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Conserved domains on  [gi|6323703|ref|NP_013774|]
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ferroxidase FET3 [Saccharomyces cerevisiae S288C]

Protein Classification

multicopper oxidase( domain architecture ID 10195112)

multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water,and which contains three cupredoxin domains that include one mononuclear and one trinuclear copper center; similar to Phanerodontia chrysosporium Fet3 protein which may as a component of a high-affinity iron-uptake protein complex (Fet3/Ftr1) be involved in iron uptake, and to Lentinula edodes uncharacterized laccase 10 (Lcc10)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 336-489 8.42e-79

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


:

Pssm-ID: 259966 [Multi-domain]  Cd Length: 160  Bit Score: 246.78  E-value: 8.42e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  336 DHVITVDVVMDNLKNGVNYAFFNNITYTAPKVPTLMTVLSSGDQANNSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPF 415
Cdd:cd13899   1 DHSITLNVDFDTFDDGVNRAAFNNITYVSPKVPTLYTALSMGDDALDPAIYGPQTNAFVLNHGEVVELVVNNWDAGKHPF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323703  416 HLHGHAFQTIQRDRTYDDAlgevphsFDPDNHPAFPEYPMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13899  81 HLHGHKFQVVQRSPDVASD-------DPNPPINEFPENPMRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWH 147
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 154-301 1.23e-74

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: 235.52  E-value: 1.23e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  154 EELSLSLSEWYHDLVTDLTKSFMSVYNPTGAEPIPQNLIVNNTMNLTWEVQPDTTYLLRIVNVGGFVSQYFWIEDHEMTV 233
Cdd:cd13877   1 EEVTLTLSDWYHDQSPDLLRDFLSPYNPTGAEPIPDSSLFNDTQNATINFEPGKTYLLRIINMGAFASQYFHIEGHDMTI 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323703  234 VEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNFAIMQKFDDTMLDVIPSDLQLNATSYMVYNK 301
Cdd:cd13877  81 IEVDGVYVKPYPVDTLYIAVGQRYSVLVKAKNDTDRNYAIINGMDKDMLDTVPDDLYLNKTNWLVYDS 148
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 24-144 8.17e-70

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: 222.14  E-value: 8.17e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   24 HTFNWTTGWDYRNVDGLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQNGTASMDGVPFLTQCP 103
Cdd:cd13851   1 VEFDWNITWVTANPDGLFERRVIGINGQWPPPPIEVNKGDTVVIHATNSLGDQPTSLHFHGLFQNGTNYMDGPVGVTQCP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6323703  104 IAPGSTMLYNFTVDYNVGTYWYHSHTDGQYEDGMKGLFIIK 144
Cdd:cd13851  81 IPPGQSFTYEFTVDTQVGTYWYHSHDGGQYPDGLRGPFIIH 121
 
Name Accession Description Interval E-value
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 336-489 8.42e-79

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


Pssm-ID: 259966 [Multi-domain]  Cd Length: 160  Bit Score: 246.78  E-value: 8.42e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  336 DHVITVDVVMDNLKNGVNYAFFNNITYTAPKVPTLMTVLSSGDQANNSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPF 415
Cdd:cd13899   1 DHSITLNVDFDTFDDGVNRAAFNNITYVSPKVPTLYTALSMGDDALDPAIYGPQTNAFVLNHGEVVELVVNNWDAGKHPF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323703  416 HLHGHAFQTIQRDRTYDDAlgevphsFDPDNHPAFPEYPMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13899  81 HLHGHKFQVVQRSPDVASD-------DPNPPINEFPENPMRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWH 147
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 154-301 1.23e-74

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: 235.52  E-value: 1.23e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  154 EELSLSLSEWYHDLVTDLTKSFMSVYNPTGAEPIPQNLIVNNTMNLTWEVQPDTTYLLRIVNVGGFVSQYFWIEDHEMTV 233
Cdd:cd13877   1 EEVTLTLSDWYHDQSPDLLRDFLSPYNPTGAEPIPDSSLFNDTQNATINFEPGKTYLLRIINMGAFASQYFHIEGHDMTI 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323703  234 VEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNFAIMQKFDDTMLDVIPSDLQLNATSYMVYNK 301
Cdd:cd13877  81 IEVDGVYVKPYPVDTLYIAVGQRYSVLVKAKNDTDRNYAIINGMDKDMLDTVPDDLYLNKTNWLVYDS 148
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 26-489 6.82e-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: 236.19  E-value: 6.82e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703     26 FNWTTGWDYRNVDGlKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQNGTASMDGVPFLTQCPIA 105
Cdd:TIGR03388   4 YKWEVEYEFWSPDC-FEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLHTEGVVIHWHGIRQIGTPWADGTAGVTQCAIN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    106 PGSTMLYNFTVDyNVGTYWYHSHTDGQYEDGMKGLFII---KDDSFPYDYDEELSLSLSEWYHDLVTDLTKSFMSvyNPT 182
Cdd:TIGR03388  83 PGETFIYNFVVD-RPGTYFYHGHYGMQRSAGLYGSLIVdvpDGEKEPFHYDGEFNLLLSDWWHKSIHEQEVGLSS--KPM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    183 GAEPIPQNLIVN-------------NTMNLT--------------WEVQPDTTYLLRIVNVGGFVSQYFWIEDHEMTVVE 235
Cdd:TIGR03388 160 RWIGEPQSLLINgrgqfncslaakfSSTNLPqcnlkgneqcapqiLHVEPGKTYRLRIASTTALAALNFAIEGHKLTVVE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    236 IDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNFAIMQKfddtMLDVIPSDLQlnATSYMVY--NKTAALPTQnyVDS 313
Cdd:TIGR03388 240 ADGNYVEPFTVKDIDIYSGETYSVLLTTDQDPSRNYWISVG----VRGRKPNTPP--GLTVLNYypNSPSRLPPT--PPP 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    314 IDNFLDDF---YLQPYEKEAIYGEPDHVITVD--VVMDNLKNGVN----YAfFNNITYTAPKVPTLMTV----LSSGDQA 380
Cdd:TIGR03388 312 VTPAWDDFdrsKAFSLAIKAAMGSPKPPETSDrrIVLLNTQNKINgytkWA-INNVSLTLPHTPYLGSLkynlLNAFDQK 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    381 NNSEIYG-----------SNTHT----FILEKDEIVEIVLNNQDT------GTHPFHLHGHAFQTiqrdrtyddaLGEVP 439
Cdd:TIGR03388 391 PPPENYPrdydifkpppnPNTTTgngiYRLKFNTTVDVILQNANTlngnnsETHPWHLHGHDFWV----------LGYGE 460

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6323703    440 HSFDPDNHPAfpEY----PMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:TIGR03388 461 GKFRPGVDEK--SYnlknPPLRNTVVIFPYGWTALRFVADNPGVWAFHCHIEPH 512
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 24-144 8.17e-70

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: 222.14  E-value: 8.17e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   24 HTFNWTTGWDYRNVDGLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQNGTASMDGVPFLTQCP 103
Cdd:cd13851   1 VEFDWNITWVTANPDGLFERRVIGINGQWPPPPIEVNKGDTVVIHATNSLGDQPTSLHFHGLFQNGTNYMDGPVGVTQCP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6323703  104 IAPGSTMLYNFTVDYNVGTYWYHSHTDGQYEDGMKGLFIIK 144
Cdd:cd13851  81 IPPGQSFTYEFTVDTQVGTYWYHSHDGGQYPDGLRGPFIIH 121
PLN02604 PLN02604
oxidoreductase
 4-489 1.64e-66

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 227.82  E-value: 1.64e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703     4 ALLSIAVLLFSML--SLAQAETHTFNWTTGWDYRNVDGLKsRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMH 81
Cdd:PLN02604   3 RFLALFFLLFSVLnfPAAEARIRRYKWEVKYEYKSPDCFK-KLVITINGRSPGPTILAQQGDTVIVELKNSLLTENVAIH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    82 FHGLFQNGTASMDGVPFLTQCPIAPGSTMLYNFTVDyNVGTYWYHSHTDGQYEDGMKGLFII-----KDDSFPYDYDEel 156
Cdd:PLN02604  82 WHGIRQIGTPWFDGTEGVTQCPILPGETFTYEFVVD-RPGTYLYHAHYGMQREAGLYGSIRVslprgKSEPFSYDYDR-- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   157 SLSLSEWYHDLVTDLTKSFMSV------------------YNPTGAEPIPQNLIVNNTMN-----LTWEVQPDTTYLLRI 213
Cdd:PLN02604 159 SIILTDWYHKSTYEQALGLSSIpfdwvgepqslliqgkgrYNCSLVSSPYLKAGVCNATNpecspYVLTVVPGKTYRLRI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   214 VNVGGFVSQYFWIEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNFAIMQKFDDTMLDVIPSDLQLNa 293
Cdd:PLN02604 239 SSLTALSALSFQIEGHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQDPSRNYWVTTSVVSRNNTTPPGLAIFN- 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   294 tsYMVYNKTAALPTqnyVDSIDNFLDDFYLQPYEKEAIYGEPDHV----ITVD--VVMDNLKNGVNYAF---FNNITYTA 364
Cdd:PLN02604 318 --YYPNHPRRSPPT---VPPSGPLWNDVEPRLNQSLAIKARHGYIhpppLTSDrvIVLLNTQNEVNGYRrwsVNNVSFNL 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   365 PKVPTLM----TVLSSGDQ-----------------ANNSEIYGSNThTFILEKDEIVEIVLNNQDT------GTHPFHL 417
Cdd:PLN02604 393 PHTPYLIalkeNLTGAFDQtpppegydfanydiyakPNNSNATSSDS-IYRLQFNSTVDIILQNANTmnannsETHPWHL 471

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323703   418 HGHAFQTiqrdrtyddaLGEVPHSFDPDNHPAfpEY----PMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:PLN02604 472 HGHDFWV----------LGYGEGKFNMSSDPK--KYnlvdPIMKNTVPVHPYGWTALRFRADNPGVWAFHCHIESH 535
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 35-489 2.61e-59

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: 204.78  E-value: 2.61e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   35 RNVDGLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTnTSMHFHGLfqNGTASMDGVPFLtqcPIAPGSTMLYNF 114
Cdd:COG2132  25 VELLPGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEP-TTVHWHGL--RVPNAMDGVPGD---PIAPGETFTYEF 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  115 TVDYNVGTYWYHSHTDG----QYEDGMKGLFIIKD--DSFPyDYDEELSLSLSEWyhDLVTDltKSFMSVYNPTGAEPIP 188
Cdd:COG2132  99 PVPQPAGTYWYHPHTHGstaeQVYRGLAGALIVEDpeEDLP-RYDRDIPLVLQDW--RLDDD--GQLLYPMDAAMGGRLG 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  189 QNLIVNNTMNLTWEVQPDTTYLLRIVNVGgfVSQYFWI---EDHEMTVVEIDGITTEKNVT-DMLYITVAQRYTVLVHTK 264
Cdd:COG2132 174 DTLLVNGRPNPTLEVRPGERVRLRLLNAS--NARIYRLalsDGRPFTVIATDGGLLPAPVEvDELLLAPGERADVLVDFS 251

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  265 NDTDKNFAIMQKFDDTMLDVIpsdLQLNATSYMvynKTAALPTQnyvdsidnflddfyLQPYEKEAiygEPDHVITVDVV 344
Cdd:COG2132 252 ADPGEEVTLANPFEGRSGRAL---LTLRVTGAA---ASAPLPAN--------------LAPLPDLE---DREAVRTRELV 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  345 MDNLKNGVNYAFfnnitytapkvptlmtvlssgdqanNSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPFHLHGHAFQT 424
Cdd:COG2132 309 LTGGMAGYVWTI-------------------------NGKAFDPDRPDLTVKLGERERWTLVNDTMMPHPFHLHGHQFQV 363

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323703  425 IQRDrtyddalgevphsfdpdnhPAFPEYPMRRDTLYVRPQSNFVIRFKADN-PGVWFFHCHIEWH 489
Cdd:COG2132 364 LSRN-------------------GKPPPEGGWKDTVLVPPGETVRILFRFDNyPGDWMFHCHILEH 410
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 29-147 9.27e-47

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 160.49  E-value: 9.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703     29 TTGWDYRNVDGLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNtNTSMHFHGLFQNGTASMDGVPFLTQCPIAPGS 108
Cdd:pfam07732   1 TVTYGTVSPLGGTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNLDE-PTSIHWHGLQQRGTPWMDGVPGVTQCPIPPGQ 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 6323703    109 TMLYNFTVDYNVGTYWYHSHTDGQYEDGMKGLFIIKDDS 147
Cdd:pfam07732  80 SFTYRFQVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDRA 118
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 362-489 2.94e-39

