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Conserved domains on  [gi|1512432618|ref|NP_001354171|]
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hephaestin isoform b [Homo sapiens]

Protein Classification

multicopper oxidase( domain architecture ID 10362920)

multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which may contain three cupredoxin domains that include one mononuclear and one trinuclear copper center

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 110-305 2.16e-131

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: 391.45  E-value: 2.16e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 110 GKVRQYFIEAHEIQWDYGPMGHDGSTGKNLREPGSISDKFFQKSSSRIGGTYWKVRYEAFQDETFQEKMHL-EEDRHLGI 188
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRsKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 189 LGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYNDGSSYPGLVAKPFEKVTYRWTVPPHAGPTAQDPACL 268
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1512432618 269 TWMYFSAADPIRDTNSGLVGPLLVCRAGALGADGKQK 305
Cdd:cd04224   161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 466-638 2.52e-111

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: 338.29  E-value: 2.52e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 466 RIYYIMAEEVEWDYCPDRSWEREWHNQSEKdSYGYIFLSNKDGLLGSRYKKAVFREYTDGTFRIPRPRTGPEEHLGILGP 545
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEE-SPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 546 LIKGEVGDILTVVFKNNASRPYSVHAHGVLESTTvWPLAAEPGEVVTYQWNIPERSGPGPNDSACVSWIYYSAVDPIKDM 625
Cdd:cd04225    80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSS-WVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDL 158

                         170
                  ....*....|...
gi 1512432618 626 YSGLVGPLAICQK 638
Cdd:cd04225   159 YSGLIGPLVICRR 171
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 308-451 9.49e-88

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: 275.51  E-value: 9.49e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 308 DKEFFLLFTVLDENKSWYSNANQAAAMLDFRLLSEDIEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 387
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512432618 388 VHGVMFQGNTVQLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNVSQC 451
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 653-796 2.20e-69

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 cd11012:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 145  Bit Score: 226.29  E-value: 2.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 653 EFALLFLIFDENKSWYLEENVATHgSQDPGSINLQDETFLESNKMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDVDL 732
Cdd:cd11012     3 EFALLFLVFDENESWYLDENIKTY-SDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512432618 733 HTIHFHAESFLYRNGENYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTVF 796
Cdd:cd11012    82 HTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
Cupredoxin super family cl19115
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 1-96 3.80e-61

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 cd11021:

Pssm-ID: 473140 [Multi-domain]  Cd Length: 141  Bit Score: 203.47  E-value: 3.80e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   1 MHAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRGHHTDVANIFPATFVTAEMVPWEPGTWLISC 80
Cdd:cd11021    46 MHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSC 125

                          90
                  ....*....|....*.
gi 1512432618  81 QVNSHFRDGMQALYKV 96
Cdd:cd11021   126 QVNDHLKAGMQAFYEV 141
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 110-305 2.16e-131

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: 391.45  E-value: 2.16e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 110 GKVRQYFIEAHEIQWDYGPMGHDGSTGKNLREPGSISDKFFQKSSSRIGGTYWKVRYEAFQDETFQEKMHL-EEDRHLGI 188
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRsKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 189 LGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYNDGSSYPGLVAKPFEKVTYRWTVPPHAGPTAQDPACL 268
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1512432618 269 TWMYFSAADPIRDTNSGLVGPLLVCRAGALGADGKQK 305
Cdd:cd04224   161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 466-638 2.52e-111

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: 338.29  E-value: 2.52e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 466 RIYYIMAEEVEWDYCPDRSWEREWHNQSEKdSYGYIFLSNKDGLLGSRYKKAVFREYTDGTFRIPRPRTGPEEHLGILGP 545
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEE-SPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 546 LIKGEVGDILTVVFKNNASRPYSVHAHGVLESTTvWPLAAEPGEVVTYQWNIPERSGPGPNDSACVSWIYYSAVDPIKDM 625
Cdd:cd04225    80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSS-WVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDL 158

                         170
                  ....*....|...
gi 1512432618 626 YSGLVGPLAICQK 638
Cdd:cd04225   159 YSGLIGPLVICRR 171
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 308-451 9.49e-88

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: 275.51  E-value: 9.49e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 308 DKEFFLLFTVLDENKSWYSNANQAAAMLDFRLLSEDIEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 387
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512432618 388 VHGVMFQGNTVQLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNVSQC 451
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 653-796 2.20e-69

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: 226.29  E-value: 2.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 653 EFALLFLIFDENKSWYLEENVATHgSQDPGSINLQDETFLESNKMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDVDL 732
Cdd:cd11012     3 EFALLFLVFDENESWYLDENIKTY-SDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512432618 733 HTIHFHAESFLYRNGENYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTVF 796
Cdd:cd11012    82 HTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1-96 3.80e-61

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: 203.47  E-value: 3.80e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   1 MHAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRGHHTDVANIFPATFVTAEMVPWEPGTWLISC 80
Cdd:cd11021    46 MHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSC 125

                          90
                  ....*....|....*.
gi 1512432618  81 QVNSHFRDGMQALYKV 96
Cdd:cd11021   126 QVNDHLKAGMQAFYEV 141
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 695-795 6.72e-16

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: 75.16  E-value: 6.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 695 NKMHAINGKLY-ANLRGLTMYQGERVAWYMLAMGQDVdlHTIHFHAESF--LYRNGENY--------------RADVVDL 757
Cdd:pfam07731  19 RNDWAINGLLFpPNTNVITLPYGTVVEWVLQNTTTGV--HPFHLHGHSFqvLGRGGGPWpeedpktynlvdpvRRDTVQV 96

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1512432618 758 FPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:pfam07731  97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVV 134
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 697-795 4.41e-12

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: 69.19  E-value: 4.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 697 MHAINGKLYANLR-GLTMYQGERVAWYMLAMGQDvdLHTIHFHAESF--LYRNG----ENYRADVVDLFPGTFEVVEMVA 769
Cdd:COG2132   317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTMM--PHPFHLHGHQFqvLSRNGkpppEGGWKDTVLVPPGETVRILFRF 394

                          90       100
                  ....*....|....*....|....*..
gi 1512432618 770 SN-PGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:COG2132   395 DNyPGDWMFHCHILEHEDAGMMGQFEV 421
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 4-100 4.70e-07

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: 50.01  E-value: 4.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   4 INGFVFGNLPELNMCAQKRVAWHLFgMGNEIDVHTAFFHGQMLT---TRGHHT-----DVANIFPATF----VTAEMvpw 71
Cdd:pfam00394  41 INGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIEGHKMTvveVDGVYVnpftvDSLDIFPGQRysvlVTANQ--- 116

                          90       100       110
                  ....*....|....*....|....*....|
gi 1512432618  72 EPGTWLISCQVN-SHFRDGMQALYKVKSCS 100
Cdd:pfam00394 117 DPGNYWIVASPNiPAFDNGTAAAILRYSGA 146
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 741-795 2.15e-06

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


Pssm-ID: 132431 [Multi-domain]  Cd Length: 538  Bit Score: 51.38  E-value: 2.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1512432618 741 SFLYRngenYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:TIGR03390 481 TMLYR----YAVKVVPGAPAGWRAWRIRVTNPGVWMMHCHILQHMVMGMQTVWVF 531
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 188-292 3.53e-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: 46.86  E-value: 3.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 188 ILGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFyekdYEGTVYNDGSSY-PGLVAKPFEKVTYRWTVPPHAGptaqdpa 266
Cdd:pfam07732  24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQ----QRGTPWMDGVPGvTQCPIPPGQSFTYRFQVKQQAG------- 92

                          90       100
                  ....*....|....*....|....*.
gi 1512432618 267 clTWMYFSAADPIRdtNSGLVGPLLV 292
Cdd:pfam07732  93 --TYWYHSHTSGQQ--AAGLAGAIII 114
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 188-380 3.76e-06

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: 50.32  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 188 ILGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDyegtvyNDGssYPGLVAKPFEKVTYRWTVPPHAGptaqdpac 267
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNA------MDG--VPGDPIAPGETFTYEFPVPQPAG-------- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 268 lTWMYFSAADPIRDTN--SGLVGPLLVcragaLGADGKQKGVDKEFFLLFTvldenkswysnanqaaamlDFRLlseDIE 345
Cdd:COG2132   106 -TYWYHPHTHGSTAEQvyRGLAGALIV-----EDPEEDLPRYDRDIPLVLQ-------------------DWRL---DDD 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1512432618 346 GFQDSNRMHAINGFLFS----N---LPRLDMCKGDTVAWHLL 380
Cdd:COG2132   158 GQLLYPMDAAMGGRLGDtllvNgrpNPTLEVRPGERVRLRLL 199
PLN02191 PLN02191
L-ascorbate oxidase
 753-793 1.88e-05

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 48.47  E-value: 1.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1512432618 753 DVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLF 793
Cdd:PLN02191  504 NTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVF 544
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 542-602 6.95e-05

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: 43.00  E-value: 6.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512432618 542 ILGPLIKGEVGDILTVVFKNNASRPYSVHAHGVLESTTVW----------PLAaePGEVVTYQWNIPERSG 602
Cdd:pfam07732  24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWmdgvpgvtqcPIP--PGQSFTYRFQVKQQAG 92
 
Name Accession Description Interval E-value
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 110-305 2.16e-131

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: 391.45  E-value: 2.16e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 110 GKVRQYFIEAHEIQWDYGPMGHDGSTGKNLREPGSISDKFFQKSSSRIGGTYWKVRYEAFQDETFQEKMHL-EEDRHLGI 188
Cdd:cd04224     1 GKVRHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRsKEEEHLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 189 LGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYNDGSSYPGLVAKPFEKVTYRWTVPPHAGPTAQDPACL 268
Cdd:cd04224    81 LGPVIRAEVGDTIKVTFRNKASRPFSIQPHGVFYEKNYEGAMYRDGDPSPGSHVSPGETFTYEWTVPEGVGPTNQDPPCL 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1512432618 269 TWMYFSAADPIRDTNSGLVGPLLVCRAGALGADGKQK 305
Cdd:cd04224   161 TYLYFSAVDPVRDTNSGLVGPLLVCKKGSLNANGRQK 197
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 466-638 2.52e-111

