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Conserved domains on  [gi|45553317|ref|NP_996186|]
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oskar, isoform C [Drosophila melanogaster]

Protein Classification

NYN domain-containing protein( domain architecture ID 11585281)

NYN domain-containing protein; the NYN domain shares a common protein fold with PIN (PilT N-terminal)-domain nucleases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OSK pfam17182
OSK domain; This entry represents the OSK domain defined by Jeske and colleagues. The domain ...
 267-468 1.29e-122

OSK domain; This entry represents the OSK domain defined by Jeske and colleagues. The domain is related to SGNH hydrolases but lacks the active site residues. The domain binds to RNA.


:

Pssm-ID: 465373  Cd Length: 202  Bit Score: 355.52  E-value: 1.29e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553317   267 YNDSLLTINSDYDAYLLDFPLMGDDFMLYLARMELKCRFRRHERVLQSGLCVSGLTINGARNRLKRVQLPEgTQIIVNIG 346
Cdd:pfam17182   1 QDDSMFSIYSDYDPYLLGFQLLGDDFFLYLARWELGCRFDRGHRILQSGLCISGQTISEARRRLRKAPLIE-TQVIVNIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553317   347 SVDIMRGKPLVQIEHDFRLLIKEMHNMRLVPILTNLAPLGNYCHDKVLCDKIYRFNKFIRSEC-CHLKVIDIHSCLINER 425
Cdd:pfam17182  80 SVDILHGRPLVDMQHDFRQLVKVLRNRNVVPILTTLAPLANSSHDKKMCDKLLKFNNFIRDECfRHLKVIDLHSCFVNER 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 45553317   426 GVVRFDCFQASPRQVTGSKEPYLFWNKIGRQRVLQVIETSLEY 468
Cdd:pfam17182 160 GVVRFDCFQPGPRRVTGSKEPYVFWNKIGRQRVLQLIETELEY 202
LOTUS_TDRD_OSKAR cd09972
The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain ...
 16-98 3.41e-19

The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7: The LOTUS containing proteins are germline-specific and are found in the nuage/polar granules of germ cells. Tudor-containing protein 5 and 7 belong to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 and TDRD7 are components of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. Oskar protein is a critical component of the pole plasm in the Drosophila oocyte, which is required for germ cell formation.The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.


:

Pssm-ID: 193586  Cd Length: 87  Bit Score: 81.77  E-value: 3.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553317  16 PDIDSEVRAILLSHaQNGITISSIKSEYRKLTGNPFPL----HDNVTDFLLTIPNVTAECSESGKRIFNLKASLKNGHLL 91
Cdd:cd09972   2 EEVKKVLRSLLISS-KGGLTLSELERDYRELEGEPIPYrklgYSSLEDFLRSIPDVVTVRSSGGEVLVKAVADEKTAHIA 80


                ....*..
gi 45553317  92 DMVLNQK 98
Cdd:cd09972  81 SLVAKQK 87
 
Name Accession Description Interval E-value
OSK pfam17182
OSK domain; This entry represents the OSK domain defined by Jeske and colleagues. The domain ...
 267-468 1.29e-122

OSK domain; This entry represents the OSK domain defined by Jeske and colleagues. The domain is related to SGNH hydrolases but lacks the active site residues. The domain binds to RNA.


Pssm-ID: 465373  Cd Length: 202  Bit Score: 355.52  E-value: 1.29e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553317   267 YNDSLLTINSDYDAYLLDFPLMGDDFMLYLARMELKCRFRRHERVLQSGLCVSGLTINGARNRLKRVQLPEgTQIIVNIG 346
Cdd:pfam17182   1 QDDSMFSIYSDYDPYLLGFQLLGDDFFLYLARWELGCRFDRGHRILQSGLCISGQTISEARRRLRKAPLIE-TQVIVNIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553317   347 SVDIMRGKPLVQIEHDFRLLIKEMHNMRLVPILTNLAPLGNYCHDKVLCDKIYRFNKFIRSEC-CHLKVIDIHSCLINER 425
Cdd:pfam17182  80 SVDILHGRPLVDMQHDFRQLVKVLRNRNVVPILTTLAPLANSSHDKKMCDKLLKFNNFIRDECfRHLKVIDLHSCFVNER 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 45553317   426 GVVRFDCFQASPRQVTGSKEPYLFWNKIGRQRVLQVIETSLEY 468
Cdd:pfam17182 160 GVVRFDCFQPGPRRVTGSKEPYVFWNKIGRQRVLQLIETELEY 202
LOTUS_TDRD_OSKAR cd09972
The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain ...
 16-98 3.41e-19

The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7: The LOTUS containing proteins are germline-specific and are found in the nuage/polar granules of germ cells. Tudor-containing protein 5 and 7 belong to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 and TDRD7 are components of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. Oskar protein is a critical component of the pole plasm in the Drosophila oocyte, which is required for germ cell formation.The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.


