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Conserved domains on  [gi|465989294|gb|EMP38009|]
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Ceruloplasmin [Chelonia mydas]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1160-1330 5.92e-99

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


:

Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 314.41  E-value: 5.92e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1160 KTYYIAAVEVEWDYSPSRTWEHERHEFHEESPGNPFLNKEDKFIGSKYKKVVYRKYTDSTFSTPKERAEEQQHLEILGPL 1239
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1240 LLANVGDKVTIVFKNLATRPYSIHAHGVKTDSSTVAVTQPGETRTYIWKIPDRSGSGKGDPSCIPWAYYSVVDKVKDTYS 1319
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                         170
                  ....*....|.
gi 465989294 1320 GLIGTLVVCPK 1330
Cdd:cd04225   161 GLIGPLVICRR 171
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 522-683 1.63e-97

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.


The actual alignment was detected with superfamily member cd04222:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 183  Bit Score: 310.89  E-value: 1.63e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  522 GYIFKDTAggQARVFLQRGPDRIGSTYKKAVYTQFTDNSFNKTVEKPSWLGFLGPIIKAEVGDFIIVHLKNFASRSYTLH 601
Cdd:cd04222    24 NQTFDDDE--HASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKAEVGDVIVVHLKNFASRPYSLH 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  602 PHGVAYTKENEGAFYPDNTKDLLKKDDAVKPGELYTYRWDVTEDHGPAEGDSNCMTRIYHSHTDAPRDVASGLVGPLITC 681
Cdd:cd04222   102 PHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIYHSHIDAPKDIASGLIGPLIIC 181


                  ..
gi 465989294  682 RK 683
Cdd:cd04222   182 KK 183
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1341-1485 4.58e-97

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


:

Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 308.34  E-value: 4.58e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1341 RVEFALLFMVFDENESWYLDENIKTYSANPDKVNKEDEEFIESNKMHAINGKLFGNLHGLTMHVGDKVSWYLMGMGNEVD 1420
Cdd:cd11012     1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 465989294 1421 MHTAHFHGHSFDYKRTGVYRADVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTVL 1485
Cdd:cd11012    81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1003-1146 9.38e-95

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


:

Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 301.71  E-value: 9.38e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1003 DKEFFLLATVFDENLSWYLDDNILMFLIKPNDIDKEDEDFQESNKMHSINGYMYGNQPGLEMCKGNTVSWHLIGLGSEVD 1082
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 465989294 1083 IHGIYFSENTFLTKGTRRDTTNLFPHTTLTAIMEPDTEGVFEVECLTTDHYTGGMKQKYKVKKC 1146
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 695-835 1.60e-91

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


:

Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 292.45  E-value: 1.60e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  695 DAEFILMFSVMDENLSWYLDDSIEKYCSEPAKVDKENEDFQESNKMHSINGYMYGYLPNLTMCEEDKVKWHLFGMGNEAD 774
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294  775 VHSAYFHGQVFTERNHRVDSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAIFEV 835
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 851-1000 2.16e-79

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.


The actual alignment was detected with superfamily member cd04224:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 197  Bit Score: 260.10  E-value: 2.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  851 VRHYYLAAEEIIWNYGPSAINHFTGQQLVI-DSESQTFFEQNEKRIGGSYKKAVYKEYTDGTFTKCKKRFPEEEHLGLLG 929
Cdd:cd04224     3 VRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGILG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  930 --------------------------------------------TEAPSSHVSPGATYTYEWKVSEDVGPTQEDPDCLTW 965
Cdd:cd04224    83 pviraevgdtikvtfrnkasrpfsiqphgvfyeknyegamyrdgDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCLTY 162

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 465989294  966 LYYSAADSVKDTNSGLVGPLLVCRKGTLLPSGKQK 1000
Cdd:cd04224   163 LYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
L6_membrane pfam05805
L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, ...
 276-449 5.85e-68

L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily it has now been found that that they are not significantly related to genuine tetraspanins, but instead constitute their own L6 family. Several members of this family have been implicated in human cancer.


:

Pssm-ID: 461745  Cd Length: 192  Bit Score: 227.06  E-value: 5.85e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   276 MGANILLYFPNGETRFASEHQLSKYVACLHGIIGGGILIFLPAAVFIGLEYDNCCGCrghenCGKSCAMLSSVLAAFIGI 355
Cdd:pfam05805   22 IIANILLLFPNGEVTYLSEGHISCEVWYFGGIIGGGLLVLLPATVFLLAGRKGGCCS-----CGNRCGMFLSILFSAIGV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   356 LGSGYCFIISALGLSHGPYCLSAV-EQNWVYPFTNSS-GGYLLERDRWSECREPRNIVEWNLTLFSILLVLGGIELILCS 433
Cdd:pfam05805   97 LGAGYCFIVSALALAEGPLCLTNGgSTSWGYPFKNNFnGNYLFNQSLWSVCLEPENIVEWHVTLFSILLLVSGLELLLCL 176

                          170
                   ....*....|....*.
gi 465989294   434 IQVINGFLGGICGVCC 449
Cdd:pfam05805  177 IQVVNGLLGCLCGTCK 192
Ggt super family cl42304
Gamma-glutamyltranspeptidase [Amino acid transport and metabolism];
47-236 8.42e-18

Gamma-glutamyltranspeptidase [Amino acid transport and metabolism];


The actual alignment was detected with superfamily member COG0405:

Pssm-ID: 440174  Cd Length: 507  Bit Score: 88.57  E-value: 8.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   47 SSAHPL--QIGWDILKNGGNVVDAAMAIAAALNVTELCGTGVGGACFCLCYDANTKQVQGLNGR---------------- 108
Cdd:COG0405     3 ATAHPLasQAGLEILRAGGNAVDAAVAAAAALAVVEPHSSGIGGGGFALIYDAKDGKVTALDGRgtapaaatpdmyldag 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  109 --------------------------FPSMELVQMCE---------------------------RKFPGYKiQLF----- 130
Cdd:COG0405    83 deipvrgplavgvpgtvagweaaherYGTLPLAELLApairlaedgfpvsprlaallaaaaerlARDPGAA-AIFlpdgr 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  131 -----------------QELAKSGKKSFSEGCVAEVIIETVQRNGGLMDLEDFKSHVTDE-------------------- 173
Cdd:COG0405   162 ppkagdilrqpdlaatlRRIAEEGADAFYRGEIAEAIVAAVQAAGGLLTLEDLAAYRAEWreplsgtyrgytvysmppps 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  174 -------------------------------IE-------------GNAEHYKV------SDNYNK-------------- 189
Cdd:COG0405   242 qgiallqilnilegfdlaalgpdsaeyvhllAEamklafadrdrylGDPDFVDVpvegllSPAYAAeraalidpdratps 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 465989294  190 ---GNLLPVGS-DTVYFTVVDAQGNASSFINSNYMGFGIGLEPGGCGFTLQ 236
Cdd:COG0405   322 prpGDPTGPESgDTTHLSVVDRDGNAVSLTQSIYGGFGSGVVVPGTGFLLN 372
L6_membrane super family cl05399
L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, ...
 472-532 1.46e-15

L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily it has now been found that that they are not significantly related to genuine tetraspanins, but instead constitute their own L6 family. Several members of this family have been implicated in human cancer.


The actual alignment was detected with superfamily member pfam05805:

Pssm-ID: 461745  Cd Length: 192  Bit Score: 76.84  E-value: 1.46e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 465989294   472 CCqseSCNKTYRSFISVVLALLGIAFSGYNVIISTLGLLQGPFCNTPAG---WGYIFKDTAGGQ 532
Cdd:pfam05805   76 CC---SCGNRCGMFLSILFSAIGVLGAGYCFIVSALALAEGPLCLTNGGstsWGYPFKNNFNGN 136
 
Name Accession Description Interval E-value
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1160-1330 5.92e-99

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 314.41  E-value: 5.92e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1160 KTYYIAAVEVEWDYSPSRTWEHERHEFHEESPGNPFLNKEDKFIGSKYKKVVYRKYTDSTFSTPKERAEEQQHLEILGPL 1239
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1240 LLANVGDKVTIVFKNLATRPYSIHAHGVKTDSSTVAVTQPGETRTYIWKIPDRSGSGKGDPSCIPWAYYSVVDKVKDTYS 1319
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                         170
                  ....*....|.
gi 465989294 1320 GLIGTLVVCPK 1330
Cdd:cd04225   161 GLIGPLVICRR 171
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 522-683 1.63e-97

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 310.89  E-value: 1.63e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  522 GYIFKDTAggQARVFLQRGPDRIGSTYKKAVYTQFTDNSFNKTVEKPSWLGFLGPIIKAEVGDFIIVHLKNFASRSYTLH 601
Cdd:cd04222    24 NQTFDDDE--HASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKAEVGDVIVVHLKNFASRPYSLH 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  602 PHGVAYTKENEGAFYPDNTKDLLKKDDAVKPGELYTYRWDVTEDHGPAEGDSNCMTRIYHSHTDAPRDVASGLVGPLITC 681
Cdd:cd04222   102 PHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIYHSHIDAPKDIASGLIGPLIIC 181


                  ..
gi 465989294  682 RK 683
Cdd:cd04222   182 KK 183
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1341-1485 4.58e-97

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 308.34  E-value: 4.58e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1341 RVEFALLFMVFDENESWYLDENIKTYSANPDKVNKEDEEFIESNKMHAINGKLFGNLHGLTMHVGDKVSWYLMGMGNEVD 1420
Cdd:cd11012     1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 465989294 1421 MHTAHFHGHSFDYKRTGVYRADVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTVL 1485
Cdd:cd11012    81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1003-1146 9.38e-95

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


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 301.71  E-value: 9.38e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1003 DKEFFLLATVFDENLSWYLDDNILMFLIKPNDIDKEDEDFQESNKMHSINGYMYGNQPGLEMCKGNTVSWHLIGLGSEVD 1082
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 465989294 1083 IHGIYFSENTFLTKGTRRDTTNLFPHTTLTAIMEPDTEGVFEVECLTTDHYTGGMKQKYKVKKC 1146
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 695-835 1.60e-91

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 292.45  E-value: 1.60e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  695 DAEFILMFSVMDENLSWYLDDSIEKYCSEPAKVDKENEDFQESNKMHSINGYMYGYLPNLTMCEEDKVKWHLFGMGNEAD 774
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294  775 VHSAYFHGQVFTERNHRVDSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAIFEV 835
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 851-1000 2.16e-79

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 260.10  E-value: 2.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  851 VRHYYLAAEEIIWNYGPSAINHFTGQQLVI-DSESQTFFEQNEKRIGGSYKKAVYKEYTDGTFTKCKKRFPEEEHLGLLG 929
Cdd:cd04224     3 VRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGILG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  930 --------------------------------------------TEAPSSHVSPGATYTYEWKVSEDVGPTQEDPDCLTW 965
Cdd:cd04224    83 pviraevgdtikvtfrnkasrpfsiqphgvfyeknyegamyrdgDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCLTY 162

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 465989294  966 LYYSAADSVKDTNSGLVGPLLVCRKGTLLPSGKQK 1000
Cdd:cd04224   163 LYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
L6_membrane pfam05805
L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, ...
 276-449 5.85e-68

L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily it has now been found that that they are not significantly related to genuine tetraspanins, but instead constitute their own L6 family. Several members of this family have been implicated in human cancer.


Pssm-ID: 461745  Cd Length: 192  Bit Score: 227.06  E-value: 5.85e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   276 MGANILLYFPNGETRFASEHQLSKYVACLHGIIGGGILIFLPAAVFIGLEYDNCCGCrghenCGKSCAMLSSVLAAFIGI 355
Cdd:pfam05805   22 IIANILLLFPNGEVTYLSEGHISCEVWYFGGIIGGGLLVLLPATVFLLAGRKGGCCS-----CGNRCGMFLSILFSAIGV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   356 LGSGYCFIISALGLSHGPYCLSAV-EQNWVYPFTNSS-GGYLLERDRWSECREPRNIVEWNLTLFSILLVLGGIELILCS 433
Cdd:pfam05805   97 LGAGYCFIVSALALAEGPLCLTNGgSTSWGYPFKNNFnGNYLFNQSLWSVCLEPENIVEWHVTLFSILLLVSGLELLLCL 176

                          170
                   ....*....|....*.
gi 465989294   434 IQVINGFLGGICGVCC 449
Cdd:pfam05805  177 IQVVNGLLGCLCGTCK 192
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1384-1488 7.40e-19

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: 84.41  E-value: 7.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  1384 NKMHAINGKLFG-NLHGLTMHVGDKVSWYLMGMGNevDMHTAHFHGHSFDYKRTGV----------------YRADVFDL 1446
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFQVLGRGGgpwpeedpktynlvdpVRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 465989294  1447 FPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTVLPKE 1488
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
Ggt COG0405
Gamma-glutamyltranspeptidase [Amino acid transport and metabolism];
47-236 8.42e-18

Gamma-glutamyltranspeptidase [Amino acid transport and metabolism];


Pssm-ID: 440174  Cd Length: 507  Bit Score: 88.57  E-value: 8.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   47 SSAHPL--QIGWDILKNGGNVVDAAMAIAAALNVTELCGTGVGGACFCLCYDANTKQVQGLNGR---------------- 108
Cdd:COG0405     3 ATAHPLasQAGLEILRAGGNAVDAAVAAAAALAVVEPHSSGIGGGGFALIYDAKDGKVTALDGRgtapaaatpdmyldag 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  109 --------------------------FPSMELVQMCE---------------------------RKFPGYKiQLF----- 130
Cdd:COG0405    83 deipvrgplavgvpgtvagweaaherYGTLPLAELLApairlaedgfpvsprlaallaaaaerlARDPGAA-AIFlpdgr 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  131 -----------------QELAKSGKKSFSEGCVAEVIIETVQRNGGLMDLEDFKSHVTDE-------------------- 173
Cdd:COG0405   162 ppkagdilrqpdlaatlRRIAEEGADAFYRGEIAEAIVAAVQAAGGLLTLEDLAAYRAEWreplsgtyrgytvysmppps 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  174 -------------------------------IE-------------GNAEHYKV------SDNYNK-------------- 189
Cdd:COG0405   242 qgiallqilnilegfdlaalgpdsaeyvhllAEamklafadrdrylGDPDFVDVpvegllSPAYAAeraalidpdratps 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 465989294  190 ---GNLLPVGS-DTVYFTVVDAQGNASSFINSNYMGFGIGLEPGGCGFTLQ 236
Cdd:COG0405   322 prpGDPTGPESgDTTHLSVVDRDGNAVSLTQSIYGGFGSGVVVPGTGFLLN 372
L6_membrane pfam05805
L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, ...
 472-532 1.46e-15

L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily it has now been found that that they are not significantly related to genuine tetraspanins, but instead constitute their own L6 family. Several members of this family have been implicated in human cancer.


