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Conserved domains on  [gi|1063727537|ref|NP_001329209|]
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SKU5 similar 9 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02792 super family cl31932
oxidoreductase
13-454 0e+00

oxidoreductase


The actual alignment was detected with superfamily member PLN02792:

Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 880.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  13 MMMTISIISFVQADDPYrFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLR 92
Cdd:PLN02792    1 MMMTTTIISFVKADDTL-FYNWRVTYGNISLLTLPRRGILINGQFPGPEIRSLTNDNLVINVHNDLDEPFLLSWNGVHMR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  93 KNSYQDGVYGTTCPIPPGKNYTYAIQVKDQIGSFFYFPSLAVHKAAGGFGGFRILSRPRIPVPFPEPAGDFTFLIGDWFK 172
Cdd:PLN02792   80 KNSYQDGVYGTTCPIPPGKNYTYDFQVKDQVGSYFYFPSLAVQKAAGGYGSLRIYSLPRIPVPFPEPAGDFTFLIGDWYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 173 HDHKVLKAILDRGHKLP-LPQGVLINGQGVSYMSSITVHKGKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEGTHTVQSM 251
Cdd:PLN02792  160 RNHTTLKKILDGGRKLPlMPDGVMINGQGVSYVYSITVDKGKTYRFRISNVGLQTSLNFEILGHQLKLIEVEGTHTVQSM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 252 YTSLDIHVGQSYSVLVTMDQPDQDYDIVVSTKFVAKKLLVSSTIHYsnsrhSHSSSANSVHVQQP-ADELDWSIKQARSI 330
Cdd:PLN02792  240 YTSLDIHVGQTYSVLVTMDQPPQNYSIVVSTRFIAAKVLVSSTLHY-----SNSKGHKIIHARQPdPDDLEWSIKQAQSI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 331 RTNLTASGPRPNPQGSYHYGRIKISRTLILESSAALVKRKQRYAINGVSFVPGDTPLKLADYFKIKGVFKMGSIPDKPRR 410
Cdd:PLN02792  315 RTNLTASGPRTNPQGSYHYGKMKISRTLILESSAALVKRKQRYAINGVSFVPSDTPLKLADHFKIKGVFKVGSIPDKPRR 394
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1063727537 411 GRGMRMETSVMGAHHRDFLEIIFQNREKIVQSYHLDGYSFWVVG 454
Cdd:PLN02792  395 GGGMRLDTSVMGAHHNAFLEIIFQNREKIVQSYHLDGYNFWVVG 438
 
Name Accession Description Interval E-value
PLN02792 PLN02792
oxidoreductase
13-454 0e+00

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 880.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  13 MMMTISIISFVQADDPYrFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLR 92
Cdd:PLN02792    1 MMMTTTIISFVKADDTL-FYNWRVTYGNISLLTLPRRGILINGQFPGPEIRSLTNDNLVINVHNDLDEPFLLSWNGVHMR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  93 KNSYQDGVYGTTCPIPPGKNYTYAIQVKDQIGSFFYFPSLAVHKAAGGFGGFRILSRPRIPVPFPEPAGDFTFLIGDWFK 172
Cdd:PLN02792   80 KNSYQDGVYGTTCPIPPGKNYTYDFQVKDQVGSYFYFPSLAVQKAAGGYGSLRIYSLPRIPVPFPEPAGDFTFLIGDWYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 173 HDHKVLKAILDRGHKLP-LPQGVLINGQGVSYMSSITVHKGKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEGTHTVQSM 251
Cdd:PLN02792  160 RNHTTLKKILDGGRKLPlMPDGVMINGQGVSYVYSITVDKGKTYRFRISNVGLQTSLNFEILGHQLKLIEVEGTHTVQSM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 252 YTSLDIHVGQSYSVLVTMDQPDQDYDIVVSTKFVAKKLLVSSTIHYsnsrhSHSSSANSVHVQQP-ADELDWSIKQARSI 330
Cdd:PLN02792  240 YTSLDIHVGQTYSVLVTMDQPPQNYSIVVSTRFIAAKVLVSSTLHY-----SNSKGHKIIHARQPdPDDLEWSIKQAQSI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 331 RTNLTASGPRPNPQGSYHYGRIKISRTLILESSAALVKRKQRYAINGVSFVPGDTPLKLADYFKIKGVFKMGSIPDKPRR 410
Cdd:PLN02792  315 RTNLTASGPRTNPQGSYHYGKMKISRTLILESSAALVKRKQRYAINGVSFVPSDTPLKLADHFKIKGVFKVGSIPDKPRR 394
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1063727537 411 GRGMRMETSVMGAHHRDFLEIIFQNREKIVQSYHLDGYSFWVVG 454
Cdd:PLN02792  395 GGGMRLDTSVMGAHHNAFLEIIFQNREKIVQSYHLDGYNFWVVG 438
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
31-146 8.49e-73

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: 224.59  E-value: 8.49e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  31 FFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNSYQDGVYGTTCPIPPG 110
Cdd:cd13846     2 FFDWNVSYITASPLGVPQQVIAINGQFPGPTINVTTNDNVVVNVFNSLDEPLLLTWNGIQQRRNSWQDGVLGTNCPIPPG 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1063727537 111 KNYTYAIQVKDQIGSFFYFPSLAVHKAAGGFGGFRI 146
Cdd:cd13846    82 WNWTYKFQVKDQIGSFFYFPSLHFQRAAGGFGGIRV 117
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
161-297 4.51e-48

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


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 161.72  E-value: 4.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 161 GDFTFLIGDWFKHDHKVLKAILDRGHKL-----PLPQGVLINGQGVSYMSSITVHKGKTYRFRISNVGLQHTLNFRIQGH 235
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKELLASGKAptdfpPVPDAVLINGKDGASLATLTVTPGKTYRLRIINVALDDSLNFSIEGH 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063727537 236 QMKLVEVEGTHTVQSMYTSLDIHVGQSYSVLVTMDQPDQDYDIVVSTKFVA-KKLLVSSTIHY 297
Cdd:pfam00394  81 KMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPNIPAfDNGTAAAILRY 143
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
30-454 3.65e-43

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: 159.53  E-value: 3.65e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  30 RFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDL-DEPFLLSWNGVQLRKNSYQDGVYGTT-CPI 107
Cdd:TIGR03388   2 RHYKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLhTEGVVIHWHGIRQIGTPWADGTAGVTqCAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 108 PPGKNYTYAIQVkDQIGSFFYFPSLAVHKAAGGFGGFRILSRPRIPVPFpEPAGDFTFLIGDWFkhdHKVLKAILDRGHK 187
Cdd:TIGR03388  82 NPGETFIYNFVV-DRPGTYFYHGHYGMQRSAGLYGSLIVDVPDGEKEPF-HYDGEFNLLLSDWW---HKSIHEQEVGLSS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 188 LPL-----PQGVLINGQG------VSYMSSI------------------TVHKGKTYRFRISNVGLQHTLNFRIQGHQMK 238
Cdd:TIGR03388 157 KPMrwigePQSLLINGRGqfncslAAKFSSTnlpqcnlkgneqcapqilHVEPGKTYRLRIASTTALAALNFAIEGHKLT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 239 LVEVEGtHTVQSMYTS-LDIHVGQSYSVLVTMDQ-PDQDYDIVVSTKFVAKKLLVSSTI-HYsnSRHSHSSSANSVHVQQ 315
Cdd:TIGR03388 237 VVEADG-NYVEPFTVKdIDIYSGETYSVLLTTDQdPSRNYWISVGVRGRKPNTPPGLTVlNY--YPNSPSRLPPTPPPVT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 316 PA-DELDWSIKQARSIrtnLTASGPRPNPQGSyhygrikiSRTLILESSAALVKRKQRYAINGVSFVPGDTPLKLADYFK 394
Cdd:TIGR03388 314 PAwDDFDRSKAFSLAI---KAAMGSPKPPETS--------DRRIVLLNTQNKINGYTKWAINNVSLTLPHTPYLGSLKYN 382
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063727537 395 IKGVFKMGSIPD---------KPRRGRGMRMETSVMGAHHRDFLEIIFQNREKI------VQSYHLDGYSFWVVG 454
Cdd:TIGR03388 383 LLNAFDQKPPPEnyprdydifKPPPNPNTTTGNGIYRLKFNTTVDVILQNANTLngnnseTHPWHLHGHDFWVLG 457
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
23-284 3.95e-21