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: 338.29  E-value: 2.52e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 466 RIYYIMAEEVEWDYCPDRSWEREWHNQSEKdSYGYIFLSNKDGLLGSRYKKAVFREYTDGTFRIPRPRTGPEEHLGILGP 545
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEE-SPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSVPKERTAEEEHLGILGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 546 LIKGEVGDILTVVFKNNASRPYSVHAHGVLESTTvWPLAAEPGEVVTYQWNIPERSGPGPNDSACVSWIYYSAVDPIKDM 625
Cdd:cd04225    80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVKTDSS-WVAPTEPGETQTYTWKIPERSGPGVEDSNCISWAYYSTVDQIKDL 158

                         170
                  ....*....|...
gi 1512432618 626 YSGLVGPLAICQK 638
Cdd:cd04225   159 YSGLIGPLVICRR 171
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 308-451 9.49e-88

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: 275.51  E-value: 9.49e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 308 DKEFFLLFTVLDENKSWYSNANQAAAMLDFRLLSEDIEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 387
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQFTLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512432618 388 VHGVMFQGNTVQLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNVSQC 451
Cdd:cd11022    81 VHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTVSQC 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 653-796 2.20e-69

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: 226.29  E-value: 2.20e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 653 EFALLFLIFDENKSWYLEENVATHgSQDPGSINLQDETFLESNKMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDVDL 732
Cdd:cd11012     3 EFALLFLVFDENESWYLDENIKTY-SDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512432618 733 HTIHFHAESFLYRNGENYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTVF 796
Cdd:cd11012    82 HTAHFHGHSFDYKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTVL 145
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 466-638 1.84e-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: 219.58  E-value: 1.84e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 466 RIYYIMAEEVEWDYCPDRSWEREWHNQSekdsygyIFLSNKDGLLGSRYKKAVFREYTDGTFRIPRPRtgpEEHLGILGP 545
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSGLAEKDLSYRN-------QYLDNGPFRIGRSYKKVVYREYTDESFTTPGPQ---PEHLGILGP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 546 LIKGEVGDILTVVFKNNASRPYSVHAHGV-----------LESTTVWPLAAE---PGEVVTYQWNIPERSGPGPNDSACV 611
Cdd:cd04199    71 TIRAEVGDTIKVHFKNKASRPYSIHPHGVsyekdsegasySDQTGPDEKKDDavaPGETYTYVWIVTEESGPTKGDPACL 150

                         170       180
                  ....*....|....*....|....*..
gi 1512432618 612 SWIYYSAVDPIKDMYSGLVGPLAICQK 638
Cdd:cd04199   151 TWAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_1_ceruloplasmin_like cd04199
Cupredoxin domains 1, 3, and 5 of ceruloplasmin and similar proteins; This family includes the ...
 113-295 2.67e-65

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: 216.50  E-value: 2.67e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 113 RQYFIEAHEIQWDYGPMGhdgsTGKNLREPGSIsdkFFQKSSSRIGGTYWKVRYEAFQDETFqeKMHLEEDRHLGILGPV 192
Cdd:cd04199     1 RHYYIAAEEIDWDYAPSG----LAEKDLSYRNQ---YLDNGPFRIGRSYKKVVYREYTDESF--TTPGPQPEHLGILGPT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 193 IRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYNDGSSYPGLVA---KPFEKVTYRWTVPPHAGPTAQDPACLT 269
Cdd:cd04199    72 IRAEVGDTIKVHFKNKASRPYSIHPHGVSYEKDSEGASYSDQTGPDEKKDdavAPGETYTYVWIVTEESGPTKGDPACLT 151

                         170       180
                  ....*....|....*....|....*.
gi 1512432618 270 WMYFSAADPIRDTNSGLVGPLLVCRA 295
Cdd:cd04199   152 WAYYSHVDLEKDINSGLIGPLLICKK 177
CuRO_3_ceruloplasmin cd04224
The third cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 466-645 3.92e-65

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: 216.57  E-value: 3.92e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 466 RIYYIMAEEVEWDYCPDRSWEREWHNQSEKDSYGYIFLSNKDGLLGSRYKKAVFREYTDGTFRIPRPRTGPEEHLGILGP 545
Cdd:cd04224     4 RHYFIAAEEIMWDYAPSGKNLFTGQNLTAPGSDSEVFFQRNETRIGGTYWKVRYVEYTDATFTTRKHRSKEEEHLGILGP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 546 LIKGEVGDILTVVFKNNASRPYSVHAHGVL-----EST-----TVWPLA-AEPGEVVTYQWNIPERSGPGPNDSACVSWI 614
Cdd:cd04224    84 VIRAEVGDTIKVTFRNKASRPFSIQPHGVFyeknyEGAmyrdgDPSPGShVSPGETFTYEWTVPEGVGPTNQDPPCLTYL 163

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1512432618 615 YYSAVDPIKDMYSGLVGPLAICQKGILEPHG 645
Cdd:cd04224   164 YFSAVDPVRDTNSGLVGPLLVCKKGSLNANG 194
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1-96 3.80e-61

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: 203.47  E-value: 3.80e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   1 MHAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRGHHTDVANIFPATFVTAEMVPWEPGTWLISC 80
Cdd:cd11021    46 MHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVDIHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSC 125

                          90
                  ....*....|....*.
gi 1512432618  81 QVNSHFRDGMQALYKV 96
Cdd:cd11021   126 QVNDHLKAGMQAFYEV 141
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 651-795 4.72e-60

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: 200.71  E-value: 4.72e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 651 DREFALLFLIFDENKSWYLEENVATHgSQDPGSINLQDETFLESNKMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDV 730
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRF-CDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512432618 731 DLHTIHFHAESFLYRngeNYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:cd04200    80 DVHSIHFHGQTFLYK---GYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 466-639 1.18e-55

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: 189.67  E-value: 1.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 466 RIYYIMAEEVEWDYCPdrswerewHNQSeKDSYGYIflsNKDGLlgsrYKKAVFREYTDGTFRIPRPRTGPEEHLGILGP 545
Cdd:cd14451     2 RRYYIAAEEEEWDYAG--------YGKS-RLDKTQN---ERDTV----FKKVVFRRYLDSTFSTPDIQGEYEEHLGILGP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 546 LIKGEVGDILTVVFKNNASRPYSVHAHGVL-----------ESTTVW---PLAAEPGEVVTYQWNIPERSGPGPNDSACV 611
Cdd:cd14451    66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSyeksseglsydDESPDWfkkDDAVQPNGTYTYVWYANPRSGPENNGSDCR 145

                         170       180
                  ....*....|....*....|....*...
gi 1512432618 612 SWIYYSAVDPIKDMYSGLVGPLAICQKG 639
Cdd:cd14451   146 TWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 651-795 5.80e-54

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: 183.83  E-value: 5.80e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 651 DREFALLFLIFDENKSWYLEENVATHGSqDPGSINLQDETFLESNKMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDV 730
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCS-EPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512432618 731 DLHTIHFHAESFLYRngeNYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:cd11021    80 DIHSAFFHGQTLTDR---GHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_5_FV_like cd14451
The fifth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 113-296 2.63e-53

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: 183.12  E-value: 2.63e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 113 RQYFIEAHEIQWDYGPMGHDGSTGKNLREPGsisdkffqksssriggTYWKVRYEAFQDETFQE-KMHLEEDRHLGILGP 191
Cdd:cd14451     2 RRYYIAAEEEEWDYAGYGKSRLDKTQNERDT----------------VFKKVVFRRYLDSTFSTpDIQGEYEEHLGILGP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 192 VIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYNDGSSY---PGLVAKPFEKVTYRWTVPPHAGPTAQDPACL 268
Cdd:cd14451    66 VIRAEVDDVIQVFFKNLASRPYSLHAHGLSYEKSSEGLSYDDESPDwfkKDDAVQPNGTYTYVWYANPRSGPENNGSDCR 145

                         170       180
                  ....*....|....*....|....*...
gi 1512432618 269 TWMYFSAADPIRDTNSGLVGPLLVCRAG 296
Cdd:cd14451   146 TWAYYSAVNPEKDIHSGLIGPLLICRKG 173
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 113-294 2.77e-53

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: 183.39  E-value: 2.77e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 113 RQYFIEAHEIQWDYGPMGHDGSTGKNLREPgSISDKFFQKSSSRIGGTYWKVRYEAFQDETFQEKmhLEEDRHLGILGPV 192
Cdd:cd04222     1 REYYIGIRETQWDYAPSGKNLITNQTFDDD-EHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRTE--IEKPVWLGFLGPI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 193 IRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYNDGSSYPGL---VAKPFEKVTYRWTVPPHAGPTAQDPACLT 269
Cdd:cd04222    78 LKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKENEGALYPDNTSGFEKaddAVPPGGSYTYTWTVPEEQAPTKADANCLT 157

                         170       180
                  ....*....|....*....|....*
gi 1512432618 270 WMYFSAADPIRDTNSGLVGPLLVCR 294
Cdd:cd04222   158 RIYHSHIDAPKDIASGLIGPLIICK 182
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 113-296 8.31e-52

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: 179.15  E-value: 8.31e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 113 RQYFIEAHEIQWDYGPmghdgsTGKNLREPGSISDKFF---QKSSSRIGGTYWKVRYEAFQDETFQEKmhLEEDRHLGIL 189
Cdd:cd04229     1 RTYYIAAEEVDWDYAP------SGKNKCCLGDDLEVSTldsQPGPYTIGSTYTKARYREYTDNSFSTP--KPTPAYLGIL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 190 GPVIRAEVGDTIQVVFYNRASQ-PFSMQPHGVFYEKDYEGTvyNDGSsypGLVAKPFEKVTYRWTVPPHAGPTAQDPACL 268
Cdd:cd04229    73 GPVIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGT--TDGA---GDVVAPGETYTYRWIVPEDAGPGPGDPSSR 147

                         170       180
                  ....*....|....*....|....*...
gi 1512432618 269 TWMYFSAADPIRDTNSGLVGPLLVCRAG 296
Cdd:cd04229   148 LWLYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 111-295 9.71e-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: 173.52  E-value: 9.71e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 111 KVRQYFIEAHEIQWDYGPMGHDgSTGKNLREpgsisdKFFQKSSSRIGGTYWKVRYEAFQDETFQEKMHLEEDRHLGILG 190
Cdd:cd14450     1 KNWEYFIAAEEVIWDYAPSIPE-NMDKRYRS------QYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKEEGILG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 191 PVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYND---GSSYPGLVAKPFEKVTYRWTVPPHAGPTAQDPAC 267
Cdd:cd14450    74 PVIRAQVRDTIKIVFKNKASRPYSIYPHGVTVSKAAEGASYPPdprGNETQNKAVQPGETYTYKWNILETDEPTARDPRC 153