Pssm-ID: 193586  Cd Length: 87  Bit Score: 81.77  E-value: 3.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553317  16 PDIDSEVRAILLSHaQNGITISSIKSEYRKLTGNPFPL----HDNVTDFLLTIPNVTAECSESGKRIFNLKASLKNGHLL 91
Cdd:cd09972   2 EEVKKVLRSLLISS-KGGLTLSELERDYRELEGEPIPYrklgYSSLEDFLRSIPDVVTVRSSGGEVLVKAVADEKTAHIA 80


                ....*..
gi 45553317  92 DMVLNQK 98
Cdd:cd09972  81 SLVAKQK 87
OST-HTH pfam12872
OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate ...
 21-78 2.94e-07

OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate TDRD5/TDRD7 proteins that nucleate or organize structurally related ribonucleoprotein (RNP) complexes, the polar granule and nuage, is poorly understood. The domain adopts the winged helix-turn- helix fold and bind RNA with a potential specificity for dsRNA.In eukaryotes this domain is often combined in the same polypeptide with protein-protein- or lipid- interaction domains that might play a role in anchoring these proteins to specific cytoskeletal structures. Thus, proteins with this domain might have a key role in the recognition and localization of dsRNA, including miRNAs, rasiRNAs and piRNAs hybridized to their targets. In other cases, this domain is fused to ubiquitin-binding, E3 ligase and ubiquitin-like domains indicating a previously under-appreciated role for ubiquitination in regulating the assembly and stability of nuage-like RNP complexes. Both bacteria and eukaryotes encode a conserved family of proteins that combines this predicted RNA-binding domain with a previously uncharacterized RNase domain belonging to the superfamily that includes the 5'->3' nucleases, PIN and NYN domains.


Pssm-ID: 463735  Cd Length: 64  Bit Score: 47.55  E-value: 2.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553317    21 EVRAILLSHAQNGITISSIKSEYRKLTGNPFPL----HDNVTDFLLTIPN-VTAECSESGKRI 78
Cdd:pfam12872   1 ELISLLRSDPDGWASLSELGSEYRKLFGEDFDPrnygFSKLSDLLKAIPDvFEIEKRGGGGLV 63
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 318-424 1.42e-03

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 39.63  E-value: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553317 318 VSGLTINGARNRLKR-VQLPEGTQIIVNIGSVDIMRGK--PLVQIEHDFRLLIKEMH--NMRLVPILTNLAPLGnycHDK 392
Cdd:COG2755  50 ISGATTADLLARLDRdLLALKPDLVVIELGTNDLLRGLgvSPEEFRANLEALIDRLRaaGPGARVVLVTPPPRL---RPN 126

                        90       100       110
                ....*....|....*....|....*....|....
gi 45553317 393 VLCDKIYRFNKFIRSEC--CHLKVIDIHSCLINE 424
Cdd:COG2755 127 YLNERIEAYNAAIRELAaeYGVPLVDLYAALRDA 160
 
Name Accession Description Interval E-value
OSK pfam17182
OSK domain; This entry represents the OSK domain defined by Jeske and colleagues. The domain ...
 267-468 1.29e-122

OSK domain; This entry represents the OSK domain defined by Jeske and colleagues. The domain is related to SGNH hydrolases but lacks the active site residues. The domain binds to RNA.


Pssm-ID: 465373  Cd Length: 202  Bit Score: 355.52  E-value: 1.29e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553317   267 YNDSLLTINSDYDAYLLDFPLMGDDFMLYLARMELKCRFRRHERVLQSGLCVSGLTINGARNRLKRVQLPEgTQIIVNIG 346
Cdd:pfam17182   1 QDDSMFSIYSDYDPYLLGFQLLGDDFFLYLARWELGCRFDRGHRILQSGLCISGQTISEARRRLRKAPLIE-TQVIVNIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553317   347 SVDIMRGKPLVQIEHDFRLLIKEMHNMRLVPILTNLAPLGNYCHDKVLCDKIYRFNKFIRSEC-CHLKVIDIHSCLINER 425
Cdd:pfam17182  80 SVDILHGRPLVDMQHDFRQLVKVLRNRNVVPILTTLAPLANSSHDKKMCDKLLKFNNFIRDECfRHLKVIDLHSCFVNER 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 45553317   426 GVVRFDCFQASPRQVTGSKEPYLFWNKIGRQRVLQVIETSLEY 468
Cdd:pfam17182 160 GVVRFDCFQPGPRRVTGSKEPYVFWNKIGRQRVLQLIETELEY 202
LOTUS_TDRD_OSKAR cd09972
The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain ...
 16-98 3.41e-19

