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Conserved domains on  [gi|544186020|ref|NP_001269638|]
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exosome complex component RRP4 isoform 3 [Homo sapiens]

Protein Classification

exosome complex component RRP4( domain architecture ID 20732369)

exosome complex component RRP4 is one of the RNA-binding proteins of the exosome complex.

Gene Ontology:  GO:0003723|GO:0006402

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KH-I_Rrp4_eukar cd22525
type I K homology (KH) RNA-binding domain found in exosome complex component Rrp4 from ...
 139-255 4.07e-61

type I K homology (KH) RNA-binding domain found in exosome complex component Rrp4 from eukaryote; The subfamily corresponds to ribosomal RNA-processing protein 4 (Rrp4) mainly from eukaryote. Rrp4, also called exosome component 2 (EXOSC2), or ribosomal RNA-processing protein 4, is a non-catalytic component of the RNA exosome complex which has 3'-->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Mutations in EXOSC2 gene are associated with a novel syndrome characterized by retinitis pigmentosa, progressive hearing loss, premature aging, short stature, mild intellectual disability and distinctive gestalt. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


:

Pssm-ID: 411953  Cd Length: 123  Bit Score: 188.63  E-value: 4.07e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186020 139 GVLVQVSPSLVKRQKTHFHDLPCGASVILGNNGFIWIYPTPEHKEEEAGGFIA----NLEPVSLADREVISRLRNCIISL 214
Cdd:cd22525    1 GILVKVPPSLIKRQKSHFHNLPCGVDVILGLNGYIWISPTVEESGEEAGGSAAiysnNNEPVSPETREAIARVRNCIKAL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 544186020 215 VTQRMMLYDTSILYCYEASLP--HQIKDILKPEIMEEIVMETR 255
Cdd:cd22525   81 AALHIPITDTSILAVYEASLElgIEVKDLLKPEVMEEIVEEAR 123
S1_Rrp4 cd05789
S1_Rrp4: Rrp4 S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
 75-136 1.36e-24

S1_Rrp4: Rrp4 S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Rrp4 protein is a subunit of the exosome complex. The exosome plays a central role in 3' to 5' RNA processing and degradation in eukarytes and archaea. Its functions include the removal of incorrectly processed RNA and the maintenance of proper levels of mRNA, rRNA and a number of small RNA species. In Saccharomyces cerevisiae, the exosome includes nine core components, six of which are homologous to bacterial RNase PH. These form a hexameric ring structure. The other three subunits (RrP4, Rrp40, and Csl4) contain an S1 RNA binding domain and are part of the "S1 pore structure".


:

Pssm-ID: 240215 [Multi-domain]  Cd Length: 86  Bit Score: 93.77  E-value: 1.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186020  75 RYIGEVGDIVVGRITE------------------------RRRSAEDELAMRGFLQEGDLISAEVQAVFSDGAVSLHTRS 130
Cdd:cd05789    1 RYIPEVGDVVIGRVTEvgfkrwkvdinspydavlplsevnLPRTDEDELNMRSYLDEGDLIVAEVQSVDSDGSVSLHTRS 80


                 ....*.
gi 544186020 131 LKYGKL 136
Cdd:cd05789   81 LKYGKL 86
ECR1_N pfam14382
Exosome complex exonuclease RRP4 N-terminal region; ECR1_N is an N-terminal region of the ...
 26-63 1.85e-13

Exosome complex exonuclease RRP4 N-terminal region; ECR1_N is an N-terminal region of the exosome complex exonuclease RRP proteins. It is a G-rich domain which structurally is a rudimentary single hybrid fold with a permuted topology.