                         170       180
                  ....*....|....*....|....*...
gi 1512432618 268 LTWMYFSAADPIRDTNSGLVGPLLVCRA 295
Cdd:cd14450   154 LTRMYHSAVDITRDIASGLIGPLLICKS 181
CuRO_1_ceruloplasmin cd04222
The first cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 466-638 2.81e-49

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: 172.22  E-value: 2.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 466 RIYYIMAEEVEWDYCPDRSweREWHNQS-EKDSYGYIFLSNKDGLLGSRYKKAVFREYTDGTFR--IPRPrtgpeEHLGI 542
Cdd:cd04222     1 REYYIGIRETQWDYAPSGK--NLITNQTfDDDEHASVFLKRGPDRIGRVYKKAVYLQYTDDTYRteIEKP-----VWLGF 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 543 LGPLIKGEVGDILTVVFKNNASRPYSVHAHGVLESTT----VWPL----------AAEPGEVVTYQWNIPERSGPGPNDS 608
Cdd:cd04222    74 LGPILKAEVGDVIVVHLKNFASRPYSLHPHGVFYNKEnegaLYPDntsgfekaddAVPPGGSYTYTWTVPEEQAPTKADA 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 1512432618 609 ACVSWIYYSAVDPIKDMYSGLVGPLAICQK 638
Cdd:cd04222   154 NCLTRIYHSHIDAPKDIASGLIGPLIICKK 183
CuRO_5_ceruloplasmin cd04225
The fifth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 113-294 1.12e-48

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: 169.96  E-value: 1.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 113 RQYFIEAHEIQWDYGPMGHDGSTGKNLREPgSISDKFFQKSSSRIGGTYWKVRYEAFQDETFQ-EKMHLEEDRHLGILGP 191
Cdd:cd04225     1 RTYYIAAEEVEWDYSPQRTWEQELHNTHEE-SPGNAFLNKGDKFIGSKYKKVVYREYTDDTFSvPKERTAEEEHLGILGP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 192 VIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEkdyegtvyndgSSYPgLVAKPFEKVTYRWTVPPHAGPTAQDPACLTWM 271
Cdd:cd04225    80 LIHAEVGEKVKIVFKNMASRPYSIHAHGVKTD-----------SSWV-APTEPGETQTYTWKIPERSGPGVEDSNCISWA 147

                         170       180
                  ....*....|....*....|...
gi 1512432618 272 YFSAADPIRDTNSGLVGPLLVCR 294
Cdd:cd04225   148 YYSTVDQIKDLYSGLIGPLVICR 170
CuRO_3_FV_like cd14450
The third cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 468-637 1.30e-48

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: 170.44  E-value: 1.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 468 YYIMAEEVEWDYCPDRSwerewhnQSEKDSYGYIFLSNKDGLLGSRYKKAVFREYTDGTFRIPRPRTGPEEhLGILGPLI 547
Cdd:cd14450     5 YFIAAEEVIWDYAPSIP-------ENMDKRYRSQYLDNFSNNIGKKYKKAVFTQYEDGSFTKRLENPRPKE-EGILGPVI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 548 KGEVGDILTVVFKNNASRPYSVHAHGVL----ESTTVWPL----------AAEPGEVVTYQWNIPERSGPGPNDSACVSW 613
Cdd:cd14450    77 RAQVRDTIKIVFKNKASRPYSIYPHGVTvskaAEGASYPPdprgnetqnkAVQPGETYTYKWNILETDEPTARDPRCLTR 156

                         170       180
                  ....*....|....*....|....
gi 1512432618 614 IYYSAVDPIKDMYSGLVGPLAICQ 637
Cdd:cd14450   157 MYHSAVDITRDIASGLIGPLLICK 180
CuRO_2_ceruloplasmin cd11021
The second cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 308-448 2.64e-47

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: 164.95  E-value: 2.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 308 DKEFFLLFTVLDENKSWYSNANQAAAMLDFRLLSEDIEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 387
Cdd:cd11021     1 DREFVLMFSVVDENLSWYLDENIKTYCSEPAKVDKDDEDFQESNKMHSINGYTFGNLPGLSMCAGDRVKWHLFGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512432618 388 VHGVMFQGNTVQLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNV 448
Cdd:cd11021    81 IHSAFFHGQTLTDRGHRTDTINLFPATFVTAEMVAQNPGKWLLSCQVNDHLKAGMQAFYEV 141
CuRO_1_Ceruloplasmin_like_1 cd04229
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 466-639 8.65e-47

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: 164.90  E-value: 8.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 466 RIYYIMAEEVEWDY---------CPDRSW-EREWhnqSEKDSYGyiflsnkdglLGSRYKKAVFREYTDGTFRIPRPRtg 535
Cdd:cd04229     1 RTYYIAAEEVDWDYapsgknkccLGDDLEvSTLD---SQPGPYT----------IGSTYTKARYREYTDNSFSTPKPT-- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 536 pEEHLGILGPLIKGEVGDILTVVFKNNASR-PYSVHAHGVLESTTVWPLAAE------PGEVVTYQWNIPERSGPGPNDS 608
Cdd:cd04229    66 -PAYLGILGPVIRAEVGDTIKVVFKNNLDEfPVNMHPHGGLYSKDNEGTTDGagdvvaPGETYTYRWIVPEDAGPGPGDP 144

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1512432618 609 ACVSWIYYSAVDPIKDMYSGLVGPLAICQKG 639
Cdd:cd04229   145 SSRLWLYHSHVDVFAHTNAGLVGPIIVTSKG 175
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 466-639 4.95e-46

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: 162.36  E-value: 4.95e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 466 RIYYIMAEEVEWDYCPDRSwerewhnqsekdsygYIFLSNKDGLLGSR-----YKKAVFREYTDGTFRIPRPRTGPEEHL 540
Cdd:cd04228     2 RHYFIAAVEVLWDYGMQRP---------------QHFLRARDPNRGRRksvpqYKKVVFREYLDGSFTQPVYRGELDEHL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 541 GILGPLIKGEVGDILTVVFKNNASRPYSVHAHGVL--ESTTVWPL--AAEPGEVVTYQWNIPERSGPGPNDSACVSWIYY 616
Cdd:cd04228    67 GILGPYIRAEVEDNIMVTFKNLASRPYSFHSSLISyeEDQRAEPRgnFVQPGEVQTYSWKVLHQMAPTKQEFDCKAWAYF 146

                         170       180
                  ....*....|....*....|...
gi 1512432618 617 SAVDPIKDMYSGLVGPLAICQKG 639
Cdd:cd04228   147 SNVDLEKDLHSGLIGPLIICKTG 169
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 651-795 9.60e-46

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: 160.73  E-value: 9.60e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 651 DREFALLFLIFDENKSWYLEENVATHgSQDPGSINLQDETFLESNKMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDV 730
Cdd:cd11022     1 DKEFFLLFTVFDENESWYLDENIQQF-TLDPRSVDKEDEDFQESNKMHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTET 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512432618 731 DLHTIHFHAESFLYRnGEnyRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:cd11022    80 DVHGIYFSGNTFLLQ-GT--RRDTANLFPHTSVTAIMQPDNEGTFEVNCQTTDHYSAGMRQIYTV 141
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 652-795 2.58e-44

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: 156.58  E-value: 2.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 652 REFALLFLIFDENKSWYLEENVATHgSQDPGSINLQDETFLESNKMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDVD 731
Cdd:cd11018     2 QEFALLFTIFDETKSWYFEENMRRN-CRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512432618 732 LHTIHFHAESFLYRNGENYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:cd11018    81 IHSVHFHGLPFTVRAKKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 468-638 5.40e-44

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: 157.01  E-value: 5.40e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 468 YYIMAEEVEWDYCPDRSwerewhnQSEKDSYGYIFLSNKDGLLGSRYKKAVFREYTDGTFRiprPRTGPEEHLGILGPLI 547
Cdd:cd04227     5 HYIAAEELDWDYAPLLS-------STDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFK---RREAKQTEKGILGPLL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 548 KGEVGDILTVVFKNNASRPYSVHAHGVlesTTVWPLAAE---------------PGEVVTYQWNIPERSGPGPNDSACVS 612
Cdd:cd04227    75 KGEVGDQIHIMFKNTASRPYNIYPHGL---TSVRPMYRSrnpagekdlktmpigPGETFGYMWELTAEDGPTEEDPRCLT 151

                         170       180
                  ....*....|....*....|....*.
gi 1512432618 613 WIYYSAVDPIKDMYSGLVGPLAICQK 638
Cdd:cd04227   152 RLYQSTVDPERDLASGLIGPLLICKK 177
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 1-96 8.55e-44

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: 155.26  E-value: 8.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   1 MHAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRGHHTDVANIFPATFVTAEMVPWEPGTWLISC 80
Cdd:cd04200    46 MHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVDVHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHC 125

                          90
                  ....*....|....*.
gi 1512432618  81 QVNSHFRDGMQALYKV 96
Cdd:cd04200   126 HNSDHRHAGMQAYFLV 141
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 113-296 3.06e-43

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: 154.63  E-value: 3.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 113 RQYFIEAHEIQWDYGPMGHdgstgknlrepgsisdkffQKSSSRIGGTYWKVRYEAFQDETFQEKMHleeDRHLGILGPV 192
Cdd:cd04226     1 REYYIAAQNIDWDYTPQSE-------------------ELRLKRSEQSFKKIVYREYEEGFKKEKPA---DLSSGLLGPT 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 193 IRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYNDGSSypgLVAK------PFEKVTYRWTVPPHAGPTAQDPA 266
Cdd:cd04226    59 LRAEVGDTLIVHFKNMADKPLSIHPQGIAYGKKSEGSLYSDNTS---PVEKlddavqPGQEYTYVWDITEEVGPTEADPP 135

