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Conserved domains on  [gi|1333122325|ref|XP_023535550|]
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L-ascorbate oxidase homolog [Cucurbita pepo subsp. pepo]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02991 super family cl33619
oxidoreductase
 22-539 0e+00

oxidoreductase


The actual alignment was detected with superfamily member PLN02991:

Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 877.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  22 VSAENPYRFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGVYG 101
Cdd:PLN02991   22 VAAEDPYRFFEWHVTYGNISPLGVAQQGILINGKFPGPDIISVTNDNLIINVFNHLDEPFLISWSGIRNWRNSYQDGVYG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 102 TTCPIPPGKNFTYILQVKDQIGSFYYFPSLAFHKAAGGFGGIRILSRPRIPVPFPDPDGDYTVLIGDWYKSNHTTLKAHL 181
Cdd:PLN02991  102 TTCPIPPGKNYTYALQVKDQIGSFYYFPSLGFHKAAGGFGAIRISSRPLIPVPFPAPADDYTVLIGDWYKTNHKDLRAQL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 182 DRGKKLPFPNGILINGRGNDTSFSVEQGKTYRLRISNVGLEHSLNFRIQGHKMKLVEVEGTHTLQTTYSSLDVHVGQSYS 261
Cdd:PLN02991  182 DNGGKLPLPDGILINGRGSGATLNIEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTHTIQTPFSSLDVHVGQSYS 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 262 VLVTADQPAQDYYIVVSTRFTYRVLSTTGILHYSNSAgPVKGPPPGGPTIQIDWSLNQARSIRTNLTASGPRPNPQGSYH 341
Cdd:PLN02991  262 VLITADQPAKDYYIVVSSRFTSKILITTGVLHYSNSA-GPVSGPIPDGPIQLSWSFDQARAIKTNLTASGPRPNPQGSYH 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 342 YGLINTTKTIILASSAGQVNRKQRYAVNSVSFNPADTPLKLADFFKIGGVFRVGSISDRPTGGGIYLDTSVMGADYRAFV 421
Cdd:PLN02991  341 YGKINITRTIRLANSAGNIEGKQRYAVNSASFYPADTPLKLADYFKIAGVYNPGSIPDQPTNGAIFPVTSVMQTDYKAFV 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 422 EIVFQNNENIVQSWHIDGYSFFVVGMDGGQWTQSSRNQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMWNVRSEFWARQ 501
Cdd:PLN02991  421 EIVFENWEDIVQTWHLDGYSFYVVGMELGKWSAASRKVYNLNDAVSRCTVQVYPRSWTAIYVSLDNVGMWNLRSELWERQ 500

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1333122325 502 YLGQQFYLRVYTPSTSLRDEFPIPKNALLCGRASGRHT 539
Cdd:PLN02991  501 YLGQQFYMRVYTTSTSLRDEYLIPKNALLCGRATGHHT 538
 
Name Accession Description Interval E-value
PLN02991 PLN02991
oxidoreductase
 22-539 0e+00

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 877.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  22 VSAENPYRFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGVYG 101
Cdd:PLN02991   22 VAAEDPYRFFEWHVTYGNISPLGVAQQGILINGKFPGPDIISVTNDNLIINVFNHLDEPFLISWSGIRNWRNSYQDGVYG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 102 TTCPIPPGKNFTYILQVKDQIGSFYYFPSLAFHKAAGGFGGIRILSRPRIPVPFPDPDGDYTVLIGDWYKSNHTTLKAHL 181
Cdd:PLN02991  102 TTCPIPPGKNYTYALQVKDQIGSFYYFPSLGFHKAAGGFGAIRISSRPLIPVPFPAPADDYTVLIGDWYKTNHKDLRAQL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 182 DRGKKLPFPNGILINGRGNDTSFSVEQGKTYRLRISNVGLEHSLNFRIQGHKMKLVEVEGTHTLQTTYSSLDVHVGQSYS 261
Cdd:PLN02991  182 DNGGKLPLPDGILINGRGSGATLNIEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTHTIQTPFSSLDVHVGQSYS 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 262 VLVTADQPAQDYYIVVSTRFTYRVLSTTGILHYSNSAgPVKGPPPGGPTIQIDWSLNQARSIRTNLTASGPRPNPQGSYH 341
Cdd:PLN02991  262 VLITADQPAKDYYIVVSSRFTSKILITTGVLHYSNSA-GPVSGPIPDGPIQLSWSFDQARAIKTNLTASGPRPNPQGSYH 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 342 YGLINTTKTIILASSAGQVNRKQRYAVNSVSFNPADTPLKLADFFKIGGVFRVGSISDRPTGGGIYLDTSVMGADYRAFV 421
Cdd:PLN02991  341 YGKINITRTIRLANSAGNIEGKQRYAVNSASFYPADTPLKLADYFKIAGVYNPGSIPDQPTNGAIFPVTSVMQTDYKAFV 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 422 EIVFQNNENIVQSWHIDGYSFFVVGMDGGQWTQSSRNQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMWNVRSEFWARQ 501
Cdd:PLN02991  421 EIVFENWEDIVQTWHLDGYSFYVVGMELGKWSAASRKVYNLNDAVSRCTVQVYPRSWTAIYVSLDNVGMWNLRSELWERQ 500

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1333122325 502 YLGQQFYLRVYTPSTSLRDEFPIPKNALLCGRASGRHT 539
Cdd:PLN02991  501 YLGQQFYMRVYTTSTSLRDEYLIPKNALLCGRATGHHT 538
CuRO_2_AAO_like_1 cd13872
The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate ...
 160-294 5.31e-78

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: 241.54  E-value: 5.31e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 160 GDYTVLIGDWYKSNHTTLKAHLDRGKKLPFPNGILINGRG------NDTSFSVEQGKTYRLRISNVGLEHSLNFRIQGHK 233
Cdd:cd13872     1 DEYTVLIGDWYKTDHKTLRQSLDKGRTLGRPDGILINGKGpygygaNETSFTVEPGKTYRLRISNVGLRTSLNFRIQGHK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333122325 234 MKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQPAQDYYIVVSTRFTYRVLSTTGILHY 294
Cdd:cd13872    81 MLLVETEGSYTAQNTYDSLDVHVGQSYSVLVTADQSPKDYYIVASSRFLSPELTGVAILHY 141
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 29-491 6.78e-70

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: 233.88  E-value: 6.78e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  29 RFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSL-DEPFLISWNGIQQRRNSYEDGVYGTT-CPI 106
Cdd:TIGR03388   2 RHYKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLhTEGVVIHWHGIRQIGTPWADGTAGVTqCAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 107 PPGKNFTYILQVkDQIGSFYYFPSLAFHKAAGGFGGIRILSRPRIPVPFpDPDGDYTVLIGDWY-KSNHTTlKAHLdrgK 185
Cdd:TIGR03388  82 NPGETFIYNFVV-DRPGTYFYHGHYGMQRSAGLYGSLIVDVPDGEKEPF-HYDGEFNLLLSDWWhKSIHEQ-EVGL---S 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 186 KLPF-----PNGILINGRG----------NDTS----------------FSVEQGKTYRLRISNVGLEHSLNFRIQGHKM 234
Cdd:TIGR03388 156 SKPMrwigePQSLLINGRGqfncslaakfSSTNlpqcnlkgneqcapqiLHVEPGKTYRLRIASTTALAALNFAIEGHKL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 235 KLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQ-PAQDYYIVVSTRftYRVLST---TGILHY-SNSAGPVKGPPPGGP 309
Cdd:TIGR03388 236 TVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQdPSRNYWISVGVR--GRKPNTppgLTVLNYyPNSPSRLPPTPPPVT 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 310 TIQIDWSLNQARSIRTNLTASGPRPNPqgsyhygliNTTKTIILASSAGQVNRKQRYAVNSVSFNPADTP--------LK 381
Cdd:TIGR03388 314 PAWDDFDRSKAFSLAIKAAMGSPKPPE---------TSDRRIVLLNTQNKINGYTKWAINNVSLTLPHTPylgslkynLL 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 382 LA--------DFFKIGGVFRVGSISDRPTGGGIYLdtsvmgADYRAFVEIVFQN----NENI--VQSWHIDGYSFFVVGM 447
Cdd:TIGR03388 385 NAfdqkpppeNYPRDYDIFKPPPNPNTTTGNGIYR------LKFNTTVDVILQNantlNGNNseTHPWHLHGHDFWVLGY 458

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1333122325 448 DGGQWTQS-SRNQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMW 491
Cdd:TIGR03388 459 GEGKFRPGvDEKSYNLKNPPLRNTVVIFPYGWTALRFVADNPGVW 503
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 160-297 2.22e-49

