NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6806890|ref|NP_033665|]
View 

galectin-9 isoform long [Homo sapiens]

Protein Classification

galectin family protein( domain architecture ID 10049251)

galectin family protein may exclusively bind beta-galactosides such as lactose in a manner independent of metal ions

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 16-146 4.73e-53

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


:

Pssm-ID: 238025  Cd Length: 127  Bit Score: 171.28  E-value: 4.73e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890   16 PFSGTIQGGLQDGLQITVNGTVLSSSGtRFAVNFQTGfsGNDIAFHFNPRFeDGGYVVCNTRQNGSWGPEERKTHMPFQK 95
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAK-RFSINLGTG--SSDIALHFNPRF-DENVIVRNSFLNGNWGPEERSGGFPFQP 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6806890   96 GMPFDLCFLVQSSDFKVMVNGILFVQYFHRVPFHRVDTISVNGSVQLSYIS 146
Cdd:cd00070  77 GQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 233-354 3.84e-50

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


:

Pssm-ID: 214904  Cd Length: 122  Bit Score: 163.53  E-value: 3.84e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890     233 GGLYPSKSILLSGTVLPSAQRFHINLCSG--NHIAFHLNPRFDENAVVRNTQIDNSWGSEERSlpRKMPFVRGQSFSVWI 310
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCGpnADIALHFNPRFDEGTIVRNSKQNGKWGKEERS--GGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 6806890     311 LCEAHCLKVAVDGQHLFEYYHRLrNLPTINRLEVGGDIQLTHVQ 354
Cdd:smart00908  80 LVEEDEFKVAVNGQHFLEFPHRL-PLESIDTLEISGDVQLTSVQ 122
Peptidase_C62 super family cl13773
Gill-associated viral 3C-like peptidase; a positive-stranded RNA virus of prawns, that has ...
 154-214 3.62e-03

Gill-associated viral 3C-like peptidase; a positive-stranded RNA virus of prawns, that has been called yellow head virus protease and gill-associated virus 3C-like peptidase. The GAV cysteine protease is predicted to be the key enzyme in the processing of the GAV replicase polyprotein precursors, pp1a and pp1ab. This protease employs a Cys(2968)-His(2879) catalytic dyad.


The actual alignment was detected with superfamily member pfam12380:

Pssm-ID: 289173  Cd Length: 284  Bit Score: 38.54  E-value: 3.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6806890    154 PVQPAFSTVPFSQPVCFPPRPRG---RRQKPPGVWPANPAPITQTVIHTVQSAPGQMFSTPAIP 214
Cdd:pfam12380 170 PVNGALTWNPETELLCGPNADYDfdpTKVDPPKVWPVEPVTALSTVLNQLNYVTGDAFTTPKLP 233
 
Name Accession Description Interval E-value
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 16-146 4.73e-53

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 171.28  E-value: 4.73e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890   16 PFSGTIQGGLQDGLQITVNGTVLSSSGtRFAVNFQTGfsGNDIAFHFNPRFeDGGYVVCNTRQNGSWGPEERKTHMPFQK 95
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAK-RFSINLGTG--SSDIALHFNPRF-DENVIVRNSFLNGNWGPEERSGGFPFQP 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6806890   96 GMPFDLCFLVQSSDFKVMVNGILFVQYFHRVPFHRVDTISVNGSVQLSYIS 146
Cdd:cd00070  77 GQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 22-146 6.03e-51

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 165.84  E-value: 6.03e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890      22 QGGLQDGLQITVNGTVLSSSGtRFAVNFQTGfSGNDIAFHFNPRFeDGGYVVCNTRQNGSWGPEERKTHMPFQKGMPFDL 101
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAK-RFSINLQCG-PNADIALHFNPRF-DEGTIVRNSKQNGKWGKEERSGGFPFQPGQPFEL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 6806890     102 CFLVQSSDFKVMVNGILFVQYFHRVPFHRVDTISVNGSVQLSYIS 146
Cdd:smart00908  78 EILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 233-354 3.84e-50