                         170       180       190
                  ....*....|....*....|....*....|
gi 1512432618 267 CLTWMYFSAADPIRDTNSGLVGPLLVCRAG 296
Cdd:cd04226   136 CLTYIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_2_ceruloplasmin_like cd04200
Cupredoxin domains 2, 4, and 6 of ceruloplasmin and similar proteins; This family includes the ...
 308-448 3.55e-43

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: 153.33  E-value: 3.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 308 DKEFFLLFTVLDENKSWYSNANQAAAMLDFRLLSEDIEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 387
Cdd:cd04200     1 DKEFVLLFAVFDENKSWYLEDNIKRFCDNPEKVDKDDEEFQESNKMHAINGYVFGNLPGLTMCAGDRVRWHLLGMGNEVD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512432618 388 VHGVMFQGNTVQLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNV 448
Cdd:cd04200    81 VHSIHFHGQTFLYKGYRIDTLTLFPATFETVEMVPSNPGTWLLHCHNSDHRHAGMQAYFLV 141
CuRO_5_FVIII_like cd04228
The fifth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 112-296 9.02e-42

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: 150.42  E-value: 9.02e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 112 VRQYFIEAHEIQWDYGpmghDGSTGKNLR--EPGSISDKFFQKsssriggtYWKVRYEAFQDETF-QEKMHLEEDRHLGI 188
Cdd:cd04228     1 IRHYFIAAVEVLWDYG----MQRPQHFLRarDPNRGRRKSVPQ--------YKKVVFREYLDGSFtQPVYRGELDEHLGI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 189 LGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEkdyegtvyNDGSSYP-GLVAKPFEKVTYRWTVPPHAGPTAQDPAC 267
Cdd:cd04228    69 LGPYIRAEVEDNIMVTFKNLASRPYSFHSSLISYE--------EDQRAEPrGNFVQPGEVQTYSWKVLHQMAPTKQEFDC 140

                         170       180
                  ....*....|....*....|....*....
gi 1512432618 268 LTWMYFSAADPIRDTNSGLVGPLLVCRAG 296
Cdd:cd04228   141 KAWAYFSNVDLEKDLHSGLIGPLIICKTG 169
CuRO_3_FVIII_like cd04227
The third cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 111-294 1.22e-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: 1.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 111 KVRQYFIEAHEIQWDYGPMghdgstgKNLREPGSISDKFFQKSSSRIGGTYWKVRYEAFQDETFQEKMHLEEDRhlGILG 190
Cdd:cd04227     1 QTWEHYIAAEELDWDYAPL-------LSSTDDRELQSRYLPTGPQRIGYKYKKVAFVEYTDKTFKRREAKQTEK--GILG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 191 PVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYNDGSS---YPGLVakPFEKVTYRWTVPPHAGPTAQDPAC 267
Cdd:cd04227    72 PLLKGEVGDQIHIMFKNTASRPYNIYPHGLTSVRPMYRSRNPAGEKdlkTMPIG--PGETFGYMWELTAEDGPTEEDPRC 149

                         170       180
                  ....*....|....*....|....*..
gi 1512432618 268 LTWMYFSAADPIRDTNSGLVGPLLVCR 294
Cdd:cd04227   150 LTRLYQSTVDPERDLASGLIGPLLICK 176
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 652-795 5.98e-39

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: 141.16  E-value: 5.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 652 REFALLFLIFDENKSWYLEEN-VATHGSQDPGSINLQDetfleSNKMHAINGKLYaNLRGLTMYQGERVAWYMLAMGQDV 730
Cdd:cd14455     2 REFVLLFMTFDEEKSWYYEKNrKRTCRENRVKDPNVQD-----NHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPK 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512432618 731 DLHTIHFHAESFLYRNGENYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:cd14455    76 DLHVVHFHGQTFTEKGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_1_FV_like cd04226
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor V is an ...
 466-639 3.03e-38

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: 140.38  E-value: 3.03e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 466 RIYYIMAEEVEWDYCPDRSWEREWHnqsekdsygyiflsnkdglLGSRYKKAVFREYTDGtFRIPRPRtgpEEHLGILGP 545
Cdd:cd04226     1 REYYIAAQNIDWDYTPQSEELRLKR-------------------SEQSFKKIVYREYEEG-FKKEKPA---DLSSGLLGP 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 546 LIKGEVGDILTVVFKNNASRPYSVHAHGV---------LESTTVWPL-----AAEPGEVVTYQWNIPERSGPGPNDSACV 611
Cdd:cd04226    58 TLRAEVGDTLIVHFKNMADKPLSIHPQGIaygkksegsLYSDNTSPVeklddAVQPGQEYTYVWDITEEVGPTEADPPCL 137

                         170       180
                  ....*....|....*....|....*...
gi 1512432618 612 SWIYYSAVDPIKDMYSGLVGPLAICQKG 639
Cdd:cd04226   138 TYIYYSHVNMVRDFNSGLIGALLICKKG 165
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 113-296 4.36e-38

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: 140.11  E-value: 4.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 113 RQYFIEAHEIQWDYgpmghdgsTGKNLREPGSISDKFfqksSSRIGGTYWKVRYEAFQDETF-QEKMhleEDRHLGILGP 191
Cdd:cd14452     1 RRYYIAAVEIGWDY--------IHSDLGDPASEQRKK----PKDIPQKYIKAVFVEYLDATFtVPKP---RPAWMGLLGP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 192 VIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYNDGSSYP---GLVAKPFEKVTYRWTVPPHAGPTAQDPACL 268
Cdd:cd14452    66 TIVAEVGDTVVITFKNLASQPYSLHAVGVSYWKASEGAGYDDSTSQHekeDDAVYPGGYHTYVWDISPKDGPTGSDPECL 145

                         170       180
                  ....*....|....*....|....*...
gi 1512432618 269 TWMYFSAADPIRDTNSGLVGPLLVCRAG 296
Cdd:cd14452   146 TYSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_4_ceruloplasmin cd11022
The fourth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase ...
 1-99 1.62e-36

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: 134.53  E-value: 1.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   1 MHAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRGHHTDVANIFPATFVTAEMVPWEPGTWLISC 80
Cdd:cd11022    46 MHSINGYMYGNQPGLDMCKGDTVSWHLFGLGTETDVHGIYFSGNTFLLQGTRRDTANLFPHTSVTAIMQPDNEGTFEVNC 125

                          90
                  ....*....|....*....
gi 1512432618  81 QVNSHFRDGMQALYKVKSC 99
Cdd:cd11022   126 QTTDHYSAGMRQIYTVSQC 144
CuRO_1_FVIII_like cd14452
The first cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 466-639 1.44e-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: 132.79  E-value: 1.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 466 RIYYIMAEEVEWDYCpdrswerewhnQSEkDSYGYIFLSNKDGLLGSRYKKAVFREYTDGTFRIPRPRTGpeeHLGILGP 545
Cdd:cd14452     1 RRYYIAAVEIGWDYI-----------HSD-LGDPASEQRKKPKDIPQKYIKAVFVEYLDATFTVPKPRPA---WMGLLGP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 546 LIKGEVGDILTVVFKNNASRPYSVHAHGV----------LESTTVWPL----AAEPGEVVTYQWNIPERSGPGPNDSACV 611
Cdd:cd14452    66 TIVAEVGDTVVITFKNLASQPYSLHAVGVsywkasegagYDDSTSQHEkeddAVYPGGYHTYVWDISPKDGPTGSDPECL 145

                         170       180
                  ....*....|....*....|....*...
gi 1512432618 612 SWIYYSAVDPIKDMYSGLVGPLAICQKG 639
Cdd:cd14452   146 TYSYSSQVDPVKDVNSGLIGALLVCRMG 173
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 651-795 5.42e-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: 129.27  E-value: 5.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 651 DREFALLFLIFDEnkswyleenvathgsqdpgsinLQDEtflESNKMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDV 730
Cdd:cd11023     1 DQEFIENSSIFLD----------------------LNVE---EAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEV 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1512432618 731 DLHTIHFHAESFLyrNGENYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:cd11023    56 DFHTPHWHGQTVE--ADKSRRTDVAELMPASMRVADMTAADVGTWLLHCHVHDHYMAGMMTQFAV 118
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 1-96 3.47e-30

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: 116.51  E-value: 3.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   1 MHAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLT---TRGHHTDVANIFPATFVTAEMVPWEPGTWL 77
Cdd:cd11012    46 MHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDIHTAHFHGHSFDykhRGVYRSDVFDLFPGTFQTVEMIPRTPGTWL 125

                          90
                  ....*....|....*....
gi 1512432618  78 ISCQVNSHFRDGMQALYKV 96
Cdd:cd11012   126 LHCHVTDHIHAGMETTYTV 144
CuRO_6_ceruloplasmin cd11012
The sixth cupredoxin domain of Ceruloplasmin; Ceruloplasmin is a multicopper oxidase essential ...
 309-448 2.17e-28

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: 111.11  E-value: 2.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 309 KEFFLLFTVLDENKSWYSNANQAAAMLDFRLLSEDIEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETDV 388
Cdd:cd11012     2 LEFALLFLVFDENESWYLDENIKTYSDHPEKVNKEDEEFIESNKMHAINGKVFGNLQGLTMHVGDEVYWYLMGMGNEIDI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512432618 389 HGVMFQGNT---VQLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNV 448
Cdd:cd11012    82 HTAHFHGHSfdyKHRGVYRSDVFDLFPGTFQTVEMIPRTPGTWLLHCHVTDHIHAGMETTYTV 144
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 309-448 2.88e-28

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: 110.38  E-value: 2.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 309 KEFFLLFTVLDENKSWYSNANQaaamldfRLLSEDIEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETDV 388
Cdd:cd11015     2 QAFVLLFAVFDEGKSWYSEVGE-------RKSRDKFKRADSRKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 389 HGVMFQGNTVQLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNV 448
Cdd:cd11015    75 HSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 1-96 1.07e-27

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: 108.47  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   1 MHAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRGH-HTDVANIFPATFVTAEMVPWEPGTWLIS 79
Cdd:cd11023    22 MHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSrRTDVAELMPASMRVADMTAADVGTWLLH 101

                          90
                  ....*....|....*..
gi 1512432618  80 CQVNSHFRDGMQALYKV 96
Cdd:cd11023   102 CHVHDHYMAGMMTQFAV 118
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 308-451 1.32e-27