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: 95.00  E-value: 3.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  23 VQADDPYRFFDWRVTYGNISPL-GIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRkNSyQDGVY 101
Cdd:COG2132     7 LLESGGGREYELTAQPATVELLpGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVP-NA-MDGVP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 102 GTtcPIPPGKNYTYAIQVKDQIGSFFYFP----SLAVHKAAGGFGGFRIlsRPRIPvPFPEPAGDFTFLIGDW-FKHDHK 176
Cdd:COG2132    85 GD--PIAPGETFTYEFPVPQPAGTYWYHPhthgSTAEQVYRGLAGALIV--EDPEE-DLPRYDRDIPLVLQDWrLDDDGQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 177 VLKAiLDRGHKLPLPQGVLINGQGVSYmssITVHKGKTYRFRISNVGLQHTLNFRIQ-GHQMKLVEVEGtHTVQSMY--T 253
Cdd:COG2132   160 LLYP-MDAAMGGRLGDTLLVNGRPNPT---LEVRPGERVRLRLLNASNARIYRLALSdGRPFTVIATDG-GLLPAPVevD 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1063727537 254 SLDIHVGQSYSVLVTMDQPDQDYDIVVSTKF 284
Cdd:COG2132   235 ELLLAPGERADVLVDFSADPGEEVTLANPFE 265
 
Name Accession Description Interval E-value
PLN02792 PLN02792
oxidoreductase
13-454 0e+00

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 880.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  13 MMMTISIISFVQADDPYrFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLR 92
Cdd:PLN02792    1 MMMTTTIISFVKADDTL-FYNWRVTYGNISLLTLPRRGILINGQFPGPEIRSLTNDNLVINVHNDLDEPFLLSWNGVHMR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  93 KNSYQDGVYGTTCPIPPGKNYTYAIQVKDQIGSFFYFPSLAVHKAAGGFGGFRILSRPRIPVPFPEPAGDFTFLIGDWFK 172
Cdd:PLN02792   80 KNSYQDGVYGTTCPIPPGKNYTYDFQVKDQVGSYFYFPSLAVQKAAGGYGSLRIYSLPRIPVPFPEPAGDFTFLIGDWYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 173 HDHKVLKAILDRGHKLP-LPQGVLINGQGVSYMSSITVHKGKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEGTHTVQSM 251
Cdd:PLN02792  160 RNHTTLKKILDGGRKLPlMPDGVMINGQGVSYVYSITVDKGKTYRFRISNVGLQTSLNFEILGHQLKLIEVEGTHTVQSM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 252 YTSLDIHVGQSYSVLVTMDQPDQDYDIVVSTKFVAKKLLVSSTIHYsnsrhSHSSSANSVHVQQP-ADELDWSIKQARSI 330
Cdd:PLN02792  240 YTSLDIHVGQTYSVLVTMDQPPQNYSIVVSTRFIAAKVLVSSTLHY-----SNSKGHKIIHARQPdPDDLEWSIKQAQSI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 331 RTNLTASGPRPNPQGSYHYGRIKISRTLILESSAALVKRKQRYAINGVSFVPGDTPLKLADYFKIKGVFKMGSIPDKPRR 410
Cdd:PLN02792  315 RTNLTASGPRTNPQGSYHYGKMKISRTLILESSAALVKRKQRYAINGVSFVPSDTPLKLADHFKIKGVFKVGSIPDKPRR 394
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1063727537 411 GRGMRMETSVMGAHHRDFLEIIFQNREKIVQSYHLDGYSFWVVG 454
Cdd:PLN02792  395 GGGMRLDTSVMGAHHNAFLEIIFQNREKIVQSYHLDGYNFWVVG 438
PLN02991 PLN02991
oxidoreductase
12-454 0e+00

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 642.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  12 MMMMTISIISFVQADDPYRFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQL 91
Cdd:PLN02991   11 MILGLLFLISFVAAEDPYRFFEWHVTYGNISPLGVAQQGILINGKFPGPDIISVTNDNLIINVFNHLDEPFLISWSGIRN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  92 RKNSYQDGVYGTTCPIPPGKNYTYAIQVKDQIGSFFYFPSLAVHKAAGGFGGFRILSRPRIPVPFPEPAGDFTFLIGDWF 171
Cdd:PLN02991   91 WRNSYQDGVYGTTCPIPPGKNYTYALQVKDQIGSFYYFPSLGFHKAAGGFGAIRISSRPLIPVPFPAPADDYTVLIGDWY 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 172 KHDHKVLKAILDRGHKLPLPQGVLINGQGVSymSSITVHKGKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEGTHTVQSM 251
Cdd:PLN02991  171 KTNHKDLRAQLDNGGKLPLPDGILINGRGSG--ATLNIEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTHTIQTP 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 252 YTSLDIHVGQSYSVLVTMDQPDQDYDIVVSTKFVAKKLLVSSTIHYSNSRHSHSSSANSVHVQqpadeLDWSIKQARSIR 331
Cdd:PLN02991  249 FSSLDVHVGQSYSVLITADQPAKDYYIVVSSRFTSKILITTGVLHYSNSAGPVSGPIPDGPIQ-----LSWSFDQARAIK 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 332 TNLTASGPRPNPQGSYHYGRIKISRTLILESSAALVKRKQRYAINGVSFVPGDTPLKLADYFKIKGVFKMGSIPDKPRRG 411
Cdd:PLN02991  324 TNLTASGPRPNPQGSYHYGKINITRTIRLANSAGNIEGKQRYAVNSASFYPADTPLKLADYFKIAGVYNPGSIPDQPTNG 403
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1063727537 412 rGMRMETSVMGAHHRDFLEIIFQNREKIVQSYHLDGYSFWVVG 454
Cdd:PLN02991  404 -AIFPVTSVMQTDYKAFVEIVFENWEDIVQTWHLDGYSFYVVG 445
PLN02835 PLN02835
oxidoreductase
17-454 0e+00

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 596.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  17 ISIISFVQADDPYRFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNSY 96
Cdd:PLN02835   17 LSSVSLVNGEDPYKYYTWTVTYGTISPLGVPQQVILINGQFPGPRLDVVTNDNIILNLINKLDQPFLLTWNGIKQRKNSW 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  97 QDGVYGTTCPIPPGKNYTYAIQVKDQIGSFFYFPSLAVHKAAGGFGGFRILSRPRIPVPFPEPAGDFTFLIGDWFKHDHK 176
Cdd:PLN02835   97 QDGVLGTNCPIPPNSNYTYKFQTKDQIGTFTYFPSTLFHKAAGGFGAINVYERPRIPIPFPLPDGDFTLLVGDWYKTSHK 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 177 VLKAILDRGHKLPLPQGVLINGQGVSYMSSitvHKGKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEGTHTVQSMYTSLD 256
Cdd:PLN02835  177 TLQQRLDSGKVLPFPDGVLINGQTQSTFSG---DQGKTYMFRISNVGLSTSLNFRIQGHTMKLVEVEGSHTIQNIYDSLD 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 257 IHVGQSYSVLVTMDQPDQDYDIVVSTKFVAKKLLVSSTIHYSNSRHSHSSSANSVhvqqPADELDWSIKQARSIRTNLTA 336
Cdd:PLN02835  254 VHVGQSVAVLVTLNQSPKDYYIVASTRFTRQILTATAVLHYSNSRTPASGPLPAL----PSGELHWSMRQARTYRWNLTA 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 337 SGPRPNPQGSYHYGRIKISRTLILESSAALVKRKQRYAINGVSFVPGDTPLKLADYFKIKGVFKMGSIPDKPRRGRGMrM 416
Cdd:PLN02835  330 SAARPNPQGSFHYGKITPTKTIVLANSAPLINGKQRYAVNGVSYVNSDTPLKLADYFGIPGVFSVNSIQSLPSGGPAF-V 408
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1063727537 417 ETSVMGAHHRDFLEIIFQNREKIVQSYHLDGYSFWVVG 454
Cdd:PLN02835  409 ATSVMQTSLHDFLEVVFQNNEKTMQSWHLDGYDFWVVG 446
PLN02354 PLN02354
copper ion binding / oxidoreductase
23-454 0e+00