:

Pssm-ID: 464162 [Multi-domain]  Cd Length: 38  Bit Score: 62.76  E-value: 1.85e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 544186020   26 LVVPGDTITTDTGFMRGHGTYMGEEKLIASVAGSVERV 63
Cdd:pfam14382   1 IVLPGERLGSDEEYMPGHGTYVRDGNIYASVAGTVEIV 38
 
Name Accession Description Interval E-value
KH-I_Rrp4_eukar cd22525
type I K homology (KH) RNA-binding domain found in exosome complex component Rrp4 from ...
 139-255 4.07e-61

type I K homology (KH) RNA-binding domain found in exosome complex component Rrp4 from eukaryote; The subfamily corresponds to ribosomal RNA-processing protein 4 (Rrp4) mainly from eukaryote. Rrp4, also called exosome component 2 (EXOSC2), or ribosomal RNA-processing protein 4, is a non-catalytic component of the RNA exosome complex which has 3'-->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Mutations in EXOSC2 gene are associated with a novel syndrome characterized by retinitis pigmentosa, progressive hearing loss, premature aging, short stature, mild intellectual disability and distinctive gestalt. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411953  Cd Length: 123  Bit Score: 188.63  E-value: 4.07e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186020 139 GVLVQVSPSLVKRQKTHFHDLPCGASVILGNNGFIWIYPTPEHKEEEAGGFIA----NLEPVSLADREVISRLRNCIISL 214
Cdd:cd22525    1 GILVKVPPSLIKRQKSHFHNLPCGVDVILGLNGYIWISPTVEESGEEAGGSAAiysnNNEPVSPETREAIARVRNCIKAL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 544186020 215 VTQRMMLYDTSILYCYEASLP--HQIKDILKPEIMEEIVMETR 255
Cdd:cd22525   81 AALHIPITDTSILAVYEASLElgIEVKDLLKPEVMEEIVEEAR 123
S1_Rrp4 cd05789
S1_Rrp4: Rrp4 S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
 75-136 1.36e-24

S1_Rrp4: Rrp4 S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Rrp4 protein is a subunit of the exosome complex. The exosome plays a central role in 3' to 5' RNA processing and degradation in eukarytes and archaea. Its functions include the removal of incorrectly processed RNA and the maintenance of proper levels of mRNA, rRNA and a number of small RNA species. In Saccharomyces cerevisiae, the exosome includes nine core components, six of which are homologous to bacterial RNase PH. These form a hexameric ring structure. The other three subunits (RrP4, Rrp40, and Csl4) contain an S1 RNA binding domain and are part of the "S1 pore structure".


Pssm-ID: 240215 [Multi-domain]  Cd Length: 86  Bit Score: 93.77  E-value: 1.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186020  75 RYIGEVGDIVVGRITE------------------------RRRSAEDELAMRGFLQEGDLISAEVQAVFSDGAVSLHTRS 130
Cdd:cd05789    1 RYIPEVGDVVIGRVTEvgfkrwkvdinspydavlplsevnLPRTDEDELNMRSYLDEGDLIVAEVQSVDSDGSVSLHTRS 80


                 ....*.
gi 544186020 131 LKYGKL 136
Cdd:cd05789   81 LKYGKL 86
PRK04163 PRK04163
exosome complex protein Rrp4;
22-184 1.96e-17

exosome complex protein Rrp4;


Pssm-ID: 235233 [Multi-domain]  Cd Length: 235  Bit Score: 78.78  E-value: 1.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186020  22 TKKHLVVPGDTITTDtGFMRGHGTYMGEEKLIASVAGSVERVNKLICVKALKTRYIGEVGDIVVGRITE----------- 90
Cdd:PRK04163   6 EDRKIVVPGDLLAEG-EFKAGRGTYKENGKIYSTVVGLVDIKDDKVRVIPLEGKYIPKVGDLVIGKVTDvtfsgwevdin 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186020  91 -------------RRRSAEDELAMRGFLQEGDLISAEVQAV--FSDGAVSLHTRSLkyGKLGQGVLVQVSPSLVKR---- 151
Cdd:PRK04163  85 spykaylpvsevlGRPVNVEGTDLRKYLDIGDYIIAKVKDVdrTRDVVLTLKGKGL--GKIEGGTIVEIKPVKVPRvigk 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 544186020 152 ---------QKThfhdlpcGASVILGNNGFIWIYPTPEHKEE 184
Cdd:PRK04163 163 kgsminmlkEET-------GCDIIVGQNGRIWIKGPDEEDEE 197
ECR1_N pfam14382
Exosome complex exonuclease RRP4 N-terminal region; ECR1_N is an N-terminal region of the ...
 26-63 1.85e-13

Exosome complex exonuclease RRP4 N-terminal region; ECR1_N is an N-terminal region of the exosome complex exonuclease RRP proteins. It is a G-rich domain which structurally is a rudimentary single hybrid fold with a permuted topology.