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: 108.80  E-value: 1.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 308 DKEFFLLFTVLDENKSWYSNAN-----QAAAMLDfrllSEDIEgFQDSNRMHAINGFLFSNLpRLDMCKGDTVAWHLLGL 382
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENihrftQTPAGVN----DTDPD-FYASNVMHTINGIVFDRR-QFVICLTDVAYWYVLSV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1512432618 383 GTETDVHGVMFQGNTVQLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNVSQC 451
Cdd:cd11016    75 GAQTDFLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVSTC 143
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1-96 3.12e-25

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: 101.91  E-value: 3.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   1 MHAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRGHHTDVANIFPATFVTAEMVPWEPGTWLISC 80
Cdd:cd11015    39 FHTINGYINASLPGLKICQRKPVIWHVIGMGTAPEVHSIFFEGHTFLVRTHRKVSLEISPMTFLTAQTKPATVGSFLIFC 118

                          90
                  ....*....|....*.
gi 1512432618  81 QVNSHFRDGMQALYKV 96
Cdd:cd11015   119 QIHSHQHDGMEAMVKV 134
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 651-777 3.59e-24

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: 99.18  E-value: 3.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 651 DREFALLFLIFDENKSWYLEENVATHGSqDPGSINLQDETFLESNKMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDV 730
Cdd:cd14454     1 DLEQHAVFAVFDENKSWYLEENINKYCS-NPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1512432618 731 DLHTIHFHAESFLYRNGENyraDVVDLFPGTFEVVEMVASNPGTWLM 777
Cdd:cd14454    80 EIITVHLSGHTFRYKGKHE---DTLNLFPMSGESITVTMDNLGTWLL 123
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 651-797 4.29e-24

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: 98.79  E-value: 4.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 651 DREFALLFLIFDENKSWYLEENVATHgSQDPGSINLQDETFLESNKMHAINGKLYANLRgLTMYQGERVAWYMLAMGQDV 730
Cdd:cd11016     1 DKDWSLLFSVFDENNSWYLKENIHRF-TQTPAGVNDTDPDFYASNVMHTINGIVFDRRQ-FVICLTDVAYWYVLSVGAQT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512432618 731 DLHTIHFHAESFLYRNgenYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTVFS 797
Cdd:cd11016    79 DFLSVFFSGNTFKHQM---VYEDVLTLFPFSGETVSMSPEVPGEWELGCFNGDFRSRGMSAQYTVST 142
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 309-448 4.30e-23

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: 96.10  E-value: 4.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 309 KEFFLLFTVLDENKSWYSNANQAAAMLDFRLLSEDIEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETDV 388
Cdd:cd11018     2 QEFALLFTIFDETKSWYFEENMRRNCRPPCHIQTQDPWFHINNKFHAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512432618 389 HGVMFQGNTVQL---QGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNV 448
Cdd:cd11018    82 HSVHFHGLPFTVrakKEYRMGVYNLYPGVFGTVEMRPSTAGIWLVECTVGEHLLAGMSALFLV 144
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 309-448 6.18e-23

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: 95.32  E-value: 6.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 309 KEFFLLFTVLDENKSWYSNANQAAAMLDFRLLSEdieGFQDSNRMHAINGFLFsNLPRLDMCKGDTVAWHLLGLGTETDV 388
Cdd:cd14455     2 REFVLLFMTFDEEKSWYYEKNRKRTCRENRVKDP---NVQDNHTFHAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512432618 389 HGVMFQGNTV---QLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNV 448
Cdd:cd14455    78 HVVHFHGQTFtekGLKDHQLGVYPLLPGSFATLEMKPSKPGLWLLETEVGESQQRGMQTLFLV 140
CuRO_6_FVIII_like cd11018
The sixth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 2-96 1.62e-22

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: 94.56  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   2 HAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRG---HHTDVANIFPATFVTAEMVPWEPGTWLI 78
Cdd:cd11018    47 HAINGYVADTLPGLVMAQHQRIRWHLLNMGSDEEIHSVHFHGLPFTVRAkkeYRMGVYNLYPGVFGTVEMRPSTAGIWLV 126

                          90
                  ....*....|....*...
gi 1512432618  79 SCQVNSHFRDGMQALYKV 96
Cdd:cd11018   127 ECTVGEHLLAGMSALFLV 144
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1-92 2.17e-22

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: 93.38  E-value: 2.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   1 MHAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRGHHTDVANIFPATFVTAEMVPWEPGTWLISC 80
Cdd:cd14453    28 KYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPELFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISS 107

                          90
                  ....*....|..
gi 1512432618  81 QVNSHFRDGMQA 92
Cdd:cd14453   108 LIMKHLQAGMYG 119
CuRO_2_FVIII_like cd11015
The second cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 652-795 6.81e-22

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: 92.28  E-value: 6.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 652 REFALLFLIFDENKSWYLEENVATHGSQDPGSINlqdetfleSNKMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDVD 731
Cdd:cd11015     2 QAFVLLFAVFDEGKSWYSEVGERKSRDKFKRADS--------RKEFHTINGYINASLPGLKICQRKPVIWHVIGMGTAPE 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512432618 732 LHTIHFHAESFLYRngeNYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:cd11015    74 VHSIFFEGHTFLVR---THRKVSLEISPMTFLTAQTKPATVGSFLIFCQIHSHQHDGMEAMVKV 134
CuRO_2_ceruloplasmin_like_2 cd11023
cupredoxin domain of ceruloplasmin homologs; Uncharacterized subfamily of ceruloplasmin ...
 348-448 1.18e-20

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: 88.05  E-value: 1.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 348 QDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETDVHGVMFQGNTVQLQGMRKG-AAMLFPHTFVMAIMQPDNLG 426
Cdd:cd11023    17 EEAGLMHSINGYVFGNLPGVTIAKGKRVRWHLVAYGNEVDFHTPHWHGQTVEADKSRRTdVAELMPASMRVADMTAADVG 96

                          90       100
                  ....*....|....*....|..
gi 1512432618 427 TFEIYCQAGSHREAGMRAIYNV 448
Cdd:cd11023    97 TWLLHCHVHDHYMAGMMTQFAV 118
CuRO_6_FV_like cd14455
The sixth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 2-96 4.39e-20

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: 87.23  E-value: 4.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   2 HAINGFVFgNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRG---HHTDVANIFPATFVTAEMVPWEPGTWLI 78
Cdd:cd14455    44 HAINGIIY-NLKGLRMYTNELVRWHLINMGGPKDLHVVHFHGQTFTEKGlkdHQLGVYPLLPGSFATLEMKPSKPGLWLL 122

                          90
                  ....*....|....*...
gi 1512432618  79 SCQVNSHFRDGMQALYKV 96
Cdd:cd14455   123 ETEVGESQQRGMQTLFLV 140
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 308-443 4.69e-20

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: 87.23  E-value: 4.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 308 DKEFFLLFTVLDENKSWYSNANQAAAMLDFRLLSEDIEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 387
Cdd:cd14454     1 DLEQHAVFAVFDENKSWYLEENINKYCSNPNNVKKDDPKFYKSNIMPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1512432618 388 VHGVMFQGNTVQLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMR 443
Cdd:cd14454    81 IITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGSFGSSKKSKGLR 136
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 308-448 4.08e-19

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: 84.14  E-value: 4.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 308 DKEFFLLFTVLDENKSWYSnanqaaamldfrllsediEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETD 387
Cdd:cd14453     1 YKEYVLMFGVFDENKSWYK------------------QNASVDSVKYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEPE 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512432618 388 VHGVMFQGNTVQLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNV 448
Cdd:cd14453    63 LFSVHFNGQVLEQNGHKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGMYGYLNI 123
CuRO_2_FV_like cd14453
The second cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 651-789 1.21e-17

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: 79.90  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 651 DREFALLFLIFDENKSWYleenvathgSQDPGSINLqdetflesnkMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDV 730
Cdd:cd14453     1 YKEYVLMFGVFDENKSWY---------KQNASVDSV----------KYTINGYTNGTLPDVSICAYDHVSWHLLGMSSEP 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1512432618 731 DLHTIHFHAESfLYRNGenYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGM 789
Cdd:cd14453    62 ELFSVHFNGQV-LEQNG--HKVSAVGLVSGSSTTASMTVVHTGRWLISSLIMKHLQAGM 117
CuRO_3_LCC_like cd04207
Cupredoxin domain 3 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 699-794 5.59e-16

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: 75.19  E-value: 5.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 699 AINGK----LYANLRGLTMYQGERVAWYMLAMGQDVDLHTIHFHAESF--LYRNGENYRA----------DVVDLFPGTF 762
Cdd:cd04207    21 VINGMpfkeGDANTDIFSVEAGDVVEIVLINAGNHDMQHPFHLHGHSFwvLGSGGGPFDAplnltnppwrDTVLVPPGGW 100

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1512432618 763 EVVEMVASNPGTWLMHCHVTDHVHAGMETLFT 794
Cdd:cd04207   101 VVIRFKADNPGVWMLHCHILEHEDAGMMTVFE 132
Cu-oxidase_2 pfam07731
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 695-795 6.72e-16

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: 75.16  E-value: 6.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 695 NKMHAINGKLY-ANLRGLTMYQGERVAWYMLAMGQDVdlHTIHFHAESF--LYRNGENY--------------RADVVDL 757
Cdd:pfam07731  19 RNDWAINGLLFpPNTNVITLPYGTVVEWVLQNTTTGV--HPFHLHGHSFqvLGRGGGPWpeedpktynlvdpvRRDTVQV 96

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1512432618 758 FPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:pfam07731  97 PPGGWVAIRFRADNPGVWLFHCHILWHLDQGMMGQFVV 134
CuRO_4_FVIII_like cd11016
The fourth cupredoxin domain of coagulation factor VIII and similar proteins; Factor VIII ...
 1-99 5.14e-15

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: 72.98  E-value: 5.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   1 MHAINGFVFGNLpELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRGHHTDVANIFPATFVTAEMVPWEPGTWLISC 80
Cdd:cd11016    46 MHTINGIVFDRR-QFVICLTDVAYWYVLSVGAQTDFLSVFFSGNTFKHQMVYEDVLTLFPFSGETVSMSPEVPGEWELGC 124