Pssm-ID: 461745  Cd Length: 192  Bit Score: 76.84  E-value: 1.46e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 465989294   472 CCqseSCNKTYRSFISVVLALLGIAFSGYNVIISTLGLLQGPFCNTPAG---WGYIFKDTAGGQ 532
Cdd:pfam05805   76 CC---SCGNRCGMFLSILFSAIGVLGAGYCFIVSALALAEGPLCLTNGGstsWGYPFKNNFNGN 136
G_glu_transpept pfam01019
Gamma-glutamyltranspeptidase;
57-236 7.67e-13

Gamma-glutamyltranspeptidase;


Pssm-ID: 425991  Cd Length: 499  Bit Score: 73.01  E-value: 7.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294    57 DILKNGGNVVDAAMAIAAALNVTELCGTGVGGACFCLCYDANTKQVQGLNGR---------------------------- 108
Cdd:pfam01019    2 DILRKGGNAVDAAVAAALCLGVVEPHSSGIGGGGFMLIYDAKTGKVLVIDARetapaaatkdmfdgkgdsklsltgglav 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   109 -----------------------------------FP-------SMELVQMCERKFPGYKiQLF---------------- 130
Cdd:pfam01019   82 gvpgevaglaeahkrygrlpwadllepaiklardgFPvspalarALARAEERLRADPGLR-KIFlptgrvlkagellkqp 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   131 ------QELAKSGKKSFSEGCVAEVIIETVQRNGGLM---DLEDFKSHVTDEIEGNAEHYKVS----------------- 184
Cdd:pfam01019  161 alaktlELIAEEGPDAFYRGELAQQLVADLQANGGIItaeDLANYRVKIREPLSADYGGYTVYspppssggiallqilni 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   185 -DNYNKG--------------------------------------NLL-----------------------PVGSDTVYF 202
Cdd:pfam01019  241 lEGFDLSsllnsaeylhllieamklayadrtrylgdpdfvpvpveNLLspeyakeraklinpnaafpssyaPEDGGTTHF 320

                          330       340       350
                   ....*....|....*....|....*....|....
gi 465989294   203 TVVDAQGNASSFINSNYMGFGIGLEPGGCGFTLQ 236
Cdd:pfam01019  321 SVVDRDGNAVSFTSTINLGFGSGVVVPGTGILLN 354
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 573-679 4.36e-11

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: 61.49  E-value: 4.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   573 FLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGAFYPDNTKdllkkdDAVKPGELYTYRWDVTEDHGpaegd 652
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*..
gi 465989294   653 sncmTRIYHSHTDAPRdvASGLVGPLI 679
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAII 113
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1386-1486 3.48e-10

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: 64.19  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1386 MHAINGKLFGNLH-GLTMHVGDKVSWYLmgmGNEVDM-HTAHFHGHSFDY-KRTGV-----YRADVFDLFPGtfQTVEML 1457
Cdd:COG2132   317 VWTINGKAFDPDRpDLTVKLGERERWTL---VNDTMMpHPFHLHGHQFQVlSRNGKpppegGWKDTVLVPPG--ETVRIL 391

                          90       100       110
                  ....*....|....*....|....*....|..
gi 465989294 1458 ---PKYPGTWLLHCHVTDHIHGGMETTYTVLP 1486
Cdd:COG2132   392 frfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 573-703 2.18e-09

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: 61.49  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  573 FLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGafYPdntkdllkkDDAVKPGELYTYRWDVTEDHGpaegd 652
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDG--VP---------GDPIAPGETFTYEFPVPQPAG----- 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 465989294  653 sncmTRIYHSHTDA--PRDVASGLVGPLItcrkgtLDGGSDK--HIDAEFILMFS 703
Cdd:COG2132   106 ----TYWYHPHTHGstAEQVYRGLAGALI------VEDPEEDlpRYDRDIPLVLQ 150
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 702-831 2.36e-08

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: 54.63  E-value: 2.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   702 FSVMDENLSWYlDDSIEKYCSEPAKVDKENEDFQESNKMHSINGYMYGYLPNLTMCEEDKVKWHLFgMGNEADVHSAYFH 781
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294   782 GQ---------VFTErNHRVDSISLFPATFVDALMVPKN-PGEWLLSCQVN-DHIEGGMQA 831
Cdd:pfam00394   79 GHkmtvvevdgVYVN-PFTVDSLDIFPGQRYSVLVTANQdPGNYWIVASPNiPAFDNGTAA 138
g_glut_trans TIGR00066
gamma-glutamyltranspeptidase; Also called gamma-glutamyltranspeptidase (ggt). Some members of ...
 45-236 1.11e-07

gamma-glutamyltranspeptidase; Also called gamma-glutamyltranspeptidase (ggt). Some members of this family have antibiotic synthesis or resistance activities. In the case of a cephalosporin acylase from Pseudomonas sp., the enzyme was shown to retain some gamma-glutamyltranspeptidase activity. Other, more distantly related proteins have ggt-related activities and score below the trusted cutoff. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 129176  Cd Length: 516  Bit Score: 56.31  E-value: 1.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294    45 LTSSAHPL--QIGWDILKNGGNVVDAAMAIAAALNVTELCGTGVGGACFCLCYDANTKQVQGLNGR-----------F-- 109
Cdd:TIGR00066    2 MVASLHALasEIGEDILKEGGNAFDAAVAVGLALAVVEPFMTGLGGGGFMLISGKKTKDTTAIDFRerapakatrdmFld 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   110 -------------------------------------------PSMELVQ--------MCE----------------RKF 122
Cdd:TIGR00066   82 ksgnplpgksltgglaigvpgtvagleaalkkygtlplkdliePAIKLARngfpineaLADtlelyeevllttkedsKDI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   123 ---------PGYKIQL------FQELAKSGKKSFSEGCVAEVIIETVQRNGGLMDLEDFKSH---VTDEIEGNAEHYKVS 184
Cdd:TIGR00066  162 fnptgkplkEGDTLVQkdlaksLELIAENGPDAFYKGDIAESIIDTLQKNGGIMTKKDLAAYdveIRKPLSGDYRGYQVY 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   185 -------------------DNYN-------------------------------KGNLLPV------------------- 195
Cdd:TIGR00066  242 ttpppssggihllqalnilENFDlsqygdgsaetyqllaeamklsyadrsrylgDPEFVDVpleelldkryakelaqsik 321

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   196 -------------------GSDTVYFTVVDAQGNASSFINSNYMGFGIGLEPGGCGFTLQ 236
Cdd:TIGR00066  322 inkvdpkstiypgayqpneGSQTTHFSVVDRDGNAVSLTTTINLEFGSGVHAPDTGILLN 381
PLN02191 PLN02191
L-ascorbate oxidase
 573-703 9.06e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 53.48  E-value: 9.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  573 FLGPIIKAEVGDFIIVHLKN-FASRSYTLHPHGVaytkENEGAFYPDNTKDLLKKddAVKPGELYTYRWDVtEDHGpaeg 651
Cdd:PLN02191   51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGI----RQKGSPWADGAAGVTQC--AINPGETFTYKFTV-EKPG---- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 465989294  652 dsncmTRIYHSHTDAPRdvASGLVGPLITcrkGTLDGGSDKHI-DAEFILMFS 703
Cdd:PLN02191  120 -----THFYHGHYGMQR--SAGLYGSLIV---DVAKGPKERLRyDGEFNLLLS 162
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1234-1295 1.44e-06

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: 48.78  E-value: 1.44e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294  1234 EILGPLLLANVGDKVTIVFKNLATRPYSIHAHGVKTDSSTVA-----VTQ----PGETRTYIWKIPDRSGS 1295
Cdd:pfam07732   23 QFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMdgvpgVTQcpipPGQSFTYRFQVKQQAGT 93
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 573-679 1.04e-05

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: 50.14  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   573 FLGPIIKAEVGDFIIVHLKN-FASRSYTLHPHGVaytkENEGAFYPDNTKDLLKKddAVKPGELYTYRWDVtedhgpaeg 651
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGI----RQIGTPWADGTAGVTQC--AINPGETFIYNFVV--------- 93

                           90       100
                   ....*....|....*....|....*...
gi 465989294   652 dSNCMTRIYHSHTDAPRdvASGLVGPLI 679
Cdd:TIGR03388   94 -DRPGTYFYHGHYGMQR--SAGLYGSLI 118
 
Name Accession Description Interval E-value
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1160-1330 5.92e-99

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 314.41  E-value: 5.92e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1160 KTYYIAAVEVEWDYSPSRTWEHERHEFHEESPGNPFLNKEDKFIGSKYKKVVYRKYTDSTFSTPKERAEEQQHLEILGPL 1239
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1240 LLANVGDKVTIVFKNLATRPYSIHAHGVKTDSSTVAVTQPGETRTYIWKIPDRSGSGKGDPSCIPWAYYSVVDKVKDTYS 1319
Cdd:cd04225    81 IHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSSWVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                         170
                  ....*....|.
gi 465989294 1320 GLIGTLVVCPK 1330
Cdd:cd04225   161 GLIGPLVICRR 171
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 522-683 1.63e-97

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 310.89  E-value: 1.63e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  522 GYIFKDTAggQARVFLQRGPDRIGSTYKKAVYTQFTDNSFNKTVEKPSWLGFLGPIIKAEVGDFIIVHLKNFASRSYTLH 601
Cdd:cd04222    24 NQTFDDDE--HASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKPVWLGFLGPILKAEVGDVIVVHLKNFASRPYSLH 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  602 PHGVAYTKENEGAFYPDNTKDLLKKDDAVKPGELYTYRWDVTEDHGPAEGDSNCMTRIYHSHTDAPRDVASGLVGPLITC 681
Cdd:cd04222   102 PHGVFYNKENEGALYPDNTSGFEKADDAVPPGGSYTYTWTVPEEQAPTKADANCLTRIYHSHIDAPKDIASGLIGPLIIC 181


                  ..
gi 465989294  682 RK 683
Cdd:cd04222   182 KK 183
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1341-1485 4.58e-97

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 308.34  E-value: 4.58e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1341 RVEFALLFMVFDENESWYLDENIKTYSANPDKVNKEDEEFIESNKMHAINGKLFGNLHGLTMHVGDKVSWYLMGMGNEVD 1420
Cdd:cd11012     1 KLEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 465989294 1421 MHTAHFHGHSFDYKRTGVYRADVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTVL 1485
Cdd:cd11012    81 IHTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1003-1146 9.38e-95

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


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 301.71  E-value: 9.38e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1003 DKEFFLLATVFDENLSWYLDDNILMFLIKPNDIDKEDEDFQESNKMHSINGYMYGNQPGLEMCKGNTVSWHLIGLGSEVD 1082
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 465989294 1083 IHGIYFSENTFLTKGTRRDTTNLFPHTTLTAIMEPDTEGVFEVECLTTDHYTGGMKQKYKVKKC 1146
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 695-835 1.60e-91

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 292.45  E-value: 1.60e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  695 DAEFILMFSVMDENLSWYLDDSIEKYCSEPAKVDKENEDFQESNKMHSINGYMYGYLPNLTMCEEDKVKWHLFGMGNEAD 774
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294  775 VHSAYFHGQVFTERNHRVDSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAIFEV 835
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 851-1000 2.16e-79

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 260.10  E-value: 2.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  851 VRHYYLAAEEIIWNYGPSAINHFTGQQLVI-DSESQTFFEQNEKRIGGSYKKAVYKEYTDGTFTKCKKRFPEEEHLGLLG 929
Cdd:cd04224     3 VRHYFIAAEEIMWDYAPSGKNLFTGQNLTApGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGILG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  930 --------------------------------------------TEAPSSHVSPGATYTYEWKVSEDVGPTQEDPDCLTW 965
Cdd:cd04224    83 pviraevgdtikvtfrnkasrpfsiqphgvfyeknyegamyrdgDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCLTY 162

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 465989294  966 LYYSAADSVKDTNSGLVGPLLVCRKGTLLPSGKQK 1000
Cdd:cd04224   163 LYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 535-683 5.40e-71

Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the first, third, and fifth cupredoxin domains of ceruloplasmin and similar proteins including the first, third and fifth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. It functions in copper transport, amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. Human Factor VIII facilitates blood clotting by acting as a cofactor for factor IXa. Factor VIII and IXa forms a complex in the presence of Ca+2 and phospholipids that converts factor X to the activated form Xa.


Pssm-ID: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 235.38  E-value: 5.40e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  535 VFLQRGPDRIGSTYKKAVYTQFTDNSFNKTVEKPSWLGFLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGA 614
Cdd:cd04199    29 QYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPEHLGILGPTIRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGA 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 465989294  615 FYPDNTKDLLKKDDAVKPGELYTYRWDVTEDHGPAEGDSNCMTRIYHSHTDAPRDVASGLVGPLITCRK 683
Cdd:cd04199   109 SYSDQTGPDEKKDDAVAPGETYTYVWIVTEESGPTKGDPACLTWAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 1343-1484 6.12e-70

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: 230.76  E-value: 6.12e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1343 EFALLFMVFDENESWYLDENIKTYSANPDKVNKEDEEFIESNKMHAINGKLFGNLHGLTMHVGDKVSWYLMGMGNEVDMH 1422
Cdd:cd04200     3 EFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 465989294 1423 TAHFHGHSFDYKRtgvYRADVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTV 1484
Cdd:cd04200    83 SIHFHGQTFLYKG---YRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
L6_membrane pfam05805
L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, ...
 276-449 5.85e-68

L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily it has now been found that that they are not significantly related to genuine tetraspanins, but instead constitute their own L6 family. Several members of this family have been implicated in human cancer.