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 163.53  E-value: 3.84e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890     233 GGLYPSKSILLSGTVLPSAQRFHINLCSG--NHIAFHLNPRFDENAVVRNTQIDNSWGSEERSlpRKMPFVRGQSFSVWI 310
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCGpnADIALHFNPRFDEGTIVRNSKQNGKWGKEERS--GGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 6806890     311 LCEAHCLKVAVDGQHLFEYYHRLrNLPTINRLEVGGDIQLTHVQ 354
Cdd:smart00908  80 LVEEDEFKVAVNGQHFLEFPHRL-PLESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 226-354 6.54e-49

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 160.49  E-value: 6.54e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890  226 PFITTILGGLYPSKSILLSGTVLPSAQRFHINL-CSGNHIAFHLNPRFDENAVVRNTQIDNSWGSEERSlpRKMPFVRGQ 304
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLgTGSSDIALHFNPRFDENVIVRNSFLNGNWGPEERS--GGFPFQPGQ 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6806890  305 SFSVWILCEAHCLKVAVDGQHLFEYYHRLRnLPTINRLEVGGDIQLTHVQ 354
Cdd:cd00070  79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSLTSVE 127
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 22-146 2.06e-48

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 159.34  E-value: 2.06e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890     22 QGGLQDGLQITVNGTVLSSSGtRFAVNFQTG-FSGNDIAFHFNPRFeDGGYVVCNTRQNGSWGPEERKTHMPFQKGMPFD 100
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQ-RFSINLQTGvGPSDDIALHFNPRF-DENVIVRNSRQNGQWGQEEREGGFPFQPGQPFE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 6806890    101 LCFLVQSSDFKVMVNGILFVQYFHRVPFHRVDTISVNGSVQLSYIS 146
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 233-354 6.57e-45

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 150.10  E-value: 6.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890    233 GGLYPSKSILLSGTVLPSAQRFHINLCSG----NHIAFHLNPRFDENAVVRNTQIDNSWGSEERSLprKMPFVRGQSFSV 308
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQTGvgpsDDIALHFNPRFDENVIVRNSRQNGQWGQEEREG--GFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 6806890    309 WILCEAHCLKVAVDGQHLFEYYHRLRNlPTINRLEVGGDIQLTHVQ 354
Cdd:pfam00337  80 TILVGDDHFKIYVNGQHFTTFKHRLPP-EDIDALQVRGDVKLTSVL 124
Peptidase_C62 pfam12380
Gill-associated viral 3C-like peptidase; a positive-stranded RNA virus of prawns, that has ...
 154-214 3.62e-03

Gill-associated viral 3C-like peptidase; a positive-stranded RNA virus of prawns, that has been called yellow head virus protease and gill-associated virus 3C-like peptidase. The GAV cysteine protease is predicted to be the key enzyme in the processing of the GAV replicase polyprotein precursors, pp1a and pp1ab. This protease employs a Cys(2968)-His(2879) catalytic dyad.


Pssm-ID: 289173  Cd Length: 284  Bit Score: 38.54  E-value: 3.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6806890    154 PVQPAFSTVPFSQPVCFPPRPRG---RRQKPPGVWPANPAPITQTVIHTVQSAPGQMFSTPAIP 214
Cdd:pfam12380 170 PVNGALTWNPETELLCGPNADYDfdpTKVDPPKVWPVEPVTALSTVLNQLNYVTGDAFTTPKLP 233
 
Name Accession Description Interval E-value
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 16-146 4.73e-53

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 171.28  E-value: 4.73e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890   16 PFSGTIQGGLQDGLQITVNGTVLSSSGtRFAVNFQTGfsGNDIAFHFNPRFeDGGYVVCNTRQNGSWGPEERKTHMPFQK 95
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAK-RFSINLGTG--SSDIALHFNPRF-DENVIVRNSFLNGNWGPEERSGGFPFQP 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6806890   96 GMPFDLCFLVQSSDFKVMVNGILFVQYFHRVPFHRVDTISVNGSVQLSYIS 146
Cdd:cd00070  77 GQPFELTILVEEDKFQIFVNGQHFFSFPHRLPLESIDYLSINGDVSLTSVE 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 22-146 6.03e-51