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: 167.11  E-value: 2.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 160 GDYTVLIGDWYKSNHTTLKAHLDRGKKLPF-----PNGILINGRGND--TSFSVEQGKTYRLRISNVGLEHSLNFRIQGH 232
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKELLASGKAPTdfppvPDAVLINGKDGAslATLTVTPGKTYRLRIINVALDDSLNFSIEGH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333122325 233 KMKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQPAQDYYIVVSTRFT-YRVLSTTGILHYSNS 297
Cdd:pfam00394  81 KMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPNIPaFDNGTAAAILRYSGA 146
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 52-278 3.13e-23

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: 102.32  E-value: 3.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  52 INGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIqqrRNSYE-DGVYGTtcPIPPGKNFTYILQVKDQIGSFYYFP- 129
Cdd:COG2132    38 YNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL---RVPNAmDGVPGD--PIAPGETFTYEFPVPQPAGTYWYHPh 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 130 ---SLAFHKAAGGFGGIRIlsRPRIPvPFPDPDGDYTVLIGDW-YKSNHTTLKAHlDRGKKLPFPNGILINGRGNDTsFS 205
Cdd:COG2132   113 thgSTAEQVYRGLAGALIV--EDPEE-DLPRYDRDIPLVLQDWrLDDDGQLLYPM-DAAMGGRLGDTLLVNGRPNPT-LE 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333122325 206 VEQGKTYRLRISNVGLEHSLNFRIQ-GHKMKLVEVEGtHTLQT--TYSSLDVHVGQSYSVLVTADQPAQDYYIVVS 278
Cdd:COG2132   188 VRPGERVRLRLLNASNARIYRLALSdGRPFTVIATDG-GLLPApvEVDELLLAPGERADVLVDFSADPGEEVTLAN 262
 
Name Accession Description Interval E-value
PLN02991 PLN02991
oxidoreductase
 22-539 0e+00

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 877.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  22 VSAENPYRFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGVYG 101
Cdd:PLN02991   22 VAAEDPYRFFEWHVTYGNISPLGVAQQGILINGKFPGPDIISVTNDNLIINVFNHLDEPFLISWSGIRNWRNSYQDGVYG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 102 TTCPIPPGKNFTYILQVKDQIGSFYYFPSLAFHKAAGGFGGIRILSRPRIPVPFPDPDGDYTVLIGDWYKSNHTTLKAHL 181
Cdd:PLN02991  102 TTCPIPPGKNYTYALQVKDQIGSFYYFPSLGFHKAAGGFGAIRISSRPLIPVPFPAPADDYTVLIGDWYKTNHKDLRAQL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 182 DRGKKLPFPNGILINGRGNDTSFSVEQGKTYRLRISNVGLEHSLNFRIQGHKMKLVEVEGTHTLQTTYSSLDVHVGQSYS 261
Cdd:PLN02991  182 DNGGKLPLPDGILINGRGSGATLNIEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTHTIQTPFSSLDVHVGQSYS 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 262 VLVTADQPAQDYYIVVSTRFTYRVLSTTGILHYSNSAgPVKGPPPGGPTIQIDWSLNQARSIRTNLTASGPRPNPQGSYH 341
Cdd:PLN02991  262 VLITADQPAKDYYIVVSSRFTSKILITTGVLHYSNSA-GPVSGPIPDGPIQLSWSFDQARAIKTNLTASGPRPNPQGSYH 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 342 YGLINTTKTIILASSAGQVNRKQRYAVNSVSFNPADTPLKLADFFKIGGVFRVGSISDRPTGGGIYLDTSVMGADYRAFV 421
Cdd:PLN02991  341 YGKINITRTIRLANSAGNIEGKQRYAVNSASFYPADTPLKLADYFKIAGVYNPGSIPDQPTNGAIFPVTSVMQTDYKAFV 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 422 EIVFQNNENIVQSWHIDGYSFFVVGMDGGQWTQSSRNQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMWNVRSEFWARQ 501
Cdd:PLN02991  421 EIVFENWEDIVQTWHLDGYSFYVVGMELGKWSAASRKVYNLNDAVSRCTVQVYPRSWTAIYVSLDNVGMWNLRSELWERQ 500

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1333122325 502 YLGQQFYLRVYTPSTSLRDEFPIPKNALLCGRASGRHT 539
Cdd:PLN02991  501 YLGQQFYMRVYTTSTSLRDEYLIPKNALLCGRATGHHT 538
PLN02792 PLN02792
oxidoreductase
 22-539 0e+00

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 844.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  22 VSAENPYrFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGVYG 101
Cdd:PLN02792   11 VKADDTL-FYNWRVTYGNISLLTLPRRGILINGQFPGPEIRSLTNDNLVINVHNDLDEPFLLSWNGVHMRKNSYQDGVYG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 102 TTCPIPPGKNFTYILQVKDQIGSFYYFPSLAFHKAAGGFGGIRILSRPRIPVPFPDPDGDYTVLIGDWYKSNHTTLKAHL 181
Cdd:PLN02792   90 TTCPIPPGKNYTYDFQVKDQVGSYFYFPSLAVQKAAGGYGSLRIYSLPRIPVPFPEPAGDFTFLIGDWYRRNHTTLKKIL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 182 DRGKKLP-FPNGILINGRGNDT--SFSVEQGKTYRLRISNVGLEHSLNFRIQGHKMKLVEVEGTHTLQTTYSSLDVHVGQ 258
Cdd:PLN02792  170 DGGRKLPlMPDGVMINGQGVSYvySITVDKGKTYRFRISNVGLQTSLNFEILGHQLKLIEVEGTHTVQSMYTSLDIHVGQ 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 259 SYSVLVTADQPAQDYYIVVSTRFTYRVLSTTGILHYSNSAGPVKGPPPGGPTIQIDWSLNQARSIRTNLTASGPRPNPQG 338
Cdd:PLN02792  250 TYSVLVTMDQPPQNYSIVVSTRFIAAKVLVSSTLHYSNSKGHKIIHARQPDPDDLEWSIKQAQSIRTNLTASGPRTNPQG 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 339 SYHYGLINTTKTIILASSAGQVNRKQRYAVNSVSFNPADTPLKLADFFKIGGVFRVGSISDRP-TGGGIYLDTSVMGADY 417
Cdd:PLN02792  330 SYHYGKMKISRTLILESSAALVKRKQRYAINGVSFVPSDTPLKLADHFKIKGVFKVGSIPDKPrRGGGMRLDTSVMGAHH 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 418 RAFVEIVFQNNENIVQSWHIDGYSFFVVGMDGGQWTQSSRNQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMWNVRSEF 497
Cdd:PLN02792  410 NAFLEIIFQNREKIVQSYHLDGYNFWVVGINKGIWSRASRREYNLKDAISRSTTQVYPESWTAVYVALDNVGMWNLRSQF 489

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1333122325 498 WARQYLGQQFYLRVYTPSTSLRDEFPIPKNALLCGRASGRHT 539
Cdd:PLN02792  490 WARQYLGQQFYLRVYSPTHSLKDEYPLPKNALLCGRASNKNM 531
PLN02835 PLN02835
oxidoreductase
 22-539 0e+00

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 768.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  22 VSAENPYRFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGVYG 101
Cdd:PLN02835   23 VNGEDPYKYYTWTVTYGTISPLGVPQQVILINGQFPGPRLDVVTNDNIILNLINKLDQPFLLTWNGIKQRKNSWQDGVLG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 102 TTCPIPPGKNFTYILQVKDQIGSFYYFPSLAFHKAAGGFGGIRILSRPRIPVPFPDPDGDYTVLIGDWYKSNHTTLKAHL 181
Cdd:PLN02835  103 TNCPIPPNSNYTYKFQTKDQIGTFTYFPSTLFHKAAGGFGAINVYERPRIPIPFPLPDGDFTLLVGDWYKTSHKTLQQRL 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 182 DRGKKLPFPNGILINGRgNDTSFSVEQGKTYRLRISNVGLEHSLNFRIQGHKMKLVEVEGTHTLQTTYSSLDVHVGQSYS 261
Cdd:PLN02835  183 DSGKVLPFPDGVLINGQ-TQSTFSGDQGKTYMFRISNVGLSTSLNFRIQGHTMKLVEVEGSHTIQNIYDSLDVHVGQSVA 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 262 VLVTADQPAQDYYIVVSTRFTYRVLSTTGILHYSNSAGPVKGPPPGGPTIQIDWSLNQARSIRTNLTASGPRPNPQGSYH 341
Cdd:PLN02835  262 VLVTLNQSPKDYYIVASTRFTRQILTATAVLHYSNSRTPASGPLPALPSGELHWSMRQARTYRWNLTASAARPNPQGSFH 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 342 YGLINTTKTIILASSAGQVNRKQRYAVNSVSFNPADTPLKLADFFKIGGVFRVGSISDRPTGGGIYLDTSVMGADYRAFV 421
Cdd:PLN02835  342 YGKITPTKTIVLANSAPLINGKQRYAVNGVSYVNSDTPLKLADYFGIPGVFSVNSIQSLPSGGPAFVATSVMQTSLHDFL 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 422 EIVFQNNENIVQSWHIDGYSFFVVGMDGGQWTQSSRNQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMWNVRSEFWARQ 501
Cdd:PLN02835  422 EVVFQNNEKTMQSWHLDGYDFWVVGYGSGQWTPAKRSLYNLVDALTRHTAQVYPKSWTTILVSLDNQGMWNMRSAIWERQ 501