Pssm-ID: 464162 [Multi-domain]  Cd Length: 38  Bit Score: 62.76  E-value: 1.85e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 544186020   26 LVVPGDTITTDTGFMRGHGTYMGEEKLIASVAGSVERV 63
Cdd:pfam14382   1 IVLPGERLGSDEEYMPGHGTYVRDGNIYASVAGTVEIV 38
KH_6 pfam15985
KH domain; KH motifs bind RNA in vitro. Auto-antibodies to Nova, a KH domain protein, cause ...
 139-181 5.19e-10

KH domain; KH motifs bind RNA in vitro. Auto-antibodies to Nova, a KH domain protein, cause para-neoplastic opsoclonus ataxia.


Pssm-ID: 464959 [Multi-domain]  Cd Length: 47  Bit Score: 53.59  E-value: 5.19e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 544186020  139 GVLVQVSPSLVKRQKTHF--HDLPC--GASVILGNNGFIWIYPTPEH 181
Cdd:pfam15985   1 GMLVKVSLSLVRRLLKSHflHELGKkgPFEIAVGLNGRIWIKSETVK 47
PRK09521 PRK09521
exosome complex RNA-binding protein Csl4; Provisional
 26-90 7.15e-07

exosome complex RNA-binding protein Csl4; Provisional


Pssm-ID: 236547 [Multi-domain]  Cd Length: 189  Bit Score: 48.43  E-value: 7.15e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544186020  26 LVVPGDTITTDTGFMRGHGTYMGEEKLIASVAGSVER--VNKLICVKA-LKTRYIGEVGDIVVGRITE 90
Cdd:PRK09521   7 LVLPGDYLAVIEEYLPGEGTYEDNGEVYASVVGKVFIddINRKISVIPfKKTPPLLKKGDIVYGRVVD 74
Csl4 COG1096
Exosome complex RNA-binding protein Csl4, contains S1 and Zn-ribbon domains [Intracellular ...
 26-89 7.85e-07

Exosome complex RNA-binding protein Csl4, contains S1 and Zn-ribbon domains [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440713 [Multi-domain]  Cd Length: 191  Bit Score: 48.36  E-value: 7.85e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544186020  26 LVVPGDTITTDTGFMRGHGTYMGEEKLIASVAGSVE--RVNKLICVKALK-TRYIGEVGDIVVGRIT 89
Cdd:COG1096    8 FVLPGDVLAVIEEFLPGEGTYEEDGKIRAAVVGKVVidDKNRVISVKPKKkPPPVPKKGDIVIGEVV 74
 
Name Accession Description Interval E-value
KH-I_Rrp4_eukar cd22525
type I K homology (KH) RNA-binding domain found in exosome complex component Rrp4 from ...
 139-255 4.07e-61

type I K homology (KH) RNA-binding domain found in exosome complex component Rrp4 from eukaryote; The subfamily corresponds to ribosomal RNA-processing protein 4 (Rrp4) mainly from eukaryote. Rrp4, also called exosome component 2 (EXOSC2), or ribosomal RNA-processing protein 4, is a non-catalytic component of the RNA exosome complex which has 3'-->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Mutations in EXOSC2 gene are associated with a novel syndrome characterized by retinitis pigmentosa, progressive hearing loss, premature aging, short stature, mild intellectual disability and distinctive gestalt. Members in this subfamily contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411953  Cd Length: 123  Bit Score: 188.63  E-value: 4.07e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186020 139 GVLVQVSPSLVKRQKTHFHDLPCGASVILGNNGFIWIYPTPEHKEEEAGGFIA----NLEPVSLADREVISRLRNCIISL 214
Cdd:cd22525    1 GILVKVPPSLIKRQKSHFHNLPCGVDVILGLNGYIWISPTVEESGEEAGGSAAiysnNNEPVSPETREAIARVRNCIKAL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 544186020 215 VTQRMMLYDTSILYCYEASLP--HQIKDILKPEIMEEIVMETR 255
Cdd:cd22525   81 AALHIPITDTSILAVYEASLElgIEVKDLLKPEVMEEIVEEAR 123
KH-I_Rrp4_Rrp40 cd22445
type I K homology (KH) RNA-binding domain found in exosome complex components Rrp4, Rrp40 and ...
 139-231 9.06e-28