Pssm-ID: 461745  Cd Length: 192  Bit Score: 227.06  E-value: 5.85e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   276 MGANILLYFPNGETRFASEHQLSKYVACLHGIIGGGILIFLPAAVFIGLEYDNCCGCrghenCGKSCAMLSSVLAAFIGI 355
Cdd:pfam05805   22 IIANILLLFPNGEVTYLSEGHISCEVWYFGGIIGGGLLVLLPATVFLLAGRKGGCCS-----CGNRCGMFLSILFSAIGV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   356 LGSGYCFIISALGLSHGPYCLSAV-EQNWVYPFTNSS-GGYLLERDRWSECREPRNIVEWNLTLFSILLVLGGIELILCS 433
Cdd:pfam05805   97 LGAGYCFIVSALALAEGPLCLTNGgSTSWGYPFKNNFnGNYLFNQSLWSVCLEPENIVEWHVTLFSILLLVSGLELLLCL 176

                          170
                   ....*....|....*.
gi 465989294   434 IQVINGFLGGICGVCC 449
Cdd:pfam05805  177 IQVVNGLLGCLCGTCK 192
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 695-835 6.52e-68

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: 224.98  E-value: 6.52e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  695 DAEFILMFSVMDENLSWYLDDSIEKYCSEPAKVDKENEDFQESNKMHSINGYMYGYLPNLTMCEEDKVKWHLFGMGNEAD 774
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294  775 VHSAYFHGQVFTERNHRVDSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAIFEV 835
Cdd:cd04200    81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 1160-1330 9.34e-66

Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the first, third, and fifth cupredoxin domains of ceruloplasmin and similar proteins including the first, third and fifth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. It functions in copper transport, amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. Human Factor VIII facilitates blood clotting by acting as a cofactor for factor IXa. Factor VIII and IXa forms a complex in the presence of Ca+2 and phospholipids that converts factor X to the activated form Xa.


Pssm-ID: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 220.36  E-value: 9.34e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1160 KTYYIAAVEVEWDYSPSRTWEHERhefheeSPGNPFLNKEDKFIGSKYKKVVYRKYTDSTFSTPKERAEeqqHLEILGPL 1239
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEKDL------SYRNQYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQPE---HLGILGPT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1240 LLANVGDKVTIVFKNLATRPYSIHAHGVKTDSS---------------TVAVTQPGETRTYIWKIPDRSGSGKGDPSCIP 1304
Cdd:cd04199    72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDsegasysdqtgpdekKDDAVAPGETYTYVWIVTEESGPTKGDPACLT 151

                         170       180
                  ....*....|....*....|....*.
gi 465989294 1305 WAYYSVVDKVKDTYSGLIGTLVVCPK 1330
Cdd:cd04199   152 WAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1343-1484 8.01e-63

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 210.40  E-value: 8.01e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1343 EFALLFMVFDENESWYLDENIKTYSANPDKVNKEDEEFIESNKMHAINGKLFGNLHGLTMHVGDKVSWYLMGMGNEVDMH 1422
Cdd:cd11021     3 EFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 465989294 1423 TAHFHGHSFDYKRtgvYRADVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTV 1484
Cdd:cd11021    83 SAFFHGQTLTDRG---HRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 695-838 9.57e-63

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


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 210.42  E-value: 9.57e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  695 DAEFILMFSVMDENLSWYLDDSIEKYCSEPAKVDKENEDFQESNKMHSINGYMYGYLPNLTMCEEDKVKWHLFGMGNEAD 774
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 465989294  775 VHSAYFHGQVFTERNHRVDSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAIFEVKDC 838
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 1003-1143 7.41e-61

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: 204.57  E-value: 7.41e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1003 DKEFFLLATVFDENLSWYLDDNILMFLIKPNDIDKEDEDFQESNKMHSINGYMYGNQPGLEMCKGNTVSWHLIGLGSEVD 1082
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294 1083 IHGIYFSENTFLTKGTRRDTTNLFPHTTLTAIMEPDTEGVFEVECLTTDHYTGGMKQKYKV 1143
Cdd:cd04200    81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1343-1484 2.08e-58

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


Pssm-ID: 259908 [Multi-domain]  Cd Length: 144  Bit Score: 197.70  E-value: 2.08e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1343 EFALLFMVFDENESWYLDENIKTYSANPDKVNKEDEEFIESNKMHAINGKLFGNLHGLTMHVGDKVSWYLMGMGNEVDMH 1422
Cdd:cd11022     3 EFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 465989294 1423 TAHFHGHSFDYKRTgvyRADVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTV 1484
Cdd:cd11022    83 GIYFSGNTFLLQGT---RRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV 141
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1158-1330 2.35e-58

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 200.01  E-value: 2.35e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1158 HEKTYYIAAVEVEWDYSPSRT-WEHERHEFHEESPGNPFLNKEDKFIGSKYKKVVYRKYTDSTFSTPKERAEEQQHLEIL 1236
Cdd:cd04224     2 KVRHYFIAAEEIMWDYAPSGKnLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1237 GPLLLANVGDKVTIVFKNLATRPYSIHAHGV------------KTDSSTVAVTQPGETRTYIWKIPDRSGSGKGDPSCIP 1304
Cdd:cd04224    82 GPVIRAEVGDTIKVTFRNKASRPFSIQPHGVfyeknyegamyrDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCLT 161

                         170       180
                  ....*....|....*....|....*.
gi 465989294 1305 WAYYSVVDKVKDTYSGLIGTLVVCPK 1330
Cdd:cd04224   162 YLYFSAVDPVRDTNSGLVGPLLVCKK 187
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1003-1143 4.41e-58

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


Pssm-ID: 259907 [Multi-domain]  Cd Length: 141  Bit Score: 196.92  E-value: 4.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1003 DKEFFLLATVFDENLSWYLDDNILMFLIKPNDIDKEDEDFQESNKMHSINGYMYGNQPGLEMCKGNTVSWHLIGLGSEVD 1082
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294 1083 IHGIYFSENTFLTKGTRRDTTNLFPHTTLTAIMEPDTEGVFEVECLTTDHYTGGMKQKYKV 1143
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 527-687 1.15e-51

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


Pssm-ID: 259886 [Multi-domain]  Cd Length: 197  Bit Score: 180.75  E-value: 1.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  527 DTAGGQARVFLQRGPDRIGSTYKKAVYTQFTDNSFnkTVEKP-----SWLGFLGPIIKAEVGDFIIVHLKNFASRSYTLH 601
Cdd:cd04224    31 TAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATF--TTRKHrskeeEHLGILGPVIRAEVGDTIKVTFRNKASRPFSIQ 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  602 PHGVAYTKENEGAFYPDntkDLLKKDDAVKPGELYTYRWDVTEDHGPAEGDSNCMTRIYHSHTDAPRDVASGLVGPLITC 681
Cdd:cd04224   109 PHGVFYEKNYEGAMYRD---GDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCLTYLYFSAVDPVRDTNSGLVGPLLVC 185


                  ....*.
gi 465989294  682 RKGTLD 687
Cdd:cd04224   186 KKGSLN 191
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 518-684 6.44e-51

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: 177.61  E-value: 6.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  518 PAGWGYIFKDTAGGQARVFLQRGPDRIGSTYKKAVYTQFTDNSFNKTVEKPSWLGFLGPIIKAEVGDFIIVHLKN-FASR 596
Cdd:cd04229    16 PSGKNKCCLGDDLEVSTLDSQPGPYTIGSTYTKARYREYTDNSFSTPKPTPAYLGILGPVIRAEVGDTIKVVFKNnLDEF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  597 SYTLHPHGVAYTKENEGAfypdntkdLLKKDDAVKPGELYTYRWDVTEDHGPAEGDSNCMTRIYHSHTDAPRDVASGLVG 676
Cdd:cd04229    96 PVNMHPHGGLYSKDNEGT--------TDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHVDVFAHTNAGLVG 167


                  ....*...
gi 465989294  677 PLITCRKG 684
Cdd:cd04229   168 PIIVTSKG 175
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 521-682 1.21e-50

The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 3 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 176.99  E-value: 1.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  521 WGY---IFKDTAGGQARVFLQRGPDRIGSTYKKAVYTQFTDNSFNKTVE--KPSWLGFLGPIIKAEVGDFIIVHLKNFAS 595
Cdd:cd14450    14 WDYapsIPENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLEnpRPKEEGILGPVIRAQVRDTIKIVFKNKAS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  596 RSYTLHPHGVAYTKENEGAFYPDNTKDLLKKDDAVKPGELYTYRWDVTEDHGPAEGDSNCMTRIYHSHTDAPRDVASGLV 675
Cdd:cd14450    94 RPYSIYPHGVTVSKAAEGASYPPDPRGNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRMYHSAVDITRDIASGLI 173


                  ....*..
gi 465989294  676 GPLITCR 682
Cdd:cd14450   174 GPLLICK 180
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 697-835 5.09e-50

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 173.90  E-value: 5.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  697 EFILMFSVMDENLSWYLDDSIEKYCSEPAKVDKENEDFQESNKMHSINGYMYGYLPNLTMCEEDKVKWHLFGMGNEADVH 776
Cdd:cd11012     3 EFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 465989294  777 SAYFHGQVFTERN---HRVDSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAIFEV 835
Cdd:cd11012    83 TAHFHGHSFDYKHrgvYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 520-684 5.52e-50

The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 1 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 174.78  E-value: 5.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  520 GWGYIFKDTagGQARVFLQRGPDRIGSTYKKAVYTQFTDNSFNKTVEKPSWLGFLGPIIKAEVGDFIIVHLKNFASRSYT 599
Cdd:cd14452    11 GWDYIHSDL--GDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPAWMGLLGPTIVAEVGDTVVITFKNLASQPYS 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  600 LHPHGVAYTKENEGAFYPDNTKDLLKKDDAVKPGELYTYRWDVTEDHGPAEGDSNCMTRIYHSHTDAPRDVASGLVGPLI 679
Cdd:cd14452    89 LHAVGVSYWKASEGAGYDDSTSQHEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLTYSYSSQVDPVKDVNSGLIGALL 168


                  ....*
gi 465989294  680 TCRKG 684
Cdd:cd14452   169 VCRMG 173
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1159-1330 1.32e-49

The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 5 of unprocessed Factor V or the first cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 173.87  E-value: 1.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1159 EKTYYIAAVEVEWDYSPsrtweherhefheesPGNPFLNKEDKFIGSKYKKVVYRKYTDSTFSTPKERAEEQQHLEILGP 1238
Cdd:cd14451     1 KRRYYIAAEEEEWDYAG---------------YGKSRLDKTQNERDTVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1239 LLLANVGDKVTIVFKNLATRPYSIHAHGVKTDSSTVAVT---------------QPGETRTYIWKIPDRSGSGKGDPSCI 1303
Cdd:cd14451    66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSyddespdwfkkddavQPNGTYTYVWYANPRSGPENNGSDCR 145

                         170       180
                  ....*....|....*....|....*..
gi 465989294 1304 PWAYYSVVDKVKDTYSGLIGTLVVCPK 1330
Cdd:cd14451   146 TWAYYSAVNPEKDIHSGLIGPLLICRK 172
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1160-1327 3.21e-49

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: 172.99  E-value: 3.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1160 KTYYIAAVEVEWDYSPSRTWEHERHEFHEESPGNPFLNKEDkfIGSKYKKVVYRKYTDSTFSTPKEraeEQQHLEILGPL 1239
Cdd:cd04229     1 RTYYIAAEEVDWDYAPSGKNKCCLGDDLEVSTLDSQPGPYT--IGSTYTKARYREYTDNSFSTPKP---TPAYLGILGPV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1240 LLANVGDKVTIVFKN-LATRPYSIHAHGV-------KTDSSTVAVTQPGETRTYIWKIPDRSGSGKGDPSCIPWAYYSVV 1311
Cdd:cd04229    76 IRAEVGDTIKVVFKNnLDEFPVNMHPHGGlyskdneGTTDGAGDVVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSHV 155

                         170
                  ....*....|....*.
gi 465989294 1312 DKVKDTYSGLIGTLVV 1327
Cdd:cd04229   156 DVFAHTNAGLVGPIIV 171
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 542-684 6.45e-49

The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 1 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259888 [Multi-domain]  Cd Length: 165  Bit Score: 171.58  E-value: 6.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  542 DRIGSTYKKAVYTQFtDNSFNKTVEKPSWLGFLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGAFYPDNTK 621
Cdd:cd04226    24 KRSEQSFKKIVYREY-EEGFKKEKPADLSSGLLGPTLRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTS 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 465989294  622 DLLKKDDAVKPGELYTYRWDVTEDHGPAEGDSNCMTRIYHSHTDAPRDVASGLVGPLITCRKG 684
Cdd:cd04226   103 PVEKLDDAVQPGQEYTYVWDITEEVGPTEADPPCLTYIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 852-990 1.73e-48

Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the first, third, and fifth cupredoxin domains of ceruloplasmin and similar proteins including the first, third and fifth cupredoxin domains of unprocessed coagulation factors V and VIII. Ceruloplasmin (ferroxidase) is a multicopper oxidase essential for normal iron homeostasis. It functions in copper transport, amine oxidation and as an antioxidant preventing free radicals in serum. The protein has 6 cupredoxin domains and exhibits internal sequence homology that appears to have evolved from the triplication of a sequence unit composed of two tandem cupredoxin domains. Human Factor VIII facilitates blood clotting by acting as a cofactor for factor IXa. Factor VIII and IXa forms a complex in the presence of Ca+2 and phospholipids that converts factor X to the activated form Xa.