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1333122325 502 YLGQQFYLRVYTPSTSLRDEFPIPKNALLCGRASGRHT 539
Cdd:PLN02835  502 YLGQQFYLRVWNQVHSLANEYDIPDNALLCGKAIGRHP 539
PLN02354 PLN02354
copper ion binding / oxidoreductase
 22-536 0e+00

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 722.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  22 VSAENPYRFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGVYG 101
Cdd:PLN02354   21 VRAEDPYFFFTWNVTYGTASPLGVPQQVILINGQFPGPNINSTSNNNIVINVFNNLDEPFLLTWSGIQQRKNSWQDGVPG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 102 TTCPIPPGKNFTYILQVKDQIGSFYYFPSLAFHKAAGGFGGIRILSRPRIPVPFPDPDGDYTVLIGDWYKSNHTTLKAHL 181
Cdd:PLN02354  101 TNCPIPPGTNFTYHFQPKDQIGSYFYYPSTGMHRAAGGFGGLRVNSRLLIPVPYADPEDDYTVLIGDWYTKSHTALKKFL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 182 DRGKKLPFPNGILINGRG------NDTSFSVEQGKTYRLRISNVGLEHSLNFRIQGHKMKLVEVEGTHTLQTTYSSLDVH 255
Cdd:PLN02354  181 DSGRTLGRPDGVLINGKSgkgdgkDEPLFTMKPGKTYRYRICNVGLKSSLNFRIQGHKMKLVEMEGSHVLQNDYDSLDVH 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 256 VGQSYSVLVTADQPAQDYYIVVSTRFTYRVLSTTGILHYSNSAGPVKGPPPGGPTIQIdWSLNQARSIRTNLTASGPRPN 335
Cdd:PLN02354  261 VGQCFSVLVTANQAPKDYYMVASTRFLKKVLTTTGIIRYEGGKGPASPELPEAPVGWA-WSLNQFRSFRWNLTASAARPN 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 336 PQGSYHYGLINTTKTIILASSAGQVNRKQRYAVNSVSFNPADTPLKLADFFKIG-GVFRVGSISDRPTG--GGIYLDTSV 412
Cdd:PLN02354  340 PQGSYHYGKINITRTIKLVNSASKVDGKLRYALNGVSHVDPETPLKLAEYFGVAdKVFKYDTIKDNPPAkiTKIKIQPNV 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 413 MGADYRAFVEIVFQNNENIVQSWHIDGYSFFVVGMDGGQWTQSSRNQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMWN 492
Cdd:PLN02354  420 LNITFRTFVEIIFENHEKSMQSWHLDGYSFFAVAVEPGTWTPEKRKNYNLLDAVSRHTVQVYPKSWAAILLTFDNAGMWN 499

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 1333122325 493 VRSEFWARQYLGQQFYLRVYTPSTSLRDEFPIPKNALLCGRASG 536
Cdd:PLN02354  500 IRSENWERRYLGQQLYASVLSPERSLRDEYNMPENALLCGKVKG 543
PLN02168 PLN02168
copper ion binding / pectinesterase
 27-535 0e+00

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 618.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  27 PYRFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGVYGTTCPI 106
Cdd:PLN02168   25 PIVSYQWVVSYSQRFILGGNKQVIVINDMFPGPLLNATANDVINVNIFNNLTEPFLMTWNGLQLRKNSWQDGVRGTNCPI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 107 PPGKNFTYILQVKDQIGSFYYFPSLAFHKAAGGFGGIRILSRPRIPVPFPDPDGDYTVLIGDWYKSNHTTLKAHLDRGKK 186
Cdd:PLN02168  105 LPGTNWTYRFQVKDQIGSYFYFPSLLLQKAAGGYGAIRIYNPELVPVPFPKPDEEYDILIGDWFYADHTVMRASLDNGHS 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 187 LPFPNGILINGRG-NDTSFSVEQGKTYRLRISNVGLEHSLNFRIQGHKMKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVT 265
Cdd:PLN02168  185 LPNPDGILFNGRGpEETFFAFEPGKTYRLRISNVGLKTCLNFRIQDHDMLLVETEGTYVQKRVYSSLDIHVGQSYSVLVT 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 266 A-DQPA---QDYYIVVSTRFTYRVLSTTGILHYSNSAGPVKGPPPGGPTIQ-IDWSLNQARSIRTNLTASGPRPNPQGSY 340
Cdd:PLN02168  265 AkTDPVgiyRSYYIVATARFTDAYLGGVALIRYPNSPLDPVGPLPLAPALHdYFSSVEQALSIRMDLNVGAARSNPQGSY 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 341 HYGLINTTKTIILASSAGQVNRKQRYAVNSVSFNPADTPLKLADFFKIGGVFRVGSISDRPTGGGIYLDTSVMGADYRAF 420
Cdd:PLN02168  345 HYGRINVTRTIILHNDVMLSSGKLRYTINGVSFVYPGTPLKLVDHFQLNDTIIPGMFPVYPSNKTPTLGTSVVDIHYKDF 424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 421 VEIVFQNNENIVQSWHIDGYSFFVVGMDGGQWTQSSRNQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMWNVRSEFWAR 500
Cdd:PLN02168  425 YHIVFQNPLFSLESYHIDGYNFFVVGYGFGAWSESKKAGYNLVDAVSRSTVQVYPYSWTAILIAMDNQGMWNVRSQKAEQ 504

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 1333122325 501 QYLGQQFYLRVY-----TPST-SLRDEFPIPKNALLCGRAS 535
Cdd:PLN02168  505 WYLGQELYMRVKgegeeDPSTiPVRDENPIPGNVIRCGKVS 545
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
 24-535 0e+00

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 523.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  24 AENPYRFFTWNVSYGNIYPLA--VRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGVYG 101
Cdd:PLN00044   23 AGDPYAYYDWEVSYVSAAPLGgvKKQEAIGINGQFPGPALNVTTNWNLVVNVRNALDEPLLLTWHGVQQRKSAWQDGVGG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 102 TTCPIPPGKNFTYILQVKDQIGSFYYFPSLAFHKAAGGFGGIRILSRPRIPVPFPDPD-GDYTVLIGDWYKSNHTTLKAH 180
Cdd:PLN00044  103 TNCAIPAGWNWTYQFQVKDQVGSFFYAPSTALHRAAGGYGAITINNRDVIPIPFGFPDgGDITLFIADWYARDHRALRRA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 181 LDRGKKLPFPNGILINGRG----NDT---------SFSVEQGKTYRLRISNVGLEHSLNFRIQGHKMKLVEVEGTHTLQT 247
Cdd:PLN00044  183 LDAGDLLGAPDGVLINAFGpyqyNDSlvppgityeRINVDPGKTYRFRVHNVGVATSLNFRIQGHNLLLVEAEGSYTSQQ 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 248 TYSSLDVHVGQSYSVLVTADQPAQ-DYYIVVSTRF----TYRVLSTTGILHYSNSAGPVKGPPPGGPTIQID--WSLNQA 320
Cdd:PLN00044  263 NYTNLDIHVGQSYSFLLTMDQNAStDYYVVASARFvdaaVVDKLTGVAILHYSNSQGPASGPLPDAPDDQYDtaFSINQA 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 321 RSIRTNLTASGPRPNPQGSYHYGLINTTKTIILASSAGQ-VNRKQRYAVNSVSFNPADTPLKLADFFKIGGVFRVgSISD 399
Cdd:PLN00044  343 RSIRWNVTASGARPNPQGSFHYGDITVTDVYLLQSMAPElIDGKLRATLNEISYIAPSTPLMLAQIFNVPGVFKL-DFPN 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 400 RPTGGGIYLDTSVMGADYRAFVEIVFQNNENIVQSWHIDGYSFFVVGMDGGQWTQSSRNQYNLRDAIARCTIQVYPFSWT 479
Cdd:PLN00044  422 HPMNRLPKLDTSIINGTYKGFMEIIFQNNATNVQSYHLDGYAFFVVGMDYGLWTDNSRGTYNKWDGVARSTIQVFPGAWT 501

