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Conserved domains on  [gi|26330860|dbj|BAC29160|]
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unnamed protein product [Mus musculus]

Protein Classification

NYN domain-containing protein( domain architecture ID 10180762)

NYN domain-containing protein; the NYN domain shares a common protein fold with PIN (PilT N-terminal)-domain nucleases; similar to Human MARF1 (meiosis regulator and mRNA stability factor 1), an essential regulator of oogenesis required for female meiotic progression to repress transposable elements and preventing their mobilization, which is essential for the germline integrity

Gene Ontology:  GO:0004540
PubMed:  17114934

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RRM1_LKAP cd12255
RNA recognition motif 1 (RRM1) found in Limkain-b1 (LKAP) and similar proteins; This subfamily ...
 279-351 4.91e-42

RNA recognition motif 1 (RRM1) found in Limkain-b1 (LKAP) and similar proteins; This subfamily corresponds to the RRM1 of LKAP, a novel peroxisomal autoantigen that co-localizes with a subset of cytoplasmic microbodies marked by ABCD3 (ATP-binding cassette subfamily D member 3, known previously as PMP-70) and/or PXF (peroxisomal farnesylated protein, known previously as PEX19). It associates with LIM kinase 2 (LIMK2) and may serve as a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. LKAP contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). However, whether those RRMs are bona fide RNA binding sites remains unclear. Moreover, there is no evidence of LAKP localization in the nucleus. Therefore, if the RRMs are functional, their interaction with RNA species would be restricted to the cytoplasm and peroxisomes.


:

Pssm-ID: 409700  Cd Length: 73  Bit Score: 144.81  E-value: 4.91e-42
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26330860 279 CHTLLYVYNLPANKDGKSISNRLRRLSDNCGGKVLSITGCSAILRFINQDSAERAQKRMENEDVFGNRIIVSF 351
Cdd:cd12255   1 CHTLLYVYNLPTNRDVKSIRNRLRQLSDNCGGKVLSVSGGSAILRFANQESAERAQKRMEGEDVFGNKISVSF 73
PIN_limkain_b1_N_like cd10910
N-terminal LabA-like PIN domain of limkain b1 and similar proteins; Limkain b1 is a human ...
 122-244 5.46e-41

N-terminal LabA-like PIN domain of limkain b1 and similar proteins; Limkain b1 is a 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, this and similar domain architectures are shared by several members of this family, and a function of these architectures in RNA binding or RNA metabolism has been suggested. The function of the N-terminal domain is unknown. This subfamily belongs to LabA-like PIN domain family which includes Synechococcus elongatus PCC 7942 LabA, human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


:

Pssm-ID: 350234  Cd Length: 126  Bit Score: 143.53  E-value: 5.46e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26330860 122 PIGVFWDIENCSVPSGRSATTVVQRIR---EKFFRgHREAEFICVCDISKENKEVIQELNNCQVTVAHINATAKNAADDK 198
Cdd:cd10910   1 KTGVFWDIENCPVPDGYDARRVGPNIRralRKLGY-SGPVSITAYGDLSKVPKDVLSELSSSGVSLVHVPHGGKKAADKK 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 26330860 199 LRQSLRRFANTHTAPATVVLVSTDV-NFALELSDLRHRhGFHIILVH 244
Cdd:cd10910  80 ILVDMLLWALDNPPPANIMLISGDVrDFAYALSRLRSR-GYNVLLAY 125
 
Name Accession Description Interval E-value
RRM1_LKAP cd12255
RNA recognition motif 1 (RRM1) found in Limkain-b1 (LKAP) and similar proteins; This subfamily ...
 279-351 4.91e-42

RNA recognition motif 1 (RRM1) found in Limkain-b1 (LKAP) and similar proteins; This subfamily corresponds to the RRM1 of LKAP, a novel peroxisomal autoantigen that co-localizes with a subset of cytoplasmic microbodies marked by ABCD3 (ATP-binding cassette subfamily D member 3, known previously as PMP-70) and/or PXF (peroxisomal farnesylated protein, known previously as PEX19). It associates with LIM kinase 2 (LIMK2) and may serve as a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. LKAP contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). However, whether those RRMs are bona fide RNA binding sites remains unclear. Moreover, there is no evidence of LAKP localization in the nucleus. Therefore, if the RRMs are functional, their interaction with RNA species would be restricted to the cytoplasm and peroxisomes.