Pssm-ID: 259862 [Multi-domain]  Cd Length: 177  Bit Score: 170.66  E-value: 1.73e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  852 RHYYLAAEEIIWNYGPSAINHFTgqqlvIDSESQtFFEQNEKRIGGSYKKAVYKEYTDGTFTKckkRFPEEEHLGLLG-- 929
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEKD-----LSYRNQ-YLDNGPFRIGRSYKKVVYREYTDESFTT---PGPQPEHLGILGpt 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  930 -----------------------------TEAPS----------------SHVSPGATYTYEWKVSEDVGPTQEDPDCLT 964
Cdd:cd04199    72 iraevgdtikvhfknkasrpysihphgvsYEKDSegasysdqtgpdekkdDAVAPGETYTYVWIVTEESGPTKGDPACLT 151

                         170       180
                  ....*....|....*....|....*.
gi 465989294  965 WLYYSAADSVKDTNSGLVGPLLVCRK 990
Cdd:cd04199   152 WAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 546-684 6.15e-46

The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 5 of unprocessed Factor V or the first cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 163.47  E-value: 6.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  546 STYKKAVYTQFTDNSFNKTV---EKPSWLGFLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGAFYPDNTKD 622
Cdd:cd14451    32 TVFKKVVFRRYLDSTFSTPDiqgEYEEHLGILGPVIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPD 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 465989294  623 LLKKDDAVKPGELYTYRWDVTEDHGPAEGDSNCMTRIYHSHTDAPRDVASGLVGPLITCRKG 684
Cdd:cd14451   112 WFKKDDAVQPNGTYTYVWYANPRSGPENNGSDCRTWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1160-1330 7.96e-45

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 160.66  E-value: 7.96e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1160 KTYYIAAVEVEWDYSPSRTWEHERHEFHEESPGNPFLNKEDKFIGSKYKKVVYRKYTDSTFSTpkeRAEEQQHLEILGPL 1239
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRT---EIEKPVWLGFLGPI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1240 LLANVGDKVTIVFKNLATRPYSIHAHGVK----------TDSSTV------AVtQPGETRTYIWKIPDRSGSGKGDPSCI 1303
Cdd:cd04222    78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFynkenegalyPDNTSGfekaddAV-PPGGSYTYTWTVPEEQAPTKADANCL 156

                         170       180
                  ....*....|....*....|....*..
gi 465989294 1304 PWAYYSVVDKVKDTYSGLIGTLVVCPK 1330
Cdd:cd04222   157 TRIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1162-1328 9.85e-44

The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 5 of unprocessed Factor VIII or the first cupredoxin domain of the light chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 156.97  E-value: 9.85e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1162 YYIAAVEVEWDYSPSRTWEHERHEFHEESPGNPFlnkedkfigSKYKKVVYRKYTDSTFSTPKERAEEQQHLEILGPLLL 1241
Cdd:cd04228     4 YFIAAVEVLWDYGMQRPQHFLRARDPNRGRRKSV---------PQYKKVVFREYLDGSFTQPVYRGELDEHLGILGPYIR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1242 ANVGDKVTIVFKNLATRPYSIHAHGVKTDSSTVA-----VTQPGETRTYIWKIPDRSGSGKGDPSCIPWAYYSVVDKVKD 1316
Cdd:cd04228    75 AEVEDNIMVTFKNLASRPYSFHSSLISYEEDQRAeprgnFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKD 154

                         170
                  ....*....|..
gi 465989294 1317 TYSGLIGTLVVC 1328
Cdd:cd04228   155 LHSGLIGPLIIC 166
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1343-1484 1.81e-42

The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 6 of unprocessed Factor VIII or the second cupredoxin domain the light chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 152.34  E-value: 1.81e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1343 EFALLFMVFDENESWYLDENIKTYSANPDKVNKEDEEFIESNKMHAINGKLFGNLHGLTMHVGDKVSWYLMGMGNEVDMH 1422
Cdd:cd11018     3 EFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 465989294 1423 TAHFHGHSFDYKRTGVYRADVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTV 1484
Cdd:cd11018    83 SVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 852-990 2.93e-42

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 152.62  E-value: 2.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  852 RHYYLAAEEIIWNYGPSAINHFTGQQLVIDSESQTFFEQNEKRIGGSYKKAVYKEYTDGTFTKCKKRFPEEEHLGLLG-- 929
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEESPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGpl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  930 -----------------------------TEAPS-SHVSPGATYTYEWKVSEDVGPTQEDPDCLTWLYYSAADSVKDTNS 979
Cdd:cd04225    81 ihaevgekvkivfknmasrpysihahgvkTDSSWvAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYS 160

                         170
                  ....*....|.
gi 465989294  980 GLVGPLLVCRK 990
Cdd:cd04225   161 GLIGPLVICRR 171
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1161-1328 7.12e-42

The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 3 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 151.95  E-value: 7.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1161 TYYIAAVEVEWDYSPSRTweherhEFHEESPGNPFLNKEDKFIGSKYKKVVYRKYTDSTFstpKERAEEQQHLE--ILGP 1238
Cdd:cd14450     4 EYFIAAEEVIWDYAPSIP------ENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSF---TKRLENPRPKEegILGP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1239 LLLANVGDKVTIVFKNLATRPYSIHAHGVKTD----------------SSTVAVtQPGETRTYIWKIPDRSGSGKGDPSC 1302
Cdd:cd14450    75 VIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSkaaegasyppdprgneTQNKAV-QPGETYTYKWNILETDEPTARDPRC 153

                         170       180
                  ....*....|....*....|....*.
gi 465989294 1303 IPWAYYSVVDKVKDTYSGLIGTLVVC 1328
Cdd:cd14450   154 LTRMYHSAVDITRDIASGLIGPLLIC 179
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 536-683 2.41e-40

The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 3 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 147.38  E-value: 2.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  536 FLQRGPDRIGSTYKKAVYTQFTDNSFNKTVEKPSWLGFLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGAF 615
Cdd:cd04227    32 YLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEKGILGPLLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSR 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 465989294  616 YPDNTKDLlkKDDAVKPGELYTYRWDVTEDHGPAEGDSNCMTRIYHSHTDAPRDVASGLVGPLITCRK 683
Cdd:cd04227   112 NPAGEKDL--KTMPIGPGETFGYMWELTAEDGPTEEDPRCLTRLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1161-1330 5.99e-40

The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 3 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 146.23  E-value: 5.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1161 TYYIAAVEVEWDYSPsrtwehERHEFHEESPGNPFLNKEDKFIGSKYKKVVYRKYTDSTFstpKERAEEQQHLEILGPLL 1240
Cdd:cd04227     4 EHYIAAEELDWDYAP------LLSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTF---KRREAKQTEKGILGPLL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1241 LANVGDKVTIVFKNLATRPYSIHAHGV--------------KTDSSTVAVTqPGETRTYIWKIPDRSGSGKGDPSCIPWA 1306
Cdd:cd04227    75 KGEVGDQIHIMFKNTASRPYNIYPHGLtsvrpmyrsrnpagEKDLKTMPIG-PGETFGYMWELTAEDGPTEEDPRCLTRL 153

                         170       180
                  ....*....|....*....|....
gi 465989294 1307 YYSVVDKVKDTYSGLIGTLVVCPK 1330
Cdd:cd04227   154 YQSTVDPERDLASGLIGPLLICKK 177
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1004-1143 1.00e-39

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


Pssm-ID: 259898 [Multi-domain]  Cd Length: 145  Bit Score: 144.63  E-value: 1.00e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1004 KEFFLLATVFDENLSWYLDDNILMFLIKPNDIDKEDEDFQESNKMHSINGYMYGNQPGLEMCKGNTVSWHLIGLGSEVDI 1083
Cdd:cd11012     2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 465989294 1084 HGIYFSENTFLTKGT---RRDTTNLFPHTTLTAIMEPDTEGVFEVECLTTDHYTGGMKQKYKV 1143
Cdd:cd11012    82 HTAHFHGHSFDYKHRgvyRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 536-683 8.40e-39

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


Pssm-ID: 259887 [Multi-domain]  Cd Length: 171  Bit Score: 142.99  E-value: 8.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  536 FLQRGPDRIGSTYKKAVYTQFTDNSFNKTVEKPS---WLGFLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVaytKENE 612
Cdd:cd04225    36 FLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAeeeHLGILGPLIHAEVGEKVKIVFKNMASRPYSIHAHGV---KTDS 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294  613 GAFYPdntkdllkkddaVKPGELYTYRWDVTEDHGPAEGDSNCMTRIYHSHTDAPRDVASGLVGPLITCRK 683
Cdd:cd04225   113 SWVAP------------TEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDLYSGLIGPLVICRR 171
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 852-990 4.20e-38

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


Pssm-ID: 259884 [Multi-domain]  Cd Length: 183  Bit Score: 141.40  E-value: 4.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  852 RHYYLAAEEIIWNYGPSAINHFTGQQLVIDSESQTFFEQNEKRIGGSYKKAVYKEYTDGTFTKCKKR------------- 918
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTEIEKpvwlgflgpilka 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  919 -------------------------FPEEEHLGLL---GTEAPSSH---VSPGATYTYEWKVSEDVGPTQEDPDCLTWLY 967
Cdd:cd04222    81 evgdvivvhlknfasrpyslhphgvFYNKENEGALypdNTSGFEKAddaVPPGGSYTYTWTVPEEQAPTKADANCLTRIY 160

                         170       180
                  ....*....|....*....|...
gi 465989294  968 YSAADSVKDTNSGLVGPLLVCRK 990
Cdd:cd04222   161 HSHIDAPKDIASGLIGPLIICKK 183
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 697-835 1.50e-37

The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 6 of unprocessed Factor VIII or the second cupredoxin domain the light chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 138.09  E-value: 1.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  697 EFILMFSVMDENLSWYLDDSIEKYCSEPAKVDKENEDFQESNKMHSINGYMYGYLPNLTMCEEDKVKWHLFGMGNEADVH 776
Cdd:cd11018     3 EFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIH 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 465989294  777 SAYFHGQVFTER---NHRVDSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAIFEV 835
Cdd:cd11018    83 SVHFHGLPFTVRakkEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1343-1484 7.70e-36

The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 6 of unprocessed Factor V or the second cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 133.07  E-value: 7.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1343 EFALLFMVFDENESWYLDENIKTYSanpDKVNKEDEEFIESNKMHAINGKLFgNLHGLTMHVGDKVSWYLMGMGNEVDMH 1422
Cdd:cd14455     3 EFVLLFMTFDEEKSWYYEKNRKRTC---RENRVKDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLH 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 465989294 1423 TAHFHGHSFDYKRTGVYRADVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTV 1484
Cdd:cd14455    79 VVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1350-1484 2.41e-35

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: 130.81  E-value: 2.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1350 VFDENESWYLDENIKtysanpdkvnkedeefiESNKMHAINGKLFGNLHGLTMHVGDKVSWYLMGMGNEVDMHTAHFHGH 1429
Cdd:cd11023     3 EFIENSSIFLDLNVE-----------------EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQ 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 465989294 1430 SFDYKRTGvyRADVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTV 1484
Cdd:cd11023    66 TVEADKSR--RTDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1160-1328 3.71e-35

The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 1 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 132.41  E-value: 3.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1160 KTYYIAAVEVEWDYSPSrtweherheFHEESPGNPflNKEDKFIGSKYKKVVYRKYTDSTFSTPKERAEeqqHLEILGPL 1239
Cdd:cd14452     1 RRYYIAAVEIGWDYIHS---------DLGDPASEQ--RKKPKDIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPT 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1240 LLANVGDKVTIVFKNLATRPYSIHAHGVKT---------DSSTVAVTQ------PGETRTYIWKIPDRSGSGKGDPSCIP 1304
Cdd:cd14452    67 IVAEVGDTVVITFKNLASQPYSLHAVGVSYwkasegagyDDSTSQHEKeddavyPGGYHTYVWDISPKDGPTGSDPECLT 146

                         170       180
                  ....*....|....*....|....
gi 465989294 1305 WAYYSVVDKVKDTYSGLIGTLVVC 1328
Cdd:cd14452   147 YSYSSQVDPVKDVNSGLIGALLVC 170
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1003-1146 9.00e-34

The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 4 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 127.29  E-value: 9.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1003 DKEFFLLATVFDENLSWYLDDNILMFLIKPNDIDKEDEDFQESNKMHSINGYMYGNQPgLEMCKGNTVSWHLIGLGSEVD 1082
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 465989294 1083 IHGIYFSENTFLTKGTRRDTTNLFPHTTLTAIMEPDTEGVFEVECLTTDHYTGGMKQKYKVKKC 1146
Cdd:cd11016    80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 1162-1330 1.40e-33

The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 1 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259888 [Multi-domain]  Cd Length: 165  Bit Score: 127.67  E-value: 1.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1162 YYIAAVEVEWDYSPSRTweherhefheespgnpflNKEDKFIGSKYKKVVYRKYtDSTFSTPKERAEEQQhleILGPLLL 1241
Cdd:cd04226     3 YYIAAQNIDWDYTPQSE------------------ELRLKRSEQSFKKIVYREY-EEGFKKEKPADLSSG---LLGPTLR 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1242 ANVGDKVTIVFKNLATRPYSIHAHGVK----------TDSSTVA-----VTQPGETRTYIWKIPDRSGSGKGDPSCIPWA 1306
Cdd:cd04226    61 AEVGDTLIVHFKNMADKPLSIHPQGIAygkksegslySDNTSPVeklddAVQPGQEYTYVWDITEEVGPTEADPPCLTYI 140

                         170       180
                  ....*....|....*....|....
gi 465989294 1307 YYSVVDKVKDTYSGLIGTLVVCPK 1330
Cdd:cd04226   141 YYSHVNMVRDFNSGLIGALLICKK 164
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 852-991 6.82e-33

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: 125.99  E-value: 6.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  852 RHYYLAAEEIIWNYGPSAINHFTgqqLVIDSESQTFFEQNEK-RIGGSYKKAVYKEYTDGTFTKCKkrfPEEEHLGLLG- 929
Cdd:cd04229     1 RTYYIAAEEVDWDYAPSGKNKCC---LGDDLEVSTLDSQPGPyTIGSTYTKARYREYTDNSFSTPK---PTPAYLGILGp 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  930 ------------------TEAP-SSH--------------------VSPGATYTYEWKVSEDVGPTQEDPDCLTWLYYSA 970
Cdd:cd04229    75 viraevgdtikvvfknnlDEFPvNMHphgglyskdnegttdgagdvVAPGETYTYRWIVPEDAGPGPGDPSSRLWLYHSH 154

                         170       180
                  ....*....|....*....|.
gi 465989294  971 ADSVKDTNSGLVGPLLVCRKG 991
Cdd:cd04229   155 VDVFAHTNAGLVGPIIVTSKG 175
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 697-835 1.25e-32

The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 6 of unprocessed Factor V or the second cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 123.82  E-value: 1.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  697 EFILMFSVMDENLSWYLDDSIEKYCSEPAKVDKEnedFQESNKMHSINGYMYGyLPNLTMCEEDKVKWHLFGMGNEADVH 776
Cdd:cd14455     3 EFVLLFMTFDEEKSWYYEKNRKRTCRENRVKDPN---VQDNHTFHAINGIIYN-LKGLRMYTNELVRWHLINMGGPKDLH 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 465989294  777 SAYFHGQVFTE---RNHRVDSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAIFEV 835
Cdd:cd14455    79 VVHFHGQTFTEkglKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 728-835 5.50e-32

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: 121.18  E-value: 5.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  728 DKENEdfQESNKMHSINGYMYGYLPNLTMCEEDKVKWHLFGMGNEADVHSAYFHGQ-VFTERNHRVDSISLFPATFVDAL 806
Cdd:cd11023    12 LDLNV--EEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQtVEADKSRRTDVAELMPASMRVAD 89

                          90       100
                  ....*....|....*....|....*....
gi 465989294  807 MVPKNPGEWLLSCQVNDHIEGGMQAIFEV 835
Cdd:cd11023    90 MTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 695-835 6.12e-32

The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 2 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 121.50  E-value: 6.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  695 DAEFILMFSVMDENLSWYlddsiekycsepakvdkeNEDFQESNKMHSINGYMYGYLPNLTMCEEDKVKWHLFGMGNEAD 774
Cdd:cd14453     1 YKEYVLMFGVFDENKSWY------------------KQNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294  775 VHSAYFHGQVFTERNHRVDSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAIFEV 835
Cdd:cd14453    63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 538-684 1.74e-31