                          90       100
                  ....*....|....*....|
gi 1512432618  81 qVNSHFRD-GMQALYKVKSC 99
Cdd:cd11016   125 -FNGDFRSrGMSAQYTVSTC 143
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 187-293 2.72e-14

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: 70.01  E-value: 2.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 187 GILGPVIRAEVGDTIQVVFYNR-ASQPFSMQPHGVFYEKDYEGtVYNDGSSYPGLvaKPFEKVTYRWTVPPHAGptaqdp 265
Cdd:cd04206    27 QFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRQPGTNDG-DGVAGLTQCPI--PPGESFTYRFTVDDQAG------ 97

                          90       100
                  ....*....|....*....|....*...
gi 1512432618 266 aclTWMYFSAADPIRDTnsGLVGPLLVC 293
Cdd:cd04206    98 ---TFWYHSHVGGQRAD--GLYGPLIVE 120
CuRO_3_CumA_like cd13906
The third cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 711-795 9.58e-13

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


Pssm-ID: 259973 [Multi-domain]  Cd Length: 138  Bit Score: 66.25  E-value: 9.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 711 LTMYQGErvaWYMLAMGQDVD-LHTIHFHAESF--LYRNG----ENYRADVVDLFPGtfEVVE--MVASNPGTWLMHCHV 781
Cdd:cd13906    49 ATLKRGR---SYVLRLVNETAfLHPMHLHGHFFrvLSRNGrpvpEPFWRDTVLLGPK--ETVDiaFVADNPGDWMFHCHI 123

                          90
                  ....*....|....
gi 1512432618 782 TDHVHAGMETLFTV 795
Cdd:cd13906   124 LEHQETGMMGVIRV 137
CuRO_D2_2dMcoN_like cd04202
The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 697-796 3.79e-12

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: 64.58  E-value: 3.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 697 MHAINGKLYANLRGLTMYQGERVAWYMLAMGQDVdlHTIHFHAESFLY--RNGEN------YRADVVDLFPGTFEVVEMV 768
Cdd:cd04202    29 YFTINGKSFPATPPLVVKEGDRVRIRLINLSMDH--HPMHLHGHFFLVtaTDGGPipgsapWPKDTLNVAPGERYDIEFV 106

                          90       100
                  ....*....|....*....|....*....
gi 1512432618 769 ASNPGTWLMHCHVTDHV-HAGMETLFTVF 796
Cdd:cd04202   107 ADNPGDWMFHCHKLHHAmNGMGGGMMTLI 135
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 697-795 4.41e-12

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: 69.19  E-value: 4.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 697 MHAINGKLYANLR-GLTMYQGERVAWYMLAMGQDvdLHTIHFHAESF--LYRNG----ENYRADVVDLFPGTFEVVEMVA 769
Cdd:COG2132   317 VWTINGKAFDPDRpDLTVKLGERERWTLVNDTMM--PHPFHLHGHQFqvLSRNGkpppEGGWKDTVLVPPGETVRILFRF 394

                          90       100
                  ....*....|....*....|....*..
gi 1512432618 770 SN-PGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:COG2132   395 DNyPGDWMFHCHILEHEDAGMMGQFEV 421
CuRO_3_CopA cd13896
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 700-795 5.36e-11

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: 60.35  E-value: 5.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 700 INGKLYANLRGLTMYQGERVAWY-----MLAmgqdvdlHTIHFHAESFLYRNGENY---RADVVDLFPGTFEVVEMVASN 771
Cdd:cd13896    19 INGKAYPDADPLRVREGERVRIVfvndtMMA-------HPMHLHGHFFQVENGNGEygpRKDTVLVPPGETVSVDFDADN 91

                          90       100
                  ....*....|....*....|....
gi 1512432618 772 PGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:cd13896    92 PGRWAFHCHNLYHMEAGMMRVVEY 115
CuRO_4_FV_like cd14454
The fourth cupredoxin domain of coagulation factor V and similar proteins; Factor V is an ...
 1-99 1.10e-09

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: 57.57  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   1 MHAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRGHHTDVANIFPATFVTAEMVPWEPGTWLISC 80
Cdd:cd14454    46 MPTINGYAYESSAPLGFCHSEVVQWHISSVGTQDEIITVHLSGHTFRYKGKHEDTLNLFPMSGESITVTMDNLGTWLLGS 125

                          90
                  ....*....|....*....
gi 1512432618  81 QVNSHFRDGMQALYKVKSC 99
Cdd:cd14454   126 FGSSKKSKGLRVRFTDVIC 144
CuRO_3_MaLCC_like cd13901
The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus ...
 751-789 1.20e-09

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: 58.01  E-value: 1.20e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1512432618 751 RADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGM 789
Cdd:cd13901   114 RRDVAMLPAGGYLVIAFKTDNPGAWLMHCHIAWHASGGL 152
CuRO_1_LCC_like cd04206
Cupredoxin domain 1 of laccase-like multicopper oxidases; including laccase, CueO, spore coat ...
 530-636 2.50e-09

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: 55.75  E-value: 2.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 530 PRPRTGPEEHLGILGPLIKGEVGDILTVVFKNN-ASRPYSVHAHGVL----------ESTTVWPLAaePGEVVTYQWNIP 598
Cdd:cd04206    16 GVLRQVITVNGQFPGPTIRVKEGDTVEVTVTNNlPNEPTSIHWHGLRqpgtndgdgvAGLTQCPIP--PGESFTYRFTVD 93

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1512432618 599 ERSGpgpndsacvSWIYYSAVDPikDMYSGLVGPLAIC 636
Cdd:cd04206    94 DQAG---------TFWYHSHVGG--QRADGLYGPLIVE 120
CuRO_3_Fet3p cd13899
The third Cupredoxin domain of multicopper oxidase Fet3p; Fet3p catalyzes the ferroxidase ...
 728-793 1.89e-08

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: 54.57  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 728 QDVDLHTIHFHAESF--LYRNGENY----------------RADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGM 789
Cdd:cd13899    73 WDAGKHPFHLHGHKFqvVQRSPDVAsddpnppinefpenpmRRDTVMVPPGGSVVIRFRADNPGVWFFHCHIEWHLEAGL 152


                  ....
gi 1512432618 790 ETLF 793
Cdd:cd13899   153 AATF 156
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 187-292 5.68e-08

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: 51.85  E-value: 5.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 187 GILGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTvyndgssyPGLVAKPF---EKVTYRWTvPPHAGptaq 263
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRLPNAMDGV--------PGLTQPPVppgESFTYEFT-PPDAG---- 94

                          90       100
                  ....*....|....*....|....*....
gi 1512432618 264 dpaclTWMYFSAADPIRDTNSGLVGPLLV 292
Cdd:cd13861    95 -----TYWYHPHVGSQEQLDRGLYGPLIV 118
CuRO_3_MCO_like_3 cd13909
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 733-795 7.21e-08

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


Pssm-ID: 259976 [Multi-domain]  Cd Length: 137  Bit Score: 52.14  E-value: 7.21e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512432618 733 HTIHFHAESF--LYRNGE--NYRaDVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:cd13909    71 HGMHLHGHHFraILPNGAlgPWR-DTLLMDRGETREIAFVADNPGDWLLHCHMLEHAAAGMMSWFRV 136
CuRO_3_MCO_like_2 cd13908
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 700-793 8.10e-08

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


Pssm-ID: 259975 [Multi-domain]  Cd Length: 122  Bit Score: 51.68  E-value: 8.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 700 INGKLYANL-RGLTMYQGERvawYMLAM--GQDvDLHTIHFHAESF-LYRNGEN----YRADVVDLFPGTFEVVEMVASN 771
Cdd:cd13908    23 INGKSYPDEdPPLVVQQGRR---YRLVFrnASD-DAHPMHLHRHTFeVTRIDGKptsgLRKDVVMLGGYQRVEVDFVADN 98

                          90       100
                  ....*....|....*....|..
gi 1512432618 772 PGTWLMHCHVTDHVHAGMETLF 793
Cdd:cd13908    99 PGLTLFHCHQQLHMDYGFMALF 120
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 190-292 2.61e-07

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: 49.96  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 190 GPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEkdyegtvYNDGSSYPglVAKPFEKVTYRWTVPPhAGptaqdpaclT 269
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIHDA-------AMDGTGLG--PIMPGESFTYEFVAEP-AG---------T 92

                          90       100
                  ....*....|....*....|....
gi 1512432618 270 WMYFSAADPIRD-TNSGLVGPLLV 292
Cdd:cd11024    93 HLYHCHVQPLKEhIAMGLYGAFIV 116
Cu-oxidase pfam00394
Multicopper oxidase; Many of the proteins in this family contain multiple similar copies of ...
 4-100 4.70e-07

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: 50.01  E-value: 4.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618   4 INGFVFGNLPELNMCAQKRVAWHLFgMGNEIDVHTAFFHGQMLT---TRGHHT-----DVANIFPATF----VTAEMvpw 71
Cdd:pfam00394  41 INGKDGASLATLTVTPGKTYRLRII-NVALDDSLNFSIEGHKMTvveVDGVYVnpftvDSLDIFPGQRysvlVTANQ--- 116

                          90       100       110
                  ....*....|....*....|....*....|
gi 1512432618  72 EPGTWLISCQVN-SHFRDGMQALYKVKSCS 100
Cdd:pfam00394 117 DPGNYWIVASPNiPAFDNGTAAAILRYSGA 146
CuRO_3_BOD cd13889
The third cupredoxin domain of Bilirubin oxidase (BOD); Bilirubin oxidase (BOD) catalyzes the ...
 690-795 9.71e-07

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


Pssm-ID: 259956 [Multi-domain]  Cd Length: 124  Bit Score: 48.46  E-value: 9.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 690 TFLESNKMHAINGKLYANLRGL--TMYQGERVAWYMLAMGQDVDlHTIHFHAESF--LYRNG--------ENYRADVVDL 757
Cdd:cd13889     7 RFGRGNGMWTINGKTWADPNRIdaAPQLGTVEIWTLINGGGGWS-HPIHIHLEDFqiLSRNGgsravppyERGRKDVVYL 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1512432618 758 FPGtfEVVEMVA---SNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:cd13889    86 GPG--EEVRVLMrfrPFRGKYMMHCHNLVHEDHDMMLRFEV 124
CuRO_3_LCC_plant cd13897
The third cupredoxin domain of the plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 764-795 9.99e-07

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: 48.79  E-value: 9.99e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1512432618 764 VVEMVASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:cd13897   105 AIRFVADNPGVWFMHCHFERHTSWGMATVFIV 136
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 190-292 1.01e-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: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 190 GPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFyekdYEGTVYNDGSsyPGLVA---KPFEKVTYRWTVPPHAGptaqdpa 266
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLF----QNGTNWMDGT--AGITQcpiPPGGSFTYNFTVDGQYG------- 96

                          90       100
                  ....*....|....*....|....*..
gi 1512432618 267 clTWMYFSAADPirdTNS-GLVGPLLV 292
Cdd:cd13857    97 --TYWYHSHYST---QYAdGLVGPLIV 118
CuRO_3_tcLLC2_insect_like cd13905
The third cupredoxin domain of the insect laccases similar to laccase 2 in Tribolium castaneum; ...
 764-804 1.38e-06

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: 49.22  E-value: 1.38e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1512432618 764 VVEMVASNPGTWLMHCHVTDHVHAGMETLFTVfSRTEHLSP 804
Cdd:cd13905   134 VIRFRADNPGYWLLHCHIEFHLLEGMALVLKV-GEPSDPPP 173
ascorbOXfungal TIGR03390
L-ascorbate oxidase, fungal type; This model describes a family of fungal ascorbate oxidases, ...
 741-795 2.15e-06

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


Pssm-ID: 132431 [Multi-domain]  Cd Length: 538  Bit Score: 51.38  E-value: 2.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1512432618 741 SFLYRngenYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:TIGR03390 481 TMLYR----YAVKVVPGAPAGWRAWRIRVTNPGVWMMHCHILQHMVMGMQTVWVF 531
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 544-602 2.63e-06

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: 47.29  E-value: 2.63e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512432618 544 GPLIKGEVGDILTVVFKNNASRPYSVHAHGVLESTTVW----P----LAAEPGEVVTYQWNIPERSG 602
Cdd:cd13850    28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGILQRGTPWsdgvPgvtqWPIQPGGSFTYRWKAEDQYG 94
CuRO_3_Tv-LCC_like cd13903
The third cupredoxin domain of the fungal laccases similar to Tv-LCC from Trametes Versicolor; ...
 727-793 2.69e-06

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: 48.04  E-value: 2.69e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1512432618 727 GQDVDLHTIHFHAESF-----LYRNGENY----RADVVDL-FPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLF 793
Cdd:cd13903    67 GAIGGPHPFHLHGHAFsvvrsAGSNTYNYvnpvRRDVVSVgTPGDGVTIRFVTDNPGPWFLHCHIDWHLEAGLAVVF 143
CuRO_D1_2dMcoN_like cd13859
The first cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar ...
 544-602 2.80e-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: 47.09  E-value: 2.80e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1512432618 544 GPLIKGEVGDILTVVFKNNASRPYSVHAHGVLESTTvWPL---------AAEPGEVVTYQWnIPERSG 602
Cdd:cd13859    31 GPLIHVKEGDDLVVHVTNNTTLPHTIHWHGVLQMGS-WKMdgvpgvtqpAIEPGESFTYKF-KAERPG 96
CuRO_3_AAO cd13893
The third cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 753-793 2.94e-06

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: 47.80  E-value: 2.94e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1512432618 753 DVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLF 793
Cdd:cd13893   104 NTVTIFPYGWTALRFKADNPGVWAFHCHIEWHFHMGMGVVF 144
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 188-292 3.53e-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: 46.86  E-value: 3.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 188 ILGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFyekdYEGTVYNDGSSY-PGLVAKPFEKVTYRWTVPPHAGptaqdpa 266
Cdd:pfam07732  24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQ----QRGTPWMDGVPGvTQCPIPPGQSFTYRFQVKQQAG------- 92

                          90       100
                  ....*....|....*....|....*.
gi 1512432618 267 clTWMYFSAADPIRdtNSGLVGPLLV 292
Cdd:pfam07732  93 --TYWYHSHTSGQQ--AAGLAGAIII 114
SufI COG2132
Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and ...
 188-380 3.76e-06

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: 50.32  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 188 ILGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDyegtvyNDGssYPGLVAKPFEKVTYRWTVPPHAGptaqdpac 267
Cdd:COG2132    42 YPGPTIRVREGDRVRVRVTNRLPEPTTVHWHGLRVPNA------MDG--VPGDPIAPGETFTYEFPVPQPAG-------- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 268 lTWMYFSAADPIRDTN--SGLVGPLLVcragaLGADGKQKGVDKEFFLLFTvldenkswysnanqaaamlDFRLlseDIE 345
Cdd:COG2132   106 -TYWYHPHTHGSTAEQvyRGLAGALIV-----EDPEEDLPRYDRDIPLVLQ-------------------DWRL---DDD 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1512432618 346 GFQDSNRMHAINGFLFS----N---LPRLDMCKGDTVAWHLL 380
Cdd:COG2132   158 GQLLYPMDAAMGGRLGDtllvNgrpNPTLEVRPGERVRLRLL 199
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 190-294 4.67e-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. 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: 46.88  E-value: 4.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 190 GPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYekdyegTVYNDGSSYPGLVAKPFEKVTYRWTVppHAGPTAQDPACL- 268
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDY------TTASDGTGMNASIVAPGDTRIYTWRT--HGGYRRADGSWAe 100

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1512432618 269 ----TWMY----FSAADPIRDTNSGLVGPLLVCR 294
Cdd:cd14449   101 gtagYWHYhdhvFGTEHGTEGLSRGLYGALIVRR 134
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 544-595 7.67e-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: 45.72  E-value: 7.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1512432618 544 GPLIKGEVGDILTVVFKNNASRPYSVHAHGV---LESTTVWPLAAePGEVVTYQW 595
Cdd:cd11024    32 GPTLRATEGDLVRIHFINTGDHPHTIHFHGIhdaAMDGTGLGPIM-PGESFTYEF 85
PLN02191 PLN02191
L-ascorbate oxidase
 753-793 1.88e-05

L-ascorbate oxidase


Pssm-ID: 177843 [Multi-domain]  Cd Length: 574  Bit Score: 48.47  E-value: 1.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1512432618 753 DVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLF 793
Cdd:PLN02191  504 NTAILYPYGWTAIRFVTDNPGVWFFHCHIEPHLHMGMGVVF 544
CuRO_1_2dMco_1 cd13860
The first cupredoxin domain of bacteria two domain multicopper oxidase; This subfamily ...
 190-292 4.88e-05

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: 43.72  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 190 GPVIRAEVGDTIQVVFYNRASQPFSMQPHGVfyekdyegTVYNDGSSYPGLVAKPF---EKVTYRWTVPPHAgptaqdpa 266
Cdd:cd13860    31 GPTIEVTEGDRVRILVTNELPEPTTVHWHGL--------PVPNGMDGVPGITQPPIqpgETFTYEFTAKQAG-------- 94

                          90       100
                  ....*....|....*....|....*.
gi 1512432618 267 clTWMYFSAADPIRDTNSGLVGPLLV 292
Cdd:cd13860    95 --TYMYHSHVDEAKQEDMGLYGAFIV 118
Cu-oxidase_3 pfam07732
Multicopper oxidase; This entry contains many divergent copper oxidase-like domains that are ...
 542-602 6.95e-05

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: 43.00  E-value: 6.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1512432618 542 ILGPLIKGEVGDILTVVFKNNASRPYSVHAHGVLESTTVW----------PLAaePGEVVTYQWNIPERSG 602
Cdd:pfam07732  24 FPGPTIRVREGDTVVVNVTNNLDEPTSIHWHGLQQRGTPWmdgvpgvtqcPIP--PGQSFTYRFQVKQQAG 92
CuRO_1_2DMCO_NIR_like cd11024
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 733-795 7.60e-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: 43.03  E-value: 7.60e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512432618 733 HTIHFHAESFLYRNGENYRadvvDLFPGTFEVVEMVASNPGTWLMHCHV---TDHVHAGMETLFTV 795
Cdd:cd11024    55 HTIHFHGIHDAAMDGTGLG----PIMPGESFTYEFVAEPAGTHLYHCHVqplKEHIAMGLYGAFIV 116
CuRO_1_Abr2_like cd13850
The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 190-259 1.74e-04

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: 41.90  E-value: 1.74e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1512432618 190 GPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFyekdYEGTVYNDGssYPGL---VAKPFEKVTYRWTVPPHAG 259
Cdd:cd13850    28 GPPIILDEGDEVEILVTNNLPVNTTIHFHGIL----QRGTPWSDG--VPGVtqwPIQPGGSFTYRWKAEDQYG 94
laccase TIGR03389
laccase, plant; Members of this protein family include the copper-containing enzyme laccase ...
 730-795 1.79e-04

laccase, plant; Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.


Pssm-ID: 274556 [Multi-domain]  Cd Length: 539  Bit Score: 45.11  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 730 VDLHTIHFHAESFlYRNGE---NY-------RADVVDlfP----------GTFEVVEMVASNPGTWLMHCHVTDHVHAGM 789
Cdd:TIGR03389 437 SENHPIHLHGYNF-FVVGTgfgNFdpkkdpaKFNLVD--PperntvgvptGGWAAIRFVADNPGVWFMHCHLEVHTTWGL 513


                  ....*.
gi 1512432618 790 ETLFTV 795
Cdd:TIGR03389 514 KMAFLV 519
ascorbase TIGR03388
L-ascorbate oxidase, plant type; Members of this protein family are the copper-containing ...
 755-793 2.09e-04

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: 44.74  E-value: 2.09e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1512432618 755 VDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLF 793
Cdd:TIGR03388 483 VVIFPYGWTALRFVADNPGVWAFHCHIEPHLHMGMGVVF 521
CuRO_3_AAO_like_2 cd13895
The third cupredoxin domain of Ascorbate oxidase homologs; This family includes fungal ...
 730-793 2.31e-04

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


Pssm-ID: 259962 [Multi-domain]  Cd Length: 188  Bit Score: 43.07  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 730 VDLHTIHFHAESFLY-------------------RNGENYRADVVDLFPGTFE-------------VVEMVASNPGTWLM 777
Cdd:cd13895    90 LDAHPWHAHGAHYYDlgsglgtysatalaneeklRGYNPIRRDTTMLYRYGGKgyypppgtgsgwrAWRLRVDDPGVWML 169

                          90
                  ....*....|....*.
gi 1512432618 778 HCHVTDHVHAGMETLF 793
Cdd:cd13895   170 HCHILQHMIMGMQTVW 185
CuRO_1_Diphenol_Ox cd13857
The first cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 544-635 2.61e-04

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: 41.47  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 544 GPLIKGEVGDILTVVFKNNASRPYSVHAHGVLESTTVW----------PLAaePGEVVTYQWNIPERSGpgpndsacVSW 613
Cdd:cd13857    30 GPLIEANQGDRIVVHVTNELDEPTSIHWHGLFQNGTNWmdgtagitqcPIP--PGGSFTYNFTVDGQYG--------TYW 99

                          90       100
                  ....*....|....*....|...
gi 1512432618 614 iYYSAVDPikdMYS-GLVGPLAI 635
Cdd:cd13857   100 -YHSHYST---QYAdGLVGPLIV 118
CuRO_3_McoC_like cd13902
The third cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 697-795 3.82e-04

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: 41.23  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 697 MHAINGKLYANLR-GLTMYQGErVAWYMLAMGQDVDlHTIHFHAESF--LYRNG----ENYRA--DVVDLFPGTFEVVEM 767
Cdd:cd13902    20 MFLINGKTFDMNRiDFVAKVGE-VEVWEVTNTSHMD-HPFHLHGTQFqvLEIDGnpqkPEYRAwkDTVNLPPGEAVRIAT 97

                          90       100
                  ....*....|....*....|....*...
gi 1512432618 768 VASNPGTWLMHCHVTDHVHAGMETLFTV 795
Cdd:cd13902    98 RQDDPGMWMYHCHILEHEDAGMMGMLHV 125
CuRO_1_CumA_like cd13861
The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) ...
 541-633 5.65e-04

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: 40.68  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 541 GILGPLIKGEVGDILTVVFKNNASRPYSVHAHGVL---ESTTVWPL---AAEPGEVVTYQWNIPErsgPGpndsacVSWi 614
Cdd:cd13861    28 QVPGPELRVRQGDTLRVRLTNRLPEPTTIHWHGLRlpnAMDGVPGLtqpPVPPGESFTYEFTPPD---AG------TYW- 97

                          90
                  ....*....|....*....
gi 1512432618 615 YYSAVDPIKDMYSGLVGPL 633
Cdd:cd13861    98 YHPHVGSQEQLDRGLYGPL 116
CuRO_3_Diphenol_Ox cd13904
The third cupredoxin domain of fungal laccase, diphenol oxidase; Diphenol oxidase belongs to ...
 751-788 6.47e-04

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


Pssm-ID: 259971 [Multi-domain]  Cd Length: 158  Bit Score: 41.13  E-value: 6.47e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1512432618 751 RADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAG 788
Cdd:cd13904   114 RRDTIVIPGGSWAVLRIPADNPGVWALHCHIGWHLAAG 151
CuRO_3_MCO_like_4 cd13910
The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) ...
 764-789 7.39e-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: 259977 [Multi-domain]  Cd Length: 166  Bit Score: 41.13  E-value: 7.39e-04
                          10        20
                  ....*....|....*....|....*.
gi 1512432618 764 VVEMVASNPGTWLMHCHVTDHVHAGM 789
Cdd:cd13910   135 VLRFVADNPGLWAFHCHILWHMAAGM 160
CuRO_3_Abr2_like cd13898
The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus ...
 764-789 1.05e-03

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: 40.70  E-value: 1.05e-03
                          10        20
                  ....*....|....*....|....*.
gi 1512432618 764 VVEMVASNPGTWLMHCHVTDHVHAGM 789
Cdd:cd13898   132 VIRYHVVNPGAWLLHCHIQSHLAGGM 157
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 186-255 1.82e-03

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 38.75  E-value: 1.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 186 LGILGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYNDGSSyPGLVAKPFEKVTYRWTVP 255
Cdd:cd00920    18 LLFGPPVLVVPVGDTVRVQFVNKLGENHSVTIAGFGVPVVAMAGGANPGLV-NTLVIGPGESAEVTFTTD 86
CuRO_1_Tv-LCC_like cd13856
The first cupredoxin domain of fungal laccases similar to Tv-LCC from Trametes versicolor; ...
 544-602 2.71e-03

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: 38.86  E-value: 2.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512432618 544 GPLIKGEVGDILTVVFKNNAS-----RPYSVHAHGVLESTTVW----------PLAaePGEVVTYQWNIPERSG 602
Cdd:cd13856    30 GPLITANKGDTFRITVVNQLTdptmrRSTSIHWHGIFQHGTNYadgpafvtqcPIA--PNHSFTYDFTAGDQAG 101
CuRO_1_LCC_plant cd13849
The first cupredoxin domain of plant laccases; Laccase is a blue multicopper oxidase (MCO) ...
 190-259 2.86e-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: 38.39  E-value: 2.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1512432618 190 GPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKdyegTVYNDGSSY----PglvAKPFEKVTYRWTVPPHAG 259
Cdd:cd13849    28 GPTIRVHEGDTVVVNVTNRSPYNITIHWHGIRQLR----SGWADGPAYitqcP---IQPGQSYTYRFTVTGQEG 94
CuRO_1_2DMCO_NIR_like_2 cd14449
The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase; The two-domain ...
 544-635 2.97e-03

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


Pssm-ID: 259991 [Multi-domain]  Cd Length: 135  Bit Score: 38.79  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 544 GPLIKGEVGDILTVVFKNNASRPYSVHAHGVLEST----TVWPLAA-EPGEVVTYQWN--IPERSGPGPNDSACV-SWIY 615
Cdd:cd14449    29 GPVIEVREGDTLKILFRNTLDVPASLHPHGVDYTTasdgTGMNASIvAPGDTRIYTWRthGGYRRADGSWAEGTAgYWHY 108

                          90       100
                  ....*....|....*....|....
gi 1512432618 616 YSAV----DPIKDMYSGLVGPLAI 635
Cdd:cd14449   109 HDHVfgteHGTEGLSRGLYGALIV 132
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 544-635 2.99e-03

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: 38.61  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 544 GPLIKGEVGDILTVVFKNNASRPYSVHAHGVlesttvwPLAAE----------PGEVVTYQWNIPErsgpgpnDSACVSW 613
Cdd:cd13855    32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGL-------PVPPDqdgnphdpvaPGNDRVYRFTLPQ-------DSAGTYW 97

                          90       100
                  ....*....|....*....|....*..
gi 1512432618 614 I-----YYSAvdpiKDMYSGLVGPLAI 635
Cdd:cd13855    98 YhphphGHTA----EQVYRGLAGAFVV 120
CuRO_1_AAO cd13845
The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the ...
 162-292 3.17e-03

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: 38.58  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 162 WKVRYEAFQDETFQEKMhleedrhLGI----LGPVIRAEVGDTIQVVFYNR-ASQPFSMQPHGVfyekDYEGTVYNDGSS 236
Cdd:cd13845     5 WKVEYMFWAPDCVEKLV-------IGIngqfPGPTIRATAGDTIVVELENKlPTEGVAIHWHGI----RQRGTPWADGTA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1512432618 237 YPGLVA-KPFEKVTYRWTVpPHAGptaqdpaclTWMYFSAADPIRdtNSGLVGPLLV 292
Cdd:cd13845    74 SVSQCPiNPGETFTYQFVV-DRPG---------TYFYHGHYGMQR--SAGLYGSLIV 118
CuRO_1_Fet3p cd13851
The first Cupredoxin domain of multicopper oxidase Fet3P; Fet3p catalyzes the ferroxidase ...
 180-259 5.03e-03

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: 38.02  E-value: 5.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1512432618 180 LEEDRHLGILG----PVIRAEVGDTIQVVFYNR-ASQPFSMQPHGVFyekdYEGTVYNDGssyPGLVAK----PFEKVTY 250
Cdd:cd13851    17 LFERRVIGINGqwppPPIEVNKGDTVVIHATNSlGDQPTSLHFHGLF----QNGTNYMDG---PVGVTQcpipPGQSFTY 89


                  ....*....
gi 1512432618 251 RWTVPPHAG 259
Cdd:cd13851    90 EFTVDTQVG 98
PLN02604 PLN02604
oxidoreductase
 769-793 6.69e-03

oxidoreductase


Pssm-ID: 215324 [Multi-domain]  Cd Length: 566  Bit Score: 40.23  E-value: 6.69e-03
                          10        20
                  ....*....|....*....|....*
gi 1512432618 769 ASNPGTWLMHCHVTDHVHAGMETLF 793
Cdd:PLN02604  520 ADNPGVWAFHCHIESHFFMGMGVVF 544
CuRO_1_CuNIR_like cd04201
Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; ...
 733-795 6.91e-03

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: 37.47  E-value: 6.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512432618 733 HTIHFHAESflyrnGENYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTD---HVHAGMETLFTV 795
Cdd:cd04201    57 HNIDFHAAT-----GAGGGAGATFIAPGETSTFSFKATQPGLYVYHCAVAPvpmHIANGMYGLILV 117
CuRO_1_McoC_like cd13855
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins; This family ...
 190-255 7.32e-03

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: 37.46  E-value: 7.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1512432618 190 GPVIRAEVGDTIQVVFYNRASQPFSMQPHGVfyekdyegTVYNDGSSYPGLVAKPFEKVTYRWTVP 255
Cdd:cd13855    32 GPLIEVFEGDTVEITFRNRLPEPTTVHWHGL--------PVPPDQDGNPHDPVAPGNDRVYRFTLP 89
CuRO_1_CopA cd13848
The first cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ...
 187-254 7.41e-03

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


Pssm-ID: 259917 [Multi-domain]  Cd Length: 116  Bit Score: 37.26  E-value: 7.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1512432618 187 GILGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTvynDGSSYPGLvaKPFEKVTYRWTV 254
Cdd:cd13848    27 QVPGPLLRFKEGDDATIRVHNRLDEDTSIHWHGLLLPNDMDGV---PGLSFPGI--KPGETFTYRFPV 89
 
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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