Pssm-ID: 409700  Cd Length: 73  Bit Score: 144.81  E-value: 4.91e-42
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26330860 279 CHTLLYVYNLPANKDGKSISNRLRRLSDNCGGKVLSITGCSAILRFINQDSAERAQKRMENEDVFGNRIIVSF 351
Cdd:cd12255   1 CHTLLYVYNLPTNRDVKSIRNRLRQLSDNCGGKVLSVSGGSAILRFANQESAERAQKRMEGEDVFGNKISVSF 73
PIN_limkain_b1_N_like cd10910
N-terminal LabA-like PIN domain of limkain b1 and similar proteins; Limkain b1 is a human ...
 122-244 5.46e-41

N-terminal LabA-like PIN domain of limkain b1 and similar proteins; Limkain b1 is a 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, this and similar domain architectures are shared by several members of this family, and a function of these architectures in RNA binding or RNA metabolism has been suggested. The function of the N-terminal domain is unknown. This subfamily belongs to LabA-like PIN domain family which includes Synechococcus elongatus PCC 7942 LabA, human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350234  Cd Length: 126  Bit Score: 143.53  E-value: 5.46e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26330860 122 PIGVFWDIENCSVPSGRSATTVVQRIR---EKFFRgHREAEFICVCDISKENKEVIQELNNCQVTVAHINATAKNAADDK 198
Cdd:cd10910   1 KTGVFWDIENCPVPDGYDARRVGPNIRralRKLGY-SGPVSITAYGDLSKVPKDVLSELSSSGVSLVHVPHGGKKAADKK 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 26330860 199 LRQSLRRFANTHTAPATVVLVSTDV-NFALELSDLRHRhGFHIILVH 244
Cdd:cd10910  80 ILVDMLLWALDNPPPANIMLISGDVrDFAYALSRLRSR-GYNVLLAY 125
NYN pfam01936
NYN domain; These domains are found in the eukaryotic proteins typified by the Nedd4-binding ...
 122-260 3.84e-23

NYN domain; These domains are found in the eukaryotic proteins typified by the Nedd4-binding protein 1 and the bacterial YacP-like proteins (Nedd4-BP1, YacP nucleases; NYN domains). The NYN domain shares a common protein fold with two other previously characterized groups of nucleases, namely the PIN (PilT N-terminal) and FLAP/5' --> 3' exonuclease superfamilies. These proteins share a common set of 4 acidic conserved residues that are predicted to constitute their active site. Based on the conservation of the acidic residues and structural elements Aravind and colleagues suggest that PIN and NYN domains are likely to bind only a single metal ion, unlike the FLAP/5' --> 3' exonuclease superfamily, which binds two metal ions. Based on conserved gene neighborhoods Aravind and colleagues infer that the bacterial members are likely to be components of the processome/degradsome that process tRNAs or ribosomal RNAs.


Pssm-ID: 426520  Cd Length: 137  Bit Score: 95.04  E-value: 3.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26330860   122 PIGVFWDIENCSVPSGRSATTVVQRIREkffrgHREA-EFICVCDISKEN-KEVIQELNNCQVTVAHINAT-AKNAADDK 198
Cdd:pfam01936   1 RVAVFIDGENCPLPDGVDYRKVLEEIRS-----GGEVvRARAYGNWGDPDlRKFPDALSSTGIPVQHKPLTkGKNAVDVG 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26330860   199 LRQSLRRFANTHTaPATVVLVSTDVNFALELSDLRHRHGF-HIILVHKNQASEALLHHANQLI 260
Cdd:pfam01936  76 LAVDALELAYDNN-PDTFVLVSGDGDFAPLLERLRERGKRvEVLGAEEPSTSDALINAADRFI 137
MARF1_RRM1 pfam11608
MARF1, RNA recognition motif 1; MARF1 (also known as Limkain-b1) is an essential protein for ...
 281-357 7.49e-21

MARF1, RNA recognition motif 1; MARF1 (also known as Limkain-b1) is an essential protein for controlling meiosis and retrotransposon surveillance in mouse oocytes, first described as a human autoantigen localized to a subset of ABCD3 and PXF marked peroxisomes. It may function both as an adaptor to recruit specific RNA targets and an effector to catalyze the specific cleavages of target RNAs. MARF1 contains an N-terminal NYN domain, two central RRMs, and C-terminal OST-HTH/LOTUS domains. This domain represents the RNA recognition motif 1 (RRM1) of MARF1.