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 165.84  E-value: 6.03e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890      22 QGGLQDGLQITVNGTVLSSSGtRFAVNFQTGfSGNDIAFHFNPRFeDGGYVVCNTRQNGSWGPEERKTHMPFQKGMPFDL 101
Cdd:smart00908   1 PGGLSPGSSITIRGIVLPDAK-RFSINLQCG-PNADIALHFNPRF-DEGTIVRNSKQNGKWGKEERSGGFPFQPGQPFEL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 6806890     102 CFLVQSSDFKVMVNGILFVQYFHRVPFHRVDTISVNGSVQLSYIS 146
Cdd:smart00908  78 EILVEEDEFKVAVNGQHFLEFPHRLPLESIDTLEISGDVQLTSVQ 122
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 17-147 2.94e-50

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 163.94  E-value: 2.94e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890      17 FSGTIQGGLQDGLQITVNGTVLSSSGtRFAVNFQTGfsGNDIAFHFNPRFEDGgYVVCNTRQNGSWGPEERKTHMPFQKG 96
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAK-RFSINLLTG--GDDIALHFNPRFNEN-KIVCNSKLNGSWGSEEREGGFPFQPG 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 6806890      97 MPFDLCFLVQSSDFKVMVNGILFVQYFHRVPFHRVDTISVNGSVQLSYISF 147
Cdd:smart00276  77 QPFDLTIIVQPDHFQIFVNGVHITTFPHRLPLESIDYLSINGDVQLTSVSF 127
Gal-bind_lectin smart00908
Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are ...
 233-354 3.84e-50

Galactoside-binding lectin; Animal lectins display a wide variety of architectures. They are classified according to the carbohydrate-recognition domain (CRD) of which there are two main types, S-type and C-type. Galectins (previously S-lectins) bind exclusively beta-galactosides like lactose. They do not require metal ions for activity. Galectins are found predominantly, but not exclusively in mammals. Their function is unclear. They are developmentally regulated and may be involved in differentiation, cellular regulation and tissue construction.


Pssm-ID: 214904  Cd Length: 122  Bit Score: 163.53  E-value: 3.84e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890     233 GGLYPSKSILLSGTVLPSAQRFHINLCSG--NHIAFHLNPRFDENAVVRNTQIDNSWGSEERSlpRKMPFVRGQSFSVWI 310
Cdd:smart00908   2 GGLSPGSSITIRGIVLPDAKRFSINLQCGpnADIALHFNPRFDEGTIVRNSKQNGKWGKEERS--GGFPFQPGQPFELEI 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 6806890     311 LCEAHCLKVAVDGQHLFEYYHRLrNLPTINRLEVGGDIQLTHVQ 354
Cdd:smart00908  80 LVEEDEFKVAVNGQHFLEFPHRL-PLESIDTLEISGDVQLTSVQ 122
GLECT cd00070
Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as ...
 226-354 6.54e-49

Galectin/galactose-binding lectin. This domain exclusively binds beta-galactosides, such as lactose, and does not require metal ions for activity. GLECT domains occur as homodimers or tandemly repeated domains. They are developmentally regulated and may be involved in differentiation, cell-cell interaction and cellular regulation.


Pssm-ID: 238025  Cd Length: 127  Bit Score: 160.49  E-value: 6.54e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890  226 PFITTILGGLYPSKSILLSGTVLPSAQRFHINL-CSGNHIAFHLNPRFDENAVVRNTQIDNSWGSEERSlpRKMPFVRGQ 304
Cdd:cd00070   1 PYKLPLPGGLKPGSTLTVKGRVLPNAKRFSINLgTGSSDIALHFNPRFDENVIVRNSFLNGNWGPEERS--GGFPFQPGQ 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6806890  305 SFSVWILCEAHCLKVAVDGQHLFEYYHRLRnLPTINRLEVGGDIQLTHVQ 354
Cdd:cd00070  79 PFELTILVEEDKFQIFVNGQHFFSFPHRLP-LESIDYLSINGDVSLTSVE 127
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 22-146 2.06e-48