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333122325 480 AIYVALDNVGMWNVRSEFWARQYLGQQFYLRVYTPS-TSLRDEFPIPKNALLCGRAS 535
Cdd:PLN00044  502 AILVFLDNAGIWNLRVENLDAWYLGQEVYINVVNPEdNSNKTVLPIPDNAIFCGALS 558
CuRO_2_AAO_like_1 cd13872
The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate ...
 160-294 5.31e-78

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: 241.54  E-value: 5.31e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 160 GDYTVLIGDWYKSNHTTLKAHLDRGKKLPFPNGILINGRG------NDTSFSVEQGKTYRLRISNVGLEHSLNFRIQGHK 233
Cdd:cd13872     1 DEYTVLIGDWYKTDHKTLRQSLDKGRTLGRPDGILINGKGpygygaNETSFTVEPGKTYRLRISNVGLRTSLNFRIQGHK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333122325 234 MKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQPAQDYYIVVSTRFTYRVLSTTGILHY 294
Cdd:cd13872    81 MLLVETEGSYTAQNTYDSLDVHVGQSYSVLVTADQSPKDYYIVASSRFLSPELTGVAILHY 141
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 30-145 3.33e-72

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: 225.75  E-value: 3.33e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  30 FFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGVYGTTCPIPPG 109
Cdd:cd13846     2 FFDWNVSYITASPLGVPQQVIAINGQFPGPTINVTTNDNVVVNVFNSLDEPLLLTWNGIQQRRNSWQDGVLGTNCPIPPG 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1333122325 110 KNFTYILQVKDQIGSFYYFPSLAFHKAAGGFGGIRI 145
Cdd:cd13846    82 WNWTYKFQVKDQIGSFFYFPSLHFQRAAGGFGGIRV 117
CuRO_3_AAO_like_1 cd13894
The third cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 375-496 4.34e-71

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: 223.08  E-value: 4.34e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 375 PADTPLKLADFFKIGGVFRVGSISDRPTGGGIYLDTSVMGADYRAFVEIVFQNNENIVQSWHIDGYSFFVVGMDGGQWTQ 454
Cdd:cd13894     1 NPDTPLKLADYFKIKGVFQLDSIPDPPTRKTPYLGTSVINGTYRGFIEIVFQNNEDTVQSWHLDGYSFFVVGMGFGDWTP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1333122325 455 SSRNQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMWNVRSE 496
Cdd:cd13894    81 EKRKSYNLLDAVSRSTTQVYPGSWTAILLELDNVGMWNVRSQ 122
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 29-491 6.78e-70

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: 233.88  E-value: 6.78e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  29 RFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSL-DEPFLISWNGIQQRRNSYEDGVYGTT-CPI 106
Cdd:TIGR03388   2 RHYKWEVEYEFWSPDCFEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLhTEGVVIHWHGIRQIGTPWADGTAGVTqCAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 107 PPGKNFTYILQVkDQIGSFYYFPSLAFHKAAGGFGGIRILSRPRIPVPFpDPDGDYTVLIGDWY-KSNHTTlKAHLdrgK 185
Cdd:TIGR03388  82 NPGETFIYNFVV-DRPGTYFYHGHYGMQRSAGLYGSLIVDVPDGEKEPF-HYDGEFNLLLSDWWhKSIHEQ-EVGL---S 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 186 KLPF-----PNGILINGRG----------NDTS----------------FSVEQGKTYRLRISNVGLEHSLNFRIQGHKM 234
Cdd:TIGR03388 156 SKPMrwigePQSLLINGRGqfncslaakfSSTNlpqcnlkgneqcapqiLHVEPGKTYRLRIASTTALAALNFAIEGHKL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 235 KLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQ-PAQDYYIVVSTRftYRVLST---TGILHY-SNSAGPVKGPPPGGP 309
Cdd:TIGR03388 236 TVVEADGNYVEPFTVKDIDIYSGETYSVLLTTDQdPSRNYWISVGVR--GRKPNTppgLTVLNYyPNSPSRLPPTPPPVT 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 310 TIQIDWSLNQARSIRTNLTASGPRPNPqgsyhygliNTTKTIILASSAGQVNRKQRYAVNSVSFNPADTP--------LK 381
Cdd:TIGR03388 314 PAWDDFDRSKAFSLAIKAAMGSPKPPE---------TSDRRIVLLNTQNKINGYTKWAINNVSLTLPHTPylgslkynLL 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 382 LA--------DFFKIGGVFRVGSISDRPTGGGIYLdtsvmgADYRAFVEIVFQN----NENI--VQSWHIDGYSFFVVGM 447
Cdd:TIGR03388 385 NAfdqkpppeNYPRDYDIFKPPPNPNTTTGNGIYR------LKFNTTVDVILQNantlNGNNseTHPWHLHGHDFWVLGY 458

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1333122325 448 DGGQWTQS-SRNQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMW 491
Cdd:TIGR03388 459 GEGKFRPGvDEKSYNLKNPPLRNTVVIFPYGWTALRFVADNPGVW 503
PLN02191 PLN02191
L-ascorbate oxidase
 23-491 9.18e-63

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 215.65  E-value: 9.18e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  23 SAENPYRFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLD-EPFLISWNGIQQRRNSYEDGVYG 101
Cdd:PLN02191   18 TASAAVREYTWEVEYKYWWPDCKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLTtEGLVIHWHGIRQKGSPWADGAAG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 102 TT-CPIPPGKNFTYILQVkDQIGSFYYFPSLAFHKAAGGFGGIrILSRPRIPVPFPDPDGDYTVLIGDWYksnHTTLKAH 180
Cdd:PLN02191   98 VTqCAINPGETFTYKFTV-EKPGTHFYHGHYGMQRSAGLYGSL-IVDVAKGPKERLRYDGEFNLLLSDWW---HESIPSQ 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 181 LDRGKKLPF-----PNGILINGRG-----------NDTS----------------FSVEQGKTYRLRISNVGLEHSLNFR 228
Cdd:PLN02191  173 ELGLSSKPMrwigeAQSILINGRGqfncslaaqfsNGTElpmctfkegdqcapqtLRVEPNKTYRIRLASTTALASLNLA 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 229 IQGHKMKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQ-PAQDYYIVVSTRftYRVLSTT---GILHYSNSAGPVKGP 304
Cdd:PLN02191  253 VQGHKLVVVEADGNYITPFTTDDIDIYSGESYSVLLTTDQdPSQNYYISVGVR--GRKPNTTqalTILNYVTAPASKLPS 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 305 PPGGPTIQIDwSLNQARSIRTNLTASGPRPNPQGSYHyglinttKTIILASSAGQVNRKQRYAVNSVSFNPADTPLKLAD 384
Cdd:PLN02191  331 SPPPVTPRWD-DFERSKNFSKKIFSAMGSPSPPKKYR-------KRLILLNTQNLIDGYTKWAINNVSLVTPATPYLGSV 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 385 FFKIGGVFRVGS----------ISDRP------TGGGIYLdtsvmgADYRAFVEIVFQNNENI------VQSWHIDGYSF 442
Cdd:PLN02191  403 KYNLKLGFNRKSpprsyrmdydIMNPPpfpnttTGNGIYV------FPFNVTVDVIIQNANVLkgvvseIHPWHLHGHDF 476

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333122325 443 FVVGMDGGQWTQS-SRNQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMW 491
Cdd:PLN02191  477 WVLGYGDGKFKPGiDEKTYNLKNPPLRNTAILYPYGWTAIRFVTDNPGVW 526
PLN02604 PLN02604
oxidoreductase
 23-498 1.68e-57

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 201.24  E-value: 1.68e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  23 SAENPYRFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSL-DEPFLISWNGIQQRRNSYEDGVYG 101
Cdd:PLN02604   19 AAEARIRRYKWEVKYEYKSPDCFKKLVITINGRSPGPTILAQQGDTVIVELKNSLlTENVAIHWHGIRQIGTPWFDGTEG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 102 TT-CPIPPGKNFTYILQVkDQIGSFYYFPSLAFHKAAGGFGGIRIlSRPR-IPVPFPdPDGDYTVLIGDWYksnHTTLKA 179
Cdd:PLN02604   99 VTqCPILPGETFTYEFVV-DRPGTYLYHAHYGMQREAGLYGSIRV-SLPRgKSEPFS-YDYDRSIILTDWY---HKSTYE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 180 HLDRGKKLPF-----PNGILINGRG-----------------NDT-------SFSVEQGKTYRLRISNVGLEHSLNFRIQ 230
Cdd:PLN02604  173 QALGLSSIPFdwvgePQSLLIQGKGryncslvsspylkagvcNATnpecspyVLTVVPGKTYRLRISSLTALSALSFQIE 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 231 GHKMKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQ-PAQDYYI---VVSTRFTyrVLSTTGIL-HYSNSAGPVKGPP 305
Cdd:PLN02604  253 GHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQdPSRNYWVttsVVSRNNT--TPPGLAIFnYYPNHPRRSPPTV 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 306 PGGPTI--QIDWSLNQARSIRTNltasgprpnpQGSYHYGLINTTKTIILASSAGQVNRKQRYAVNSVSFNPADTPLKLA 383
Cdd:PLN02604  331 PPSGPLwnDVEPRLNQSLAIKAR----------HGYIHPPPLTSDRVIVLLNTQNEVNGYRRWSVNNVSFNLPHTPYLIA 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 384 DFFKIGGVF-----------RVGSISDRPTGGGIYLDTSVMGADYRAFVEIVFQN------NENIVQSWHIDGYSFFVVG 446
Cdd:PLN02604  401 LKENLTGAFdqtpppegydfANYDIYAKPNNSNATSSDSIYRLQFNSTVDIILQNantmnaNNSETHPWHLHGHDFWVLG 480

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333122325 447 MDGGQWTQSSR-NQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMW----NVRSEFW 498
Cdd:PLN02604  481 YGEGKFNMSSDpKKYNLVDPIMKNTVPVHPYGWTALRFRADNPGVWafhcHIESHFF 537
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 29-491 1.79e-54

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: 192.26  E-value: 1.79e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  29 RFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDG-VYGTTCPIP 107
Cdd:TIGR03389   4 RHYTFDVQEKNVTRLCSTKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQYNVTIHWHGVRQLRNGWADGpAYITQCPIQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 108 PGKNFTYILQVKDQIGSFYYFPSLAFHKAAGgFGGIRILSRPRIPVPFPDPDGDYTVLIGDWYKSN-HTTLKAHLDRGKK 186
Cdd:TIGR03389  84 PGQSYVYNFTITGQRGTLWWHAHISWLRATV-YGAIVILPKPGVPYPFPKPDREVPIILGEWWNADvEAVINQANQTGGA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 187 LPFPNGILINGRGNDTS---------FSVEQGKTYRLRISNVGLEHSLNFRIQGHKMKLVEVEGTHTLQTTYSSLDVHVG 257
Cdd:TIGR03389 163 PNVSDAYTINGHPGPLYncsskdtfkLTVEPGKTYLLRIINAALNDELFFAIANHTLTVVEVDATYTKPFKTKTIVIGPG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 258 QSYSVLVTADQPAQDYYIVV----STRFTYRVLSTTGILHYSNSAGPVKGPPPGGPTIQ-IDWSLNQARSIRTNLTASGP 332
Cdd:TIGR03389 243 QTTNVLLTADQSPGRYFMAArpymDAPGAFDNTTTTAILQYKGTSNSAKPILPTLPAYNdTAAATNFSNKLRSLNSAQYP 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 333 RPNPQGSYHygliNTTKTIILASSAGQVNRKQ-----RYA--VNSVSFNPADTPLKLADFFKIGGVFRVgSISDRP---- 401
Cdd:TIGR03389 323 ANVPVTIDR----RLFFTIGLGLDPCPNNTCQgpngtRFAasMNNISFVMPTTALLQAHYFGISGVFTT-DFPANPptkf 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 402 --TGGGIYLDTSVMGA------DYRAFVEIVFQNNeNIVQS----WHIDGYSFFVVGMDGGQW-TQSSRNQYNLRDAIAR 468
Cdd:TIGR03389 398 nyTGTNLPNNLFTTNGtkvvrlKFNSTVELVLQDT-SILGSenhpIHLHGYNFFVVGTGFGNFdPKKDPAKFNLVDPPER 476

                         490       500
                  ....*....|....*....|...
gi 1333122325 469 CTIQVYPFSWTAIYVALDNVGMW 491
Cdd:TIGR03389 477 NTVGVPTGGWAAIRFVADNPGVW 499
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 160-297 2.22e-49

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: 167.11  E-value: 2.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 160 GDYTVLIGDWYKSNHTTLKAHLDRGKKLPF-----PNGILINGRGND--TSFSVEQGKTYRLRISNVGLEHSLNFRIQGH 232
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKELLASGKAPTdfppvPDAVLINGKDGAslATLTVTPGKTYRLRIINVALDDSLNFSIEGH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333122325 233 KMKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQPAQDYYIVVSTRFT-YRVLSTTGILHYSNS 297
Cdd:pfam00394  81 KMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQDPGNYWIVASPNIPaFDNGTAAAILRYSGA 146
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 34-149 4.38e-49

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: 165.11  E-value: 4.38e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  34 NVSYGNIYPLA-VRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGV-YGTTCPIPPGKN 111
Cdd:pfam07732   1 TVTYGTVSPLGgTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVpGVTQCPIPPGQS 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1333122325 112 FTYILQVKDQIGSFYYFPSLAFHKAAGGFGGIRILSRP 149
Cdd:pfam07732  81 FTYRFQVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDRA 118
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 377-517 5.24e-35

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


Pssm-ID: 462246 [Multi-domain]  Cd Length: 138  Bit Score: 128.32  E-value: 5.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 377 DTPLKLADFFKI-GGVFRVGsisDRPTGGGIY-LDTSVMGADYRAFVEIVFQNNENIVQSWHIDGYSFFVVGMDGGQWTQ 454
Cdd:pfam07731   1 DTPPKLPTLLQItSGNFRRN---DWAINGLLFpPNTNVITLPYGTVVEWVLQNTTTGVHPFHLHGHSFQVLGRGGGPWPE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333122325 455 SSRNQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMWNVRSEFWarQYLGQQFYLRVYTPSTS 517
Cdd:pfam07731  78 EDPKTYNLVDPVRRDTVQVPPGGWVAIRFRADNPGVWLFHCHIL--WHLDQGMMGQFVVRPGD 138
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 162-294 3.86e-28

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: 109.76  E-value: 3.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 162 YTVLIGDWYKSNHTTLKAHLDR--GKKLPFPNGILINGRG--NDTS-----------FSVEQGKTYRLRISNVGLEHSLN 226
Cdd:cd04205     1 RVLLLSDWYHDSAEDVLAGYMPnsFGNEPVPDSLLINGRGrfNCSMavcnsgcplpvITVEPGKTYRLRLINAGSFASFN 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333122325 227 FRIQGHKMKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQPAQDYYIVVSTRFT----YRVLSTTGILHY 294
Cdd:cd04205    81 FAIDGHNMTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKADQPPGNYWIRASADGRtfdeGGNPNGTAILRY 152
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 29-143 4.08e-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: 105.83  E-value: 4.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  29 RFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLD-EPFLISWNGIQQRRNSYEDGV-YGTTCPI 106
Cdd:cd04206     1 REYELTITETTVNPDGVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNLPnEPTSIHWHGLRQPGTNDGDGVaGLTQCPI 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1333122325 107 PPGKNFTYILQVKDQIGSFYYFPSLAFHKAAGGFGGI 143
Cdd:cd04206    81 PPGESFTYRFTVDDQAGTFWYHSHVGGQRADGLYGPL 117
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 29-145 8.59e-27

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: 104.65  E-value: 8.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  29 RFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGVYGTT-CPIP 107
Cdd:cd13857     1 REYNFTISEITGAPDGFVRPMLVINGQFPGPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTNWMDGTAGITqCPIP 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1333122325 108 PGKNFTYILQVKDQIGSFYYFPSLAFHKAAGGFGGIRI 145
Cdd:cd13857    81 PGGSFTYNFTVDGQYGTYWYHSHYSTQYADGLVGPLIV 118
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 35-506 5.25e-25

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


Pssm-ID: 132431 [Multi-domain]  Cd Length: 538  Bit Score: 108.78  E-value: 5.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  35 VSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSL-DEPFLISWNGIQQRRNSYEDGV-YGTTCPIPPGKNF 112
Cdd:TIGR03390  15 VTSDNIKIACSSRYSVVVNGTSPGPEIRLQEGQTTWIRVYNDIpDNNVTMHWHGLTQRTAPFSDGTpLASQWPIPPGHFF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 113 TYILQVK-DQIGSFYYFPSLAFhKAAGGFGGIRILSRPRIPVPFpdpDGDYTVLIGDWYKSNHTTLKAHLdrgKKLPF-- 189
Cdd:TIGR03390  95 DYEIKPEpGDAGSYFYHSHVGF-QAVTAFGPLIVEDCEPPPYKY---DDERILLVSDFFSATDEEIEQGL---LSTPFtw 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 190 ---PNGILINGRGNDTSF---------------SVEQGKTYRLR-ISNVGLEHsLNFRIQGHK-MKLVEVEGTHTLQTTY 249
Cdd:TIGR03390 168 sgeTEAVLLNGKSGNKSFyaqinpsgscmlpviDVEPGKTYRLRfIGATALSL-ISLGIEDHEnLTIIEADGSYTKPAKI 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 250 SSLDVHVGQSYSVLVTADQPA-------QDYYIVVSTRFTYRVLSTTGILHYSNSAGPVKGPPPGGPTIQI-----DWSL 317
Cdd:TIGR03390 247 DHLQLGGGQRYSVLFKAKTEDelcggdkRQYFIQFETRDRPKVYRGYAVLRYRSDKASKLPSVPETPPLPLpnstyDWLE 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 318 NQARSIRTNLTASGPRpnpqgsyhygLINTTKTIILASS--AGQVNRKQRYAVNSVSFNPA--DTPLkLADFFKiGGVFR 393
Cdd:TIGR03390 327 YELEPLSEENNQDFPT----------LDEVTRRVVIDAHqnVDPLNGRVAWLQNGLSWTESvrQTPY-LVDIYE-NGLPA 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 394 VGSISDRPTGGGIYLDTSVMGADYRAFVEIVFQNNENIVQS--------WHIDGYSFFVVGMDGGQWtQSSRNQYNLRD- 464
Cdd:TIGR03390 395 TPNYTAALANYGFDPETRAFPAKVGEVLEIVWQNTGSYTGPnggvdthpFHAHGRHFYDIGGGDGEY-NATANEAKLENy 473

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333122325 465 -AIARCTIQVY----------PFSWTAIYVALDNVGMWNVRSEFWARQYLGQQ 506
Cdd:TIGR03390 474 tPVLRDTTMLYryavkvvpgaPAGWRAWRIRVTNPGVWMMHCHILQHMVMGMQ 526
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 159-280 7.57e-25

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: 101.08  E-value: 7.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 159 DGDYTVLIGDWYksnHTTLKAHLDRGKKLPF-----PNGILINGRG---------NDTS-----------------FSVE 207
Cdd:cd13871     1 DGELNILLSDWW---HKSIYEQETGLSSKPFrwvgePQSLLIEGRGryncslapaYPSSlpspvcnksnpqcapfiLHVS 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333122325 208 QGKTYRLRISNVGLEHSLNFRIQGHKMKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQ-PAQDYYIVVSTR 280
Cdd:cd13871    78 PGKTYRLRIASVTALSSLNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTADQdPSRNYWVSVNVR 151
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 161-278 3.02e-23

The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259945 [Multi-domain]  Cd Length: 148  Bit Score: 95.70  E-value: 3.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 161 DYTVLIGDWYKSNHTTL-KAHLDR---GKKLPFPNGILINGRGNDTsFSVEQGKTYRLRISNVGLEHSLNFRIQGHKMKL 236
Cdd:cd13877     2 EVTLTLSDWYHDQSPDLlRDFLSPynpTGAEPIPDSSLFNDTQNAT-INFEPGKTYLLRIINMGAFASQYFHIEGHDMTI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1333122325 237 VEVEGTHTLQTTYSSLDVHVGQSYSVLVTA-DQPAQDYYIVVS 278
Cdd:cd13877    81 IEVDGVYVKPYPVDTLYIAVGQRYSVLVKAkNDTDRNYAIING 123
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 52-278 3.13e-23

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: 102.32  E-value: 3.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  52 INGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIqqrRNSYE-DGVYGTtcPIPPGKNFTYILQVKDQIGSFYYFP- 129
Cdd:COG2132    38 YNGQYPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGL---RVPNAmDGVPGD--PIAPGETFTYEFPVPQPAGTYWYHPh 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 130 ---SLAFHKAAGGFGGIRIlsRPRIPvPFPDPDGDYTVLIGDW-YKSNHTTLKAHlDRGKKLPFPNGILINGRGNDTsFS 205
Cdd:COG2132   113 thgSTAEQVYRGLAGALIV--EDPEE-DLPRYDRDIPLVLQDWrLDDDGQLLYPM-DAAMGGRLGDTLLVNGRPNPT-LE 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333122325 206 VEQGKTYRLRISNVGLEHSLNFRIQ-GHKMKLVEVEGtHTLQT--TYSSLDVHVGQSYSVLVTADQPAQDYYIVVS 278
Cdd:COG2132   188 VRPGERVRLRLLNASNARIYRLALSdGRPFTVIATDG-GLLPApvEVDELLLAPGERADVLVDFSADPGEEVTLAN 262
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 26-145 5.72e-23

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: 94.23  E-value: 5.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  26 NPYRFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSL-DEPFLISWNGIQQRRNSYEDGVYGTT- 103
Cdd:cd13854     1 GVTRKYTLTITNSTLAPDGVEKEVMLINGQYPGPLIEANWGDTIEVTVINKLqDNGTSIHWHGIRQLNTNWQDGVPGVTe 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1333122325 104 CPIPPGKNFTYILQVkDQIGSFYYFPSLAFHKAAGGFGGIRI 145
Cdd:cd13854    81 CPIAPGDTRTYRFRA-TQYGTSWYHSHYSAQYGDGVVGPIVI 121
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 31-127 6.93e-22

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: 91.24  E-value: 6.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  31 FTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFL-----ISWNGIQQRRNSYEDGV-YGTTC 104
Cdd:cd13856     3 YTLNIVNTRLAPDGFERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTMrrstsIHWHGIFQHGTNYADGPaFVTQC 82

                          90       100
                  ....*....|....*....|...
gi 1333122325 105 PIPPGKNFTYILQVKDQIGSFYY 127
Cdd:cd13856    83 PIAPNHSFTYDFTAGDQAGTFWY 105
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 163-275 1.50e-21

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: 91.32  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 163 TVL-IGDWYksnHTTLKAHLDRGKK-LPFPNGILINGRG----NDTS----FSVEQGKTYRLRISNVGLEHSLNFRIQGH 232
Cdd:cd13882     1 TVItLGDWY---HTAAPDLLATTAGvPPVPDSGTINGKGrfdgGPTSplavINVKRGKRYRFRVINISCIPSFTFSIDGH 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1333122325 233 KMKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQPAQDYYI 275
Cdd:cd13882    78 NLTVIEADGVETKPLTVDSVQIYAGQRYSVVVEANQPVDNYWI 120
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 31-127 4.80e-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: 88.51  E-value: 4.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  31 FTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGVYGTT-CPIPPG 109
Cdd:cd13850     1 FTLTVTEGSPDGDGGEREVILINGQFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTPWSDGVPGVTqWPIQPG 80

                          90
                  ....*....|....*...
gi 1333122325 110 KNFTYILQVKDQIGSFYY 127
Cdd:cd13850    81 GSFTYRWKAEDQYGLYWY 98
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 162-295 7.61e-21

The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs 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: 89.64  E-value: 7.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 162 YTVLIGDWYksnHTTLKAHLDR------GKKLPFPNGILING------------------RGNDTSFSVEQGKTYRLRIS 217
Cdd:cd13886     1 VVVMVNDYY---HDPSSVLLARylapgnEGDEPVPDNGLINGigqfdcasatykiyccasNGTYYNFTLEPNKTYRLRLI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 218 NVGLEHSLNFRIQGHKMKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQPAQD-YYI---VVSTRFTY--RVLSTT-- 289
Cdd:cd13886    78 NAGSFADFTFSVDGHPLTVIEADGTLVEPVEVHSITISVAQRYSVILTTNQPTGGnFWMraeLNTDCFTYdnPNLDPDvr 157


                  ....*.
gi 1333122325 290 GILHYS 295
Cdd:cd13886   158 AIVSYT 163
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 29-143 1.32e-20

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: 87.50  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  29 RFFTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSL-DEPFLISWNGIQQRRNSYEDGV-YGTTCPI 106
Cdd:cd13845     1 RHYKWKVEYMFWAPDCVEKLVIGINGQFPGPTIRATAGDTIVVELENKLpTEGVAIHWHGIRQRGTPWADGTaSVSQCPI 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1333122325 107 PPGKNFTYILQVkDQIGSFYYFPSLAFHKAAGGFGGI 143
Cdd:cd13845    81 NPGETFTYQFVV-DRPGTYFYHGHYGMQRSAGLYGSL 116
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 31-127 5.47e-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: 85.78  E-value: 5.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  31 FTWNVSYGNIYP--LAVRQQgILINGQFPGPDIHCVTNDNLIINVFNSL-DEPFLISWNGIQQRRNSYEDGVYGTT-CPI 106
Cdd:cd13851     3 FDWNITWVTANPdgLFERRV-IGINGQWPPPPIEVNKGDTVVIHATNSLgDQPTSLHFHGLFQNGTNYMDGPVGVTqCPI 81

                          90       100
                  ....*....|....*....|.
gi 1333122325 107 PPGKNFTYILQVKDQIGSFYY 127
Cdd:cd13851    82 PPGQSFTYEFTVDTQVGTYWY 102
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 50-143 1.05e-19

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: 84.13  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  50 ILINGQFPGPDIHCVTNDNLIINVFNSLD-EPFLISWNGIQQRRNSYEDGV-YGTTCPIPPGKNFTYILQVkDQIGSFYY 127
Cdd:cd13858     8 ITVNGQLPGPSIEVCEGDTVVVDVKNRLPgESTTIHWHGIHQRGTPYMDGVpMVTQCPILPGQTFRYKFKA-DPAGTHWY 86

                          90
                  ....*....|....*.
gi 1333122325 128 FPSLAFHKAAGGFGGI 143
Cdd:cd13858    87 HSHSGTQRADGLFGAL 102
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 31-129 1.40e-18

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: 81.54  E-value: 1.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  31 FTWNVSYGNIYPLAVRQQGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGV-YGTTCPIPPG 109
Cdd:cd13849     1 YTFVVQEKNVTRLCSTKSILTVNGQFPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLRSGWADGPaYITQCPIQPG 80

                          90       100
                  ....*....|....*....|
gi 1333122325 110 KNFTYILQVKDQIGSFYYFP 129
Cdd:cd13849    81 QSYTYRFTVTGQEGTLWWHA 100
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
 163-294 4.40e-18

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: 81.11  E-value: 4.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 163 TVLIGDWYKSNHTTLKAH-LDRGKKLPFPNGILINGR--------GNDT-SFSVEQGKTYRLRISNVGLEHSLNFRIQGH 232
Cdd:cd13875     2 PIILGEWWNRDVNDVEDQaLLTGGGPNISDAYTINGQpgdlyncsSKDTfVLTVEPGKTYLLRIINAALNEELFFKIANH 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333122325 233 KMKLVEVEGTHT--LQTTYssLDVHVGQSYSVLVTADQPAQDYYIVVStrfTYRVLS--------TTGILHY 294
Cdd:cd13875    82 TLTVVAVDASYTkpFTTDY--ILIAPGQTTDVLLTADQPPGRYYMAAR---PYQSAPpvpfdnttATAILEY 148
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
 161-294 7.94e-17

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: 77.66  E-value: 7.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 161 DYTVLIGDWYKSNHTTLKAHLDRGKKLPFPNGILINGRGN-------------DTSFSVEQGKTYRLRISNVG-LEHSLN 226
Cdd:cd13884     1 EHVILIQDWTHELSSERFVGRGHNGGGQPPDSILINGKGRyydpktgntnntpLEVFTVEQGKRYRFRLINAGaTNCPFR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 227 FRIQGHKMKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQPAQDYYIVVST--RFTYRVLSTTGILHY 294
Cdd:cd13884    81 VSIDGHTLTVIASDGNDVEPVEVDSIIIYPGERYDFVLNANQPIGNYWIRARGleDCDNRRLQQLAILRY 150
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 163-298 5.22e-15

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: 72.67  E-value: 5.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 163 TVLIGDWYKSNHTTLKAHLDRGKKLPFPNGILINGRGN-DTS--------FSVEQGKTYRLRISNVGLEHSLNFRIQGHK 233
Cdd:cd13880     3 PVLLTDWYHRSAFELFSEELPTGGPPPMDNILINGKGKfPCStgagsyfeTTFTPGKKYRLRLINTGVDTTFRFSIDGHN 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333122325 234 MK-----LVEVEGTHTlqttySSLDVHVGQSYSVLVTADQ-PAQDYYIVV-----STRFTYRVLSTTGILHYSNSA 298
Cdd:cd13880    83 LTviaadFVPIVPYTT-----DSLNIGIGQRYDVIVEANQdPVGNYWIRAepatgCSGTNNNPDNRTGILRYDGAS 153
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 375-491 3.91e-14

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: 69.41  E-value: 3.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 375 PADTPLKLADFFKIGGVFRVgSISDRPTGGGiYLDTSVMGADYRAFVEIVFQNNEN--IVQSWHIDGYSFFVVGMDGGQW 452
Cdd:cd04207     1 DRTRRLVLSQTGAPDGTTRW-VINGMPFKEG-DANTDIFSVEAGDVVEIVLINAGNhdMQHPFHLHGHSFWVLGSGGGPF 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1333122325 453 TQssrnQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMW 491
Cdd:cd04207    79 DA----PLNLTNPPWRDTVLVPPGGWVVIRFKADNPGVW 113
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 164-294 2.10e-13

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: 67.23  E-value: 2.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 164 VLIGDWYKSNHT-TLKAHLDRGKKLPFPNGILINGRGNDT--SFSVEQGKTYR-LRISNVGLEHSLNFRIQGHKMKLVEV 239
Cdd:cd13876     3 IILSDWRHLTSEeYWKIMRASGIEPFCYDSILINGKGRVYclIVIVDPGERWVsLNFINAGGFHTLAFSIDEHPMWVYAV 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333122325 240 EGTHTLQTTYSSLDVHVGQSYSVLVTADQPAQDYYI-VVSTRFTyRVLSTTGILHY 294
Cdd:cd13876    83 DGGYIEPQLVDAISITNGERYSVLVKLDKPPGDYTIrVASTGAP-QVISGYAILRY 137
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 48-145 2.62e-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: 66.54  E-value: 2.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  48 QGILINGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNsyEDGVYG-TTCPIPPGKNFTYILQVKdQIGSFY 126
Cdd:cd13848    20 EAITVNGQVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPND--MDGVPGlSFPGIKPGETFTYRFPVR-QSGTYW 96

                          90
                  ....*....|....*....
gi 1333122325 127 YFPSLAFHKAAGGFGGIRI 145
Cdd:cd13848    97 YHSHSGLQEQTGLYGPIII 115
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 164-270 2.63e-13

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: 67.75  E-value: 2.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 164 VLIGDWYKSNHTTLKAHLD-----RGKKL-PFPNGILINGRG-------------NDTS---FSVEQGKTYRLRISNVGL 221
Cdd:cd13883     3 LFISDWYHDQSEVIVAGLLspqgyKGSPAaPSPDSALINGIGqfncsaadpgtccTQTSppeIQVEAGKRTRFRLINAGS 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333122325 222 EHSLNFRIQGHKMKLVEVEGTHTLQTTY-SSLDVHVGQSYSVLVTADQPA 270
Cdd:cd13883    83 HAMFRFSVDNHTLNVVEADDTPVYGPTVvHRIPIHNGQRYSVIIDTTSGK 132
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 53-127 4.95e-13

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: 65.96  E-value: 4.95e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333122325  53 NGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNSYEDGVYGTTC-PIPPGKNFTYILQVkDQIGSFYY 127
Cdd:cd13859    26 NGQVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGSWKMDGVPGVTQpAIEPGESFTYKFKA-ERPGTLWY 100
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 348-508 4.98e-13

The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259960 [Multi-domain]  Cd Length: 155  Bit Score: 66.67  E-value: 4.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 348 TKTIILASSAGQVNRKQRYAVNSVSFNPADTPlKLADFfkiggvfrvgsisdrptggGIYldTSVMGAdyraFVEIVFQN 427
Cdd:cd13893     2 TRTLLLLNTQNLINGQLRWAINNVSYVPPPTP-YLAAL-------------------PVY--PFKGGD----VVDVILQN 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 428 NENIVQS------WHIDGYSFFVVGMDGGQWTQSSR-NQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMWNVRSEFWAR 500
Cdd:cd13893    56 ANTNTRNaseqhpWHLHGHDFWVLGYGLGGFDPAADpSSLNLVNPPMRNTVTIFPYGWTALRFKADNPGVWAFHCHIEWH 135


                  ....*...
gi 1333122325 501 QYLGQQFY 508
Cdd:cd13893   136 FHMGMGVV 143
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
 160-294 5.67e-13