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: 141.03  E-value: 2.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    362 YTAPKVPTLMTVLSSG----DQANNSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPFHLHGHAFQTIQRDRTYDDALGE 437
Cdd:pfam07731   1 DTPPKLPTLLQITSGNfrrnDWAINGLLFPPNTNVITLPYGTVVEWVLQNTTTGVHPFHLHGHSFQVLGRGGGPWPEEDP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6323703    438 VPHSFdpdnhpafpEYPMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:pfam07731  81 KTYNL---------VDPVRRDTVQVPPGGWVAIRFRADNPGVWLFHCHILWH 123
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 154-301 2.67e-35

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: 130.13  E-value: 2.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    154 EELSLSLSEWYHDLVTDLTK-SFMSVYNPTGAEPIPQNLIVNNTM---NLTWEVQPDTTYLLRIVNVGGFVSQYFWIEDH 229
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKeLLASGKAPTDFPPVPDAVLINGKDgasLATLTVTPGKTYRLRIINVALDDSLNFSIEGH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323703    230 EMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDtDKNFAIMQKFddtmldVIPSDLQLNATSYMVYNK 301
Cdd:pfam00394  81 KMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQD-PGNYWIVASP------NIPAFDNGTAAAILRYSG 145
PRK10965 PRK10965
multicopper oxidase; Provisional
 19-146 1.26e-13

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 73.90  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    19 AQAETHTF---NWTTGWDYrnvdglksrpvitcNGQFPWPDITVNKGDRVQIYLTNGMNNTnTSMHFHGLFQNGTAsmDG 95
Cdd:PRK10965  52 IQAGQSSFagkTATATWGY--------------NGNLLGPAVRLQRGKAVTVDITNQLPEE-TTLHWHGLEVPGEV--DG 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6323703    96 VPfltQCPIAPGSTMLYNFTVDYNVGTYWYHSHTDG----QYEDGMKGLFIIKDD 146
Cdd:PRK10965 115 GP---QGIIAPGGKRTVTFTVDQPAATCWFHPHQHGktgrQVAMGLAGLVLIEDD 166
 
Name Accession Description Interval E-value
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 336-489 8.42e-79

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


Pssm-ID: 259966 [Multi-domain]  Cd Length: 160  Bit Score: 246.78  E-value: 8.42e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  336 DHVITVDVVMDNLKNGVNYAFFNNITYTAPKVPTLMTVLSSGDQANNSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPF 415
Cdd:cd13899   1 DHSITLNVDFDTFDDGVNRAAFNNITYVSPKVPTLYTALSMGDDALDPAIYGPQTNAFVLNHGEVVELVVNNWDAGKHPF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323703  416 HLHGHAFQTIQRDRTYDDAlgevphsFDPDNHPAFPEYPMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13899  81 HLHGHKFQVVQRSPDVASD-------DPNPPINEFPENPMRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWH 147
CuRO_2_Fet3p_like cd13877
The second Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 154-301 1.23e-74

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: 235.52  E-value: 1.23e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  154 EELSLSLSEWYHDLVTDLTKSFMSVYNPTGAEPIPQNLIVNNTMNLTWEVQPDTTYLLRIVNVGGFVSQYFWIEDHEMTV 233
Cdd:cd13877   1 EEVTLTLSDWYHDQSPDLLRDFLSPYNPTGAEPIPDSSLFNDTQNATINFEPGKTYLLRIINMGAFASQYFHIEGHDMTI 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323703  234 VEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNFAIMQKFDDTMLDVIPSDLQLNATSYMVYNK 301
Cdd:cd13877  81 IEVDGVYVKPYPVDTLYIAVGQRYSVLVKAKNDTDRNYAIINGMDKDMLDTVPDDLYLNKTNWLVYDS 148
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 26-489 6.82e-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: 236.19  E-value: 6.82e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703     26 FNWTTGWDYRNVDGlKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQNGTASMDGVPFLTQCPIA 105
Cdd:TIGR03388   4 YKWEVEYEFWSPDC-FEKLVIGINGQFPGPTIRAQAGDTIVVELTNKLHTEGVVIHWHGIRQIGTPWADGTAGVTQCAIN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    106 PGSTMLYNFTVDyNVGTYWYHSHTDGQYEDGMKGLFII---KDDSFPYDYDEELSLSLSEWYHDLVTDLTKSFMSvyNPT 182
Cdd:TIGR03388  83 PGETFIYNFVVD-RPGTYFYHGHYGMQRSAGLYGSLIVdvpDGEKEPFHYDGEFNLLLSDWWHKSIHEQEVGLSS--KPM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    183 GAEPIPQNLIVN-------------NTMNLT--------------WEVQPDTTYLLRIVNVGGFVSQYFWIEDHEMTVVE 235
Cdd:TIGR03388 160 RWIGEPQSLLINgrgqfncslaakfSSTNLPqcnlkgneqcapqiLHVEPGKTYRLRIASTTALAALNFAIEGHKLTVVE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    236 IDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNFAIMQKfddtMLDVIPSDLQlnATSYMVY--NKTAALPTQnyVDS 313
Cdd:TIGR03388 240 ADGNYVEPFTVKDIDIYSGETYSVLLTTDQDPSRNYWISVG----VRGRKPNTPP--GLTVLNYypNSPSRLPPT--PPP 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    314 IDNFLDDF---YLQPYEKEAIYGEPDHVITVD--VVMDNLKNGVN----YAfFNNITYTAPKVPTLMTV----LSSGDQA 380
Cdd:TIGR03388 312 VTPAWDDFdrsKAFSLAIKAAMGSPKPPETSDrrIVLLNTQNKINgytkWA-INNVSLTLPHTPYLGSLkynlLNAFDQK 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    381 NNSEIYG-----------SNTHT----FILEKDEIVEIVLNNQDT------GTHPFHLHGHAFQTiqrdrtyddaLGEVP 439
Cdd:TIGR03388 391 PPPENYPrdydifkpppnPNTTTgngiYRLKFNTTVDVILQNANTlngnnsETHPWHLHGHDFWV----------LGYGE 460

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6323703    440 HSFDPDNHPAfpEY----PMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:TIGR03388 461 GKFRPGVDEK--SYnlknPPLRNTVVIFPYGWTALRFVADNPGVWAFHCHIEPH 512
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 24-144 8.17e-70

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: 222.14  E-value: 8.17e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   24 HTFNWTTGWDYRNVDGLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQNGTASMDGVPFLTQCP 103
Cdd:cd13851   1 VEFDWNITWVTANPDGLFERRVIGINGQWPPPPIEVNKGDTVVIHATNSLGDQPTSLHFHGLFQNGTNYMDGPVGVTQCP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6323703  104 IAPGSTMLYNFTVDYNVGTYWYHSHTDGQYEDGMKGLFIIK 144
Cdd:cd13851  81 IPPGQSFTYEFTVDTQVGTYWYHSHDGGQYPDGLRGPFIIH 121
PLN02604 PLN02604
oxidoreductase
 4-489 1.64e-66

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 227.82  E-value: 1.64e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703     4 ALLSIAVLLFSML--SLAQAETHTFNWTTGWDYRNVDGLKsRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMH 81
Cdd:PLN02604   3 RFLALFFLLFSVLnfPAAEARIRRYKWEVKYEYKSPDCFK-KLVITINGRSPGPTILAQQGDTVIVELKNSLLTENVAIH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    82 FHGLFQNGTASMDGVPFLTQCPIAPGSTMLYNFTVDyNVGTYWYHSHTDGQYEDGMKGLFII-----KDDSFPYDYDEel 156
Cdd:PLN02604  82 WHGIRQIGTPWFDGTEGVTQCPILPGETFTYEFVVD-RPGTYLYHAHYGMQREAGLYGSIRVslprgKSEPFSYDYDR-- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   157 SLSLSEWYHDLVTDLTKSFMSV------------------YNPTGAEPIPQNLIVNNTMN-----LTWEVQPDTTYLLRI 213
Cdd:PLN02604 159 SIILTDWYHKSTYEQALGLSSIpfdwvgepqslliqgkgrYNCSLVSSPYLKAGVCNATNpecspYVLTVVPGKTYRLRI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   214 VNVGGFVSQYFWIEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNFAIMQKFDDTMLDVIPSDLQLNa 293
Cdd:PLN02604 239 SSLTALSALSFQIEGHNMTVVEADGHYVEPFVVKNLFIYSGETYSVLVKADQDPSRNYWVTTSVVSRNNTTPPGLAIFN- 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   294 tsYMVYNKTAALPTqnyVDSIDNFLDDFYLQPYEKEAIYGEPDHV----ITVD--VVMDNLKNGVNYAF---FNNITYTA 364
Cdd:PLN02604 318 --YYPNHPRRSPPT---VPPSGPLWNDVEPRLNQSLAIKARHGYIhpppLTSDrvIVLLNTQNEVNGYRrwsVNNVSFNL 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   365 PKVPTLM----TVLSSGDQ-----------------ANNSEIYGSNThTFILEKDEIVEIVLNNQDT------GTHPFHL 417
Cdd:PLN02604 393 PHTPYLIalkeNLTGAFDQtpppegydfanydiyakPNNSNATSSDS-IYRLQFNSTVDIILQNANTmnannsETHPWHL 471

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323703   418 HGHAFQTiqrdrtyddaLGEVPHSFDPDNHPAfpEY----PMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:PLN02604 472 HGHDFWV----------LGYGEGKFNMSSDPK--KYnlvdPIMKNTVPVHPYGWTALRFRADNPGVWAFHCHIESH 535
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 35-489 2.61e-59

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: 204.78  E-value: 2.61e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   35 RNVDGLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTnTSMHFHGLfqNGTASMDGVPFLtqcPIAPGSTMLYNF 114
Cdd:COG2132  25 VELLPGKPTTVWGYNGQYPGPTIRVREGDRVRVRVTNRLPEP-TTVHWHGL--RVPNAMDGVPGD---PIAPGETFTYEF 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  115 TVDYNVGTYWYHSHTDG----QYEDGMKGLFIIKD--DSFPyDYDEELSLSLSEWyhDLVTDltKSFMSVYNPTGAEPIP 188
Cdd:COG2132  99 PVPQPAGTYWYHPHTHGstaeQVYRGLAGALIVEDpeEDLP-RYDRDIPLVLQDW--RLDDD--GQLLYPMDAAMGGRLG 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  189 QNLIVNNTMNLTWEVQPDTTYLLRIVNVGgfVSQYFWI---EDHEMTVVEIDGITTEKNVT-DMLYITVAQRYTVLVHTK 264
Cdd:COG2132 174 DTLLVNGRPNPTLEVRPGERVRLRLLNAS--NARIYRLalsDGRPFTVIATDGGLLPAPVEvDELLLAPGERADVLVDFS 251

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  265 NDTDKNFAIMQKFDDTMLDVIpsdLQLNATSYMvynKTAALPTQnyvdsidnflddfyLQPYEKEAiygEPDHVITVDVV 344
Cdd:COG2132 252 ADPGEEVTLANPFEGRSGRAL---LTLRVTGAA---ASAPLPAN--------------LAPLPDLE---DREAVRTRELV 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  345 MDNLKNGVNYAFfnnitytapkvptlmtvlssgdqanNSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPFHLHGHAFQT 424
Cdd:COG2132 309 LTGGMAGYVWTI-------------------------NGKAFDPDRPDLTVKLGERERWTLVNDTMMPHPFHLHGHQFQV 363

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323703  425 IQRDrtyddalgevphsfdpdnhPAFPEYPMRRDTLYVRPQSNFVIRFKADN-PGVWFFHCHIEWH 489
Cdd:COG2132 364 LSRN-------------------GKPPPEGGWKDTVLVPPGETVRILFRFDNyPGDWMFHCHILEH 410
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 41-489 5.41e-58

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: 204.20  E-value: 5.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703     41 KSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNtNTSMHFHGLFQNGTASMDGVPFLTQCPIAPGSTMLYNFTVDYNV 120
Cdd:TIGR03389  20 STKSILTVNGKFPGPTLYAREGDTVIVNVTNNVQY-NVTIHWHGVRQLRNGWADGPAYITQCPIQPGQSYVYNFTITGQR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    121 GTYWYHSHTDgQYEDGMKGLFII---KDDSFPYDY-DEELSLSLSEWYHDLVTDLTKSFMSvynpTGAEP-IPQNLIVN- 194
Cdd:TIGR03389  99 GTLWWHAHIS-WLRATVYGAIVIlpkPGVPYPFPKpDREVPIILGEWWNADVEAVINQANQ----TGGAPnVSDAYTINg 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    195 -----------NTMNLTweVQPDTTYLLRIVNVGGFVSQYFWIEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHT 263
Cdd:TIGR03389 174 hpgplyncsskDTFKLT--VEPGKTYLLRIINAALNDELFFAIANHTLTVVEVDATYTKPFKTKTIVIGPGQTTNVLLTA 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    264 KNDTDKNFAIMQKFDDTMLDVIPSD----LQLNATSYMVYNKTAALPTQNYVDSIDNFLDDFYLQPYEKEA--IYGEPDH 337
Cdd:TIGR03389 252 DQSPGRYFMAARPYMDAPGAFDNTTttaiLQYKGTSNSAKPILPTLPAYNDTAAATNFSNKLRSLNSAQYPanVPVTIDR 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    338 VI--TVDVVMDNLK-------NGVNY-AFFNNITYTAPKVPTLmtvlssgdQANNSEIYGSNTHTF-------------- 393
Cdd:TIGR03389 332 RLffTIGLGLDPCPnntcqgpNGTRFaASMNNISFVMPTTALL--------QAHYFGISGVFTTDFpanpptkfnytgtn 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    394 --------------ILEKDEIVEIVLnnQDT-----GTHPFHLHGHAFQTIqrdrtyddalGEVPHSFDPDNHPA-FPEY 453
Cdd:TIGR03389 404 lpnnlfttngtkvvRLKFNSTVELVL--QDTsilgsENHPIHLHGYNFFVV----------GTGFGNFDPKKDPAkFNLV 471