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 560.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  23 VQADDPYRFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNSYQDGVYG 102
Cdd:PLN02354   21 VRAEDPYFFFTWNVTYGTASPLGVPQQVILINGQFPGPNINSTSNNNIVINVFNNLDEPFLLTWSGIQQRKNSWQDGVPG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 103 TTCPIPPGKNYTYAIQVKDQIGSFFYFPSLAVHKAAGGFGGFRILSRPRIPVPFPEPAGDFTFLIGDWFKHDHKVLKAIL 182
Cdd:PLN02354  101 TNCPIPPGTNFTYHFQPKDQIGSYFYYPSTGMHRAAGGFGGLRVNSRLLIPVPYADPEDDYTVLIGDWYTKSHTALKKFL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 183 DRGHKLPLPQGVLINGQGVSYMSS----ITVHKGKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEGTHTVQSMYTSLDIH 258
Cdd:PLN02354  181 DSGRTLGRPDGVLINGKSGKGDGKdeplFTMKPGKTYRYRICNVGLKSSLNFRIQGHKMKLVEMEGSHVLQNDYDSLDVH 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 259 VGQSYSVLVTMDQPDQDYDIVVSTKFVAKKLLVSSTIHYSNSRHshsssansvhvqQPADELD-------WSIKQARSIR 331
Cdd:PLN02354  261 VGQCFSVLVTANQAPKDYYMVASTRFLKKVLTTTGIIRYEGGKG------------PASPELPeapvgwaWSLNQFRSFR 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 332 TNLTASGPRPNPQGSYHYGRIKISRTLILESSAALVKRKQRYAINGVSFVPGDTPLKLADYFKI-KGVFKMGSIPDKPRR 410
Cdd:PLN02354  329 WNLTASAARPNPQGSYHYGKINITRTIKLVNSASKVDGKLRYALNGVSHVDPETPLKLAEYFGVaDKVFKYDTIKDNPPA 408
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1063727537 411 GRG-MRMETSVMGAHHRDFLEIIFQNREKIVQSYHLDGYSFWVVG 454
Cdd:PLN02354  409 KITkIKIQPNVLNITFRTFVEIIFENHEKSMQSWHLDGYSFFAVA 453
PLN02168 PLN02168
copper ion binding / pectinesterase
12-454 6.10e-169

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 486.02  E-value: 6.10e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  12 MMMMTISIISFVQADDPYRFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQL 91
Cdd:PLN02168    9 FVLISLVILELSYAFAPIVSYQWVVSYSQRFILGGNKQVIVINDMFPGPLLNATANDVINVNIFNNLTEPFLMTWNGLQL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  92 RKNSYQDGVYGTTCPIPPGKNYTYAIQVKDQIGSFFYFPSLAVHKAAGGFGGFRILSRPRIPVPFPEPAGDFTFLIGDWF 171
Cdd:PLN02168   89 RKNSWQDGVRGTNCPILPGTNWTYRFQVKDQIGSYFYFPSLLLQKAAGGYGAIRIYNPELVPVPFPKPDEEYDILIGDWF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 172 KHDHKVLKAILDRGHKLPLPQGVLINGQGVSyMSSITVHKGKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEGTHTVQSM 251
Cdd:PLN02168  169 YADHTVMRASLDNGHSLPNPDGILFNGRGPE-ETFFAFEPGKTYRLRISNVGLKTCLNFRIQDHDMLLVETEGTYVQKRV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 252 YTSLDIHVGQSYSVLVTM-DQP---DQDYDIVVSTKFVAKKLLVSSTIHYSNSRHSHSSSANSVHVQQpadELDWSIKQA 327
Cdd:PLN02168  248 YSSLDIHVGQSYSVLVTAkTDPvgiYRSYYIVATARFTDAYLGGVALIRYPNSPLDPVGPLPLAPALH---DYFSSVEQA 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 328 RSIRTNLTASGPRPNPQGSYHYGRIKISRTLILESSAALVKRKQRYAINGVSFVPGDTPLKLADYFKIKGVFKMGSIPDK 407
Cdd:PLN02168  325 LSIRMDLNVGAARSNPQGSYHYGRINVTRTIILHNDVMLSSGKLRYTINGVSFVYPGTPLKLVDHFQLNDTIIPGMFPVY 404
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1063727537 408 PRRGRGMrMETSVMGAHHRDFLEIIFQNREKIVQSYHLDGYSFWVVG 454
Cdd:PLN02168  405 PSNKTPT-LGTSVVDIHYKDFYHIVFQNPLFSLESYHIDGYNFFVVG 450
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
25-454 2.73e-149

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 437.94  E-value: 2.73e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  25 ADDPYRFFDWRVTYGNISPLG--IPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNSYQDGVYG 102
Cdd:PLN00044   23 AGDPYAYYDWEVSYVSAAPLGgvKKQEAIGINGQFPGPALNVTTNWNLVVNVRNALDEPLLLTWHGVQQRKSAWQDGVGG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 103 TTCPIPPGKNYTYAIQVKDQIGSFFYFPSLAVHKAAGGFGGFRILSRPRIPVPFPEP-AGDFTFLIGDWFKHDHKVLKAI 181
Cdd:PLN00044  103 TNCAIPAGWNWTYQFQVKDQVGSFFYAPSTALHRAAGGYGAITINNRDVIPIPFGFPdGGDITLFIADWYARDHRALRRA 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 182 LDRGHKLPLPQGVLING------------QGVSYmSSITVHKGKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEGTHTVQ 249
Cdd:PLN00044  183 LDAGDLLGAPDGVLINAfgpyqyndslvpPGITY-ERINVDPGKTYRFRVHNVGVATSLNFRIQGHNLLLVEAEGSYTSQ 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 250 SMYTSLDIHVGQSYSVLVTMDQ-PDQDYDIVVSTKFV----AKKLLVSSTIHYSNSRHSHSSSANsvhvQQPADELD--W 322
Cdd:PLN00044  262 QNYTNLDIHVGQSYSFLLTMDQnASTDYYVVASARFVdaavVDKLTGVAILHYSNSQGPASGPLP----DAPDDQYDtaF 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 323 SIKQARSIRTNLTASGPRPNPQGSYHYGRIKISRTLILESSAA-LVKRKQRYAINGVSFVPGDTPLKLADYFKIKGVFKM 401
Cdd:PLN00044  338 SINQARSIRWNVTASGARPNPQGSFHYGDITVTDVYLLQSMAPeLIDGKLRATLNEISYIAPSTPLMLAQIFNVPGVFKL 417
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063727537 402 gSIPDKPrRGRGMRMETSVMGAHHRDFLEIIFQNREKIVQSYHLDGYSFWVVG 454
Cdd:PLN00044  418 -DFPNHP-MNRLPKLDTSIINGTYKGFMEIIFQNNATNVQSYHLDGYAFFVVG 468
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
31-146 8.49e-73

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: 224.59  E-value: 8.49e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  31 FFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNSYQDGVYGTTCPIPPG 110
Cdd:cd13846     2 FFDWNVSYITASPLGVPQQVIAINGQFPGPTINVTTNDNVVVNVFNSLDEPLLLTWNGIQQRRNSWQDGVLGTNCPIPPG 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1063727537 111 KNYTYAIQVKDQIGSFFYFPSLAVHKAAGGFGGFRI 146
Cdd:cd13846    82 WNWTYKFQVKDQIGSFFYFPSLHFQRAAGGFGGIRV 117
CuRO_2_AAO_like_1 cd13872
The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate ...
161-297 6.47e-68

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: 213.03  E-value: 6.47e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 161 GDFTFLIGDWFKHDHKVLKAILDRGHKLPLPQGVLINGQG----VSYMSSITVHKGKTYRFRISNVGLQHTLNFRIQGHQ 236
Cdd:cd13872     1 DEYTVLIGDWYKTDHKTLRQSLDKGRTLGRPDGILINGKGpygyGANETSFTVEPGKTYRLRISNVGLRTSLNFRIQGHK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063727537 237 MKLVEVEGTHTVQSMYTSLDIHVGQSYSVLVTMDQPDQDYDIVVSTKFVAKKLLVSSTIHY 297
Cdd:cd13872    81 MLLVETEGSYTAQNTYDSLDVHVGQSYSVLVTADQSPKDYYIVASSRFLSPELTGVAILHY 141
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
161-297 4.51e-48

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


Pssm-ID: 395317 [Multi-domain]  Cd Length: 146  Bit Score: 161.72  E-value: 4.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 161 GDFTFLIGDWFKHDHKVLKAILDRGHKL-----PLPQGVLINGQGVSYMSSITVHKGKTYRFRISNVGLQHTLNFRIQGH 235
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKELLASGKAptdfpPVPDAVLINGKDGASLATLTVTPGKTYRLRIINVALDDSLNFSIEGH 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063727537 236 QMKLVEVEGTHTVQSMYTSLDIHVGQSYSVLVTMDQPDQDYDIVVSTKFVA-KKLLVSSTIHY 297
Cdd:pfam00394  81 KMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPNIPAfDNGTAAAILRY 143
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
36-150 3.05e-47

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 158.56  E-value: 3.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  36 VTYGNISPLGIP-QRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNSYQDGV-YGTTCPIPPGKNY 113
Cdd:pfam07732   2 VTYGTVSPLGGTrQAVIGVNGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVpGVTQCPIPPGQSF 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063727537 114 TYAIQVKDQIGSFFYFPSLAVHKAAGGFGGFRILSRP 150
Cdd:pfam07732  82 TYRFQVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDRA 118
PLN02191 PLN02191
L-ascorbate oxidase
3-454 2.20e-46

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 169.04  E-value: 2.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537   3 WWLngavwtmmmMTISIISFVQADDPYRFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLD-EP 81
Cdd:PLN02191    6 WWI---------VTVVAVLTHTASAAVREYTWEVEYKYWWPDCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLTtEG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  82 FLLSWNGVQLRKNSYQDGVYGTT-CPIPPGKNYTYAIQVkDQIGSFFYFPSLAVHKAAGGFGGFrILSRPRIPVPFPEPA 160
Cdd:PLN02191   77 LVIHWHGIRQKGSPWADGAAGVTqCAINPGETFTYKFTV-EKPGTHFYHGHYGMQRSAGLYGSL-IVDVAKGPKERLRYD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 161 GDFTFLIGDWFkhdHKVLKAILDRGHKLPL-----PQGVLINGQG------VSYMSS-------------------ITVH 210
Cdd:PLN02191  155 GEFNLLLSDWW---HESIPSQELGLSSKPMrwigeAQSILINGRGqfncslAAQFSNgtelpmctfkegdqcapqtLRVE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 211 KGKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEGTHTVQSMYTSLDIHVGQSYSVLVTMDQ-PDQDYDIVVSTKFVAKKL 289
Cdd:PLN02191  232 PNKTYRIRLASTTALASLNLAVQGHKLVVVEADGNYITPFTTDDIDIYSGESYSVLLTTDQdPSQNYYISVGVRGRKPNT 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 290 LVSSTIHYSNSRHSHSSSANSVHVQQPADELDwsikQARSIRTNLTASGPRPNPQGSYHygrikisRTLILESSAALVKR 369
Cdd:PLN02191  312 TQALTILNYVTAPASKLPSSPPPVTPRWDDFE----RSKNFSKKIFSAMGSPSPPKKYR-------KRLILLNTQNLIDG 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 370 KQRYAINGVSFVPGDTPLKLADYFKIKGVFKMGSIPdkprrgRGMRMETSVM------------GAHHRDF---LEIIFQ 434
Cdd:PLN02191  381 YTKWAINNVSLVTPATPYLGSVKYNLKLGFNRKSPP------RSYRMDYDIMnpppfpntttgnGIYVFPFnvtVDVIIQ 454
                         490       500
                  ....*....|....*....|....*.
gi 1063727537 435 NREKI------VQSYHLDGYSFWVVG 454
Cdd:PLN02191  455 NANVLkgvvseIHPWHLHGHDFWVLG 480
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
30-454 3.65e-43

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: 159.53  E-value: 3.65e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  30 RFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDL-DEPFLLSWNGVQLRKNSYQDGVYGTT-CPI 107
Cdd:TIGR03388   2 RHYKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLhTEGVVIHWHGIRQIGTPWADGTAGVTqCAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 108 PPGKNYTYAIQVkDQIGSFFYFPSLAVHKAAGGFGGFRILSRPRIPVPFpEPAGDFTFLIGDWFkhdHKVLKAILDRGHK 187
Cdd:TIGR03388  82 NPGETFIYNFVV-DRPGTYFYHGHYGMQRSAGLYGSLIVDVPDGEKEPF-HYDGEFNLLLSDWW---HKSIHEQEVGLSS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 188 LPL-----PQGVLINGQG------VSYMSSI------------------TVHKGKTYRFRISNVGLQHTLNFRIQGHQMK 238
Cdd:TIGR03388 157 KPMrwigePQSLLINGRGqfncslAAKFSSTnlpqcnlkgneqcapqilHVEPGKTYRLRIASTTALAALNFAIEGHKLT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 239 LVEVEGtHTVQSMYTS-LDIHVGQSYSVLVTMDQ-PDQDYDIVVSTKFVAKKLLVSSTI-HYsnSRHSHSSSANSVHVQQ 315
Cdd:TIGR03388 237 VVEADG-NYVEPFTVKdIDIYSGETYSVLLTTDQdPSRNYWISVGVRGRKPNTPPGLTVlNY--YPNSPSRLPPTPPPVT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 316 PA-DELDWSIKQARSIrtnLTASGPRPNPQGSyhygrikiSRTLILESSAALVKRKQRYAINGVSFVPGDTPLKLADYFK 394
Cdd:TIGR03388 314 PAwDDFDRSKAFSLAI---KAAMGSPKPPETS--------DRRIVLLNTQNKINGYTKWAINNVSLTLPHTPYLGSLKYN 382
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063727537 395 IKGVFKMGSIPD---------KPRRGRGMRMETSVMGAHHRDFLEIIFQNREKI------VQSYHLDGYSFWVVG 454
Cdd:TIGR03388 383 LLNAFDQKPPPEnyprdydifKPPPNPNTTTGNGIYRLKFNTTVDVILQNANTLngnnseTHPWHLHGHDFWVLG 457
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
30-454 6.08e-39

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: 147.58  E-value: 6.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  30 RFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNSYQDG-VYGTTCPIP 108
Cdd:TIGR03389   4 RHYTFDVQEKNVTRLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQYNVTIHWHGVRQLRNGWADGpAYITQCPIQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 109 PGKNYTYAIQVKDQIGSFFYFPSLAVHKAAgGFGGFRILSRPRIPVPFPEPAGDFTFLIGDWFKHD-HKVLKAILDRGHK 187
Cdd:TIGR03389  84 PGQSYVYNFTITGQRGTLWWHAHISWLRAT-VYGAIVILPKPGVPYPFPKPDREVPIILGEWWNADvEAVINQANQTGGA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 188 LPLPQGVLINGQ-GVSYMSS------ITVHKGKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEGTHTVQSMYTSLDIHVG 260
Cdd:TIGR03389 163 PNVSDAYTINGHpGPLYNCSskdtfkLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEVDATYTKPFKTKTIVIGPG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 261 QSYSVLVTMDQPDQDYDIVVS---TKFVA-KKLLVSSTIHYSNSRHSHSSSANSVhvqQPADELDWSIKQARSIRTNLTA 336
Cdd:TIGR03389 243 QTTNVLLTADQSPGRYFMAARpymDAPGAfDNTTTTAILQYKGTSNSAKPILPTL---PAYNDTAAATNFSNKLRSLNSA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 337 SGPRPNPQgsyhygriKISRTLILESSAALVKRKQ---------RYA--INGVSFVPGDTPLKLADYFKIKGVFKMgSIP 405
Cdd:TIGR03389 320 QYPANVPV--------TIDRRLFFTIGLGLDPCPNntcqgpngtRFAasMNNISFVMPTTALLQAHYFGISGVFTT-DFP 390
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063727537 406 DKP-----RRGRGMRMETSVMGA------HHRDFLEIIFQNREKI-VQSY--HLDGYSFWVVG 454
Cdd:TIGR03389 391 ANPptkfnYTGTNLPNNLFTTNGtkvvrlKFNSTVELVLQDTSILgSENHpiHLHGYNFFVVG 453
PLN02604 PLN02604
oxidoreductase
8-454 1.82e-36

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 141.15  E-value: 1.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537   8 AVWTMMMMTISIISFVQADDPYRFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDL-DEPFLLSW 86
Cdd:PLN02604    3 RFLALFFLLFSVLNFPAAEARIRRYKWEVKYEYKSPDCFKKLVITINGRSPGPTILAQQGDTVIVELKNSLlTENVAIHW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  87 NGVQLRKNSYQDGVYGTT-CPIPPGKNYTYAIQVkDQIGSFFYFPSLAVHKAAGGFGGFRIlsrpRIPVPFPEPAG---D 162
Cdd:PLN02604   83 HGIRQIGTPWFDGTEGVTqCPILPGETFTYEFVV-DRPGTYLYHAHYGMQREAGLYGSIRV----SLPRGKSEPFSydyD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 163 FTFLIGDWFkhdHKVLKAILDRGHKLPL-----PQGVLINGQGVSYMS----------------------SITVHKGKTY 215
Cdd:PLN02604  158 RSIILTDWY---HKSTYEQALGLSSIPFdwvgePQSLLIQGKGRYNCSlvsspylkagvcnatnpecspyVLTVVPGKTY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 216 RFRISNVGLQHTLNFRIQGHQMKLVEVEGTHTVQSMYTSLDIHVGQSYSVLVTMDQ-PDQDYdiVVSTKFVAKKLLVS-- 292
Cdd:PLN02604  235 RLRISSLTALSALSFQIEGHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQdPSRNY--WVTTSVVSRNNTTPpg 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 293 -STIHYSNSRhshsssansvHVQQPA---------DELDWSIKQARSIRTNltasgprpnpQGSYHYGRIKISRTLILES 362
Cdd:PLN02604  313 lAIFNYYPNH----------PRRSPPtvppsgplwNDVEPRLNQSLAIKAR----------HGYIHPPPLTSDRVIVLLN 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 363 SAALVKRKQRYAINGVSFVPGDTPLKLADYFKIKGVFKMGSIPD-----------KPRRGRGmrmeTSVMGAHHRDF--- 428
Cdd:PLN02604  373 TQNEVNGYRRWSVNNVSFNLPHTPYLIALKENLTGAFDQTPPPEgydfanydiyaKPNNSNA----TSSDSIYRLQFnst 448
                         490       500       510
                  ....*....|....*....|....*....|..
gi 1063727537 429 LEIIFQNREKIVQS------YHLDGYSFWVVG 454
Cdd:PLN02604  449 VDIILQNANTMNANnsethpWHLHGHDFWVLG 480
CuRO_3_AAO_like_1 cd13894
The third cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
384-454 3.90e-30

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: 113.29  E-value: 3.90e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063727537 384 DTPLKLADYFKIKGVFKMGSIPDKPRRgRGMRMETSVMGAHHRDFLEIIFQNREKIVQSYHLDGYSFWVVG 454
Cdd:cd13894     3 DTPLKLADYFKIKGVFQLDSIPDPPTR-KTPYLGTSVINGTYRGFIEIVFQNNEDTVQSWHLDGYSFFVVG 72
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
30-144 1.46e-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: 106.22  E-value: 1.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  30 RFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLD-EPFLLSWNGVQLRKNSYQDGV-YGTTCPI 107
Cdd:cd04206     1 REYELTITETTVNPDGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNLPnEPTSIHWHGLRQPGTNDGDGVaGLTQCPI 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063727537 108 PPGKNYTYAIQVKDQIGSFFYFPSLAVHKAAGGFGGF 144
Cdd:cd04206    81 PPGESFTYRFTVDDQAGTFWYHSHVGGQRADGLYGPL 117
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
30-146 1.68e-26

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: 103.11  E-value: 1.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  30 RFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNSYQDGVYGTT-CPIP 108
Cdd:cd13857     1 REYNFTISEITGAPDGFVRPMLVINGQFPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTNWMDGTAGITqCPIP 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1063727537 109 PGKNYTYAIQVKDQIGSFFYFPSLAVHKAAGGFGGFRI 146
Cdd:cd13857    81 PGGSFTYNFTVDGQYGTYWYHSHYSTQYADGLVGPLIV 118
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
164-284 1.51e-24

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: 98.97  E-value: 1.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 164 TFLIGDWFkHD--HKVLKAI-LDRGHKLPLPQGVLINGQGVSYMSS-----------ITVHKGKTYRFRISNVGLQHTLN 229
Cdd:cd04205     2 VLLLSDWY-HDsaEDVLAGYmPNSFGNEPVPDSLLINGRGRFNCSMavcnsgcplpvITVEPGKTYRLRLINAGSFASFN 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063727537 230 FRIQGHQMKLVEVEGtHTVQSMYTS-LDIHVGQSYSVLVTMDQPDQDYDIVVSTKF 284
Cdd:cd04205    81 FAIDGHNMTVIEVDG-GYVEPLEVDnLDLAPGQRYDVLVKADQPPGNYWIRASADG 135
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
30-128 1.05e-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: 92.69  E-value: 1.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  30 RFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDL-DEPFLLSWNGVQLRKNSYQDGVYGTT-CPI 107
Cdd:cd13854     4 RKYTLTITNSTLAPDGVEKEVMLINGQYPGPLIEANWGDTIEVTVINKLqDNGTSIHWHGIRQLNTNWQDGVPGVTeCPI 83
                          90       100
                  ....*....|....*....|.
gi 1063727537 108 PPGKNYTYAIQVkDQIGSFFY 128
Cdd:cd13854    84 APGDTRTYRFRA-TQYGTSWY 103
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
35-454 4.43e-22

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: 98.76  E-value: 4.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  35 RVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDL-DEPFLLSWNGVQLRKNSYQDGV-YGTTCPIPPGKN 112
Cdd:TIGR03390  14 RVTSDNIKIACSSRYSVVVNGTSPGPEIRLQEGQTTWIRVYNDIpDNNVTMHWHGLTQRTAPFSDGTpLASQWPIPPGHF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 113 YTYAIQVK-DQIGSFFYFPSLAVhKAAGGFGGFRILSRPRIPVPFPEpagDFTFLIGDWF-KHDHKVL------------ 178
Cdd:TIGR03390  94 FDYEIKPEpGDAGSYFYHSHVGF-QAVTAFGPLIVEDCEPPPYKYDD---ERILLVSDFFsATDEEIEqgllstpftwsg 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 179 --KAILDRGHKLPLPQGVLINGQGVSYMSSITVHKGKTYRFR-ISNVGLQhTLNFRIQGHQ-MKLVEVEGTHTVQSMYTS 254
Cdd:TIGR03390 170 etEAVLLNGKSGNKSFYAQINPSGSCMLPVIDVEPGKTYRLRfIGATALS-LISLGIEDHEnLTIIEADGSYTKPAKIDH 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 255 LDIHVGQSYSVLVTMDQPD-------QDYDIVVSTKFVAKKLLVSSTIHYSNSRHSHSSSANSVHV----QQPADELDWS 323
Cdd:TIGR03390 249 LQLGGGQRYSVLFKAKTEDelcggdkRQYFIQFETRDRPKVYRGYAVLRYRSDKASKLPSVPETPPlplpNSTYDWLEYE 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 324 IKQARSIRTN--LTASgprpnpqgsyhygriKISRTLILESSAALVKRKQR--YAINGVSFVPG--DTPLkLADYFKikg 397
Cdd:TIGR03390 329 LEPLSEENNQdfPTLD---------------EVTRRVVIDAHQNVDPLNGRvaWLQNGLSWTESvrQTPY-LVDIYE--- 389
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063727537 398 vFKMGSIPD--KPRRGRGMRMETSVMGAHHRDFLEIIFQNREKIVQS--------YHLDGYSFWVVG 454
Cdd:TIGR03390 390 -NGLPATPNytAALANYGFDPETRAFPAKVGEVLEIVWQNTGSYTGPnggvdthpFHAHGRHFYDIG 455
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
32-128 2.34e-21

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: 88.89  E-value: 2.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  32 FDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNSYQDGVYGTT-CPIPPG 110
Cdd:cd13850     1 FTLTVTEGSPDGDGGEREVILINGQFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTPWSDGVPGVTqWPIQPG 80
                          90
                  ....*....|....*...
gi 1063727537 111 KNYTYAIQVKDQIGSFFY 128
Cdd:cd13850    81 GSFTYRWKAEDQYGLYWY 98
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
23-284 3.95e-21

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: 95.00  E-value: 3.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  23 VQADDPYRFFDWRVTYGNISPL-GIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRkNSyQDGVY 101
Cdd:COG2132     7 LLESGGGREYELTAQPATVELLpGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVP-NA-MDGVP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 102 GTtcPIPPGKNYTYAIQVKDQIGSFFYFP----SLAVHKAAGGFGGFRIlsRPRIPvPFPEPAGDFTFLIGDW-FKHDHK 176
Cdd:COG2132    85 GD--PIAPGETFTYEFPVPQPAGTYWYHPhthgSTAEQVYRGLAGALIV--EDPEE-DLPRYDRDIPLVLQDWrLDDDGQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 177 VLKAiLDRGHKLPLPQGVLINGQGVSYmssITVHKGKTYRFRISNVGLQHTLNFRIQ-GHQMKLVEVEGtHTVQSMY--T 253
Cdd:COG2132   160 LLYP-MDAAMGGRLGDTLLVNGRPNPT---LEVRPGERVRLRLLNASNARIYRLALSdGRPFTVIATDG-GLLPAPVevD 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1063727537 254 SLDIHVGQSYSVLVTMDQPDQDYDIVVSTKF 284
Cdd:COG2132   235 ELLLAPGERADVLVDFSADPGEEVTLANPFE 265
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
167-278 1.58e-20

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: 87.85  E-value: 1.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 167 IGDWFkhdHKVLKAILDRG-HKLPLPQGVLINGQG------VSYMSSITVHKGKTYRFRISNVGLQHTLNFRIQGHQMKL 239
Cdd:cd13882     5 LGDWY---HTAAPDLLATTaGVPPVPDSGTINGKGrfdggpTSPLAVINVKRGKRYRFRVINISCIPSFTFSIDGHNLTV 81
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063727537 240 VEVEGTHTVQSMYTSLDIHVGQSYSVLVTMDQPDQDYDI 278
Cdd:cd13882    82 IEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWI 120
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
32-128 2.90e-20

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: 86.17  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  32 FDWRVTYGNISPLGI-PQRGILINGQYPGPDIYSVTNDNLIINVHNDL-DEPFLLSWNGVQLRKNSYQDGVYGTT-CPIP 108
Cdd:cd13851     3 FDWNITWVTANPDGLfERRVIGINGQWPPPPIEVNKGDTVVIHATNSLgDQPTSLHFHGLFQNGTNYMDGPVGVTqCPIP 82
                          90       100
                  ....*....|....*....|
gi 1063727537 109 PGKNYTYAIQVKDQIGSFFY 128
Cdd:cd13851    83 PGQSFTYEFTVDTQVGTYWY 102
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
35-128 2.93e-20

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: 86.24  E-value: 2.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  35 RVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLS-----WNGVQLRKNSYQDGV-YGTTCPIP 108
Cdd:cd13856     6 NIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTMRRstsihWHGIFQHGTNYADGPaFVTQCPIA 85
                          90       100
                  ....*....|....*....|
gi 1063727537 109 PGKNYTYAIQVKDQIGSFFY 128
Cdd:cd13856    86 PNHSFTYDFTAGDQAGTFWY 105
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
161-283 3.55e-20

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: 87.21  E-value: 3.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 161 GDFTFLIGDWFkhdHKVLKAILDRGHKLPL-----PQGVLINGQG-------VSYMSSI-----------------TVHK 211
Cdd:cd13871     2 GELNILLSDWW---HKSIYEQETGLSSKPFrwvgePQSLLIEGRGryncslaPAYPSSLpspvcnksnpqcapfilHVSP 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063727537 212 GKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEGtHTVQSMYTS-LDIHVGQSYSVLVTMDQ-PDQDYDIVVSTK 283
Cdd:cd13871    79 GKTYRLRIASVTALSSLNFIIEGHNLTVVEADG-NYVQPFEVSnLDIYSGETYSVLVTADQdPSRNYWVSVNVR 151
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
162-281 4.17e-20

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: 86.45  E-value: 4.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 162 DFTFLIGDWFKHDHKVL-KAILDR---GHKLPLPQGVLINGqgvSYMSSITVHKGKTYRFRISNVGLQHTLNFRIQGHQM 237
Cdd:cd13877     2 EVTLTLSDWYHDQSPDLlRDFLSPynpTGAEPIPDSSLFND---TQNATINFEPGKTYLLRIINMGAFASQYFHIEGHDM 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1063727537 238 KLVEVEGTHTVQSMYTSLDIHVGQSYSVLVTM-DQPDQDYDIVVS 281
Cdd:cd13877    79 TIIEVDGVYVKPYPVDTLYIAVGQRYSVLVKAkNDTDRNYAIING 123
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
30-142 1.47e-17

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: 78.26  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  30 RFFDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDL-DEPFLLSWNGVQLRKNSYQDGV-YGTTCPI 107
Cdd:cd13845     1 RHYKWKVEYMFWAPDCVEKLVIGINGQFPGPTIRATAGDTIVVELENKLpTEGVAIHWHGIRQRGTPWADGTaSVSQCPI 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1063727537 108 PPGKNYTYAIQVkDQIGSFFYFPSLAVHKAAGGFG 142
Cdd:cd13845    81 NPGETFTYQFVV-DRPGTYFYHGHYGMQRSAGLYG 114
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
32-130 2.18e-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: 77.68  E-value: 2.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  32 FDWRVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNSYQDGV-YGTTCPIPPG 110
Cdd:cd13849     1 YTFVVQEKNVTRLCSTKSILTVNGQFPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLRSGWADGPaYITQCPIQPG 80
                          90       100
                  ....*....|....*....|
gi 1063727537 111 KNYTYAIQVKDQIGSFFYFP 130
Cdd:cd13849    81 QSYTYRFTVTGQEGTLWWHA 100
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
47-144 1.05e-16

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: 75.27  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  47 PQRGIL-INGQYPGPDIYSVTNDNLIINVHNDLD-EPFLLSWNGVQLRKNSYQDGV-YGTTCPIPPGKNYTYAIQVkDQI 123
Cdd:cd13858     3 VERPVItVNGQLPGPSIEVCEGDTVVVDVKNRLPgESTTIHWHGIHQRGTPYMDGVpMVTQCPILPGQTFRYKFKA-DPA 81
                          90       100
                  ....*....|....*....|.
gi 1063727537 124 GSFFYFPSLAVHKAAGGFGGF 144
Cdd:cd13858    82 GTHWYHSHSGTQRADGLFGAL 102
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
163-273 1.15e-16

The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs 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: 77.31  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 163 FTFLIGDWFkhdHKVLKAILDR------GHKLPLPQGVLINGQGVSYMSS----------------ITVHKGKTYRFRIS 220
Cdd:cd13886     1 VVVMVNDYY---HDPSSVLLARylapgnEGDEPVPDNGLINGIGQFDCASatykiyccasngtyynFTLEPNKTYRLRLI 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063727537 221 NVGLQHTLNFRIQGHQMKLVEVEGThTVQSMYT-SLDIHVGQSYSVLVTMDQPD 273
Cdd:cd13886    78 NAGSFADFTFSVDGHPLTVIEADGT-LVEPVEVhSITISVAQRYSVILTTNQPT 130
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
163-286 1.68e-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: 67.62  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 163 FTFLIGDWFKHDHK-VLKAILDRGHKLPLPQGVLINGQ-GVSY------MSSITVHKGKTYRFRISNVGLQHTLNFRIQG 234
Cdd:cd13875     1 VPIILGEWWNRDVNdVEDQALLTGGGPNISDAYTINGQpGDLYncsskdTFVLTVEPGKTYLLRIINAALNEELFFKIAN 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063727537 235 HQMKLVEVEGTHTvQSMYTS-LDIHVGQSYSVLVTMDQPDQDYDIVVSTKFVA 286
Cdd:cd13875    81 HTLTVVAVDASYT-KPFTTDyILIAPGQTTDVLLTADQPPGRYYMAARPYQSA 132
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
45-146 5.62e-13

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: 65.38  E-value: 5.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  45 GIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNsyQDGVYG-TTCPIPPGKNYTYAIQVKdQI 123
Cdd:cd13848    16 GKEGEAITVNGQVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPND--MDGVPGlSFPGIKPGETFTYRFPVR-QS 92
                          90       100
                  ....*....|....*....|...
gi 1063727537 124 GSFFYFPSLAVHKAAGGFGGFRI 146
Cdd:cd13848    93 GTYWYHSHSGLQEQTGLYGPIII 115
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
162-282 1.10e-12

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: 65.33  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 162 DFTFLIGDWFKHDHKVLKAILDRGHKLPLPQGVLINGQGVSY-----------MSSITVHKGKTYRFRISNVG-LQHTLN 229
Cdd:cd13884     1 EHVILIQDWTHELSSERFVGRGHNGGGQPPDSILINGKGRYYdpktgntnntpLEVFTVEQGKRYRFRLINAGaTNCPFR 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063727537 230 FRIQGHQMKLVEVEGTHTVQSMYTSLDIHVGQSYSVLVTMDQPDQDYDIVVST 282
Cdd:cd13884    81 VSIDGHTLTVIASDGNDVEPVEVDSIIIYPGERYDFVLNANQPIGNYWIRARG 133
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
54-144 7.50e-12

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: 62.21  E-value: 7.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  54 NGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNsyQDGVYGTT-CPIPPGKNYTYAIQVKdQIGSFFYFP-- 130
Cdd:cd13860    26 NGSVPGPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNG--MDGVPGITqPPIQPGETFTYEFTAK-QAGTYMYHShv 102
                          90
                  ....*....|....
gi 1063727537 131 SLAVHKAAGGFGGF 144
Cdd:cd13860   103 DEAKQEDMGLYGAF 116
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
164-273 2.17e-11

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: 62.27  E-value: 2.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 164 TFLIGDWFkhdHKVLKAILDRGHKL---PLPQGVLINGQGVSYMSS-------ITVHKGKTYRFRISNVGLQHTLNFRIQ 233
Cdd:cd13880     3 PVLLTDWY---HRSAFELFSEELPTggpPPMDNILINGKGKFPCSTgagsyfeTTFTPGKKYRLRLINTGVDTTFRFSID 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1063727537 234 GHQMKLVEVEGTHTVQSMYTSLDIHVGQSYSVLVTMDQPD 273
Cdd:cd13880    80 GHNLTVIAADFVPIVPYTTDSLNIGIGQRYDVIVEANQDP 119
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
161-266 2.57e-11

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: 61.92  E-value: 2.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 161 GDFTFLIGDWF-KHDHKVLKAILDRGHKLP-LPQGVLINGQGVSYMSS--------------ITVHKGKTYRFR-ISNVG 223
Cdd:cd13873     1 EERILLFSDYFpKTDSTIETGLTATPFVWPgEPNALLVNGKSGGTCNKsategcttschppvIDVEPGKTYRFRfIGATA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1063727537 224 LQHtLNFRIQGHQ-MKLVEVEGTHTvQSMYTS-LDIHVGQSYSVL 266
Cdd:cd13873    81 LSF-VSLGIEGHDnLTIIEADGSYT-KPAETDhLQLGSGQRYSFL 123
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
165-273 4.14e-11

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: 61.20  E-value: 4.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 165 FLIGDWFkHDHK---VLKAILDRGHK----LPLPQGVLINGQGVSYMS--------------SITVHKGKTYRFRISNVG 223
Cdd:cd13883     3 LFISDWY-HDQSeviVAGLLSPQGYKgspaAPSPDSALINGIGQFNCSaadpgtcctqtsppEIQVEAGKRTRFRLINAG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063727537 224 LQHTLNFRIQGHQMKLVEVEGTHTVQSMY-TSLDIHVGQSYSVLVTMDQPD 273
Cdd:cd13883    82 SHAMFRFSVDNHTLNVVEADDTPVYGPTVvHRIPIHNGQRYSVIIDTTSGK 132
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
54-128 4.32e-11

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: 60.18  E-value: 4.32e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063727537  54 NGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVqLRKNSYQ-DGVYGTTC-PIPPGKNYTYAIQVkDQIGSFFY 128
Cdd:cd13859    26 NGQVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGV-LQMGSWKmDGVPGVTQpAIEPGESFTYKFKA-ERPGTLWY 100
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
384-454 4.37e-11

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: 60.53  E-value: 4.37e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063727537 384 DTPLKLADYFKIK-GVFKMGsipDKPRRGRGMRMETSVMGAHHRDFLEIIFQNREKIVQSYHLDGYSFWVVG 454
Cdd:pfam07731   1 DTPPKLPTLLQITsGNFRRN---DWAINGLLFPPNTNVITLPYGTVVEWVLQNTTTGVHPFHLHGHSFQVLG 69
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
54-130 4.71e-11

The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida, which is involved in the oxidation of Mn(II). However, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCO catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259930 [Multi-domain]  Cd Length: 119  Bit Score: 59.94  E-value: 4.71e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063727537  54 NGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRkNSYqDGVYGTT-CPIPPGKNYTYAIQVKDQiGSFFYFP 130
Cdd:cd13861    26 NGQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLP-NAM-DGVPGLTqPPVPPGESFTYEFTPPDA-GTYWYHP 100
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
47-128 1.76e-08

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: 52.53  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  47 PQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFL-LSWNGVQLRKNSYQDGVYGTT-CPIPPGKNYTYAIQV-KDQI 123
Cdd:cd13847    14 PRPSTLINGSFPGPELRVQEGQHLWVRVYNDLEAGNTtMHFHGLSQYMSPFSDGTPLASqWPIPPGKFFDYEFPLeAGDA 93

                  ....*
gi 1063727537 124 GSFFY 128
Cdd:cd13847    94 GTYYY 98
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
54-146 2.33e-08

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. Three copper ions of type 1 lie close to one another near the surface of the central part of the trimer, and, effectively, a trimeric substrate binding site is formed in their vicinity. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities.