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: 66.93  E-value: 5.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 160 GDYTVLIGDWYKSNHTTLKAHLdrgKKLPF-----PNGILINGRGNDTSFS----------------VEQGKTYRLR-IS 217
Cdd:cd13873     1 EERILLFSDYFPKTDSTIETGL---TATPFvwpgePNALLVNGKSGGTCNKsategcttschppvidVEPGKTYRFRfIG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 218 NVGLEHsLNFRIQGH-KMKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQPAQ-------DYYIVVSTRFTYRVLSTT 289
Cdd:cd13873    78 ATALSF-VSLGIEGHdNLTIIEADGSYTKPAETDHLQLGSGQRYSFLLKTKSLEElaalnktTFWIQIETRWRPTNDTGY 156


                  ....*
gi 1333122325 290 GILHY 294
Cdd:cd13873   157 AVLRY 161
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 53-129 6.25e-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: 59.56  E-value: 6.25e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333122325  53 NGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIqqR-RNSYeDGVYGTT-CPIPPGKNFTYILQVKDQiGSFYYFP 129
Cdd:cd13861    26 NGQVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGL--RlPNAM-DGVPGLTqPPVPPGESFTYEFTPPDA-GTYWYHP 100
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 410-491 7.01e-11

The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Plants usually express multiple laccase genes, but their precise physiological/biochemical roles remain largely unclear. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259964 [Multi-domain]  Cd Length: 139  Bit Score: 60.35  E-value: 7.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 410 TSVMGADYRAFVEIVFQNNeNIVQS----WHIDGYSFFVVGMDGGQWTQS-SRNQYNLRDAIARCTIQVYPFSWTAIYVA 484
Cdd:cd13897    31 TKVKVLEYGSTVEIVLQGT-SLLAAenhpMHLHGFDFYVVGRGFGNFDPStDPATFNLVDPPLRNTVGVPRGGWAAIRFV 109


                  ....*..
gi 1333122325 485 LDNVGMW 491
Cdd:cd13897   110 ADNPGVW 116
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 53-127 4.60e-10

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: 57.21  E-value: 4.60e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333122325  53 NGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQrRNSYeDGVYGTT-CPIPPGKNFTYILQVKdQIGSFYY 127
Cdd:cd13860    26 NGSVPGPTIEVTEGDRVRILVTNELPEPTTVHWHGLPV-PNGM-DGVPGITqPPIQPGETFTYEFTAK-QAGTYMY 98
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 32-140 8.14e-09

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: 53.69  E-value: 8.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  32 TWNVSYGNIYPLAVRQQgILINGQFPGPDIHCVTNDNLIINVFNSLDEPFL-ISWNGIQQRRNSYEDGVYGTT-CPIPPG 109
Cdd:cd13847     1 PDATLRVSCDPFGPRPS-TLINGSFPGPELRVQEGQHLWVRVYNDLEAGNTtMHFHGLSQYMSPFSDGTPLASqWPIPPG 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1333122325 110 KNFTYILQV-KDQIGSFYYFPSLAFH--KAAGGF 140
Cdd:cd13847    80 KFFDYEFPLeAGDAGTYYYHSHVGFQsvTAYGAL 113
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 368-491 1.31e-08

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


Pssm-ID: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 54.22  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 368 VNSVSFNPAD---TPLKLADFFKIGGVFRVGSISDRPTGGGIYLDTSVmgadyRAFVEIVFQNNENIVQSWHIDGYSFFV 444
Cdd:cd13910    20 FNGTSWRPLPgpaTLLLALDADNAEEVAAGNGLSTFDGNQLVITVDDI-----DKVVDLVINNLDDGDHPFHLHGHKFWV 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333122325 445 VGM-----DGGQWTQSSRNQYNLRDAIARCTIQVYPFSWTAIYVALDNVGMW 491
Cdd:cd13910    95 LGSgdgryGGGGYTAPDGTSLNTTNPLRRDTVSVPGFGWAVLRFVADNPGLW 146
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 53-145 8.53e-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: 50.73  E-value: 8.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  53 NGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIqqrRNSYEDGVYGTtcPIPPGKNFTYILqVKDQIGSFYY---FP 129
Cdd:cd11024    27 NGTVPGPTLRATEGDLVRIHFINTGDHPHTIHFHGI---HDAAMDGTGLG--PIMPGESFTYEF-VAEPAGTHLYhchVQ 100

                          90
                  ....*....|....*.
gi 1333122325 130 SLAFHKAAGGFGGIRI 145
Cdd:cd11024   101 PLKEHIAMGLYGAFIV 116
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 53-143 5.53e-06

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: 45.54  E-value: 5.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  53 NGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGI----QQRRNSYEdgvygttcPIPPGKNFTYILQV-KDQIGSFYY 127
Cdd:cd13855    27 NGSVPGPLIEVFEGDTVEITFRNRLPEPTTVHWHGLpvppDQDGNPHD--------PVAPGNDRVYRFTLpQDSAGTYWY 98

                          90
                  ....*....|....*.
gi 1333122325 128 FPSLAFHKAAGGFGGI 143
Cdd:cd13855    99 HPHPHGHTAEQVYRGL 114
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
 194-268 7.01e-06

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: 45.40  E-value: 7.01e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333122325 194 LINGR--GNDTSFSVEQGKTYRLRISNVGLEHSLNFRIQGHKMKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVTADQ 268
Cdd:cd13870    19 LINGRppEDPAVFTARPGDRLRLRLINAAGDTAFRVALAGHRLTVTHTDGFPVEPVEVDALLIGMGERYDAIVTANN 95
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 159-269 1.03e-05

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: 45.32  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 159 DGDYTVLIGDWyksnhTTLKAHLDRGKKLPFPNGILINGRG--NDTSFSVEQGKTYRLRISNVGLE-HSLNfrIQGHKMK 235
Cdd:cd04202     1 DRDYTLVLQEW-----FVDPGTTPMPPEGMDFNYFTINGKSfpATPPLVVKEGDRVRIRLINLSMDhHPMH--LHGHFFL 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1333122325 236 LVEVEGtHTLQTTYS----SLDVHVGQSYSVLVTADQP 269
Cdd:cd04202    74 VTATDG-GPIPGSAPwpkdTLNVAPGERYDIEFVADNP 110
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 49-124 1.13e-04

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 43.23  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325  49 GILingqfpGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQRRNS----YEDGVYGTTCPIPPGKNFTYILQVKDQIGS 124
Cdd:cd04224    79 GIL------GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYegamYRDGDPSPGSHVSPGETFTYEWTVPEGVGP 152
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 52-129 1.78e-03

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: 38.32  E-value: 1.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333122325  52 INGQFPGPDIHCVTNDNLIINVFNSLDEPFLISWNGIQQrrNSYEDGvyGTTCPIPPGKNFTYILQVKDQIGSFYYFP 129
Cdd:cd04232    25 YNGSYLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHV--PGEMDG--GPHQPIAPGQTWSPTFTIDQPAATLWYHP 98
CuRO_2_CopA cd13874
The second cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 193-265 2.39e-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: 38.04  E-value: 2.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333122325 193 ILINGRG---NDTSfSVEQGKTYRLRISNVGLEHSLNFRIQGHKMKLVEVEGTHTLQTTYSSLDVHVGQSYSVLVT 265
Cdd:cd13874    14 YLINGKPpedNWTG-LFKPGERVRLRFINAAASTYFDVRIPGGKMTVVAADGQDVRPVEVDEFRIGVAETYDVIVT 88
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 410-515 3.36e-03

The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; This multicopper oxidase (MCO) family includes the majority of insect laccases. One member of the family is laccase 2 from Tribolium castaneum. Laccase 2 is required for beetle cuticle tanning. Laccase (polyphenol oxidase EC 1.10.3.2) is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic - notably phenolic and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi, plants and insects. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259972 [Multi-domain]  Cd Length: 174  Bit Score: 38.81  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333122325 410 TSVMGADYRAFVEIVFQNNENIVQS---WHIDGYSFFVVGM-------DGGQWTQSSRNQY----------NLRDAIARC 469
Cdd:cd13905    44 THVIKLPLNSVVEIVLINEGPGPGLshpFHLHGHSFYVLGMgfpgynsTTGEILSQNWNNKlldrgglpgrNLVNPPLKD 123

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1333122325 470 TIQVYPFSWTAIYVALDNVGMWNVRS--EFWARQylGQQFYLRVYTPS 515
Cdd:cd13905   124 TVVVPNGGYVVIRFRADNPGYWLLHChiEFHLLE--GMALVLKVGEPS 169
 
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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