type I K homology (KH) RNA-binding domain found in exosome complex components Rrp4, Rrp40 and similar proteins; The family includes two ribosomal RNA-processing proteins, Rrp4 and Rrp40. They are non-catalytic components of the RNA exosome complex which has 3'-->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Eukaryotic Rrp4 and Rrp40 contain a divergent KH domain that lacks the RNA-binding GXXG motif.


Pssm-ID: 411873 [Multi-domain]  Cd Length: 78  Bit Score: 101.95  E-value: 9.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186020 139 GVLVQVSPSLVKRQKT------HFHDLPCGASVILGNNGFIWIYPTPehkeeeaggfianlepvsladREVISRLRNCII 212
Cdd:cd22445    1 GLLVKVTPGLVRRLLApdceiiQEVGKLYPLEIVFGMNGRIWVKAKT---------------------RQQTSILANIIE 59

                         90
                 ....*....|....*....
gi 544186020 213 SLVTQRMMLYDTSILYCYE 231
Cdd:cd22445   60 ACEHMHTSDQRKQIFSRLA 78
S1_Rrp4 cd05789
S1_Rrp4: Rrp4 S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
 75-136 1.36e-24

S1_Rrp4: Rrp4 S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Rrp4 protein is a subunit of the exosome complex. The exosome plays a central role in 3' to 5' RNA processing and degradation in eukarytes and archaea. Its functions include the removal of incorrectly processed RNA and the maintenance of proper levels of mRNA, rRNA and a number of small RNA species. In Saccharomyces cerevisiae, the exosome includes nine core components, six of which are homologous to bacterial RNase PH. These form a hexameric ring structure. The other three subunits (RrP4, Rrp40, and Csl4) contain an S1 RNA binding domain and are part of the "S1 pore structure".


Pssm-ID: 240215 [Multi-domain]  Cd Length: 86  Bit Score: 93.77  E-value: 1.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186020  75 RYIGEVGDIVVGRITE------------------------RRRSAEDELAMRGFLQEGDLISAEVQAVFSDGAVSLHTRS 130
Cdd:cd05789    1 RYIPEVGDVVIGRVTEvgfkrwkvdinspydavlplsevnLPRTDEDELNMRSYLDEGDLIVAEVQSVDSDGSVSLHTRS 80


                 ....*.
gi 544186020 131 LKYGKL 136
Cdd:cd05789   81 LKYGKL 86
S1_Rrp4_like cd04454
S1_Rrp4_like: Rrp4-like, S1-like RNA-binding domain. S1-like RNA-binding domains are found in ...
 75-136 2.89e-18

S1_Rrp4_like: Rrp4-like, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Rrp4 protein, and Rrp40 and Csl4 proteins, also represented in this group, are subunits of the exosome complex. The exosome plays a central role in 3' to 5' RNA processing and degradation in eukarytes and archaea. Its functions include the removal of incorrectly processed RNA and the maintenance of proper levels of mRNA, rRNA and a number of small RNA species. In Saccharomyces cerevisiae, the exosome includes nine core components, six of which are homologous to bacterial RNase PH. These form a hexameric ring structure. The other three subunits (RrP4, Rrp40, and Csl4) contain an S1 RNA binding domain and are part of the "S1 pore structure".


Pssm-ID: 239901 [Multi-domain]  Cd Length: 82  Bit Score: 77.20  E-value: 2.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186020  75 RYIGEVGDIVVGRITER--------------------RRSAEDELAMRGFLQEGDLISAEVQAVFSDGAVSLHTRSLKYG 134
Cdd:cd04454    1 RYLPDVGDIVIGIVTEVnsrfwkvdilsrgtarledsSATEKDKKEIRKSLQPGDLILAKVISLGDDMNVLLTTADNELG 80


                 ..
gi 544186020 135 KL 136
Cdd:cd04454   81 VI 82
PRK04163 PRK04163
exosome complex protein Rrp4;
22-184 1.96e-17

exosome complex protein Rrp4;