The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7; The first LOTUS domain in Oskar and Tudor-containing proteins 5 and 7: The LOTUS containing proteins are germline-specific and are found in the nuage/polar granules of germ cells. Tudor-containing protein 5 and 7 belong to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 and TDRD7 are components of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. Oskar protein is a critical component of the pole plasm in the Drosophila oocyte, which is required for germ cell formation.The exact molecular function of LOTUS domain remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.


Pssm-ID: 193586  Cd Length: 87  Bit Score: 81.77  E-value: 3.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553317  16 PDIDSEVRAILLSHaQNGITISSIKSEYRKLTGNPFPL----HDNVTDFLLTIPNVTAECSESGKRIFNLKASLKNGHLL 91
Cdd:cd09972   2 EEVKKVLRSLLISS-KGGLTLSELERDYRELEGEPIPYrklgYSSLEDFLRSIPDVVTVRSSGGEVLVKAVADEKTAHIA 80


                ....*..
gi 45553317  92 DMVLNQK 98
Cdd:cd09972  81 SLVAKQK 87
OST-HTH pfam12872
OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate ...
 21-78 2.94e-07

OST-HTH/LOTUS domain; A predicted RNA-binding domain found in insect Oskar and vertebrate TDRD5/TDRD7 proteins that nucleate or organize structurally related ribonucleoprotein (RNP) complexes, the polar granule and nuage, is poorly understood. The domain adopts the winged helix-turn- helix fold and bind RNA with a potential specificity for dsRNA.In eukaryotes this domain is often combined in the same polypeptide with protein-protein- or lipid- interaction domains that might play a role in anchoring these proteins to specific cytoskeletal structures. Thus, proteins with this domain might have a key role in the recognition and localization of dsRNA, including miRNAs, rasiRNAs and piRNAs hybridized to their targets. In other cases, this domain is fused to ubiquitin-binding, E3 ligase and ubiquitin-like domains indicating a previously under-appreciated role for ubiquitination in regulating the assembly and stability of nuage-like RNP complexes. Both bacteria and eukaryotes encode a conserved family of proteins that combines this predicted RNA-binding domain with a previously uncharacterized RNase domain belonging to the superfamily that includes the 5'->3' nucleases, PIN and NYN domains.


Pssm-ID: 463735  Cd Length: 64  Bit Score: 47.55  E-value: 2.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553317    21 EVRAILLSHAQNGITISSIKSEYRKLTGNPFPL----HDNVTDFLLTIPN-VTAECSESGKRI 78
Cdd:pfam12872   1 ELISLLRSDPDGWASLSELGSEYRKLFGEDFDPrnygFSKLSDLLKAIPDvFEIEKRGGGGLV 63
LOTUS cd08824
LOTUS is an uncharacterized small globular domain found in Limkain b1, Oskar and ...
 21-78 6.92e-06

LOTUS is an uncharacterized small globular domain found in Limkain b1, Oskar and Tudor-containing proteins 5 and 7; LOTUS is an uncharacterized small globular domain found in Limkain b1, Oskar and Tudor-containing proteins 5 and 7. The LOTUS containing proteins are germline-specific and are found in the nuage/polar granules of germ cells. Tudor-containing protein 5 and 7 belong to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 and TDRD7 are components of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. Oskar protein is a critical component of the pole plasm in the Drosophila oocyte, which is required for germ cell formation. Limkain b1 is a novel human autoantigen, localized to a subset of ABCD3 and PXF marked peroxisomes. Limkain b1 may be a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. Limkain b1 contains multiple copies of LOTUS domains and a conserved RNA recognition motif. The exact molecular function of LOTUS domain remains to be characterized. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.