The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 5 of unprocessed Factor VIII or the first cupredoxin domain of the light chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 121.92  E-value: 1.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  538 QRGPDRigsTYKKAVYTQFTDNSFNKTV---EKPSWLGFLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYtkENEGA 614
Cdd:cd04228    33 RRKSVP---QYKKVVFREYLDGSFTQPVyrgELDEHLGILGPYIRAEVEDNIMVTFKNLASRPYSFHSSLISY--EEDQR 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  615 FYPdntkdllkKDDAVKPGELYTYRWDVTEDHGPAEGDSNCMTRIYHSHTDAPRDVASGLVGPLITCRKG 684
Cdd:cd04228   108 AEP--------RGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 697-835 3.35e-31

The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 2 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 119.62  E-value: 3.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  697 EFILMFSVMDENLSWYLDDSiekycsEPAKVDKENEDfQESNKMHSINGYMYGYLPNLTMCEEDKVKWHLFGMGNEADVH 776
Cdd:cd11015     3 AFVLLFAVFDEGKSWYSEVG------ERKSRDKFKRA-DSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVH 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 465989294  777 SAYFHGQVFTERNHRVDSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAIFEV 835
Cdd:cd11015    76 SIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 695-838 6.23e-31

The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 4 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 119.20  E-value: 6.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  695 DAEFILMFSVMDENLSWYLDDSIEKYCSEPAKVDKENEDFQESNKMHSINGYMYGYLpNLTMCEEDKVKWHLFGMGNEAD 774
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 465989294  775 VHSAYFHGQVFTERNHRVDSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAIFEVKDC 838
Cdd:cd11016    80 FLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 852-991 2.14e-30

The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 5 of unprocessed Factor V or the first cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259993 [Multi-domain]  Cd Length: 173  Bit Score: 118.79  E-value: 2.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  852 RHYYLAAEEIIWNYGPSAinhftgqqlvidsESQTFFEQNEKRigGSYKKAVYKEYTDGTFTKCKKRFPEEEHLGLLG-- 929
Cdd:cd14451     2 RRYYIAAEEEEWDYAGYG-------------KSRLDKTQNERD--TVFKKVVFRRYLDSTFSTPDIQGEYEEHLGILGpv 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  930 ----------------------------------------TEAP-----SSHVSPGATYTYEWKVSEDVGPTQEDPDCLT 964
Cdd:cd14451    67 iraevddviqvffknlasrpyslhahglsyeksseglsydDESPdwfkkDDAVQPNGTYTYVWYANPRSGPENNGSDCRT 146

                         170       180
                  ....*....|....*....|....*..
gi 465989294  965 WLYYSAADSVKDTNSGLVGPLLVCRKG 991
Cdd:cd14451   147 WAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 854-989 2.23e-30

The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 3 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259992 [Multi-domain]  Cd Length: 181  Bit Score: 119.21  E-value: 2.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  854 YYLAAEEIIWNYGPSAINHFTGqqlviDSESQtFFEQNEKRIGGSYKKAVYKEYTDGTFTKcKKRFPEEEHLGLLG---- 929
Cdd:cd14450     5 YFIAAEEVIWDYAPSIPENMDK-----RYRSQ-YLDNFSNNIGKKYKKAVFTQYEDGSFTK-RLENPRPKEEGILGpvir 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  930 -------------------------------------------TEAPSSHVSPGATYTYEWKVSEDVGPTQEDPDCLTWL 966
Cdd:cd14450    78 aqvrdtikivfknkasrpysiyphgvtvskaaegasyppdprgNETQNKAVQPGETYTYKWNILETDEPTARDPRCLTRM 157

                         170       180
                  ....*....|....*....|...
gi 465989294  967 YYSAADSVKDTNSGLVGPLLVCR 989
Cdd:cd14450   158 YHSAVDITRDIASGLIGPLLICK 180
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 851-991 3.35e-30

The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 5 of unprocessed Factor VIII or the first cupredoxin domain of the light chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259890 [Multi-domain]  Cd Length: 169  Bit Score: 118.07  E-value: 3.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  851 VRHYYLAAEEIIWNYGPSAINHFTgQQLVIDSESQTFFEQnekriggsYKKAVYKEYTDGTFTKCKKRFPEEEHLGLLG- 929
Cdd:cd04228     1 IRHYFIAAVEVLWDYGMQRPQHFL-RARDPNRGRRKSVPQ--------YKKVVFREYLDGSFTQPVYRGELDEHLGILGp 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  930 ------------------------------------TEAPSSHVSPGATYTYEWKVSEDVGPTQEDPDCLTWLYYSAADS 973
Cdd:cd04228    72 yiraevednimvtfknlasrpysfhsslisyeedqrAEPRGNFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYFSNVDL 151

                         170
                  ....*....|....*...
gi 465989294  974 VKDTNSGLVGPLLVCRKG 991
Cdd:cd04228   152 EKDLHSGLIGPLIICKTG 169
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1003-1146 5.09e-30

The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 4 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 116.51  E-value: 5.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1003 DKEFFLLATVFDENLSWYLDDNILMFLIKPNDIDKEDEDFQESNKMHSINGYMYGNQPGLEMCKGNTVSWHLIGLGSEVD 1082
Cdd:cd14454     1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 465989294 1083 IHGIYFSENTFLTKGTRRDTTNLFPHTTLTAIMEPDTEGVFEVECLTTDHYTGGMKQKYKVKKC 1146
Cdd:cd14454    81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLRVRFTDVIC 144
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1346-1485 6.84e-29

The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 4 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259902 [Multi-domain]  Cd Length: 143  Bit Score: 113.42  E-value: 6.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1346 LLFMVFDENESWYLDENIKTYSANPDKVNKEDEEFIESNKMHAINGKLFGNLHgLTMHVGDKVSWYLMGMGNEVDMHTAH 1425
Cdd:cd11016     6 LLFSVFDENNSWYLKENIHRFTQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQTDFLSVF 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1426 FHGHSFDYKrtGVYRaDVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTVL 1485
Cdd:cd11016    85 FSGNTFKHQ--MVYE-DVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVS 141
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1004-1143 2.74e-28

The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 6 of unprocessed Factor VIII or the second cupredoxin domain the light chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259904 [Multi-domain]  Cd Length: 144  Bit Score: 111.51  E-value: 2.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1004 KEFFLLATVFDENLSWYLDDNILMFLIKPNDIDKEDEDFQESNKMHSINGYMYGNQPGLEMCKGNTVSWHLIGLGSEVDI 1083
Cdd:cd11018     2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 465989294 1084 HGIYFSENTFLTKGT---RRDTTNLFPHTTLTAIMEPDTEGVFEVECLTTDHYTGGMKQKYKV 1143
Cdd:cd11018    82 HSVHFHGLPFTVRAKkeyRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1342-1466 9.62e-28

The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 4 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 109.96  E-value: 9.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1342 VEFALLFMVFDENESWYLDENIKTYSANPDKVNKEDEEFIESNKMHAINGKLFGNLHGLTMHVGDKVSWYLMGMGNEVDM 1421
Cdd:cd14454     2 LEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEI 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 465989294 1422 HTAHFHGHSFDYKRTgvyRADVFDLFPGTFQTVEMLPKYPGTWLL 1466
Cdd:cd14454    82 ITVHLSGHTFRYKGK---HEDTLNLFPMSGESITVTMDNLGTWLL 123
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 695-818 1.11e-27

The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 4 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259996 [Multi-domain]  Cd Length: 144  Bit Score: 109.96  E-value: 1.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  695 DAEFILMFSVMDENLSWYLDDSIEKYCSEPAKVDKENEDFQESNKMHSINGYMYGYLPNLTMCEEDKVKWHLFGMGNEAD 774
Cdd:cd14454     1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 465989294  775 VHSAYFHGQVFTERNHRVDSISLFPATFVDALMVPKNPGEWLLS 818
Cdd:cd14454    81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLG 124
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 852-991 1.13e-27

The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 1 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259888 [Multi-domain]  Cd Length: 165  Bit Score: 110.72  E-value: 1.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  852 RHYYLAAEEIIWNYGPsainhftgqqlvidsESQtffEQNEKRIGGSYKKAVYKEYTDGtFTKCKkrfPEEEHLGLLG-- 929
Cdd:cd04226     1 REYYIAAQNIDWDYTP---------------QSE---ELRLKRSEQSFKKIVYREYEEG-FKKEK---PADLSSGLLGpt 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  930 -----------------TEAPSSH----------------------------VSPGATYTYEWKVSEDVGPTQEDPDCLT 964
Cdd:cd04226    59 lraevgdtlivhfknmaDKPLSIHpqgiaygkksegslysdntspveklddaVQPGQEYTYVWDITEEVGPTEADPPCLT 138

                         170       180
                  ....*....|....*....|....*..
gi 465989294  965 WLYYSAADSVKDTNSGLVGPLLVCRKG 991
Cdd:cd04226   139 YIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 854-990 4.45e-26

The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 3 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259889 [Multi-domain]  Cd Length: 177  Bit Score: 106.55  E-value: 4.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  854 YYLAAEEIIWNYGPSAInhftgqqLVIDSESQT-FFEQNEKRIGGSYKKAVYKEYTDGTFtkcKKRFPEEEHLGLLG--- 929
Cdd:cd04227     5 HYIAAEELDWDYAPLLS-------STDDRELQSrYLPTGPQRIGYKYKKVAFVEYTDKTF---KRREAKQTEKGILGpll 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  930 -----------------------------------TEAPSSH-------VSPGATYTYEWKVSEDVGPTQEDPDCLTWLY 967
Cdd:cd04227    75 kgevgdqihimfkntasrpyniyphgltsvrpmyrSRNPAGEkdlktmpIGPGETFGYMWELTAEDGPTEEDPRCLTRLY 154

                         170       180
                  ....*....|....*....|...
gi 465989294  968 YSAADSVKDTNSGLVGPLLVCRK 990
Cdd:cd04227   155 QSTVDPERDLASGLIGPLLICKK 177
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1039-1143 1.53e-25

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: 103.07  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1039 DEDFQESNKMHSINGYMYGNQPGLEMCKGNTVSWHLIGLGSEVDIHGIYFSENTFLTKGTRR-DTTNLFPHTTLTAIMEP 1117
Cdd:cd11023    13 DLNVEEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRtDVAELMPASMRVADMTA 92

                          90       100
                  ....*....|....*....|....*.
gi 465989294 1118 DTEGVFEVECLTTDHYTGGMKQKYKV 1143
Cdd:cd11023    93 ADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 852-991 6.05e-24

The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 1 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259994 [Multi-domain]  Cd Length: 173  Bit Score: 100.44  E-value: 6.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  852 RHYYLAAEEIIWNYGPSAinhftgqqlviDSESQTFFEQNEKRIGGSYKKAVYKEYTDGTFTKCKKRFPeeeHLGLLGT- 930
Cdd:cd14452     1 RRYYIAAVEIGWDYIHSD-----------LGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGPt 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  931 ----------------------------------------------EAPSSHVSPGATYTYEWKVSEDVGPTQEDPDCLT 964
Cdd:cd14452    67 ivaevgdtvvitfknlasqpyslhavgvsywkasegagyddstsqhEKEDDAVYPGGYHTYVWDISPKDGPTGSDPECLT 146

                         170       180
                  ....*....|....*....|....*..
gi 465989294  965 WLYYSAADSVKDTNSGLVGPLLVCRKG 991
Cdd:cd14452   147 YSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1004-1143 7.98e-24

The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 2 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 98.44  E-value: 7.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1004 KEFFLLATVFDENLSWY--LDDNILMFLIKPNDIDKEdedfqesnkMHSINGYMYGNQPGLEMCKGNTVSWHLIGLGSEV 1081
Cdd:cd11015     2 QAFVLLFAVFDEGKSWYseVGERKSRDKFKRADSRKE---------FHTINGYINASLPGLKICQRKPVIWHVIGMGTAP 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 465989294 1082 DIHGIYFSENTFLTKGTRRDTTNLFPHTTLTAIMEPDTEGVFEVECLTTDHYTGGMKQKYKV 1143
Cdd:cd11015    73 EVHSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1343-1484 2.60e-21

The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII functions in the factor X-activating complex of the intrinsic coagulation pathway. It facilitates blood clotting by acting as a cofactor for factor IXa. In the presence of Ca2+ and phospholipids, Factor VIII and IXa form a complex that converts factor X to the activated form Xa. A variety of mutations in the Factor VIII gene can cause hemophilia A, which typically requires replacement therapy with purified protein. Factor VIII is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor VIII is initially processed through proteolysis to generate a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2), which circulates in a tight complex with von Willebrand factor (VWF). Further processing of the heavy chain produces activated factor VIIIa, a heterotrimer composed of polypeptides (1-2), (3-4), and the light chain. This model represents the cupredoxin domain 2 of unprocessed Factor VIII or the heavy chain of circulating Factor VIII, and similar proteins.