Pssm-ID: 259910 [Multi-domain]  Cd Length: 119  Bit Score: 52.27  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  54 NGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQlrkNSYQDGVYGTtcPIPPGKNYTYAIqVKDQIGSFFY---FP 130
Cdd:cd11024    27 NGTVPGPTLRATEGDLVRIHFINTGDHPHTIHFHGIH---DAAMDGTGLG--PIMPGESFTYEF-VAEPAGTHLYhchVQ 100
                          90
                  ....*....|....*.
gi 1063727537 131 SLAVHKAAGGFGGFRI 146
Cdd:cd11024   101 PLKEHIAMGLYGAFIV 116
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
166-281 2.81e-08

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: 52.59  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 166 LIGDW-FKHDHKVLKAILDRGHKLPLPQGVLINGQGVSYMSSITVHKGKTYR-FRISNVGLQHTLNFRIQGHQMKLVEVE 243
Cdd:cd13876     4 ILSDWrHLTSEEYWKIMRASGIEPFCYDSILINGKGRVYCLIVIVDPGERWVsLNFINAGGFHTLAFSIDEHPMWVYAVD 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063727537 244 G----THTVQSMYtsldIHVGQSYSVLVTMDQPDQDYDIVVS 281
Cdd:cd13876    84 GgyiePQLVDAIS----ITNGERYSVLVKLDKPPGDYTIRVA 121
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
50-125 1.45e-05

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 45.54  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  50 GILingqypGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNS----YQDGVYGTTCPIPPGKNYTYAIQVKDQIGS 125
Cdd:cd04224    79 GIL------GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYegamYRDGDPSPGSHVSPGETFTYEWTVPEGVGP 152
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
54-130 1.60e-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: 44.00  E-value: 1.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063727537  54 NGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLRKNsyQDGvyGTTCPIPPGKNYTYAIQV-KDQIGSFFYFP 130
Cdd:cd13855    27 NGSVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPD--QDG--NPHDPVAPGNDRVYRFTLpQDSAGTYWYHP 100
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
53-130 8.10e-05

The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins; CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. FtsP does not contain any copper binding sites.


Pssm-ID: 259894 [Multi-domain]  Cd Length: 120  Bit Score: 42.18  E-value: 8.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063727537  53 INGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGVQLrkNSYQDGvyGTTCPIPPGKNYTYAIQVKDQIGSFFYFP 130
Cdd:cd04232    25 YNGSYLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHV--PGEMDG--GPHQPIAPGQTWSPTFTIDQPAATLWYHP 98
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
162-272 1.13e-04

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


Pssm-ID: 259865 [Multi-domain]  Cd Length: 138  Bit Score: 41.86  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 162 DFTFLIGDWFkhdhkVLKAILDRGHKLPLPQGVLINGQGVSYMSSITVHKGKTYRFRISNVGLQHTlNFRIQGHQMKLVE 241
Cdd:cd04202     3 DYTLVLQEWF-----VDPGTTPMPPEGMDFNYFTINGKSFPATPPLVVKEGDRVRIRLINLSMDHH-PMHLHGHFFLVTA 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1063727537 242 VEGtHTVQSMY----TSLDIHVGQSYSVLVTMDQP 272
Cdd:cd04202    77 TDG-GPIPGSApwpkDTLNVAPGERYDIEFVADNP 110
CuRO_2_McoC_like cd13881
The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
177-279 1.18e-03

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


Pssm-ID: 259948 [Multi-domain]  Cd Length: 142  Bit Score: 39.13  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537 177 VLKAI-LDRGHKLPLP---------QG--VLINGQgvsYMSSITVHKGKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEG 244
Cdd:cd13881     5 VLSDLtLDGDGQLAEPsaadwmfgrEGdlVLVNGQ---LNPTITVRPGEVQRWRIVNAASARYFRLALDGHKFRLIGTDG 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1063727537 245 THTVQSMY-TSLDIHVGQSYSVLVTMDQPDQDYDIV 279
Cdd:cd13881    82 GLLEAPREvDELLLAPGERAEVLVTAGEPGGRLVLL 117
CuRO_2_CopA cd13874
The second cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
195-268 1.29e-03

The second cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259942 [Multi-domain]  Cd Length: 112  Bit Score: 38.43  E-value: 1.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063727537 195 LINGQGVSYMSSITVHKGKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEGTHTVQSMYTSLDIHVGQSYSVLVT 268
Cdd:cd13874    15 LINGKPPEDNWTGLFKPGERVRLRFINAAASTYFDVRIPGGKMTVVAADGQDVRPVEVDEFRIGVAETYDVIVT 88
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
195-271 1.32e-03

The second cupredoxin domain of CopA copper resistance protein like family; The members of this family are copper resistance protein (CopA) homologs. CopA is multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. CopA is involved in copper resistance in bacteria. CopA mutant causes a loss of function, including copper tolerance and oxidase activity, and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259938 [Multi-domain]  Cd Length: 117  Bit Score: 38.47  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063727537 195 LINGQGVSYMSSITVHKGKTYRFRISNVGLQHTLNFRIQGHQMKLVEVEGTHTVQSMYTSLDIHVGQSYSVLVTMDQ 271
Cdd:cd13870    19 LINGRPPEDPAVFTARPGDRLRLRLINAAGDTAFRVALAGHRLTVTHTDGFPVEPVEVDALLIGMGERYDAIVTANN 95
CuRO_1_LCC_like_3 cd13865
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
74-128 3.49e-03

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


Pssm-ID: 259933 [Multi-domain]  Cd Length: 115  Bit Score: 37.29  E-value: 3.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063727537  74 VHNDLDEPFLLSWNGvQLRKNSyQDGV-YGTTCPIPPGKNYTYAIQVkDQIGSFFY 128
Cdd:cd13865    43 LENRLDEPTTIHWHG-LIPPNL-QDGVpDVTQPPIPPGQSQRYDFPL-VQPGTFWM 95
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
45-130 3.69e-03

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


Pssm-ID: 259921 [Multi-domain]  Cd Length: 114  Bit Score: 37.27  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  45 GIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFLLSWNGvqLRKNSYQDGVYGTTcpIPPGKNYTYAIQVKDQIG 124
Cdd:cd13852    10 GDPAALQNLPDSYLGPILRLRKGQKVRITFKNNLPEPTIIHWHG--LHVPAAMDGHPRYA--IDPGETYVYEFEVLNRAG 85

                  ....*.
gi 1063727537 125 SFFYFP 130
Cdd:cd13852    86 TYWYHP 91
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
382-454 3.80e-03

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: 37.44  E-value: 3.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063727537 382 PGDTPLKLADYFK--IKGVFKMGSIPDKPRRGrgmrmETSVMGAHHRDFLEIIFQNREK--IVQSYHLDGYSFWVVG 454
Cdd:cd04207     1 DRTRRLVLSQTGApdGTTRWVINGMPFKEGDA-----NTDIFSVEAGDVVEIVLINAGNhdMQHPFHLHGHSFWVLG 72
PRK10965 PRK10965
multicopper oxidase; Provisional
53-147 6.69e-03

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 38.85  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  53 INGQYPGPDIY-----SVTndnliINVHNDLDEPFLLSWNGVQLRKNsyQDGvyGTTCPIPPGKNYTYAIQVkDQIGSFF 127
Cdd:PRK10965   70 YNGNLLGPAVRlqrgkAVT-----VDITNQLPEETTLHWHGLEVPGE--VDG--GPQGIIAPGGKRTVTFTV-DQPAATC 139
                          90       100
                  ....*....|....*....|....
gi 1063727537 128 YF-PSL---AVHKAAGGFGGFRIL 147
Cdd:PRK10965  140 WFhPHQhgkTGRQVAMGLAGLVLI 163
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
35-142 7.86e-03

The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus; The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259922 [Multi-domain]  Cd Length: 139  Bit Score: 36.85  E-value: 7.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063727537  35 RVTYGNISPLGIPQRGILINGQYPGPDIYSVTNDNLIINVHNDLDEPFL-----------------LSWNGVQLRKNSYQ 97
Cdd:cd13853     7 TVEYGRVTLAGLPVTLRTYNGSIPGPTLRVRPGDTLRITLKNDLPPEGAaneapapntphcpnttnLHFHGLHVSPTGNS 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063727537  98 DGVYGTtcpIPPGKNYTYAIQV-KDQ-IGSFFYFP----SLAVHKAAGGFG 142
Cdd:cd13853    87 DNVFLT---IAPGESFTYEYDIpADHpPGTYWYHPhlhgSTALQVAGGMAG 134
 
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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