Pssm-ID: 193585 [Multi-domain]  Cd Length: 70  Bit Score: 43.76  E-value: 6.92e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45553317  21 EVRAILLSHaQNGITISSIKSEYRKLTGNPFPLHD----NVTDFLLTIPNVTAECSESGKRI 78
Cdd:cd08824   7 QLRSLLQSY-PGGLPLSKLPQLYKKKFGKPLDLSEygfsKLSDLLEALPGVVIVLSQGGERI 67
LOTUS_1_TDRD5 cd09985
The first LOTUS domain on Tudor-containing protein 5 (TDRD5); The first LOTUS domain on ...
 16-83 1.11e-05

The first LOTUS domain on Tudor-containing protein 5 (TDRD5); The first LOTUS domain on Tudor-containing protein 5 (TDRD5): TDRD5 contains three N-terminal LOTUS domains and a C-terminal Tudor domain. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD5 is a component of the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs), which are cytoplasmic ribonucleoprotein granules involved in RNA processing for spermatogenesis. The exact molecular function of LOTUS domain on TDRD5 remains to be identified. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.


Pssm-ID: 193599  Cd Length: 95  Bit Score: 44.00  E-value: 1.11e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45553317  16 PDIDSEVRAILLShAQNGITISSIKSEYRKLTGNPFPLHD----NVTDFLLTIPNVTAECSESGKRIFnLKA 83
Cdd:cd09985   6 ERLKKDVRSLLIS-SKNGLTPEQLEQDYLAMVGSPLPLRSlgfrSTMELVLDMPDVVRVHPQLDGTVI-LKA 75
LOTUS_1_TDRD7 cd09986
The first LOTUS domain on Tudor-containing protein 7 (TDRD7); The first LOTUS domain on ...
 22-98 2.24e-05

The first LOTUS domain on Tudor-containing protein 7 (TDRD7); The first LOTUS domain on Tudor-containing protein 7 (TDRD7): TDRD7 contains three N-terminal LOTUS domains and three Tudor domain repeats at the C-terminus. It belongs to the evolutionary conserved Tudor domain-containing protein (TDRD) family involved in germ cell development. In mice, TDRD7 together with TDRD1/MTR-1, TDRD5 and TDRD6 forms a ribonucleoprotein complex in the intermitochondrial cements (IMCs) and the chromatoid bodies (CBs) involving in RNA processing for spermatogenesis. TDRD7 is functionally essential for the differentiation of germ cells. The exact molecular function of LOTUS domain on TDRD7 remains to be characterized. Its occurrence in proteins associated with RNA metabolism suggests that it might be involved in RNA binding function. The presence of several basic residues and RNA fold recognition motifs support this hypothesis. The RNA binding function might be the first step of regulating mRNA translation or localization.


Pssm-ID: 193600  Cd Length: 88  Bit Score: 42.87  E-value: 2.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553317  22 VRAILLSHaQNGITISSIKSEYRKLTGNPFPL----HDNVTDFLLTIPN-VTAECSESGKRIFNLKASLKNGHLLDMVLN 96
Cdd:cd09986   8 LRAVLQSS-KGGVSLPRLQGEYKELTGEQIPFkqlgYHTLDALLRSMPSvVRLERSRSGEVMCFASLCNETAHIAKLVAR 86


                ..
gi 45553317  97 QK 98
Cdd:cd09986  87 QR 88
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 318-424 1.42e-03

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 39.63  E-value: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553317 318 VSGLTINGARNRLKR-VQLPEGTQIIVNIGSVDIMRGK--PLVQIEHDFRLLIKEMH--NMRLVPILTNLAPLGnycHDK 392
Cdd:COG2755  50 ISGATTADLLARLDRdLLALKPDLVVIELGTNDLLRGLgvSPEEFRANLEALIDRLRaaGPGARVVLVTPPPRL---RPN 126

                        90       100       110
                ....*....|....*....|....*....|....
gi 45553317 393 VLCDKIYRFNKFIRSEC--CHLKVIDIHSCLINE 424
Cdd:COG2755 127 YLNERIEAYNAAIRELAaeYGVPLVDLYAALRDA 160
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 295-419 2.51e-03

GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.


Pssm-ID: 463889  Cd Length: 176  Bit Score: 38.68  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553317   295 YLARMeLKCRFRRHERVLQSglcVSGLTIN-GARNRLKRVQLPEGTQIIVNIGSVDIMRGKPLVQIEHDFRLLIKEMH-- 371
Cdd:pfam13472  22 WLARL-LARRLGADVVNNLG---ISGATTRlDLLERLDDVLRLKPDLVVILLGTNDLGRGVSAARAAANLEALIDALRaa 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 45553317   372 --NMRLVPILTNLAPLGNYCHDKVLCDKIYRFNKFIRSEC--CHLKVIDIHS 419
Cdd:pfam13472  98 gpDARVLLIGPLPVGPPPPLDERRLNARIAEYNAAIREVAaeRGVPYVDLWD 149
 
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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