Pssm-ID: 259901 [Multi-domain]  Cd Length: 134  Bit Score: 91.51  E-value: 2.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1343 EFALLFMVFDENESWYLDENiktYSANPDKVNKEDEEfiesNKMHAINGKLFGNLHGLTMHVGDKVSWYLMGMGNEVDMH 1422
Cdd:cd11015     3 AFVLLFAVFDEGKSWYSEVG---ERKSRDKFKRADSR----KEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVH 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 465989294 1423 TAHFHGHSFDYKRtgvYRADVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTV 1484
Cdd:cd11015    76 SIFFEGHTFLVRT---HRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1384-1488 7.40e-19

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: 84.41  E-value: 7.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  1384 NKMHAINGKLFG-NLHGLTMHVGDKVSWYLMGMGNevDMHTAHFHGHSFDYKRTGV----------------YRADVFDL 1446
Cdd:pfam07731   19 RNDWAINGLLFPpNTNVITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFQVLGRGGgpwpeedpktynlvdpVRRDTVQV 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 465989294  1447 FPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTVLPKE 1488
Cdd:pfam07731   97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRPGD 138
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1343-1478 1.09e-18

The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 2 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 83.37  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1343 EFALLFMVFDENESWYldeniktySANPDkvnkedeefiESNKMHAINGKLFGNLHGLTMHVGDKVSWYLMGMGNEVDMH 1422
Cdd:cd14453     3 EYVLMFGVFDENKSWY--------KQNAS----------VDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELF 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 465989294 1423 TAHFHGHSFDYKRtgvYRADVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGM 1478
Cdd:cd14453    65 SVHFNGQVLEQNG---HKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1003-1137 2.54e-18

The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 2 of unprocessed Factor V or the heavy chain of Factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259995 [Multi-domain]  Cd Length: 123  Bit Score: 82.60  E-value: 2.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1003 DKEFFLLATVFDENLSWYlddnilmfliKPNDidkededfQESNKMHSINGYMYGNQPGLEMCKGNTVSWHLIGLGSEVD 1082
Cdd:cd14453     1 YKEYVLMFGVFDENKSWY----------KQNA--------SVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 465989294 1083 IHGIYFSENTFLTKGTRRDTTNLFPHTTLTAIMEPDTEGVFEVECLTTDHYTGGM 1137
Cdd:cd14453    63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
Ggt COG0405
Gamma-glutamyltranspeptidase [Amino acid transport and metabolism];
47-236 8.42e-18

Gamma-glutamyltranspeptidase [Amino acid transport and metabolism];


Pssm-ID: 440174  Cd Length: 507  Bit Score: 88.57  E-value: 8.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   47 SSAHPL--QIGWDILKNGGNVVDAAMAIAAALNVTELCGTGVGGACFCLCYDANTKQVQGLNGR---------------- 108
Cdd:COG0405     3 ATAHPLasQAGLEILRAGGNAVDAAVAAAAALAVVEPHSSGIGGGGFALIYDAKDGKVTALDGRgtapaaatpdmyldag 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  109 --------------------------FPSMELVQMCE---------------------------RKFPGYKiQLF----- 130
Cdd:COG0405    83 deipvrgplavgvpgtvagweaaherYGTLPLAELLApairlaedgfpvsprlaallaaaaerlARDPGAA-AIFlpdgr 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  131 -----------------QELAKSGKKSFSEGCVAEVIIETVQRNGGLMDLEDFKSHVTDE-------------------- 173
Cdd:COG0405   162 ppkagdilrqpdlaatlRRIAEEGADAFYRGEIAEAIVAAVQAAGGLLTLEDLAAYRAEWreplsgtyrgytvysmppps 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  174 -------------------------------IE-------------GNAEHYKV------SDNYNK-------------- 189
Cdd:COG0405   242 qgiallqilnilegfdlaalgpdsaeyvhllAEamklafadrdrylGDPDFVDVpvegllSPAYAAeraalidpdratps 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 465989294  190 ---GNLLPVGS-DTVYFTVVDAQGNASSFINSNYMGFGIGLEPGGCGFTLQ 236
Cdd:COG0405   322 prpGDPTGPESgDTTHLSVVDRDGNAVSLTQSIYGGFGSGVVVPGTGFLLN 372
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1004-1143 8.49e-18

The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an essential coagulation protein with both pro- and anti-coagulant functions. Aberrant expression of human factor V can lead to bleeding or thromboembolic disease, which may be life-threatening. Bovine factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation. Factor V is synthesized as a single polypeptide with six cupredoxin domains and a domain structure of 1-2-3-4-B-5-6-C1-C2, where 1-6 are cupredoxin domains, B is a domain with no known structural homologs and is dispensible for coagulant activity, and C are domains distantly related to discoidin protein-fold family members. Factor V has little activity prior to proteolytic cleavage by thrombin or FXa upon secretion. The resulting Factor Va is a heterodimer consisting of a heavy chain (1-2-3-4) and a light chain (5-6-C1-C2). This model represents the cupredoxin domain 6 of unprocessed Factor V or the second cupredoxin domain of the light chain of coagulation factor Va, and similar proteins including pseutarin C non-catalytic subunit. Pseutarin C is a prothrombin activator from Pseudonaja textilis venom.


Pssm-ID: 259997 [Multi-domain]  Cd Length: 140  Bit Score: 81.45  E-value: 8.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1004 KEFFLLATVFDENLSWYLDDNilmflikPNDIDKE----DEDFQESNKMHSINGYMYgNQPGLEMCKGNTVSWHLIGLGS 1079
Cdd:cd14455     2 REFVLLFMTFDEEKSWYYEKN-------RKRTCREnrvkDPNVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 465989294 1080 EVDIHGIYFSENTFLTKGT---RRDTTNLFPHTTLTAIMEPDTEGVFEVECLTTDHYTGGMKQKYKV 1143
Cdd:cd14455    74 PKDLHVVHFHGQTFTEKGLkdhQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 572-679 6.46e-17

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: 78.10  E-value: 6.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  572 GFLGPIIKAEVGDFIIVHLKN-FASRSYTLHPHGVAYTKENEGAFYPDNTKdllkkdDAVKPGELYTYRWDVTEDHGpae 650
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTNDGDGVAGLTQ------CPIPPGESFTYRFTVDDQAG--- 97

                          90       100
                  ....*....|....*....|....*....
gi 465989294  651 gdsncmTRIYHSHTDAprDVASGLVGPLI 679
Cdd:cd04206    98 ------TFWYHSHVGG--QRADGLYGPLI 118
L6_membrane pfam05805
L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, ...
 472-532 1.46e-15

L6 membrane protein; This family consists of several eukaryotic L6 membrane proteins. L6, IL-TMP, and TM4SF5 are cell surface proteins predicted to have four transmembrane domains. Previous sequence analysis led to their assignment as members of the tetraspanin superfamily it has now been found that that they are not significantly related to genuine tetraspanins, but instead constitute their own L6 family. Several members of this family have been implicated in human cancer.


Pssm-ID: 461745  Cd Length: 192  Bit Score: 76.84  E-value: 1.46e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 465989294   472 CCqseSCNKTYRSFISVVLALLGIAFSGYNVIISTLGLLQGPFCNTPAG---WGYIFKDTAGGQ 532
Cdd:pfam05805   76 CC---SCGNRCGMFLSILFSAIGVLGAGYCFIVSALALAEGPLCLTNGGstsWGYPFKNNFNGN 136
G_glu_transpept pfam01019
Gamma-glutamyltranspeptidase;
57-236 7.67e-13

Gamma-glutamyltranspeptidase;


Pssm-ID: 425991  Cd Length: 499  Bit Score: 73.01  E-value: 7.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294    57 DILKNGGNVVDAAMAIAAALNVTELCGTGVGGACFCLCYDANTKQVQGLNGR---------------------------- 108
Cdd:pfam01019    2 DILRKGGNAVDAAVAAALCLGVVEPHSSGIGGGGFMLIYDAKTGKVLVIDARetapaaatkdmfdgkgdsklsltgglav 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   109 -----------------------------------FP-------SMELVQMCERKFPGYKiQLF---------------- 130
Cdd:pfam01019   82 gvpgevaglaeahkrygrlpwadllepaiklardgFPvspalarALARAEERLRADPGLR-KIFlptgrvlkagellkqp 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   131 ------QELAKSGKKSFSEGCVAEVIIETVQRNGGLM---DLEDFKSHVTDEIEGNAEHYKVS----------------- 184
Cdd:pfam01019  161 alaktlELIAEEGPDAFYRGELAQQLVADLQANGGIItaeDLANYRVKIREPLSADYGGYTVYspppssggiallqilni 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   185 -DNYNKG--------------------------------------NLL-----------------------PVGSDTVYF 202
Cdd:pfam01019  241 lEGFDLSsllnsaeylhllieamklayadrtrylgdpdfvpvpveNLLspeyakeraklinpnaafpssyaPEDGGTTHF 320

                          330       340       350
                   ....*....|....*....|....*....|....
gi 465989294   203 TVVDAQGNASSFINSNYMGFGIGLEPGGCGFTLQ 236
Cdd:pfam01019  321 SVVDRDGNAVSFTSTINLGFGSGVVVPGTGILLN 354
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 1388-1483 1.79e-12

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: 65.94  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1388 AINGKLF----GNLHGLTMHVGDKVSWYLMGMGNEVDMHTAHFHGHSF------------DYKRTGVYRADVFDLFPGTF 1451
Cdd:cd04207    21 VINGMPFkegdANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFwvlgsgggpfdaPLNLTNPPWRDTVLVPPGGW 100

                          90       100       110
                  ....*....|....*....|....*....|..
gi 465989294 1452 QTVEMLPKYPGTWLLHCHVTDHIHGGMETTYT 1483
Cdd:cd04207   101 VVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 1386-1481 1.15e-11

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: 63.81  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1386 MHAINGKLFGNLHGLTMHVGDKVSWYLMGMGNEVdmHTAHFHGHSFD-YKRTGV-------YRADVFDLFPGTFQTVEML 1457
Cdd:cd04202    29 YFTINGKSFPATPPLVVKEGDRVRIRLINLSMDH--HPMHLHGHFFLvTATDGGpipgsapWPKDTLNVAPGERYDIEFV 106

                          90       100
                  ....*....|....*....|....*...
gi 465989294 1458 PKYPGTWLLHCHVTDHI----HGGMETT 1481
Cdd:cd04202   107 ADNPGDWMFHCHKLHHAmngmGGGMMTL 134
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 573-679 4.36e-11

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: 61.49  E-value: 4.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   573 FLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGAFYPDNTKdllkkdDAVKPGELYTYRWDVTEDHGpaegd 652
Cdd:pfam07732   24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMDGVPGVTQ------CPIPPGQSFTYRFQVKQQAG----- 92

                           90       100
                   ....*....|....*....|....*..
gi 465989294   653 sncmTRIYHSHTDAPRdvASGLVGPLI 679
Cdd:pfam07732   93 ----TYWYHSHTSGQQ--AAGLAGAII 113
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 575-679 1.04e-10

The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily includes bacterial two domain multicopper oxidases (2dMCOs) with similarity to McoN from Nitrosomonas europaea. 2dMCO is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals.


Pssm-ID: 259929 [Multi-domain]  Cd Length: 119  Bit Score: 60.67  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  575 GPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGAfyPDNTKDllkkddAVKPGELYTYRWDVTEdHGpaegdsn 654
Cdd:cd13860    31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGMDGV--PGITQP------PIQPGETFTYEFTAKQ-AG------- 94

                          90       100
                  ....*....|....*....|....*
gi 465989294  655 cmTRIYHSHTDAPRDVASGLVGPLI 679
Cdd:cd13860    95 --TYMYHSHVDEAKQEDMGLYGAFI 117
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 1386-1486 3.48e-10

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: 64.19  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1386 MHAINGKLFGNLH-GLTMHVGDKVSWYLmgmGNEVDM-HTAHFHGHSFDY-KRTGV-----YRADVFDLFPGtfQTVEML 1457
Cdd:COG2132   317 VWTINGKAFDPDRpDLTVKLGERERWTL---VNDTMMpHPFHLHGHQFQVlSRNGKpppegGWKDTVLVPPG--ETVRIL 391

                          90       100       110
                  ....*....|....*....|....*....|..
gi 465989294 1458 ---PKYPGTWLLHCHVTDHIHGGMETTYTVLP 1486
Cdd:COG2132   392 frfDNYPGDWMFHCHILEHEDAGMMGQFEVVP 423
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 1235-1328 5.48e-10

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: 58.45  E-value: 5.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1235 ILGPLLLANVGDKVTIVFKN-LATRPYSIHAHGVKTDSS-----TVAVTQ----PGETRTYIWKIPDRSGSgkgdpscip 1304
Cdd:cd04206    28 FPGPTIRVKEGDTVEVTVTNnLPNEPTSIHWHGLRQPGTndgdgVAGLTQcpipPGESFTYRFTVDDQAGT--------- 98

                          90       100
                  ....*....|....*....|....
gi 465989294 1305 WAYYSVVDkvKDTYSGLIGTLVVC 1328
Cdd:cd04206    99 FWYHSHVG--GQRADGLYGPLIVE 120
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1237-1330 9.31e-10

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: 58.43  E-value: 9.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1237 GPLLLANVGDKVTIVFKNLATRPYSIHAHGVKTDSSTV------AVTQPGETRTYIWK--IPDRSGSGKGDP-SCIPWAY 1307
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDgtgmnaSIVAPGDTRIYTWRthGGYRRADGSWAEgTAGYWHY 108

                          90       100
                  ....*....|....*....|....*..
gi 465989294 1308 YS-VVDKVKDT---YSGLIGTLVVCPK 1330
Cdd:cd14449   109 HDhVFGTEHGTeglSRGLYGALIVRRV 135
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 731-834 1.43e-09

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: 57.86  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  731 NEDFQESNKMH-SING----YMYGYLPNLTMCEEDKVKWHLFGMGNEADVHSAYFHGQVF-------TERNHRV------ 792
Cdd:cd04207     9 SQTGAPDGTTRwVINGmpfkEGDANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFwvlgsggGPFDAPLnltnpp 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 465989294  793 --DSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAIFE 834
Cdd:cd04207    89 wrDTVLVPPGGWVVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 1388-1484 1.47e-09

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 57.78  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1388 AINGKLFGNLHG-------LTMHVGDkvsWYLMGMGNEVD-MHTAHFHGHSFD-YKRTGV-----YRADVFDLFPGtfQT 1453
Cdd:cd13906    30 AINGTSWTGGDHshlppplATLKRGR---SYVLRLVNETAfLHPMHLHGHFFRvLSRNGRpvpepFWRDTVLLGPK--ET 104

                          90       100       110
                  ....*....|....*....|....*....|...
gi 465989294 1454 VE--MLPKYPGTWLLHCHVTDHIHGGMETTYTV 1484
Cdd:cd13906   105 VDiaFVADNPGDWMFHCHILEHQETGMMGVIRV 137
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 572-679 1.64e-09

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: 57.24  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  572 GFLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGAfyPDNTKDllkkddAVKPGELYTYRWdVTEDHGpaeg 651
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV--PGLTQP------PVPPGESFTYEF-TPPDAG---- 94

                          90       100
                  ....*....|....*....|....*...
gi 465989294  652 dsncmTRIYHSHTDAPRDVASGLVGPLI 679
Cdd:cd13861    95 -----TYWYHPHVGSQEQLDRGLYGPLI 117
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 763-836 1.77e-09

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 57.78  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  763 KWHLFGMGNEAD-VHSAYFHGQVFT--ERN-------HRVDSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAI 832
Cdd:cd13906    55 RSYVLRLVNETAfLHPMHLHGHFFRvlSRNgrpvpepFWRDTVLLGPKETVDIAFVADNPGDWMFHCHILEHQETGMMGV 134


                  ....
gi 465989294  833 FEVK 836
Cdd:cd13906   135 IRVA 138
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 573-703 2.18e-09

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: 61.49  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  573 FLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGafYPdntkdllkkDDAVKPGELYTYRWDVTEDHGpaegd 652
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNAMDG--VP---------GDPIAPGETFTYEFPVPQPAG----- 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 465989294  653 sncmTRIYHSHTDA--PRDVASGLVGPLItcrkgtLDGGSDK--HIDAEFILMFS 703
Cdd:COG2132   106 ----TYWYHPHTHGstAEQVYRGLAGALI------VEDPEEDlpRYDRDIPLVLQ 150
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 575-679 2.81e-09

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: 56.51  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  575 GPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGAFYPdntkdllkkddaVKPGELYTYRWDVTedhgPAeGdsn 654
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDAAMDGTGLGP------------IMPGESFTYEFVAE----PA-G--- 91

                          90       100
                  ....*....|....*....|....*..
gi 465989294  655 cmTRIYHSHTdAP--RDVASGLVGPLI 679
Cdd:cd11024    92 --THLYHCHV-QPlkEHIAMGLYGAFI 115
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 573-679 7.54e-09

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: 55.34  E-value: 7.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  573 FLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVaytkENEGAFYPDNTKDLLKKddAVKPGELYTYRWDVTEDHGpaegd 652
Cdd:cd13857    28 FPGPLIEANQGDRIVVHVTNELDEPTSIHWHGL----FQNGTNWMDGTAGITQC--PIPPGGSFTYNFTVDGQYG----- 96

                          90       100
                  ....*....|....*....|....*..
gi 465989294  653 sncmTRIYHSHTDAprDVASGLVGPLI 679
Cdd:cd13857    97 ----TYWYHSHYST--QYADGLVGPLI 117
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 575-679 8.97e-09

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: 55.18  E-value: 8.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  575 GPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTkeneGAFYPDNTKDLLKKddAVKPGELYTYRWDVtEDHGpaegdsn 654
Cdd:cd13859    31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQM----GSWKMDGVPGVTQP--AIEPGESFTYKFKA-ERPG------- 96

                          90       100
                  ....*....|....*....|....*.
gi 465989294  655 cmTRIYHSHTDAPRDVA-SGLVGPLI 679
Cdd:cd13859    97 --TLWYHCHVNVNEHVGmRGMWGPLI 120
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 702-831 2.36e-08

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: 54.63  E-value: 2.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   702 FSVMDENLSWYlDDSIEKYCSEPAKVDKENEDFQESNKMHSINGYMYGYLPNLTMCEEDKVKWHLFgMGNEADVHSAYFH 781
Cdd:pfam00394    1 EDYVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294   782 GQ---------VFTErNHRVDSISLFPATFVDALMVPKN-PGEWLLSCQVN-DHIEGGMQA 831
Cdd:pfam00394   79 GHkmtvvevdgVYVN-PFTVDSLDIFPGQRYSVLVTANQdPGNYWIVASPNiPAFDNGTAA 138
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 575-683 3.87e-08

The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers, and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. 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: 53.81  E-value: 3.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  575 GPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGAFYPDNtkdllkkddAVKPGELYTYRWDVTEDHGPAEGDSN 654
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTASDGTGMNAS---------IVAPGDTRIYTWRTHGGYRRADGSWA 99

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 465989294  655 CMTR---IYHSHT----DAPRDVASGLVGPLITCRK 683
Cdd:cd14449   100 EGTAgywHYHDHVfgteHGTEGLSRGLYGALIVRRV 135
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 1389-1484 3.92e-08

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: 53.03  E-value: 3.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1389 INGKLFGNLHGLTMHVGDKVswyLMGMGNEVDM-HTAHFHGHSFDYKR-TGVYRA--DVFDLFPGTFQTVEMLPKYPGTW 1464
Cdd:cd13896    19 INGKAYPDADPLRVREGERV---RIVFVNDTMMaHPMHLHGHFFQVENgNGEYGPrkDTVLVPPGETVSVDFDADNPGRW 95

                          90       100
                  ....*....|....*....|
gi 465989294 1465 LLHCHVTDHIHGGMETTYTV 1484
Cdd:cd13896    96 AFHCHNLYHMEAGMMRVVEY 115
g_glut_trans TIGR00066
gamma-glutamyltranspeptidase; Also called gamma-glutamyltranspeptidase (ggt). Some members of ...
 45-236 1.11e-07

gamma-glutamyltranspeptidase; Also called gamma-glutamyltranspeptidase (ggt). Some members of this family have antibiotic synthesis or resistance activities. In the case of a cephalosporin acylase from Pseudomonas sp., the enzyme was shown to retain some gamma-glutamyltranspeptidase activity. Other, more distantly related proteins have ggt-related activities and score below the trusted cutoff. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 129176  Cd Length: 516  Bit Score: 56.31  E-value: 1.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294    45 LTSSAHPL--QIGWDILKNGGNVVDAAMAIAAALNVTELCGTGVGGACFCLCYDANTKQVQGLNGR-----------F-- 109
Cdd:TIGR00066    2 MVASLHALasEIGEDILKEGGNAFDAAVAVGLALAVVEPFMTGLGGGGFMLISGKKTKDTTAIDFRerapakatrdmFld 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   110 -------------------------------------------PSMELVQ--------MCE----------------RKF 122
Cdd:TIGR00066   82 ksgnplpgksltgglaigvpgtvagleaalkkygtlplkdliePAIKLARngfpineaLADtlelyeevllttkedsKDI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   123 ---------PGYKIQL------FQELAKSGKKSFSEGCVAEVIIETVQRNGGLMDLEDFKSH---VTDEIEGNAEHYKVS 184
Cdd:TIGR00066  162 fnptgkplkEGDTLVQkdlaksLELIAENGPDAFYKGDIAESIIDTLQKNGGIMTKKDLAAYdveIRKPLSGDYRGYQVY 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   185 -------------------DNYN-------------------------------KGNLLPV------------------- 195
Cdd:TIGR00066  242 ttpppssggihllqalnilENFDlsqygdgsaetyqllaeamklsyadrsrylgDPEFVDVpleelldkryakelaqsik 321

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   196 -------------------GSDTVYFTVVDAQGNASSFINSNYMGFGIGLEPGGCGFTLQ 236
Cdd:TIGR00066  322 inkvdpkstiypgayqpneGSQTTHFSVVDRDGNAVSLTTTINLEFGSGVHAPDTGILLN 381
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 1386-1478 1.62e-07

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: 51.63  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1386 MHAINGKLFG-NLHGLTMHVGDKVSWYLMgmgNEVDM-HTAHFHGHSF------DYKRTGVYRA--DVFDLFPGTFQTVE 1455
Cdd:cd13902    20 MFLINGKTFDmNRIDFVAKVGEVEVWEVT---NTSHMdHPFHLHGTQFqvleidGNPQKPEYRAwkDTVNLPPGEAVRIA 96

                          90       100
                  ....*....|....*....|...
gi 465989294 1456 MLPKYPGTWLLHCHVTDHIHGGM 1478
Cdd:cd13902    97 TRQDDPGMWMYHCHILEHEDAGM 119
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 566-678 1.91e-07

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: 51.14  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  566 EKPSWLG---FLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAY--TKENEGAfyPDNTKdllkkdDAVKPGELYTYRW 640
Cdd:cd13850    16 EREVILIngqFPGPPIILDEGDEVEILVTNNLPVNTTIHFHGILQrgTPWSDGV--PGVTQ------WPIQPGGSFTYRW 87

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 465989294  641 DVTEDHGpaegdsncmTRIYHSHTdapRDVAS-GLVGPL 678
Cdd:cd13850    88 KAEDQYG---------LYWYHSHY---RGYYMdGLYGPI 114
PLN02191 PLN02191
L-ascorbate oxidase
 573-703 9.06e-07

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 53.48  E-value: 9.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  573 FLGPIIKAEVGDFIIVHLKN-FASRSYTLHPHGVaytkENEGAFYPDNTKDLLKKddAVKPGELYTYRWDVtEDHGpaeg 651
Cdd:PLN02191   51 FPGPTIDAVAGDTIVVHLTNkLTTEGLVIHWHGI----RQKGSPWADGAAGVTQC--AINPGETFTYKFTV-EKPG---- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 465989294  652 dsncmTRIYHSHTDAPRdvASGLVGPLITcrkGTLDGGSDKHI-DAEFILMFS 703
Cdd:PLN02191  120 -----THFYHGHYGMQR--SAGLYGSLIV---DVAKGPKERLRyDGEFNLLLS 162
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 572-679 1.18e-06

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: 48.98  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  572 GFLGPIIKAEVGDFIIVHLKN-FASRSYTLHPHGVaytkENEGAFYPDNTKDLLKKddAVKPGELYTYRWDVtedhgpae 650
Cdd:cd13845    27 QFPGPTIRATAGDTIVVELENkLPTEGVAIHWHGI----RQRGTPWADGTASVSQC--PINPGETFTYQFVV-------- 92

                          90       100
                  ....*....|....*....|....*....
gi 465989294  651 gdSNCMTRIYHSHTDAPRdvASGLVGPLI 679
Cdd:cd13845    93 --DRPGTYFYHGHYGMQR--SAGLYGSLI 117
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 1234-1295 1.44e-06

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: 48.78  E-value: 1.44e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294  1234 EILGPLLLANVGDKVTIVFKNLATRPYSIHAHGVKTDSSTVA-----VTQ----PGETRTYIWKIPDRSGS 1295
Cdd:pfam07732   23 QFPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWMdgvpgVTQcpipPGQSFTYRFQVKQQAGT 93
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1237-1288 1.62e-06

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: 48.42  E-value: 1.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 465989294 1237 GPLLLANVGDKVTIVFKNLATRPYSIHAHGV---KTDSSTVAVTQPGETRTYIWK 1288
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIhdaAMDGTGLGPIMPGESFTYEFV 86
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 1235-1327 1.80e-06

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: 48.38  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1235 ILGPLLLANVGDKVTIVFKNLATRPYSIHAHGVKTDSS---TVAVTQ----PGETRTYIWKIPDrSGSgkgdpscipWAY 1307
Cdd:cd13861    29 VPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAmdgVPGLTQppvpPGESFTYEFTPPD-AGT---------YWY 98

                          90       100
                  ....*....|....*....|
gi 465989294 1308 YSVVDKVKDTYSGLIGTLVV 1327
Cdd:cd13861    99 HPHVGSQEQLDRGLYGPLIV 118
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 1237-1327 2.08e-06

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: 48.41  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1237 GPLLLANVGDKVTIVFKNLATRPYSIHAHGVKTDSS-----TVAVTQ----PGETRTYIWKIPDRSGSgkgdpsciPW-- 1305
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTnwmdgTAGITQcpipPGGSFTYNFTVDGQYGT--------YWyh 101

                          90       100
                  ....*....|....*....|...
gi 465989294 1306 AYYSVvdkvkdTYS-GLIGTLVV 1327
Cdd:cd13857   102 SHYST------QYAdGLVGPLIV 118
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 695-836 2.12e-06

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: 48.79  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  695 DAEFILMFSvmdenlSWYLDDSIEKYcsepakvDKENEDFQesnkMHSINGYMYGYLPNLTMCEEDKVKWHLFGMGNeaD 774
Cdd:cd04202     1 DRDYTLVLQ------EWFVDPGTTPM-------PPEGMDFN----YFTINGKSFPATPPLVVKEGDRVRIRLINLSM--D 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 465989294  775 VHSAYFHGQVF--TERN-HRV--------DSISLFPATFVDALMVPKNPGEWLLSCQVNDHIE----GGMQAIFEVK 836
Cdd:cd04202    62 HHPMHLHGHFFlvTATDgGPIpgsapwpkDTLNVAPGERYDIEFVADNPGDWMFHCHKLHHAMngmgGGMMTLIGYE 138
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 1234-1295 3.77e-06

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: 47.47  E-value: 3.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294 1234 EILGPLLLANVGDKVTIVFKNLATRPYSIHAHGV-KTDS----STVAVTQ----PGETRTYIWKIpDRSGS 1295
Cdd:cd13859    28 QVPGPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVlQMGSwkmdGVPGVTQpaiePGESFTYKFKA-ERPGT 97
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1422-1485 5.11e-06

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: 47.51  E-value: 5.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 465989294 1422 HTAHFHGHSF-----DYKRtGVYRaDVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYTVL 1485
Cdd:cd13909    71 HGMHLHGHHFrailpNGAL-GPWR-DTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGMMSWFRVT 137
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 575-679 5.88e-06

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: 46.85  E-value: 5.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  575 GPIIKAEVGDFIIVHLKNFASRSYT-LHPHGV--AYTKENEGAfyPDNTKDllkkddAVKPGELYTYRWDVTEdHGpaeg 651
Cdd:cd13854    33 GPLIEANWGDTIEVTVINKLQDNGTsIHWHGIrqLNTNWQDGV--PGVTEC------PIAPGDTRTYRFRATQ-YG---- 99

                          90       100
                  ....*....|....*....|....*...
gi 465989294  652 dsncmTRIYHSHTDAprDVASGLVGPLI 679
Cdd:cd13854   100 -----TSWYHSHYSA--QYGDGVVGPIV 120
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 573-679 1.04e-05

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: 50.14  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   573 FLGPIIKAEVGDFIIVHLKN-FASRSYTLHPHGVaytkENEGAFYPDNTKDLLKKddAVKPGELYTYRWDVtedhgpaeg 651
Cdd:TIGR03388   29 FPGPTIRAQAGDTIVVELTNkLHTEGVVIHWHGI----RQIGTPWADGTAGVTQC--AINPGETFIYNFVV--------- 93

                           90       100
                   ....*....|....*....|....*...
gi 465989294   652 dSNCMTRIYHSHTDAPRdvASGLVGPLI 679
Cdd:TIGR03388   94 -DRPGTYFYHGHYGMQR--SAGLYGSLI 118
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 1421-1478 1.22e-05

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: 46.83  E-value: 1.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 465989294 1421 MHTAHFHGHSF----------DYKRTGVY-----RADVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGM 1478
Cdd:cd13901    80 PHPIHLHGHDFyilaqgtgtfDDDGTILNlnnppRRDVAMLPAGGYLVIAFKTDNPGAWLMHCHIAWHASGGL 152
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 1237-1327 1.84e-05

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 45.54  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1237 GPLLLANVGDKVTIVFKNLATRPYSIHAHGV----KTDSSTVAVTQPGETRTYIWKIPDRSGsgkGDPSCIPWAYYSVVD 1312
Cdd:cd13855    32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLpvppDQDGNPHDPVAPGNDRVYRFTLPQDSA---GTYWYHPHPHGHTAE 108

                          90
                  ....*....|....*
gi 465989294 1313 KVkdtYSGLIGTLVV 1327
Cdd:cd13855   109 QV---YRGLAGAFVV 120
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 1237-1295 2.40e-05

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: 44.98  E-value: 2.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 465989294 1237 GPLLLANVGDKVTIVFKNLATRPYSIHAHGVKTDSSTVA-----VTQ----PGETRTYIWKIPDRSGS 1295
Cdd:cd13850    28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTPWSdgvpgVTQwpiqPGGSFTYRWKAEDQYGL 95
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 576-679 3.58e-05