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 6323703    454 -PMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:TIGR03389 472 dPPERNTVGVPTGGWAAIRFVADNPGVWFMHCHLEVH 508
PLN02191 PLN02191
L-ascorbate oxidase
 5-489 9.76e-55

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 196.00  E-value: 9.76e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703     5 LLSIAVLLFSMLSLAQAETHtfnWTTGWDYRNVDgLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHG 84
Cdd:PLN02191   8 IVTVVAVLTHTASAAVREYT---WEVEYKYWWPD-CKEGAVMTVNGQFPGPTIDAVAGDTIVVHLTNKLTTEGLVIHWHG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    85 LFQNGTASMDGVPFLTQCPIAPGSTMLYNFTVDyNVGTYWYHSHTDGQYEDGMKGLFIIKDDSFPYD---YDEELSLSLS 161
Cdd:PLN02191  84 IRQKGSPWADGAAGVTQCAINPGETFTYKFTVE-KPGTHFYHGHYGMQRSAGLYGSLIVDVAKGPKErlrYDGEFNLLLS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   162 EWYHDLVTDLTKSFMSvyNPTGAEPIPQNLIVNNTMNL----------------------------TWEVQPDTTYLLRI 213
Cdd:PLN02191 163 DWWHESIPSQELGLSS--KPMRWIGEAQSILINGRGQFncslaaqfsngtelpmctfkegdqcapqTLRVEPNKTYRIRL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   214 VNVGGFVSQYFWIEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNFAImqkfddtmldvipsdlqlna 293
Cdd:PLN02191 241 ASTTALASLNLAVQGHKLVVVEADGNYITPFTTDDIDIYSGESYSVLLTTDQDPSQNYYI-------------------- 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   294 tSYMVY----NKTAALPTQNYVDSIDNFL-----------DDFYLQPYEKEAIY---GEP-------DHVITVDVvmDNL 348
Cdd:PLN02191 301 -SVGVRgrkpNTTQALTILNYVTAPASKLpsspppvtprwDDFERSKNFSKKIFsamGSPsppkkyrKRLILLNT--QNL 377

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   349 KNGVNYAFFNNITYTAPKVPTLMTV---LSSG-DQANNSEIY-----------------GSNTHTFILekDEIVEIVLNN 407
Cdd:PLN02191 378 IDGYTKWAINNVSLVTPATPYLGSVkynLKLGfNRKSPPRSYrmdydimnpppfpntttGNGIYVFPF--NVTVDVIIQN 455

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   408 QD------TGTHPFHLHGHAFQTiqrdrtyddaLGEVPHSFDP--DNHPAFPEYPMRRDTLYVRPQSNFVIRFKADNPGV 479
Cdd:PLN02191 456 ANvlkgvvSEIHPWHLHGHDFWV----------LGYGDGKFKPgiDEKTYNLKNPPLRNTAILYPYGWTAIRFVTDNPGV 525

                        570
                 ....*....|
gi 6323703   480 WFFHCHIEWH 489
Cdd:PLN02191 526 WFFHCHIEPH 535
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 24-144 1.70e-49

Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins; Laccase-like multicopper oxidases (MCOs) in this family contain three cupredoxin domains. They are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites; Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Also included in this family are cupredoxin domains 1, 3, and 5 of the 6-domain MCO ceruloplasmin and similar proteins.


Pssm-ID: 259869 [Multi-domain]  Cd Length: 120  Bit Score: 167.85  E-value: 1.70e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   24 HTFNWTTGWDYRNVDGlKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQNGTASMDGVPFLTQCP 103
Cdd:cd04206   1 REYELTITETTVNPDG-VLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNLPNEPTSIHWHGLRQPGTNDGDGVAGLTQCP 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6323703  104 IAPGSTMLYNFTVDYNVGTYWYHSHTDGQYEDGMKGLFIIK 144
Cdd:cd04206  80 IPPGESFTYRFTVDDQAGTFWYHSHVGGQRADGLYGPLIVE 120
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 29-147 9.27e-47

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


Pssm-ID: 462247 [Multi-domain]  Cd Length: 119  Bit Score: 160.49  E-value: 9.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703     29 TTGWDYRNVDGLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNtNTSMHFHGLFQNGTASMDGVPFLTQCPIAPGS 108
Cdd:pfam07732   1 TVTYGTVSPLGGTRQAVIGVNGQFPGPTIRVREGDTVVVNVTNNLDE-PTSIHWHGLQQRGTPWMDGVPGVTQCPIPPGQ 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 6323703    109 TMLYNFTVDYNVGTYWYHSHTDGQYEDGMKGLFIIKDDS 147
Cdd:pfam07732  80 SFTYRFQVKQQAGTYWYHSHTSGQQAAGLAGAIIIEDRA 118
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 42-489 2.15e-42

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: 160.78  E-value: 2.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703     42 SRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQNGTASMDGVPFLTQCPIAPGSTMLYNFTVDY-NV 120
Cdd:TIGR03390  26 SRYSVVVNGTSPGPEIRLQEGQTTWIRVYNDIPDNNVTMHWHGLTQRTAPFSDGTPLASQWPIPPGHFFDYEIKPEPgDA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    121 GTYWYHSHTDGQYEDGmKGLFIIKD-DSFPYDYDEELSLSLSEWY--------HDLVTD-----------------LTKS 174
Cdd:TIGR03390 106 GSYFYHSHVGFQAVTA-FGPLIVEDcEPPPYKYDDERILLVSDFFsatdeeieQGLLSTpftwsgeteavllngksGNKS 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    175 FMSVYNPTGAEPIPqnlivnntmnlTWEVQPDTTYLLRIVNVGGFVSQYFWIEDHE-MTVVEIDGITTEKNVTDMLYITV 253
Cdd:TIGR03390 185 FYAQINPSGSCMLP-----------VIDVEPGKTYRLRFIGATALSLISLGIEDHEnLTIIEADGSYTKPAKIDHLQLGG 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    254 AQRYTVLVHTKNDT-----DKNFAIMQKFDDTMLDVIPSDLQLNATSymvyNKTAALPT------QNYVDSIDNFLdDFY 322
Cdd:TIGR03390 254 GQRYSVLFKAKTEDelcggDKRQYFIQFETRDRPKVYRGYAVLRYRS----DKASKLPSvpetppLPLPNSTYDWL-EYE 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    323 LQPYEKEAIYGEPDH-------VITVDVVMDNLKNGVNYAfFNNITYT--APKVPTLMTVLSSGDQANNS-----EIYG- 387
Cdd:TIGR03390 329 LEPLSEENNQDFPTLdevtrrvVIDAHQNVDPLNGRVAWL-QNGLSWTesVRQTPYLVDIYENGLPATPNytaalANYGf 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    388 -SNTHTFILEKDEIVEIVLNNQDTGT--------HPFHLHGHAFQTI-QRDRTYDDAlgevphsfdpDNHPAFPEY-PMR 456
Cdd:TIGR03390 408 dPETRAFPAKVGEVLEIVWQNTGSYTgpnggvdtHPFHAHGRHFYDIgGGDGEYNAT----------ANEAKLENYtPVL 477

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 6323703    457 RDT--LY--------VRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:TIGR03390 478 RDTtmLYryavkvvpGAPAGWRAWRIRVTNPGVWMMHCHILQH 520
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 26-143 2.20e-42

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: 148.56  E-value: 2.20e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   26 FNWTTGWDYRNVDGLKsRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTnTSMHFHGLFQNGTASMDGVPFLTQCPIA 105
Cdd:cd13857   3 YNFTISEITGAPDGFV-RPMLVINGQFPGPLIEANQGDRIVVHVTNELDEP-TSIHWHGLFQNGTNWMDGTAGITQCPIP 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6323703  106 PGSTMLYNFTVDYNVGTYWYHSHTDGQYEDGMKGLFII 143
Cdd:cd13857  81 PGGSFTYNFTVDGQYGTYWYHSHYSTQYADGLVGPLIV 118
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 38-145 6.53e-41

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: 144.79  E-value: 6.53e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   38 DGLkSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTN----TSMHFHGLFQNGTASMDGVPFLTQCPIAPGSTMLYN 113
Cdd:cd13856  15 DGF-ERSAVLANGQFPGPLITANKGDTFRITVVNQLTDPTmrrsTSIHWHGIFQHGTNYADGPAFVTQCPIAPNHSFTYD 93

                        90       100       110
                ....*....|....*....|....*....|..
gi 6323703  114 FTVDYNVGTYWYHSHTDGQYEDGMKGLFIIKD 145
Cdd:cd13856  94 FTAGDQAGTFWYHSHLSTQYCDGLRGPLVIYD 125
CuRO_1_tcLCC2_insect_like cd13858
The first cupredoxin domain of insect laccases similar to laccase 2 in Tribolium castaneum; ...
 38-144 8.37e-41

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: 143.83  E-value: 8.37e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   38 DGLkSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQNGTASMDGVPFLTQCPIAPGSTMLYNFTVD 117
Cdd:cd13858   1 DGV-ERPVITVNGQLPGPSIEVCEGDTVVVDVKNRLPGESTTIHWHGIHQRGTPYMDGVPMVTQCPILPGQTFRYKFKAD 79

                        90       100
                ....*....|....*....|....*..
gi 6323703  118 yNVGTYWYHSHTDGQYEDGMKGLFIIK 144
Cdd:cd13858  80 -PAGTHWYHSHSGTQRADGLFGALIVR 105
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 362-489 2.94e-39

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: 141.03  E-value: 2.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    362 YTAPKVPTLMTVLSSG----DQANNSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPFHLHGHAFQTIQRDRTYDDALGE 437
Cdd:pfam07731   1 DTPPKLPTLLQITSGNfrrnDWAINGLLFPPNTNVITLPYGTVVEWVLQNTTTGVHPFHLHGHSFQVLGRGGGPWPEEDP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6323703    438 VPHSFdpdnhpafpEYPMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:pfam07731  81 KTYNL---------VDPVRRDTVQVPPGGWVAIRFRADNPGVWLFHCHILWH 123
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 25-144 3.31e-36

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: 131.65  E-value: 3.31e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   25 TFNWTTGWdyRNVDGlKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNnTNTSMHFHGLFQNGTASMDGVPFLTQCPI 104
Cdd:cd13850   2 TLTVTEGS--PDGDG-GEREVILINGQFPGPPIILDEGDEVEILVTNNLP-VNTTIHFHGILQRGTPWSDGVPGVTQWPI 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 6323703  105 APGSTMLYNFTVDYNVGTYWYHSHTDGQYEDGMKGLFIIK 144
Cdd:cd13850  78 QPGGSFTYRWKAEDQYGLYWYHSHYRGYYMDGLYGPIYIR 117
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 154-301 2.67e-35

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: 130.13  E-value: 2.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    154 EELSLSLSEWYHDLVTDLTK-SFMSVYNPTGAEPIPQNLIVNNTM---NLTWEVQPDTTYLLRIVNVGGFVSQYFWIEDH 229
Cdd:pfam00394   1 EDYVITLSDWYHKDAKDLEKeLLASGKAPTDFPPVPDAVLINGKDgasLATLTVTPGKTYRLRIINVALDDSLNFSIEGH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323703    230 EMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDtDKNFAIMQKFddtmldVIPSDLQLNATSYMVYNK 301
Cdd:pfam00394  81 KMTVVEVDGVYVNPFTVDSLDIFPGQRYSVLVTANQD-PGNYWIVASP------NIPAFDNGTAAAILRYSG 145
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 349-489 3.75e-35

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: 130.49  E-value: 3.75e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  349 KNGVNYAFFNNITYTAPKVPTLMTVLSsgDQANNSEIYGSNT------HTFIL---EKDEIVEIVLNNQDTGTHPFHLHG 419
Cdd:cd13910  12 YNNLPRGFFNGTSWRPLPGPATLLLAL--DADNAEEVAAGNGlstfdgNQLVItvdDIDKVVDLVINNLDDGDHPFHLHG 89

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323703  420 HAFQTIQRDRTY---DDALGEVPHSFDPDNhpafpeyPMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13910  90 HKFWVLGSGDGRyggGGYTAPDGTSLNTTN-------PLRRDTVSVPGFGWAVLRFVADNPGLWAFHCHILWH 155
CuRO_2_LCC_like cd04205
Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 158-299 7.02e-35

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: 129.02  E-value: 7.02e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  158 LSLSEWYHDLVTDLTKSFMsvYNPTGAEPIPQNLIVNNTM--------------NLTWEVQPDTTYLLRIVNVGGFVSQY 223
Cdd:cd04205   3 LLLSDWYHDSAEDVLAGYM--PNSFGNEPVPDSLLINGRGrfncsmavcnsgcpLPVITVEPGKTYRLRLINAGSFASFN 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323703  224 FWIEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTkNDTDKNFAIMQKFDDTMLDvipSDLQLNATSYMVY 299
Cdd:cd04205  81 FAIDGHNMTVIEVDGGYVEPLEVDNLDLAPGQRYDVLVKA-DQPPGNYWIRASADGRTFD---EGGNPNGTAILRY 152
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 23-143 1.51e-32

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: 121.58  E-value: 1.51e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   23 THTFNWTTGWDYRNVDGlKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQNGTASMDGVPFLTQC 102
Cdd:cd13854   3 TRKYTLTITNSTLAPDG-VEKEVMLINGQYPGPLIEANWGDTIEVTVINKLQDNGTSIHWHGIRQLNTNWQDGVPGVTEC 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6323703  103 PIAPGSTMLYNFTVDyNVGTYWYHSHTDGQYEDGMKGLFII 143
Cdd:cd13854  82 PIAPGDTRTYRFRAT-QYGTSWYHSHYSAQYGDGVVGPIVI 121
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 336-489 7.60e-31

The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; This subfamily of fungal laccases includes Tv-LCC from Trametes versicolor and Rs-LCC2 from plant pathogenic fungus Rhizoctonia solani. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259970 [Multi-domain]  Cd Length: 147  Bit Score: 117.77  E-value: 7.60e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  336 DHVITVDVvmdNLKNGVNYAFFNNITYTAPKVPTLMTVLSSgdqANNSEIYGSNTHTFILEKDEIVEIVL-NNQDTGTHP 414
Cdd:cd13903   1 DVNITLTF---GLNGTTGLFTINGVSYVSPTVPVLLQILSG---ATSAEDLLPTESTIILPRNKVVEITIpGGAIGGPHP 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323703  415 FHLHGHAFQTIQrdrtydDALGEVPHSFDPdnhpafpeypMRRDTLYV-RPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13903  75 FHLHGHAFSVVR------SAGSNTYNYVNP----------VRRDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWH 134
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 336-489 1.06e-30

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: 116.79  E-value: 1.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  336 DHVITVDVVMDNLKNGVNYAFFNNITYTApkvptlmtvlssgdqannseiYGSNTHTFILEKDEIVEIVLNNQD--TGTH 413
Cdd:cd04207   1 DRTRRLVLSQTGAPDGTTRWVINGMPFKE---------------------GDANTDIFSVEAGDVVEIVLINAGnhDMQH 59

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323703  414 PFHLHGHAFQTIQRDrtyddalgevphsFDPDNHPAFPEYPMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd04207  60 PFHLHGHSFWVLGSG-------------GGPFDAPLNLTNPPWRDTVLVPPGGWVVIRFKADNPGVWMLHCHILEH 122
copper_res_A TIGR01480
copper-resistance protein, CopA family; This model represents the CopA copper resistance ...
 26-489 1.11e-29

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


Pssm-ID: 273649 [Multi-domain]  Cd Length: 587  Bit Score: 124.22  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703     26 FNWTTGWDYRNVDGlKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNtNTSMHFHGLFQngTASMDGVPFLTQCPIA 105
Cdd:TIGR01480  48 FDLTIGETMVNFTG-RARPAITVNGSIPGPLLRWREGDTVRLRVTNTLPE-DTSIHWHGILL--PFQMDGVPGVSFAGIA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    106 PGSTMLYNFTVDYNvGTYWYHSHTDGQYEDGMKGLFIIKD-DSFPYDYDEELSLSLSEWY----HDLVTDLTKS--FMSV 178
Cdd:TIGR01480 124 PGETFTYRFPVRQS-GTYWYHSHSGFQEQAGLYGPLIIDPaEPDPVRADREHVVLLSDWTdldpAALFRKLKVMagHDNY 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    179 YNPTGAEPI------------------------PQNL----------IVNNTM---NLTWEVQPDTTYLLRIVNVGGFVS 221
Cdd:TIGR01480 203 YKRTVADFFrdvrndglkqtladrkmwgqmrmtPTDLadvngstytyLMNGTTpagNWTGLFRPGEKVRLRFINGSAMTY 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    222 QYFWIEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTKNdtDKNFAIMQKFDD---------------------- 279
Cdd:TIGR01480 283 FDVRIPGLKLTVVAVDGQYVHPVSVDEFRIAPAETFDVIVEPTG--DDAFTIFAQDSDrtgyargtlavrlgltapvpal 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    280 ------TMLDVI------PSDLQLNATSYMVYNKTAALPTQNYVDSIDNFLDDFYLQPYEKEAIYGEPD-HVITVDVVMD 346
Cdd:TIGR01480 361 dprpllTMKDMGmggmhhGMDHSKMSMGGMPGMDMSMRAQSNAPMDHSQMAMDASPKHPASEPLNPLVDmIVDMPMDRMD 440

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    347 NLKNGVNYAFFNNITYTAPKvpTLMTVLSSGDQANNSEI-----------------YGSNThTFILEKDEIVEIVLNNQD 409
Cdd:TIGR01480 441 DPGIGLRDNGRRVLTYADLH--SLFPPPDGRAPGREIELhltgnmerfawsfdgeaFGLKT-PLRFNYGERLRVVLVNDT 517

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    410 TGTHPFHLHGHAFQTIqrdrtyddalgevphsfDPDNhpafpEYPMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:TIGR01480 518 MMAHPIHLHGMWSELE-----------------DGQG-----EFQVRKHTVDVPPGGKRSFRVTADALGRWAYHCHMLLH 575
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 343-489 2.53e-29

The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259971 [Multi-domain]  Cd Length: 158  Bit Score: 113.93  E-value: 2.53e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  343 VVMDNLKNGVNYAFFNNITYTA-PKVPTLMTVLSSGDQANNSEIYGSNThtfiLEKDEIVEIVLNNQDTG-THPFHLHGH 420
Cdd:cd13904  10 TFVDPNGNALGRFFVNNVTWTNyIYQPLLHQVASGGGGTLNSSEVASVT----FPTDGWYDIVINNLDPAiDHPYHLHGV 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323703  421 AFQTIQRD--RTYDDALGEVphSFDPDNhpafpeyPMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13904  86 DFHIVARGsgTLTLEQLANV--QYNTTN-------PLRRDTIVIPGGSWAVLRIPADNPGVWALHCHIGWH 147
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 24-143 1.91e-28

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


Pssm-ID: 259914 [Multi-domain]  Cd Length: 120  Bit Score: 109.84  E-value: 1.91e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   24 HTFNWTTGWDYRNVDGLKSRpVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQNGTASMDGVPFLTQCP 103
Cdd:cd13845   1 RHYKWKVEYMFWAPDCVEKL-VIGINGQFPGPTIRATAGDTIVVELENKLPTEGVAIHWHGIRQRGTPWADGTASVSQCP 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 6323703  104 IAPGSTMLYNFTVDyNVGTYWYHSHTDGQYEDGMKGLFII 143
Cdd:cd13845  80 INPGETFTYQFVVD-RPGTYFYHGHYGMQRSAGLYGSLIV 118
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 49-143 1.29e-26

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: 104.59  E-value: 1.29e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   49 NGQFPWPDITVNKGDRVQIYLTNGMNnTNTSMHFHGL-FQNGtasMDGVPFLTQCPIAPGSTMLYNFTVDyNVGTYWYHS 127
Cdd:cd13860  26 NGSVPGPTIEVTEGDRVRILVTNELP-EPTTVHWHGLpVPNG---MDGVPGITQPPIQPGETFTYEFTAK-QAGTYMYHS 100

                        90
                ....*....|....*...
gi 6323703  128 HTDGQYED--GMKGLFII 143
Cdd:cd13860 101 HVDEAKQEdmGLYGAFIV 118
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 36-144 1.02e-25

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: 101.97  E-value: 1.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   36 NVDGlKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNnTNTSMHFHGLFQngTASMDGVPFLTQCPIAPGSTMLYNFT 115
Cdd:cd13848  13 NIGG-KEGEAITVNGQVPGPLLRFKEGDDATIRVHNRLD-EDTSIHWHGLLL--PNDMDGVPGLSFPGIKPGETFTYRFP 88

                        90       100
                ....*....|....*....|....*....
gi 6323703  116 VdYNVGTYWYHSHTDGQYEDGMKGLFIIK 144
Cdd:cd13848  89 V-RQSGTYWYHSHSGLQEQTGLYGPIIID 116
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 41-143 1.58e-25

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: 101.54  E-value: 1.58e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   41 KSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTnTSMHFHGLfqNGTASMDGVPFLTQCPIAPGSTMLYNFTVDyNV 120
Cdd:cd13861  18 PTTRTWGYNGQVPGPELRVRQGDTLRVRLTNRLPEP-TTIHWHGL--RLPNAMDGVPGLTQPPVPPGESFTYEFTPP-DA 93

                        90       100
                ....*....|....*....|....*
gi 6323703  121 GTYWYHSHTDGQY--EDGMKGLFII 143
Cdd:cd13861  94 GTYWYHPHVGSQEqlDRGLYGPLIV 118
PLN02168 PLN02168
copper ion binding / pectinesterase
 5-267 2.21e-25

copper ion binding / pectinesterase


Pssm-ID: 215113 [Multi-domain]  Cd Length: 545  Bit Score: 110.45  E-value: 2.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703     5 LLSIAVLlfsMLSLAQAETHTFNWTTGWDYRNVDGLkSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTsMHFHG 84
Cdd:PLN02168  11 LISLVIL---ELSYAFAPIVSYQWVVSYSQRFILGG-NKQVIVINDMFPGPLLNATANDVINVNIFNNLTEPFL-MTWNG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    85 LFQNGTASMDGVPFlTQCPIAPGSTMLYNFTVDYNVGTYWYHSHTDGQYEDGMKGLFIIKDDS-----FPYDyDEELSLS 159
Cdd:PLN02168  86 LQLRKNSWQDGVRG-TNCPILPGTNWTYRFQVKDQIGSYFYFPSLLLQKAAGGYGAIRIYNPElvpvpFPKP-DEEYDIL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   160 LSEWYHDLVTDLTKSF---MSVYNPTGAepipqnLIVNNTMNLT-WEVQPDTTYLLRIVNVGGFVSQYFWIEDHEMTVVE 235
Cdd:PLN02168 164 IGDWFYADHTVMRASLdngHSLPNPDGI------LFNGRGPEETfFAFEPGKTYRLRISNVGLKTCLNFRIQDHDMLLVE 237

                        250       260       270
                 ....*....|....*....|....*....|..
gi 6323703   236 IDGITTEKNVTDMLYITVAQRYTVLVHTKNDT 267
Cdd:PLN02168 238 TEGTYVQKRVYSSLDIHVGQSYSVLVTAKTDP 269
CuRO_2_MCO_like_1 cd13886
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 160-300 1.37e-24

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: 100.42  E-value: 1.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  160 LSEWYHDLVTDLTKSFMSVYNPtGAEPIPQNLIVN-------------------NTMNLTWEVQPDTTYLLRIVNVGGFV 220
Cdd:cd13886   5 VNDYYHDPSSVLLARYLAPGNE-GDEPVPDNGLINgigqfdcasatykiyccasNGTYYNFTLEPNKTYRLRLINAGSFA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  221 SQYFWIEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNFAIMQKFDDTMLDVIPSDLQLNATSYMVYN 300
Cdd:cd13886  84 DFTFSVDGHPLTVIEADGTLVEPVEVHSITISVAQRYSVILTTNQPTGGNFWMRAELNTDCFTYDNPNLDPDVRAIVSYT 163
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 333-489 1.20e-23

The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces; The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259968 [Multi-domain]  Cd Length: 157  Bit Score: 97.68  E-value: 1.20e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  333 GEPDHVITVDVVMDNLKNGVNYAFFNNITYTAP-KVPTLMTVLSsgdqaNNSEIYGSNTHTFILEK-DEIVEIVLNNQDT 410
Cdd:cd13901   4 PDPSPTQTLTIDLGPNATGVFLWTLNGSSFRVDwNDPTLLLVAD-----GNTSTFPPEWNVIELPKaNKWVYIVIQNNSP 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323703  411 GTHPFHLHGHAFQTiqrdrtyddaLGEVPHSFDPDNHPAFPEYPMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13901  79 LPHPIHLHGHDFYI----------LAQGTGTFDDDGTILNLNNPPRRDVAMLPAGGYLVIAFKTDNPGAWLMHCHIAWH 147
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 41-145 1.61e-23

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: 95.79  E-value: 1.61e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   41 KSRPVITCNGQFPWPDITVNKGDRVQIYLTNgMNNTNTSMHFHGLFQNGTASMDGVPFLTQCPIAPGSTMLYNFTVDYNV 120
Cdd:cd13849  15 STKSILTVNGQFPGPTIRVHEGDTVVVNVTN-RSPYNITIHWHGIRQLRSGWADGPAYITQCPIQPGQSYTYRFTVTGQE 93

                        90       100
                ....*....|....*....|....*
gi 6323703  121 GTYWYHSHTDGQyEDGMKGLFIIKD 145
Cdd:cd13849  94 GTLWWHAHISWL-RATVYGAFIIRP 117
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 357-489 2.81e-23

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: 96.98  E-value: 2.81e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  357 FNNITYTAPKVPTL----MTVLSSGDQANNSEIYGSN-----THTFILEKDEIVEIVLNNQDTG---THPFHLHGHAFQT 424
Cdd:cd13905   2 INGISFVFPSSPLLsqpeDLSDSSSCDFCNVPSKCCTepcecTHVIKLPLNSVVEIVLINEGPGpglSHPFHLHGHSFYV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  425 I-----QRDRTYDDALGEV--PHSFDPDNHPA--FPeYPMRRDTL------YVrpqsnfVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13905  82 LgmgfpGYNSTTGEILSQNwnNKLLDRGGLPGrnLV-NPPLKDTVvvpnggYV------VIRFRADNPGYWLLHCHIEFH 154
PLN02354 PLN02354
copper ion binding / oxidoreductase
 1-271 1.61e-22

copper ion binding / oxidoreductase


Pssm-ID: 177987 [Multi-domain]  Cd Length: 552  Bit Score: 101.79  E-value: 1.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703     1 MTNALLSIAVLLFSMLSL-AQAET--HTFNWTTGWDYRNVDGLKSRpVITCNGQFPWPDITVNKGDRVQIyltNGMNNTN 77
Cdd:PLN02354   2 MGGRLLAVLLCLAAAVALvVRAEDpyFFFTWNVTYGTASPLGVPQQ-VILINGQFPGPNINSTSNNNIVI---NVFNNLD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    78 TSMHF--HGLFQNGTASMDGVPFlTQCPIAPGSTMLYNFTVDYNVGTYWYHSHTDGQ-YEDGMKGLFIIKDDSFPYDYDE 154
Cdd:PLN02354  78 EPFLLtwSGIQQRKNSWQDGVPG-TNCPIPPGTNFTYHFQPKDQIGSYFYYPSTGMHrAAGGFGGLRVNSRLLIPVPYAD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   155 ---ELSLSLSEWY---HDLVTDLTKSFMSVYNPTGAEPIPQNLIVNNTMNLTWEVQPDTTYLLRIVNVGGFVSQYFWIED 228
Cdd:PLN02354 157 pedDYTVLIGDWYtksHTALKKFLDSGRTLGRPDGVLINGKSGKGDGKDEPLFTMKPGKTYRYRICNVGLKSSLNFRIQG 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 6323703   229 HEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVhTKNDTDKNF 271
Cdd:PLN02354 237 HKMKLVEMEGSHVLQNDYDSLDVHVGQCFSVLV-TANQAPKDY 278
CuRO_1_MCO_like_2 cd13864
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 43-143 1.63e-22

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


Pssm-ID: 259932 [Multi-domain]  Cd Length: 139  Bit Score: 93.75  E-value: 1.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   43 RPVITCNGQFPW--PDITVNKGDRVQIYLTNGMNNTN-----------TSMHFHGLFQNGTA-----SMDGVPFLTQCPI 104
Cdd:cd13864  18 KQIISINGSNDTigPTIRVKSGDTLNLLVTNHLCNEQelskiwqdycpTSIHFHGLVLENFGkqlanLVDGVPGLTQYPI 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 6323703  105 APGSTMLYNFTVDYNV-GTYWYHSHTDGQYEDGMKGLFII 143
Cdd:cd13864  98 GVGESYWYNFTIPEDTcGTFWYHSHSSVQYGDGLRGVFIV 137
PLN02792 PLN02792
oxidoreductase
 14-480 1.29e-21

oxidoreductase


Pssm-ID: 178389 [Multi-domain]  Cd Length: 536  Bit Score: 98.90  E-value: 1.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    14 SMLSLAQAE-THTFNWTTGWDYRNVDGLKSRPVITcNGQFPWPDITVNKGDRVQIYLTNGMNNTNTsMHFHGLFQNGTAS 92
Cdd:PLN02792   6 TIISFVKADdTLFYNWRVTYGNISLLTLPRRGILI-NGQFPGPEIRSLTNDNLVINVHNDLDEPFL-LSWNGVHMRKNSY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    93 MDGVpFLTQCPIAPGSTMLYNFTVDYNVGTYWYH-SHTDGQYEDGMKGLFIIKDDSFPYDYDE---ELSLSLSEWYHDLV 168
Cdd:PLN02792  84 QDGV-YGTTCPIPPGKNYTYDFQVKDQVGSYFYFpSLAVQKAAGGYGSLRIYSLPRIPVPFPEpagDFTFLIGDWYRRNH 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   169 TDLTKSFMSVYN-PTgaepIPQNLIVN-----NTMNLTweVQPDTTYLLRIVNVGGFVSQYFWIEDHEMTVVEIDGITTE 242
Cdd:PLN02792 163 TTLKKILDGGRKlPL----MPDGVMINgqgvsYVYSIT--VDKGKTYRFRISNVGLQTSLNFEILGHQLKLIEVEGTHTV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   243 KNVTDMLYITVAQRYTVLVhTKNDTDKNFAIM--QKFddtmldvIPSDLQLNATSYMVYNK-----TAALPTQNYVD--- 312
Cdd:PLN02792 237 QSMYTSLDIHVGQTYSVLV-TMDQPPQNYSIVvsTRF-------IAAKVLVSSTLHYSNSKghkiiHARQPDPDDLEwsi 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   313 ----SIDNFLDDFYLQPyEKEAIYGEPDHVITVDVVMDN----LKNGVNYAfFNNITYTAPKVP----------TLMTVL 374
Cdd:PLN02792 309 kqaqSIRTNLTASGPRT-NPQGSYHYGKMKISRTLILESsaalVKRKQRYA-INGVSFVPSDTPlkladhfkikGVFKVG 386

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   375 SSGDQANNSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPFHLHGHAFQTIQRDR-TYddalgevphsfdpdNHPAFPEY 453
Cdd:PLN02792 387 SIPDKPRRGGGMRLDTSVMGAHHNAFLEIIFQNREKIVQSYHLDGYNFWVVGINKgIW--------------SRASRREY 452

                        490       500       510
                 ....*....|....*....|....*....|.
gi 6323703   454 PMR----RDTLYVRPQSNFVIRFKADNPGVW 480
Cdd:PLN02792 453 NLKdaisRSTTQVYPESWTAVYVALDNVGMW 483
PLN02835 PLN02835
oxidoreductase
 1-480 1.53e-21

oxidoreductase


Pssm-ID: 178429 [Multi-domain]  Cd Length: 539  Bit Score: 98.50  E-value: 1.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703     1 MTNALLSIAVLLFSMLSLAQAET--HTFNWTTgwDYRNVDGLKS-RPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTN 77
Cdd:PLN02835   5 VNLHLLLGVLAVLSSVSLVNGEDpyKYYTWTV--TYGTISPLGVpQQVILINGQFPGPRLDVVTNDNIILNLINKLDQPF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    78 TsMHFHGLFQNGTASMDGVpFLTQCPIAPGSTMLYNFTVDYNVGTYWYHSHTD-GQYEDGMKGLFIIKDDSFPYDY---D 153
Cdd:PLN02835  83 L-LTWNGIKQRKNSWQDGV-LGTNCPIPPNSNYTYKFQTKDQIGTFTYFPSTLfHKAAGGFGAINVYERPRIPIPFplpD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   154 EELSLSLSEWYHdlvTDlTKSFMSVYNPTGAEPIPQNLIVNNTMNLTWEVQPDTTYLLRIVNVGGFVSQYFWIEDHEMTV 233
Cdd:PLN02835 161 GDFTLLVGDWYK---TS-HKTLQQRLDSGKVLPFPDGVLINGQTQSTFSGDQGKTYMFRISNVGLSTSLNFRIQGHTMKL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   234 VEIDGITTEKNVTDMLYITVAQRYTVLVhTKNDTDKNFAIM--QKFDDTMLDVIpSDLQLNATSYMVYNKTAALPTQNYV 311
Cdd:PLN02835 237 VEVEGSHTIQNIYDSLDVHVGQSVAVLV-TLNQSPKDYYIVasTRFTRQILTAT-AVLHYSNSRTPASGPLPALPSGELH 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   312 DSIDNF------LDDFYLQPYEKEAI-YGEPDHVITVDVVMDN-LKNGVNYAFFNNITYTAPKVP--------------- 368
Cdd:PLN02835 315 WSMRQArtyrwnLTASAARPNPQGSFhYGKITPTKTIVLANSApLINGKQRYAVNGVSYVNSDTPlkladyfgipgvfsv 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   369 -TLMTVLSSGDQANNSEIYGSNTHTFIlekdeivEIVLNNQDTGTHPFHLHGHAFQTI---------QRDRTYD--DALg 436
Cdd:PLN02835 395 nSIQSLPSGGPAFVATSVMQTSLHDFL-------EVVFQNNEKTMQSWHLDGYDFWVVgygsgqwtpAKRSLYNlvDAL- 466

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 6323703   437 evphsfdpdnhpafpeypmRRDTLYVRPQSNFVIRFKADNPGVW 480
Cdd:PLN02835 467 -------------------TRHTAQVYPKSWTTILVSLDNQGMW 491
CuRO_1_AAO_like_2 cd13847
The first cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 36-132 9.92e-21

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: 87.97  E-value: 9.92e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   36 NVDGLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQNGTASMDGVPFLTQCPIAPGSTMLYNFT 115
Cdd:cd13847   8 SCDPFGPRPSTLINGSFPGPELRVQEGQHLWVRVYNDLEAGNTTMHFHGLSQYMSPFSDGTPLASQWPIPPGKFFDYEFP 87

                        90
                ....*....|....*...
gi 6323703  116 VDY-NVGTYWYHSHTDGQ 132
Cdd:cd13847  88 LEAgDAGTYYYHSHVGFQ 105
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 347-489 1.04e-20

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: 89.02  E-value: 1.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  347 NLKNGVNYAFFNNITYTAPKVPTLMTVlssgdqannsEIYgsnthtfILEKDEIVEIVLNNQDT------GTHPFHLHGH 420
Cdd:cd13893  12 NLINGQLRWAINNVSYVPPPTPYLAAL----------PVY-------PFKGGDVVDVILQNANTntrnasEQHPWHLHGH 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323703  421 AFQTiqrdrtyddaLGEVPHSFDPDNHPAFPEY--PMRRDTLYVRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13893  75 DFWV----------LGYGLGGFDPAADPSSLNLvnPPMRNTVTIFPYGWTALRFKADNPGVWAFHCHIEWH 135
PLN02991 PLN02991
oxidoreductase
 12-480 1.86e-20

oxidoreductase


Pssm-ID: 215536 [Multi-domain]  Cd Length: 543  Bit Score: 95.47  E-value: 1.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    12 LFSMLSLAQAET--HTFNWTTgwDYRNVDGLK-SRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTsMHFHGLFQN 88
Cdd:PLN02991  15 LLFLISFVAAEDpyRFFEWHV--TYGNISPLGvAQQGILINGKFPGPDIISVTNDNLIINVFNHLDEPFL-ISWSGIRNW 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    89 GTASMDGVpFLTQCPIAPGSTMLYNFTVDYNVGTYWYHSHTDGQYEDGMKGLFIIKDDS-----FPYDYDEeLSLSLSEW 163
Cdd:PLN02991  92 RNSYQDGV-YGTTCPIPPGKNYTYALQVKDQIGSFYYFPSLGFHKAAGGFGAIRISSRPlipvpFPAPADD-YTVLIGDW 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   164 YHDLVTDLTKSFmsvyNPTGAEPIPQNLIVNN-TMNLTWEVQPDTTYLLRIVNVGGFVSQYFWIEDHEMTVVEIDGITTE 242
Cdd:PLN02991 170 YKTNHKDLRAQL----DNGGKLPLPDGILINGrGSGATLNIEPGKTYRLRISNVGLQNSLNFRIQNHTMKLVEVEGTHTI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   243 KNVTDMLYITVAQRYTVLVhTKNDTDKNFAIM--QKFDDTMLdVIPSDLQLNATSYMVYNKTAALPTQ-----NYVDSID 315
Cdd:PLN02991 246 QTPFSSLDVHVGQSYSVLI-TADQPAKDYYIVvsSRFTSKIL-ITTGVLHYSNSAGPVSGPIPDGPIQlswsfDQARAIK 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   316 NFLDDFYLQPYEKEAI-YGEPDHVITVDVV--MDNLKNGVNYAFFNNITYTAP---------KVPTLMTVLSSGDQANNS 383
Cdd:PLN02991 324 TNLTASGPRPNPQGSYhYGKINITRTIRLAnsAGNIEGKQRYAVNSASFYPADtplkladyfKIAGVYNPGSIPDQPTNG 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   384 EIYGSnthTFILEKD--EIVEIVLNNQDTGTHPFHLHGHAFQTIQRDrtyddaLGEvphsFDPDNHPAFP-EYPMRRDTL 460
Cdd:PLN02991 404 AIFPV---TSVMQTDykAFVEIVFENWEDIVQTWHLDGYSFYVVGME------LGK----WSAASRKVYNlNDAVSRCTV 470

                        490       500
                 ....*....|....*....|
gi 6323703   461 YVRPQSNFVIRFKADNPGVW 480
Cdd:PLN02991 471 QVYPRSWTAIYVSLDNVGMW 490
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 49-145 2.97e-20

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: 86.47  E-value: 2.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   49 NGQFPWPDITVNKGDRVQIYLTNGMNNTnTSMHFHGLFQNGTasMDGVPfltQCPIAPGSTMLYNFTVDYNVGTYWYHSH 128
Cdd:cd04232  26 NGSYLGPTIRVKKGDTVRINVTNNLDEE-TTVHWHGLHVPGE--MDGGP---HQPIAPGQTWSPTFTIDQPAATLWYHPH 99

                        90       100
                ....*....|....*....|.
gi 6323703  129 TDG----QYEDGMKGLFIIKD 145
Cdd:cd04232 100 THGktaeQVYRGLAGLFIIED 120
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 26-140 4.93e-20

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: 85.99  E-value: 4.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   26 FNWTTGWDYRNVDGLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTsMHFHGLFQNGTASMDGVPFLTQCPIA 105
Cdd:cd13859   3 FEMTIDETVITVVPGLDFKTFAFNGQVPGPLIHVKEGDDLVVHVTNNTTLPHT-IHWHGVLQMGSWKMDGVPGVTQPAIE 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 6323703  106 PGSTMLYNFTVDyNVGTYWYHSHTDGQYEDGMKGL 140
Cdd:cd13859  82 PGESFTYKFKAE-RPGTLWYHCHVNVNEHVGMRGM 115
PLN00044 PLN00044
multi-copper oxidase-related protein; Provisional
 39-480 9.80e-20

multi-copper oxidase-related protein; Provisional


Pssm-ID: 165622 [Multi-domain]  Cd Length: 596  Bit Score: 93.19  E-value: 9.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    39 GLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTnTSMHFHGLFQNGTASMDGVpFLTQCPIAPGSTMLYNFTVDY 118
Cdd:PLN00044  44 GVKKQEAIGINGQFPGPALNVTTNWNLVVNVRNALDEP-LLLTWHGVQQRKSAWQDGV-GGTNCAIPAGWNWTYQFQVKD 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   119 NVGTYWYHSHTDGQYEDGMKGLFIIKDDS-----FPYDYDEELSLSLSEWYHDLVTDLTKSfMSVYNPTGAepiPQNLIV 193
Cdd:PLN00044 122 QVGSFFYAPSTALHRAAGGYGAITINNRDvipipFGFPDGGDITLFIADWYARDHRALRRA-LDAGDLLGA---PDGVLI 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   194 N--------NTM---NLTWE---VQPDTTYLLRIVNVGGFVSQYFWIEDHEMTVVEIDG-ITTEKNVTDMlYITVAQRYT 258
Cdd:PLN00044 198 NafgpyqynDSLvppGITYErinVDPGKTYRFRVHNVGVATSLNFRIQGHNLLLVEAEGsYTSQQNYTNL-DIHVGQSYS 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   259 VLVHTKNDTDKNFAIMQK---FDDTMLDvipsdlQLNATSYMVYNKTAALPTQNYVDSIDNFLDDFY------------- 322
Cdd:PLN00044 277 FLLTMDQNASTDYYVVASarfVDAAVVD------KLTGVAILHYSNSQGPASGPLPDAPDDQYDTAFsinqarsirwnvt 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   323 ---LQPYEKEAI-YGEpdhVITVDVVM-----DNLKNGVNYAFFNNITYTAPKVPTLMTVLSSG------DQANNSEIYG 387
Cdd:PLN00044 351 asgARPNPQGSFhYGD---ITVTDVYLlqsmaPELIDGKLRATLNEISYIAPSTPLMLAQIFNVpgvfklDFPNHPMNRL 427

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   388 SNTHTFILEK--DEIVEIVLNNQDTGTHPFHLHGHAFQTIQRDRTY--DDALGEVpHSFDpdnhpafpeyPMRRDTLYVR 463
Cdd:PLN00044 428 PKLDTSIINGtyKGFMEIIFQNNATNVQSYHLDGYAFFVVGMDYGLwtDNSRGTY-NKWD----------GVARSTIQVF 496

                        490
                 ....*....|....*..
gi 6323703   464 PQSNFVIRFKADNPGVW 480
Cdd:PLN00044 497 PGAWTAILVFLDNAGIW 513
CuRO_1_LCC_like_3 cd13865
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 37-145 1.32e-17

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


Pssm-ID: 259933 [Multi-domain]  Cd Length: 115  Bit Score: 78.89  E-value: 1.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   37 VDGlKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTnTSMHFHGL-FQNgtaSMDGVPFLTQCPIAPGSTMLYNFT 115
Cdd:cd13865  12 VNG-KAATVYGIRQPDGTEGLRLTEGDRFDVELENRLDEP-TTIHWHGLiPPN---LQDGVPDVTQPPIPPGQSQRYDFP 86

                        90       100       110
                ....*....|....*....|....*....|
gi 6323703  116 VDYNvGTYWYHSHTDGQYEDGMKGLFIIKD 145
Cdd:cd13865  87 LVQP-GTFWMHSHYGLQEQKLLAAPLIIRS 115
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 390-489 5.08e-17

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: 78.07  E-value: 5.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  390 THTFILEKDEIVEIVL---NNQDTGTHPFHLHGHAFQTIQRdrtyddALGevphSFDPDNHPA-FPEY-PMRRDTLYVRP 464
Cdd:cd13897  31 TKVKVLEYGSTVEIVLqgtSLLAAENHPMHLHGFDFYVVGR------GFG----NFDPSTDPAtFNLVdPPLRNTVGVPR 100

                        90       100
                ....*....|....*....|....*
gi 6323703  465 QSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13897 101 GGWAAIRFVADNPGVWFMHCHFERH 125
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 388-489 1.11e-16

The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259963 [Multi-domain]  Cd Length: 115  Bit Score: 76.14  E-value: 1.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  388 SNTHTFILEKDEIVEIVLNNQDTGTHPFHLHGHAFQTIQRDrtyddalgevphsfdpdnhpafPEYPMRRDTLYVRPQSN 467
Cdd:cd13896  25 PDADPLRVREGERVRIVFVNDTMMAHPMHLHGHFFQVENGN----------------------GEYGPRKDTVLVPPGET 82

                        90       100
                ....*....|....*....|..
gi 6323703  468 FVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13896  83 VSVDFDADNPGRWAFHCHNLYH 104
CuRO_2_MaLCC_like cd13880
The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 160-271 1.46e-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: 74.59  E-value: 1.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  160 LSEWYHDLVTDLTksfmSVYNPTGAEPIPQNLIVNNTMNL----------TWEVQPDTTYLLRIVNVGGFVSQYFWIEDH 229
Cdd:cd13880   6 LTDWYHRSAFELF----SEELPTGGPPPMDNILINGKGKFpcstgagsyfETTFTPGKKYRLRLINTGVDTTFRFSIDGH 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 6323703  230 EMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNF 271
Cdd:cd13880  82 NLTVIAADFVPIVPYTTDSLNIGIGQRYDVIVEANQDPVGNY 123
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 55-146 4.62e-15

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


Pssm-ID: 259921 [Multi-domain]  Cd Length: 114  Bit Score: 71.55  E-value: 4.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   55 PDITVNKGDRVQIYLTNGMNNtNTSMHFHGLFQNgtASMDGVPFLTqcpIAPGSTMLYNFTVDYNVGTYWYHSHTDG--- 131
Cdd:cd13852  25 PILRLRKGQKVRITFKNNLPE-PTIIHWHGLHVP--AAMDGHPRYA---IDPGETYVYEFEVLNRAGTYWYHPHPHGlta 98

                        90
                ....*....|....*.
gi 6323703  132 -QYEDGMKGLFIIKDD 146
Cdd:cd13852  99 kQVYRGLAGLFLVTDE 114
CuRO_1_Tth-MCO_like cd13853
The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 49-144 1.82e-14

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


Pssm-ID: 259922 [Multi-domain]  Cd Length: 139  Bit Score: 70.74  E-value: 1.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   49 NGQFPWPDITVNKGDRVQIYLTNGM------------------NNTNtsMHFHGLFQNGTASMDGVpFLTqcpIAPGSTM 110
Cdd:cd13853  26 NGSIPGPTLRVRPGDTLRITLKNDLppegaaneapapntphcpNTTN--LHFHGLHVSPTGNSDNV-FLT---IAPGESF 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 6323703  111 LYNFTVDYN--VGTYWYHSH----TDGQYEDGMKGLFIIK 144
Cdd:cd13853 100 TYEYDIPADhpPGTYWYHPHlhgsTALQVAGGMAGALVVE 139
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 382-489 3.68e-14

The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family includes bacteria multicopper oxidases (MCOs) represented by McoC from pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic multicopper oxidase, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. They are capable of oxidizing a vast range of substrates, varying from aromatic compunds to inorganic compounds such as metals. Most MCOs have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259969 [Multi-domain]  Cd Length: 125  Bit Score: 69.35  E-value: 3.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  382 NSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPFHLHGHAFQTIQRDRTyddalgevphsfdpdnhPAFPEYPMRRDTLY 461
Cdd:cd13902  24 NGKTFDMNRIDFVAKVGEVEVWEVTNTSHMDHPFHLHGTQFQVLEIDGN-----------------PQKPEYRAWKDTVN 86

                        90       100
                ....*....|....*....|....*...
gi 6323703  462 VRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13902  87 LPPGEAVRIATRQDDPGMWMYHCHILEH 114
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 343-489 4.63e-14

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


Pssm-ID: 259962 [Multi-domain]  Cd Length: 188  Bit Score: 70.81  E-value: 4.63e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  343 VVMDN---LKNGVNYAFFNNITY--TAPKVPTLMTVLSSGDQ---------ANNSeiYGSNTHTFILEKDEIVEIVLNNQ 408
Cdd:cd13895   6 IIITIqqlNADGGVLWAQNGLTWteTLPSVPYLVQLYEYGTSllpdyeaalANGG--FDPETNTFPAKLGEVLDIVWQNT 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  409 DTGT-----HPFHLHGHAFqtiqrdrtYDdaLGEVPHSFDP---DNHPAFPEY-PMRRDTLYVR-------------PQS 466
Cdd:cd13895  84 ASPTggldaHPWHAHGAHY--------YD--LGSGLGTYSAtalANEEKLRGYnPIRRDTTMLYryggkgyypppgtGSG 153

                       170       180
                ....*....|....*....|...
gi 6323703  467 NFVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13895 154 WRAWRLRVDDPGVWMLHCHILQH 176
PRK10965 PRK10965
multicopper oxidase; Provisional
 19-146 1.26e-13

multicopper oxidase; Provisional


Pssm-ID: 236810 [Multi-domain]  Cd Length: 523  Bit Score: 73.90  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    19 AQAETHTF---NWTTGWDYrnvdglksrpvitcNGQFPWPDITVNKGDRVQIYLTNGMNNTnTSMHFHGLFQNGTAsmDG 95
Cdd:PRK10965  52 IQAGQSSFagkTATATWGY--------------NGNLLGPAVRLQRGKAVTVDITNQLPEE-TTLHWHGLEVPGEV--DG 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6323703    96 VPfltQCPIAPGSTMLYNFTVDYNVGTYWYHSHTDG----QYEDGMKGLFIIKDD 146
Cdd:PRK10965 115 GP---QGIIAPGGKRTVTFTVDQPAATCWFHPHQHGktgrQVAMGLAGLVLIEDD 166
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 393-489 3.03e-13

The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida, which is involved in the oxidation of Mn(II). However, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCO catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 67.02  E-value: 3.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  393 FILEKDEIVEIVLNNQDTGTHPFHLHGHAFQTIQRDRtyddalGEVPHsfdpdnhpafpeyPMRRDTLYVRPQSNFVIRF 472
Cdd:cd13906  49 ATLKRGRSYVLRLVNETAFLHPMHLHGHFFRVLSRNG------RPVPE-------------PFWRDTVLLGPKETVDIAF 109

                        90
                ....*....|....*..
gi 6323703  473 KADNPGVWFFHCHIEWH 489
Cdd:cd13906 110 VADNPGDWMFHCHILEH 126
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 389-489 4.48e-13

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: 66.51  E-value: 4.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  389 NTHTFILEKDEIVEIVLNNQDTGTHPFHLHGHAFQTIQRDrtyddalgevphsfdpdNHPAFPEYPMRRDTLYVRPQSNF 468
Cdd:cd04202  39 ATPPLVVKEGDRVRIRLINLSMDHHPMHLHGHFFLVTATD-----------------GGPIPGSAPWPKDTLNVAPGERY 101

                        90       100
                ....*....|....*....|.
gi 6323703  469 VIRFKADNPGVWFFHCHIEWH 489
Cdd:cd04202 102 DIEFVADNPGDWMFHCHKLHH 122
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 41-144 3.83e-12

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 63.65  E-value: 3.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   41 KSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTsMHFHGLfqNGTASMDGVPfltQCPIAPGSTMLYNFTV-DYN 119
Cdd:cd13855  19 KPTEFWAYNGSVPGPLIEVFEGDTVEITFRNRLPEPTT-VHWHGL--PVPPDQDGNP---HDPVAPGNDRVYRFTLpQDS 92

                        90       100
                ....*....|....*....|....*....
gi 6323703  120 VGTYWYHSHTDG----QYEDGMKGLFIIK 144
Cdd:cd13855  93 AGTYWYHPHPHGhtaeQVYRGLAGAFVVK 121
CuRO_2_Tv-LCC_like cd13882
The second cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 158-273 2.29e-11

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: 62.43  E-value: 2.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  158 LSLSEWYHDLVTDLTKsfmsvyNPTGAEPIPQNLIVN--------NTMNL-TWEVQPDTTYLLRIVNVGGFVSQYFWIED 228
Cdd:cd13882   3 ITLGDWYHTAAPDLLA------TTAGVPPVPDSGTINgkgrfdggPTSPLaVINVKRGKRYRFRVINISCIPSFTFSIDG 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6323703  229 HEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVhTKNDTDKNFAI 273
Cdd:cd13882  77 HNLTVIEADGVETKPLTVDSVQIYAGQRYSVVV-EANQPVDNYWI 120
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 44-143 4.07e-11

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: 60.36  E-value: 4.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   44 PVITCNGQFPWPDITVNKGDRVQIYLTNGMNNTNTsMHFHGlfqNGTASMDGVPFLtqcPIAPGSTMLYNFtVDYNVGTY 123
Cdd:cd11024  22 KAWTYNGTVPGPTLRATEGDLVRIHFINTGDHPHT-IHFHG---IHDAAMDGTGLG---PIMPGESFTYEF-VAEPAGTH 93

                        90       100
                ....*....|....*....|...
gi 6323703  124 WYHSHTDGQYED---GMKGLFII 143
Cdd:cd11024  94 LYHCHVQPLKEHiamGLYGAFIV 116
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 399-489 6.73e-11

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


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 60.61  E-value: 6.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  399 EIVEIVLNNQDTGTHPFHLHGHAFQTIQRDRTYDDAlgevphsfdpdnhpafpeypmrRDTLYVRPQSNFVIRFKADNPG 478
Cdd:cd13909  57 ETVRIEMVNNTGFPHGMHLHGHHFRAILPNGALGPW----------------------RDTLLMDRGETREIAFVADNPG 114

                        90
                ....*....|.
gi 6323703  479 VWFFHCHIEWH 489
Cdd:cd13909 115 DWLLHCHMLEH 125
CuRO_2_AAO cd13871
The second cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 153-271 1.72e-10

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: 59.86  E-value: 1.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  153 DEELSLSLSEWYHDLVTDLTKSFMSV------------------YN-------PTGAEPIPQNLIVNNTMNLTWEVQPDT 207
Cdd:cd13871   1 DGELNILLSDWWHKSIYEQETGLSSKpfrwvgepqslliegrgrYNcslapayPSSLPSPVCNKSNPQCAPFILHVSPGK 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323703  208 TYLLRIVNVGGFVSQYFWIEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTKNDTDKNF 271
Cdd:cd13871  81 TYRLRIASVTALSSLNFIIEGHNLTVVEADGNYVQPFEVSNLDIYSGETYSVLVTADQDPSRNY 144
CuRO_1_AAO_like_1 cd13846
The first cupredoxin domain of plant Ascorbate oxidase homologs; This subfamily is composed of ...
 26-125 3.05e-10

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: 57.80  E-value: 3.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   26 FNWTTGWDYRNVDGLKSRpVITCNGQFPWPDITVNKGDRVQIyltNGMNNTNTSMHFH--GLFQNGTASMDGVPFlTQCP 103
Cdd:cd13846   3 FDWNVSYITASPLGVPQQ-VIAINGQFPGPTINVTTNDNVVV---NVFNSLDEPLLLTwnGIQQRRNSWQDGVLG-TNCP 77

                        90       100
                ....*....|....*....|..
gi 6323703  104 IAPGSTMLYNFTVDYNVGTYWY 125
Cdd:cd13846  78 IPPGWNWTYKFQVKDQIGSFFY 99
CuRO_2_AAO_like_1 cd13872
The second cupredoxin domain of plant pollen multicopper oxidase homologous to ascorbate ...
 154-282 3.30e-10

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: 58.57  E-value: 3.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  154 EELSLSLSEWYHDLVTDLTKSfmsvyNPTGAE-PIPQNLIVN-------NTMNLTWEVQPDTTYLLRIVNVGGFVSQYFW 225
Cdd:cd13872   1 DEYTVLIGDWYKTDHKTLRQS-----LDKGRTlGRPDGILINgkgpygyGANETSFTVEPGKTYRLRISNVGLRTSLNFR 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6323703  226 IEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVhTKNDTDKNFAIM--QKFDDTML 282
Cdd:cd13872  76 IQGHKMLLVETEGSYTAQNTYDSLDVHVGQSYSVLV-TADQSPKDYYIVasSRFLSPEL 133
CuRO_2_LCC_plant cd13875
The second cupredoxin domain of the plant laccases; Laccase is a blue multi-copper enzyme that ...
 160-264 1.08e-09

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: 57.22  E-value: 1.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  160 LSEWYHDLVTDLTKSFMSvynpTGAEP-IPQNLIVN------------NTMNLTweVQPDTTYLLRIVNVGGFVSQYFWI 226
Cdd:cd13875   5 LGEWWNRDVNDVEDQALL----TGGGPnISDAYTINgqpgdlyncsskDTFVLT--VEPGKTYLLRIINAALNEELFFKI 78

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6323703  227 EDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTK 264
Cdd:cd13875  79 ANHTLTVVAVDASYTKPFTTDYILIAPGQTTDVLLTAD 116
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 382-489 1.32e-09

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


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 56.31  E-value: 1.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  382 NSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPFHLHGHAFQTIQRDRTyddalgevphsfdpdnhpafPEYPMRRDTLY 461
Cdd:cd13908  24 NGKSYPDEDPPLVVQQGRRYRLVFRNASDDAHPMHLHRHTFEVTRIDGK--------------------PTSGLRKDVVM 83

                        90       100
                ....*....|....*....|....*...
gi 6323703  462 VRPQSNFVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13908  84 LGGYQRVEVDFVADNPGLTLFHCHQQLH 111
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 47-143 2.42e-09

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


Pssm-ID: 259906 [Multi-domain]  Cd Length: 119  Bit Score: 55.29  E-value: 2.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   47 TCNGQFPWPDITVNKGDRVQIYLTNGMNNTNT-SMHFHGlfqngtASMDGVPFLTQcpIAPGSTMLYNFTVDYnVGTYWY 125
Cdd:cd11020  25 TFNGQVPGPVIRVREGDTVELTLTNPGTNTMPhSIDFHA------ATGPGGGEFTT--IAPGETKTFSFKALY-PGVFMY 95

                        90       100
                ....*....|....*....|.
gi 6323703  126 HSHTDGQYE---DGMKGLFII 143
Cdd:cd11020  96 HCATAPVLMhiaNGMYGAIIV 116
CuRO_2_AAO_like_2 cd13873
The second cupredoxin domain of plant Ascorbate oxidase homologs; This family includes plant ...
 202-264 6.89e-09

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: 55.37  E-value: 6.89e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323703  202 EVQPDTTYLLRIVNVGGFVSQYFWIEDH-EMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTK 264
Cdd:cd13873  64 DVEPGKTYRFRFIGATALSFVSLGIEGHdNLTIIEADGSYTKPAETDHLQLGSGQRYSFLLKTK 127
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 400-489 6.90e-09

The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus; Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259965 [Multi-domain]  Cd Length: 164  Bit Score: 55.34  E-value: 6.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  400 IVEIVLNNQDTGT--HPFHLHG-HAF-----QTIQRDRTYDDALGEVPHSFDPDNhpafpeyPMRRDTLYVRPQSN---- 467
Cdd:cd13898  58 WVDLIFQVTGPPQppHPIHKHGnKAFvigtgTGPFNWSSVAEAAEAAPENFNLVN-------PPLRDTFTTPPSTEgpsw 130

                        90       100
                ....*....|....*....|..
gi 6323703  468 FVIRFKADNPGVWFFHCHIEWH 489
Cdd:cd13898 131 LVIRYHVVNPGAWLLHCHIQSH 152
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 57-142 5.79e-08

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 51.08  E-value: 5.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   57 ITVNKGDRVQIYLTNGmNNTNTSMHFHGLFQNG-TASMDGVPFLTQCP-IAPGSTmlYNFTVDY-NVGTYWYHSHTDGQY 133
Cdd:cd00920  25 LVVPVGDTVRVQFVNK-LGENHSVTIAGFGVPVvAMAGGANPGLVNTLvIGPGES--AEVTFTTdQAGVYWFYCTIPGHN 101


                ....*....
gi 6323703  134 EDGMKGLFI 142
Cdd:cd00920 102 HAGMVGTIN 110
CuRO_2_Diphenol_Ox cd13883
The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 158-267 7.67e-08

The second cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Laccase is a multicopper oxidase (MCO) composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.


Pssm-ID: 259950 [Multi-domain]  Cd Length: 164  Bit Score: 52.34  E-value: 7.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  158 LSLSEWYHDLVTDLTKSFMSV--YNPTGAEPIPQNLIVN-----------------NTMNLTWEVQPDTTYLLRIVNVGG 218
Cdd:cd13883   3 LFISDWYHDQSEVIVAGLLSPqgYKGSPAAPSPDSALINgigqfncsaadpgtcctQTSPPEIQVEAGKRTRFRLINAGS 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6323703  219 FVSQYFWIEDHEMTVVEIDGITTEK-NVTDMLYITVAQRYTVLVHTKNDT 267
Cdd:cd13883  83 HAMFRFSVDNHTLNVVEADDTPVYGpTVVHRIPIHNGQRYSVIIDTTSGK 132
CuRO_1_MCO_like_1 cd13862
The first cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 46-143 1.50e-07

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


Pssm-ID: 259931 [Multi-domain]  Cd Length: 123  Bit Score: 50.59  E-value: 1.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   46 ITCNGQFPWPDITVNKGDRVQIYLTNgMNNTNTSMHFHGLFQngTASMDGVPFLTQCPIAPGSTMLYNFTVDyNVGTYWY 125
Cdd:cd13862  23 LGYNGQVPGPLLRMRQGVSVTVDVFN-DTDIPEYVHWHGLPL--PADVDGAMEEGTPSVPPHGHRRYRMTPR-PAGFRWY 98

                        90       100
                ....*....|....*....|....*
gi 6323703  126 HSH-------TDGQYEdGMKGLFII 143
Cdd:cd13862  99 HTHvmtmddlTRGQYS-GLFGFVYI 122
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 382-486 1.79e-07

The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus; The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259967 [Multi-domain]  Cd Length: 123  Bit Score: 50.32  E-value: 1.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  382 NSEIYGSNTHTFILEKDEIVEIVLNNQDTGTHPFHLHGHAFQTIQRDRtyddalgevphsfDPDNHPAFpeypmrRDTLY 461
Cdd:cd13900  23 NGKPFDPDRPDRTVRLGTVEEWTLINTSGEDHPFHIHVNPFQVVSING-------------KPGLPPVW------RDTVN 83

                        90       100
                ....*....|....*....|....*..
gi 6323703  462 VRPQSNFVIR--FKaDNPGVWFFHCHI 486
Cdd:cd13900  84 VPAGGSVTIRtrFR-DFTGEFVLHCHI 109
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 47-143 1.82e-07

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


Pssm-ID: 259864 [Multi-domain]  Cd Length: 120  Bit Score: 50.18  E-value: 1.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   47 TCNGQFPWPDITVNKGDRVQIYLTNGMNNTNT-SMHFHGLFQngtASMDGVpfLTQcpIAPGSTMLYNFTVdYNVGTYWY 125
Cdd:cd04201  25 TFDGDIPGPMLRVREGDTVELHFSNNPSSTMPhNIDFHAATG---AGGGAG--ATF--IAPGETSTFSFKA-TQPGLYVY 96

                        90       100
                ....*....|....*....|.
gi 6323703  126 HSHTDG---QYEDGMKGLFII 143
Cdd:cd04201  97 HCAVAPvpmHIANGMYGLILV 117
CuRO_2_Abr2_like cd13876
The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 201-273 7.56e-07

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: 48.74  E-value: 7.56e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323703  201 WEVQPDTT--YL-LRIVNVGGFVSQYFWIEDHEMTVVEIDG--ITTEKnvTDMLYITVAQRYTVLVHTKNDTDkNFAI 273
Cdd:cd13876  44 LIVIVDPGerWVsLNFINAGGFHTLAFSIDEHPMWVYAVDGgyIEPQL--VDAISITNGERYSVLVKLDKPPG-DYTI 118
CuRO_3_CueO_FtsP cd13890
The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 401-489 1.28e-06

The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins; CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. FtsP does not contain any copper binding sites.


Pssm-ID: 259957 [Multi-domain]  Cd Length: 124  Bit Score: 47.63  E-value: 1.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  401 VEI-VLNNQDTGTHPFHLHGHAFQTIQRdrtyddalgevphsfdpDNHPAFPEYPMRRDTLYVRP--QSNFVIRFK--AD 475
Cdd:cd13890  37 TEIwEVTNTDGMPHPFHIHGVQFRILSR-----------------NGQPPPPNEAGWKDTVWVPPgeTVRILVKFDhyAD 99

                        90
                ....*....|....
gi 6323703  476 NPGVWFFHCHIEWH 489
Cdd:cd13890 100 PTGPFMYHCHILEH 113
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 55-143 2.01e-06

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


Pssm-ID: 259891 [Multi-domain]  Cd Length: 175  Bit Score: 48.57  E-value: 2.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   55 PDITVNKGDRVQIYLTNGMNNTNTSMHFHGLFQngTASMDGVPFLTQCPIAPGSTMLYNFTVDYNVG---------TYWY 125
Cdd:cd04229  74 PVIRAEVGDTIKVVFKNNLDEFPVNMHPHGGLY--SKDNEGTTDGAGDVVAPGETYTYRWIVPEDAGpgpgdpssrLWLY 151

                        90       100
                ....*....|....*....|
gi 6323703  126 HSHTDGQYED--GMKGLFII 143
Cdd:cd04229 152 HSHVDVFAHTnaGLVGPIIV 171
CuRO_2_tcLCC_insect_like cd13884
The second cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium ...
 155-273 5.27e-05

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: 43.76  E-value: 5.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  155 ELSLSLSEWYHDLVTDLtksFMSVYNPTGaEPIPQNLIVN-------------NTMNLTW-EVQPDTTYLLRIVNVGGFV 220
Cdd:cd13884   1 EHVILIQDWTHELSSER---FVGRGHNGG-GQPPDSILINgkgryydpktgntNNTPLEVfTVEQGKRYRFRLINAGATN 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 6323703  221 SQY-FWIEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLVHTkNDTDKNFAI 273
Cdd:cd13884  77 CPFrVSIDGHTLTVIASDGNDVEPVEVDSIIIYPGERYDFVLNA-NQPIGNYWI 129
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 392-489 1.82e-04

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 41.45  E-value: 1.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  392 TFILEKDEIVEIVLNNQDTGTHPFHLHGHAfqtiqrdrtyddalgevphsfDPDNHPAFPEYPMRRDTLYVRPQSNFVIR 471
Cdd:cd00920  24 VLVVPVGDTVRVQFVNKLGENHSVTIAGFG---------------------VPVVAMAGGANPGLVNTLVIGPGESAEVT 82

                        90
                ....*....|....*...
gi 6323703  472 FKADNPGVWFFHCHIEWH 489
Cdd:cd00920  83 FTTDQAGVYWFYCTIPGH 100
CuRO_2_CopA cd13874
The second cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 196-261 2.28e-04

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: 41.13  E-value: 2.28e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323703  196 TMNLTWEVQPDTTYLLRIVNVGGfvSQYFW--IEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLV 261
Cdd:cd13874  22 EDNWTGLFKPGERVRLRFINAAA--STYFDvrIPGGKMTVVAADGQDVRPVEVDEFRIGVAETYDVIV 87
CuRO_3_CotA_like cd13891
The third Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat ...
 399-486 4.49e-04

The third Cupredoxin domain of bacterial laccases including CotA, a bacterial endospore coat component; CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and is required for spore resistance against hydrogen peroxide and UV light. CotA belongs to the laccase-like multicopper oxidase (MCO) family, which are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259958 [Multi-domain]  Cd Length: 143  Bit Score: 40.74  E-value: 4.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  399 EIVEIVlnNQDTGTHPFHLHGHAFQTIQRDR-TYDDALGEVPHSFDPDNHPAFPEYPMRRDTLYVRPQS--NFVIRFKAD 475
Cdd:cd13891  42 EIWEII--NLTPDAHPIHLHLVQFQVLDRQPfDVDEYNATGEIYYTGPPRPPAPNERGWKDTVRAYPGEvtRIIVRFDGP 119

                        90
                ....*....|..
gi 6323703  476 NPG-VWffHCHI 486
Cdd:cd13891 120 EGGyVW--HCHI 129
CuRO_3_BOD cd13889
The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the ...
 401-485 4.54e-04

The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. It is used in diagnosing jaundice through the determination of bilirubin in serum. BOD is a member of the multicopper oxidase (MCO) family that also includes laccase, ascorbate oxidase and ceruloplasmin. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259956 [Multi-domain]  Cd Length: 124  Bit Score: 40.37  E-value: 4.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  401 VEI-VLNNQDTG-THPFHLHGHAFQTIQRDRtyddalgevphsfdpdNHPAFPEY-PMRRDTLYVRPQSNFVIRFK-ADN 476
Cdd:cd13889  37 VEIwTLINGGGGwSHPIHIHLEDFQILSRNG----------------GSRAVPPYeRGRKDVVYLGPGEEVRVLMRfRPF 100


                ....*....
gi 6323703  477 PGVWFFHCH 485
Cdd:cd13889 101 RGKYMMHCH 109
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 49-137 5.61e-04

The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.


Pssm-ID: 259963 [Multi-domain]  Cd Length: 115  Bit Score: 39.93  E-value: 5.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   49 NGQfPWPD---ITVNKGDRVQIYLTNgmnntNTSM----HFHGL-FQNGTASMDGVPFLTQCPIAPGSTMLYNFTVDyNV 120
Cdd:cd13896  20 NGK-AYPDadpLRVREGERVRIVFVN-----DTMMahpmHLHGHfFQVENGNGEYGPRKDTVLVPPGETVSVDFDAD-NP 92

                        90
                ....*....|....*..
gi 6323703  121 GTYWYHSHTDGQYEDGM 137
Cdd:cd13896  93 GRWAFHCHNLYHMEAGM 109
PRK10883 PRK10883
FtsI repressor; Provisional
 38-146 5.84e-04

FtsI repressor; Provisional


Pssm-ID: 182808 [Multi-domain]  Cd Length: 471  Bit Score: 42.77  E-value: 5.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703    38 DGLKSRPVITCNGQFPWPDITVNKGDRVQIYLTNGMNNtNTSMHFHGLFQNGTAsMDGVPFLtqcpIAPGSTMLYNFTVD 117
Cdd:PRK10883  60 TGGTKASVWGINGRYLGPTIRVWKGDDVKLIYSNRLTE-PVSMTVSGLQVPGPL-MGGPARM----MSPNADWAPVLPIR 133

                         90       100       110
                 ....*....|....*....|....*....|...
gi 6323703   118 YNVGTYWYHSHTDG----QYEDGMKGLFIIKDD 146
Cdd:PRK10883 134 QNAATCWYHANTPNrmaqHVYNGLAGMWLVEDE 166
CuRO_2_CopA_like_1 cd13870
The second cupredoxin domain of CopA copper resistance protein like family; The members of ...
 200-261 9.89e-04

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: 39.24  E-value: 9.89e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323703  200 TWEVQPDTTYLLRIVNVGGFVSQYFWIEDHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLV 261
Cdd:cd13870  30 VFTARPGDRLRLRLINAAGDTAFRVALAGHRLTVTHTDGFPVEPVEVDALLIGMGERYDAIV 91
CuRO_2_McoC_like cd13881
The second cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 191-261 2.65e-03

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


Pssm-ID: 259948 [Multi-domain]  Cd Length: 142  Bit Score: 38.75  E-value: 2.65e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323703  191 LIVNNTMNLTWEVQPDTTYLLRIVNVGgfVSQYFW--IEDHEMTVVEIDGITTEKNVT-DMLYITVAQRYTVLV 261
Cdd:cd13881  34 VLVNGQLNPTITVRPGEVQRWRIVNAA--SARYFRlaLDGHKFRLIGTDGGLLEAPREvDELLLAPGERAEVLV 105
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 53-140 4.04e-03

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers, and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities. This subfamily has lost the type 1 (T1) copper binding site in domain 1 that is present in other two-domain laccases.


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 38.02  E-value: 4.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   53 PWPDITVNKGDRVQIYLTNGMnNTNTSMHFHGLfqNGTASMDGVpFLTQCPIAPGSTMLYNF------------TVDYNV 120
Cdd:cd14449  28 PGPVIEVREGDTLKILFRNTL-DVPASLHPHGV--DYTTASDGT-GMNASIVAPGDTRIYTWrthggyrradgsWAEGTA 103

                        90       100
                ....*....|....*....|
gi 6323703  121 GTYWYHSHTDGQyEDGMKGL 140
Cdd:cd14449 104 GYWHYHDHVFGT-EHGTEGL 122
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 55-143 4.29e-03

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


Pssm-ID: 259909 [Multi-domain]  Cd Length: 118  Bit Score: 37.59  E-value: 4.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   55 PDITVNKGDRVQIYLTnGMNNT--NTSMHFHGlfqnGTASMDGVPFLTQCPIAPGSTMLYNFTVDyNVGTYWYHSHTDGQ 132
Cdd:cd11023  34 PGVTIAKGKRVRWHLV-AYGNEvdFHTPHWHG----QTVEADKSRRTDVAELMPASMRVADMTAA-DVGTWLLHCHVHDH 107

                        90
                ....*....|.
gi 6323703  133 YEDGMKGLFII 143
Cdd:cd11023 108 YMAGMMTQFAV 118
CuRO_2_MCO_like_2 cd13887
The second cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases ...
 202-261 5.04e-03

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


Pssm-ID: 259954 [Multi-domain]  Cd Length: 114  Bit Score: 37.30  E-value: 5.04e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323703  202 EVQPDTTYLLRIVNvgGFVSQYFWIE--DHEMTVVEIDGITTEKNVTDMLYITVAQRYTVLV 261
Cdd:cd13887  27 RVEPGGRVRLRVIN--GSTATNFHIDlgDLKGTLIAVDGNPVQPVEGRRFPLATAQRLDLLV 86
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 380-486 5.62e-03

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: 37.46  E-value: 5.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703  380 ANNSEIYGSNTHtfILEKDEIVeIVLNNQDTGTHPFHLHGhafqTIQRDRTYDDAlgeVPHSFDPDnhpafpeypmrrdt 459
Cdd:cd13859  24 AFNGQVPGPLIH--VKEGDDLV-VHVTNNTTLPHTIHWHG----VLQMGSWKMDG---VPGVTQPA-------------- 79

                        90       100
                ....*....|....*....|....*..
gi 6323703  460 lyVRPQSNFVIRFKADNPGVWFFHCHI 486
Cdd:cd13859  80 --IEPGESFTYKFKAERPGTLWYHCHV 104
CuRO_3_MCO_like_1 cd13907
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 413-485 5.63e-03

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


Pssm-ID: 259974 [Multi-domain]  Cd Length: 154  Bit Score: 37.85  E-value: 5.63e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323703  413 HPFHLHGHAFQTIQRDRTYDDALG--EVPHSFDPDNHpafpeypmrRDTLYVRPQSNFVI--RFKaDNPGVWFFHCH 485
Cdd:cd13907  72 HPIHLHGVQFQVLERSVGPKDRAYwaTVKDGFIDEGW---------KDTVLVMPGERVRIikPFD-DYKGLFLYHCH 138
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 55-143 6.35e-03

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


Pssm-ID: 259863 [Multi-domain]  Cd Length: 141  Bit Score: 37.39  E-value: 6.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323703   55 PDITVNKGDRVQIYLTN-GMNNTNTSMHFHG-LFQNGTASMDGVPfltqcpIAPGSTMLYNFTVDyNVGTYWYHSHTDGQ 132
Cdd:cd04200  58 PGLTMCAGDRVRWHLLGmGNEVDVHSIHFHGqTFLYKGYRIDTLT------LFPATFETVEMVPS-NPGTWLLHCHNSDH 130

                        90
                ....*....|.
gi 6323703  133 YEDGMKGLFII 143
Cdd:cd04200 131 RHAGMQAYFLV 141
 
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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