Pssm-ID: 235233 [Multi-domain]  Cd Length: 235  Bit Score: 78.78  E-value: 1.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186020  22 TKKHLVVPGDTITTDtGFMRGHGTYMGEEKLIASVAGSVERVNKLICVKALKTRYIGEVGDIVVGRITE----------- 90
Cdd:PRK04163   6 EDRKIVVPGDLLAEG-EFKAGRGTYKENGKIYSTVVGLVDIKDDKVRVIPLEGKYIPKVGDLVIGKVTDvtfsgwevdin 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186020  91 -------------RRRSAEDELAMRGFLQEGDLISAEVQAV--FSDGAVSLHTRSLkyGKLGQGVLVQVSPSLVKR---- 151
Cdd:PRK04163  85 spykaylpvsevlGRPVNVEGTDLRKYLDIGDYIIAKVKDVdrTRDVVLTLKGKGL--GKIEGGTIVEIKPVKVPRvigk 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 544186020 152 ---------QKThfhdlpcGASVILGNNGFIWIYPTPEHKEE 184
Cdd:PRK04163 163 kgsminmlkEET-------GCDIIVGQNGRIWIKGPDEEDEE 197
ECR1_N pfam14382
Exosome complex exonuclease RRP4 N-terminal region; ECR1_N is an N-terminal region of the ...
 26-63 1.85e-13

Exosome complex exonuclease RRP4 N-terminal region; ECR1_N is an N-terminal region of the exosome complex exonuclease RRP proteins. It is a G-rich domain which structurally is a rudimentary single hybrid fold with a permuted topology.


Pssm-ID: 464162 [Multi-domain]  Cd Length: 38  Bit Score: 62.76  E-value: 1.85e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 544186020   26 LVVPGDTITTDTGFMRGHGTYMGEEKLIASVAGSVERV 63
Cdd:pfam14382   1 IVLPGERLGSDEEYMPGHGTYVRDGNIYASVAGTVEIV 38
KH_6 pfam15985
KH domain; KH motifs bind RNA in vitro. Auto-antibodies to Nova, a KH domain protein, cause ...
 139-181 5.19e-10

KH domain; KH motifs bind RNA in vitro. Auto-antibodies to Nova, a KH domain protein, cause para-neoplastic opsoclonus ataxia.


Pssm-ID: 464959 [Multi-domain]  Cd Length: 47  Bit Score: 53.59  E-value: 5.19e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 544186020  139 GVLVQVSPSLVKRQKTHF--HDLPC--GASVILGNNGFIWIYPTPEH 181
Cdd:pfam15985   1 GMLVKVSLSLVRRLLKSHflHELGKkgPFEIAVGLNGRIWIKSETVK 47
PRK09521 PRK09521
exosome complex RNA-binding protein Csl4; Provisional
 26-90 7.15e-07

exosome complex RNA-binding protein Csl4; Provisional


Pssm-ID: 236547 [Multi-domain]  Cd Length: 189  Bit Score: 48.43  E-value: 7.15e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544186020  26 LVVPGDTITTDTGFMRGHGTYMGEEKLIASVAGSVER--VNKLICVKA-LKTRYIGEVGDIVVGRITE 90
Cdd:PRK09521   7 LVLPGDYLAVIEEYLPGEGTYEDNGEVYASVVGKVFIddINRKISVIPfKKTPPLLKKGDIVYGRVVD 74
Csl4 COG1096
Exosome complex RNA-binding protein Csl4, contains S1 and Zn-ribbon domains [Intracellular ...
 26-89 7.85e-07

Exosome complex RNA-binding protein Csl4, contains S1 and Zn-ribbon domains [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440713 [Multi-domain]  Cd Length: 191  Bit Score: 48.36  E-value: 7.85e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544186020  26 LVVPGDTITTDTGFMRGHGTYMGEEKLIASVAGSVE--RVNKLICVKALK-TRYIGEVGDIVVGRIT 89
Cdd:COG1096    8 FVLPGDVLAVIEEFLPGEGTYEEDGKIRAAVVGKVVidDKNRVISVKPKKkPPPVPKKGDIVIGEVV 74
 
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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