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: 44.57  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  576 PIIKAEVGDFIIVHLKN-FASRSYTLHPHGVAY--TKENEGAFY----PdntkdllkkddaVKPGELYTYRWDVTEDHGp 648
Cdd:cd13851    32 PPIEVNKGDTVVIHATNsLGDQPTSLHFHGLFQngTNYMDGPVGvtqcP------------IPPGQSFTYEFTVDTQVG- 98

                          90       100       110
                  ....*....|....*....|....*....|.
gi 465989294  649 aegdsncmTRIYHSHTDAprDVASGLVGPLI 679
Cdd:cd13851    99 --------TYWYHSHDGG--QYPDGLRGPFI 119
CuRO_1_CueO_FtsP cd04232
The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, ...
 573-679 3.70e-05

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


Pssm-ID: 259894 [Multi-domain]  Cd Length: 120  Bit Score: 44.49  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  573 FLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGAfyPDNTkdllkkddaVKPGELYTYRWDVTEdhgPAegd 652
Cdd:cd04232    29 YLGPTIRVKKGDTVRINVTNNLDEETTVHWHGLHVPGEMDGG--PHQP---------IAPGQTWSPTFTIDQ---PA--- 91

                          90       100
                  ....*....|....*....|....*....
gi 465989294  653 SNCMtriYHSHTDA--PRDVASGLVGPLI 679
Cdd:cd04232    92 ATLW---YHPHTHGktAEQVYRGLAGLFI 117
CuRO_3_Tth-MCO_like cd13900
The third cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus ...
 1389-1478 5.59e-05

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: 44.16  E-value: 5.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1389 INGKLFG-NLHGLTMHVGDKVSWYLMGMGNEvdMHTAHFHGHSF-------DYKRTGVYRaDVFDLFPGtfQTVEMLPK- 1459
Cdd:cd13900    22 INGKPFDpDRPDRTVRLGTVEEWTLINTSGE--DHPFHIHVNPFqvvsingKPGLPPVWR-DTVNVPAG--GSVTIRTRf 96

                          90       100
                  ....*....|....*....|.
gi 465989294 1460 --YPGTWLLHCHVTDHIHGGM 1478
Cdd:cd13900    97 rdFTGEFVLHCHILDHEDQGM 117
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 1350-1482 6.42e-05

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: 44.62  E-value: 6.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  1350 VFDENESWYlDENIKTYSANPDKVNKEDEEFIESNKMHAINGKLFGNLHGLTMHVGDKVSWYLMgMGNEVDMHTAHFHGH 1429
Cdd:pfam00394    3 YVITLSDWY-HKDAKDLEKELLASGKAPTDFPPVPDAVLINGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIEGH 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  1430 SF-----DYKRTGVYRADVFDLFPGTFQTVEMLPK-YPGTWLLHCHVT-DHIHGGMETTY 1482
Cdd:pfam00394   81 KMtvvevDGVYVNPFTVDSLDIFPGQRYSVLVTANqDPGNYWIVASPNiPAFDNGTAAAI 140
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 733-837 7.11e-05

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: 44.35  E-value: 7.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294   733 DFQESNKMHSINGYMYGYLPN-LTMCEEDKVKWHLFGMGNeaDVHSAYFHGQVF---------------TERNH----RV 792
Cdd:pfam07731   14 SGNFRRNDWAINGLLFPPNTNvITLPYGTVVEWVLQNTTT--GVHPFHLHGHSFqvlgrgggpwpeedpKTYNLvdpvRR 91

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 465989294   793 DSISLFPATFVDALMVPKNPGEWLLSCQVNDHIEGGMQAIFEVKD 837
Cdd:pfam07731   92 DTVQVPPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVVRP 136
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 1422-1487 9.27e-05

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: 43.41  E-value: 9.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 465989294 1422 HTAHFHGHSFDYKRTGVYRadvfDLFPGTFQTVEMLPKYPGTWLLHCHV---TDHIHGGMETTYTVLPK 1487
Cdd:cd11024    55 HTIHFHGIHDAAMDGTGLG----PIMPGESFTYEFVAEPAGTHLYHCHVqplKEHIAMGLYGAFIVDPK 119
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 1416-1478 1.02e-04

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: 44.19  E-value: 1.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 465989294 1416 GNEVDMHTAHFHGHSFDYKR---TGVY------RADVFDL-FPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGM 1478
Cdd:cd13903    67 GAIGGPHPFHLHGHAFSVVRsagSNTYnyvnpvRRDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGL 139
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 1389-1477 1.12e-04

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


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 43.21  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1389 INGKLFGNLHG-LTMHVGDKvswYLMGMGNEV-DMHTAHFHGHSFDYKR-----TGVYRADVFDLFPGTFQTVEMLPKYP 1461
Cdd:cd13908    23 INGKSYPDEDPpLVVQQGRR---YRLVFRNASdDAHPMHLHRHTFEVTRidgkpTSGLRKDVVMLGGYQRVEVDFVADNP 99

                          90
                  ....*....|....*.
gi 465989294 1462 GTWLLHCHVTDHIHGG 1477
Cdd:cd13908   100 GLTLFHCHQQLHMDYG 115
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 1390-1487 1.49e-04

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: 42.86  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1390 NGKLFGNLhgLTMHVGDKVSWYLMGMGNEVDMHTAHFHGhsfdykRTGVYRADVFDLF-PGTFQTVEMLPKYPGTWLLHC 1468
Cdd:cd04201    27 DGDIPGPM--LRVREGDTVELHFSNNPSSTMPHNIDFHA------ATGAGGGAGATFIaPGETSTFSFKATQPGLYVYHC 98

                          90       100
                  ....*....|....*....|..
gi 465989294 1469 HVTD---HIHGGMETTYTVLPK 1487
Cdd:cd04201    99 AVAPvpmHIANGMYGLILVEPK 120
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 1236-1295 1.91e-04

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: 42.66  E-value: 1.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 465989294 1236 LGPLLLANVGDKVTIVFKNLATRPYSIHAHGV----KTDSSTVAVTQPGETRTYIWKIPDRSGS 1295
Cdd:cd13852    23 LGPILRLRKGQKVRITFKNNLPEPTIIHWHGLhvpaAMDGHPRYAIDPGETYVYEFEVLNRAGT 86
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 575-679 1.96e-04

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


Pssm-ID: 259924 [Multi-domain]  Cd Length: 121  Bit Score: 42.46  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  575 GPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGafypdntkdllKKDDAVKPGELYTYRWDVTEDhgpaegdsN 654
Cdd:cd13855    32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGLPVPPDQDG-----------NPHDPVAPGNDRVYRFTLPQD--------S 92

                          90       100
                  ....*....|....*....|....*..
gi 465989294  655 CMTRIYHSHTD--APRDVASGLVGPLI 679
Cdd:cd13855    93 AGTYWYHPHPHghTAEQVYRGLAGAFV 119
CuRO_1_MaLCC_like cd13854
The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 1237-1288 2.04e-04

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: 42.61  E-value: 2.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 465989294 1237 GPLLLANVGDKVTI-VFKNLATRPYSIHAHGVK-----TDSSTVAVTQ----PGETRTYIWK 1288
Cdd:cd13854    33 GPLIEANWGDTIEVtVINKLQDNGTSIHWHGIRqlntnWQDGVPGVTEcpiaPGDTRTYRFR 94
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 1238-1295 2.20e-04

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: 42.64  E-value: 2.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 465989294 1238 PLLLANVGDKVTI-VFKNLATRPYSIHAHGVKTDSST-----VAVTQ----PGETRTYIWKIPDRSGS 1295
Cdd:cd13851    32 PPIEVNKGDTVVIhATNSLGDQPTSLHFHGLFQNGTNymdgpVGVTQcpipPGQSFTYEFTVDTQVGT 99
CuRO_1_CuNIR cd11020
Cupredoxin domain 1 of Copper-containing nitrite reductase; Copper-containing nitrite ...
 1237-1294 2.28e-04

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: 42.20  E-value: 2.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 465989294 1237 GPLLLANVGDKVTIVFKNLATR--PYSIHAHGVKTDSSTVAVT-QPGETRTYIWKiPDRSG 1294
Cdd:cd11020    32 GPVIRVREGDTVELTLTNPGTNtmPHSIDFHAATGPGGGEFTTiAPGETKTFSFK-ALYPG 91
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 1237-1327 3.53e-04

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: 41.80  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1237 GPLLLANVGDKVTIVFKNLATRPYSIHAHGVKTDSS-------TVAVTQPGETRTYIWKIpDRSGSgkgdpscipWAYYS 1309
Cdd:cd13860    31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGLPVPNGmdgvpgiTQPPIQPGETFTYEFTA-KQAGT---------YMYHS 100

                          90
                  ....*....|....*...
gi 465989294 1310 VVDKVKDTYSGLIGTLVV 1327
Cdd:cd13860   101 HVDEAKQEDMGLYGAFIV 118
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 1235-1288 3.82e-04

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: 41.71  E-value: 3.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 465989294 1235 ILGPLLLANVGDKVTIVFKN--LATRPYSIHAHGVKTDSSTVAVTQ--PGETRTYIWK 1288
Cdd:cd04201    30 IPGPMLRVREGDTVELHFSNnpSSTMPHNIDFHAATGAGGGAGATFiaPGETSTFSFK 87
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 1422-1486 4.37e-04

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: 42.63  E-value: 4.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1422 HTAHFHGHSFD--YKRTGVY----------------RADVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGMETTYT 1483
Cdd:cd13899    78 HPFHLHGHKFQvvQRSPDVAsddpnppinefpenpmRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGLAATFI 157


                  ...
gi 465989294 1484 VLP 1486
Cdd:cd13899   158 EAP 160
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 1439-1478 4.77e-04

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: 42.63  E-value: 4.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 465989294 1439 YRaDVFDLFPGTFQTVEMLPKY----PGTWLLHCHVTDHIHGGM 1478
Cdd:cd13898   115 LR-DTFTTPPSTEGPSWLVIRYhvvnPGAWLLHCHIQSHLAGGM 157
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 573-679 5.03e-04

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: 41.55  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  573 FLGPIIKAEVGDFIIVHLKNFAS-----RSYTLHPHGVAYTKENegafYPDNTKDLLKKddAVKPGELYTYRWDVTEDHG 647
Cdd:cd13856    28 FPGPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTN----YADGPAFVTQC--PIAPNHSFTYDFTAGDQAG 101

                          90       100       110
                  ....*....|....*....|....*....|..
gi 465989294  648 paegdsncmTRIYHSHTDAprDVASGLVGPLI 679
Cdd:cd13856   102 ---------TFWYHSHLST--QYCDGLRGPLV 122
CuRO_1_McoP_like cd13852
The first cupredoxin domain of multicopper oxidase McoP and similar proteins; This family ...
 572-679 5.48e-04

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: 41.12  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  572 GFLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVAYTKENEGafYPDNtkdllkkddAVKPGELYTYRWDVTEDHGpaeg 651
Cdd:cd13852    21 SYLGPILRLRKGQKVRITFKNNLPEPTIIHWHGLHVPAAMDG--HPRY---------AIDPGETYVYEFEVLNRAG---- 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 465989294  652 dsncmTRIYHSHTD--APRDVASGLVGPLI 679
Cdd:cd13852    86 -----TYWYHPHPHglTAKQVYRGLAGLFL 110
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 1417-1490 9.82e-04

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: 41.25  E-value: 9.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1417 NEVDMHTAHFHGHSF---DYKrTGVYRA---------------DVFDLFPGTFQTVEMLPKYPGTWLLHCHVTDHIHGGM 1478
Cdd:cd13893    62 NASEQHPWHLHGHDFwvlGYG-LGGFDPaadpsslnlvnppmrNTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGM 140

                          90
                  ....*....|..
gi 465989294 1479 ETTYTVLPKEVR 1490
Cdd:cd13893   141 GVVFAEGVERVG 152
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 573-679 1.71e-03

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: 39.94  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  573 FLGPIIKAEVGDFIIVHLKNFASRSYTLHPHGVaYTKEN---EGAFY----PdntkdllkkddaVKPGELYTYRWDVTED 645
Cdd:cd13849    26 FPGPTIRVHEGDTVVVNVTNRSPYNITIHWHGI-RQLRSgwaDGPAYitqcP------------IQPGQSYTYRFTVTGQ 92

                          90       100       110
                  ....*....|....*....|....*....|....
gi 465989294  646 HGpaegdsncmTRIYHSHTDAPRdvaSGLVGPLI 679
Cdd:cd13849    93 EG---------TLWWHAHISWLR---ATVYGAFI 114
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 936-988 1.91e-03

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: 39.58  E-value: 1.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 465989294  936 HVSPGATYTYEWKVSEDVGptqedpdclTWLYYSAADSVKDTnsGLVGPLLVC 988
Cdd:cd04206    79 PIPPGESFTYRFTVDDQAG---------TFWYHSHVGGQRAD--GLYGPLIVE 120
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 1461-1484 4.25e-03

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: 39.16  E-value: 4.25e-03
                          10        20
                  ....*....|....*....|....
gi 465989294 1461 PGTWLLHCHVTDHIHGGMETTYTV 1484
Cdd:cd13897   113 PGVWFMHCHFERHTSWGMATVFIV 136
PLN02604 PLN02604
oxidoreductase
 572-679 5.96e-03

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 41.00  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294  572 GFLGPIIKAEVGDFIIVHLKN-FASRSYTLHPHGVaytkENEGAFYPDNTKDLLKKddAVKPGELYTYRWDVTEdhgPAe 650
Cdd:PLN02604   51 RSPGPTILAQQGDTVIVELKNsLLTENVAIHWHGI----RQIGTPWFDGTEGVTQC--PILPGETFTYEFVVDR---PG- 120

                          90       100
                  ....*....|....*....|....*....
gi 465989294  651 gdsncmTRIYHSHTDAPRdvASGLVGPLI 679
Cdd:PLN02604  121 ------TYLYHAHYGMQR--EAGLYGSIR 141
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 1422-1479 7.51e-03

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


Pssm-ID: 259972 [Multi-domain]  Cd Length: 174  Bit Score: 39.20  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 465989294 1422 HTAHFHGHSF--------DYKRTG---------VYRADVFDLFPGTFQ------TVeMLPKY-----------PGTWLLH 1467
Cdd:cd13905    70 HPFHLHGHSFyvlgmgfpGYNSTTgeilsqnwnNKLLDRGGLPGRNLVnpplkdTV-VVPNGgyvvirfradnPGYWLLH 148

                          90
                  ....*....|..
gi 465989294 1468 CHVTDHIHGGME 1479
Cdd:cd13905   149 CHIEFHLLEGMA 160
 
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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