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 159.34  E-value: 2.06e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890     22 QGGLQDGLQITVNGTVLSSSGtRFAVNFQTG-FSGNDIAFHFNPRFeDGGYVVCNTRQNGSWGPEERKTHMPFQKGMPFD 100
Cdd:pfam00337   1 PGGLQPGSSLTIKGIVLPDAQ-RFSINLQTGvGPSDDIALHFNPRF-DENVIVRNSRQNGQWGQEEREGGFPFQPGQPFE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 6806890    101 LCFLVQSSDFKVMVNGILFVQYFHRVPFHRVDTISVNGSVQLSYIS 146
Cdd:pfam00337  79 LTILVGDDHFKIYVNGQHFTTFKHRLPPEDIDALQVRGDVKLTSVL 124
Gal-bind_lectin pfam00337
Galactoside-binding lectin; This family contains galactoside binding lectins. The family also ...
 233-354 6.57e-45

Galactoside-binding lectin; This family contains galactoside binding lectins. The family also includes enzymes such as human eosinophil lysophospholipase (EC:3.1.1.5).


Pssm-ID: 459768  Cd Length: 124  Bit Score: 150.10  E-value: 6.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890    233 GGLYPSKSILLSGTVLPSAQRFHINLCSG----NHIAFHLNPRFDENAVVRNTQIDNSWGSEERSLprKMPFVRGQSFSV 308
Cdd:pfam00337   2 GGLQPGSSLTIKGIVLPDAQRFSINLQTGvgpsDDIALHFNPRFDENVIVRNSRQNGQWGQEEREG--GFPFQPGQPFEL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 6806890    309 WILCEAHCLKVAVDGQHLFEYYHRLRNlPTINRLEVGGDIQLTHVQ 354
Cdd:pfam00337  80 TILVGDDHFKIYVNGQHFTTFKHRLPP-EDIDALQVRGDVKLTSVL 124
GLECT smart00276
Galectin; Galectin - galactose-binding lectin
 227-354 7.41e-44

Galectin; Galectin - galactose-binding lectin


Pssm-ID: 214596  Cd Length: 128  Bit Score: 147.76  E-value: 7.41e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6806890     227 FITTILGGLYPSKSILLSGTVLPSAQRFHINL-CSGNHIAFHLNPRFDENAVVRNTQIDNSWGSEERSlpRKMPFVRGQS 305
Cdd:smart00276   1 FTLPIPGGLKPGQTLTVRGIVLPDAKRFSINLlTGGDDIALHFNPRFNENKIVCNSKLNGSWGSEERE--GGFPFQPGQP 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 6806890     306 FSVWILCEAHCLKVAVDGQHLFEYYHRLrNLPTINRLEVGGDIQLTHVQ 354
Cdd:smart00276  79 FDLTIIVQPDHFQIFVNGVHITTFPHRL-PLESIDYLSINGDVQLTSVS 126
Peptidase_C62 pfam12380
Gill-associated viral 3C-like peptidase; a positive-stranded RNA virus of prawns, that has ...
 154-214 3.62e-03

Gill-associated viral 3C-like peptidase; a positive-stranded RNA virus of prawns, that has been called yellow head virus protease and gill-associated virus 3C-like peptidase. The GAV cysteine protease is predicted to be the key enzyme in the processing of the GAV replicase polyprotein precursors, pp1a and pp1ab. This protease employs a Cys(2968)-His(2879) catalytic dyad.


Pssm-ID: 289173  Cd Length: 284  Bit Score: 38.54  E-value: 3.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6806890    154 PVQPAFSTVPFSQPVCFPPRPRG---RRQKPPGVWPANPAPITQTVIHTVQSAPGQMFSTPAIP 214
Cdd:pfam12380 170 PVNGALTWNPETELLCGPNADYDfdpTKVDPPKVWPVEPVTALSTVLNQLNYVTGDAFTTPKLP 233
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH