152
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
162-297 2.50e-07

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: 50.36  E-value: 2.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 162 GDFTLLVSDWFSNmTHKDLRKSLDAGsalPL-----PDALLINGVSKGLIFTGQQ----------------GKTYKFRVs 220
Cdd:cd13873   1 EERILLFSDYFPK-TDSTIETGLTAT---PFvwpgePNALLVNGKSGGTCNKSATegcttschppvidvepGKTYRFRF- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 221 nVGiATSINF---RIQNH-TMSLIEVEGAHTLQESYESLDVHVGQSMTVLVTLK--ASVRD-----YFIVASTRFTKPVL 289
Cdd:cd13873  76 -IG-ATALSFvslGIEGHdNLTIIEADGSYTKPAETDHLQLGSGQRYSFLLKTKslEELAAlnkttFWIQIETRWRPTND 153

                ....*...
gi 15235448 290 TTTASLRY 297
Cdd:cd13873 154 TGYAVLRY 161
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
55-129 4.61e-07

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: 48.73  E-value: 4.61e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15235448  55 NGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVkqRRTSWQDGVLG-TNCPIQPNSNWTYQFQLKdQIGTYTY 129
Cdd:cd13860  26 NGSVPGPTIEVTEGDRVRILVTNELPEPTTVHWHGL--PVPNGMDGVPGiTQPPIQPGETFTYEFTAK-QAGTYMY 98
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
46-129 4.25e-05

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: 42.99  E-value: 4.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  46 GVPQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVkqRRTSWQDGVLG-TNCPIQPNSNWTYQFQLKDQi 124
Cdd:cd13861  17 GPTTRTWGYNGQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGL--RLPNAMDGVPGlTQPPVPPGESFTYEFTPPDA- 93

                ....*
gi 15235448 125 GTYTY 129
Cdd:cd13861  94 GTYWY 98
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
55-145 5.30e-05

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: 42.85  E-value: 5.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  55 NGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQrrTSWQDGvlGTNCPIQPNSNWTYQFQL-KDQIGTYTYFAST 133
Cdd:cd13855  27 NGSVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPV--PPDQDG--NPHDPVAPGNDRVYRFTLpQDSAGTYWYHPHP 102
                        90
                ....*....|..
gi 15235448 134 SLHRASGAFGAL 145
Cdd:cd13855 103 HGHTAEQVYRGL 114
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
55-129 5.46e-05

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: 42.85  E-value: 5.46e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235448  55 NGQFPGPAIEAVTNNNIVVNLINKLDEPFLITWNGVKQrRTSWQ-DGVLG-TNCPIQPNSNWTYQFQlKDQIGTYTY 129
Cdd:cd13859  26 NGQVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQ-MGSWKmDGVPGvTQPAIEPGESFTYKFK-AERPGTLWY 100
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
48-149 1.03e-04

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: 41.75  E-value: 1.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448  48 PQQVILINGQFPGPAIEAVTNNNIVVNLINKLDEPFL-ITWNGVKQRRTSWQDGV-LGTNCPIQPNSNWTYQFQL-KDQI 124
Cdd:cd13847  14 PRPSTLINGSFPGPELRVQEGQHLWVRVYNDLEAGNTtMHFHGLSQYMSPFSDGTpLASQWPIPPGKFFDYEFPLeAGDA 93
                        90       100
                ....*....|....*....|....*
gi 15235448 125 GTYTYFASTSLhRASGAFGALNINQ 149
Cdd:cd13847  94 GTYYYHSHVGF-QSVTAYGALIVED 117
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
371-494 6.17e-03

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


Pssm-ID: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 37.66  E-value: 6.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235448 371 VNRISYI---NPTTPLKLADWYNISGVfdfktiisTPTTGPAHIGTS--VIDV-ELHEFVEIVFQN-DERSiQSWHMDGT 443
Cdd:cd13910  20 FNGTSWRplpGPATLLLALDADNAEEV--------AAGNGLSTFDGNqlVITVdDIDKVVDLVINNlDDGD-HPFHLHGH 90
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15235448 444 SAYAVG-----YGSGTWNVTMRKRYNLVDAVPRHTFQVYPLSWTTILVSLDNKGMW 494
Cdd:cd13910  91 KFWVLGsgdgrYGGGGYTAPDGTSLNTTNPLRRDTVSVPGFGWAVLRFVADNPGLW 146
 
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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