Pssm-ID: 463307  Cd Length: 89  Bit Score: 87.10  E-value: 7.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26330860   281 TLLYVYNLPANKDgKSISN----RLRRLSDNCGGKVLSITGCSAILRFINQDSAERAQKRMENEDVFGNRIIVSFTPKHR 356
Cdd:pfam11608   3 NLLFVRNLPVNCD-KSLQNavkhRLRRLSDNCGGKVLGISQGTAVLRFGSPEAASRACKRMENEDVYGHRISLSFSLGPR 81


                  .
gi 26330860   357 E 357
Cdd:pfam11608  82 D 82
 
Name Accession Description Interval E-value
RRM1_LKAP cd12255
RNA recognition motif 1 (RRM1) found in Limkain-b1 (LKAP) and similar proteins; This subfamily ...
 279-351 4.91e-42

RNA recognition motif 1 (RRM1) found in Limkain-b1 (LKAP) and similar proteins; This subfamily corresponds to the RRM1 of LKAP, a novel peroxisomal autoantigen that co-localizes with a subset of cytoplasmic microbodies marked by ABCD3 (ATP-binding cassette subfamily D member 3, known previously as PMP-70) and/or PXF (peroxisomal farnesylated protein, known previously as PEX19). It associates with LIM kinase 2 (LIMK2) and may serve as a relatively common target of human autoantibodies reactive to cytoplasmic vesicle-like structures. LKAP contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). However, whether those RRMs are bona fide RNA binding sites remains unclear. Moreover, there is no evidence of LAKP localization in the nucleus. Therefore, if the RRMs are functional, their interaction with RNA species would be restricted to the cytoplasm and peroxisomes.


Pssm-ID: 409700  Cd Length: 73  Bit Score: 144.81  E-value: 4.91e-42
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26330860 279 CHTLLYVYNLPANKDGKSISNRLRRLSDNCGGKVLSITGCSAILRFINQDSAERAQKRMENEDVFGNRIIVSF 351
Cdd:cd12255   1 CHTLLYVYNLPTNRDVKSIRNRLRQLSDNCGGKVLSVSGGSAILRFANQESAERAQKRMEGEDVFGNKISVSF 73
PIN_limkain_b1_N_like cd10910
N-terminal LabA-like PIN domain of limkain b1 and similar proteins; Limkain b1 is a human ...
 122-244 5.46e-41

N-terminal LabA-like PIN domain of limkain b1 and similar proteins; Limkain b1 is a 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, this and similar domain architectures are shared by several members of this family, and a function of these architectures in RNA binding or RNA metabolism has been suggested. The function of the N-terminal domain is unknown. This subfamily belongs to LabA-like PIN domain family which includes Synechococcus elongatus PCC 7942 LabA, human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.


Pssm-ID: 350234  Cd Length: 126  Bit Score: 143.53  E-value: 5.46e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26330860 122 PIGVFWDIENCSVPSGRSATTVVQRIR---EKFFRgHREAEFICVCDISKENKEVIQELNNCQVTVAHINATAKNAADDK 198
Cdd:cd10910   1 KTGVFWDIENCPVPDGYDARRVGPNIRralRKLGY-SGPVSITAYGDLSKVPKDVLSELSSSGVSLVHVPHGGKKAADKK 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 26330860 199 LRQSLRRFANTHTAPATVVLVSTDV-NFALELSDLRHRhGFHIILVH 244
Cdd:cd10910  80 ILVDMLLWALDNPPPANIMLISGDVrDFAYALSRLRSR-GYNVLLAY 125
PIN_LabA-like cd06167
PIN domain of Synechococcus elongatus LabA (low-amplitude and bright) and related proteins; ...
 124-245 1.41e-23

PIN domain of Synechococcus elongatus LabA (low-amplitude and bright) and related proteins; The LabA-like PIN domain family includes Synechococcus elongatus PCC 7942 LabA which participates in cyanobacterial circadian timing. It is required for negative feedback regulation of the autokinase/autophosphatase KaiC, a central component of the circadian clock system. In particular, LabA seems necessary for KaiC-dependent repression of gene expression. This family also includes the N-terminal domain of limkain b1, a human autoantigen associated with cytoplasmic vesicles. Other members are the LabA-like PIN domains of human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into this family.


Pssm-ID: 350201  Cd Length: 113  Bit Score: 95.56  E-value: 1.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26330860 124 GVFWDIENCSVPSGrsatTVVQRIREKFFRGhreAEFICVCDIsKENKEVIQELNNCQVTVAHINATAKNAADDKLRQSL 203
Cdd:cd06167   1 GVLVDADNCSNGFG----ALILRRYAGLFLQ---MGFEKYANI-NAQPLLVPPSNNRGFTVIRVAAKRKDAADVALVRQA 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 26330860 204 RRFANTHTaPATVVLVSTDvnfALELSDLRHR---HGFHIILVHK 245
Cdd:cd06167  73 GRLAYTGA-PDTVVLVSGD---KLDFSDLIEKakeAGLNVIVVGP 113
NYN pfam01936
NYN domain; These domains are found in the eukaryotic proteins typified by the Nedd4-binding ...
 122-260 3.84e-23

NYN domain; These domains are found in the eukaryotic proteins typified by the Nedd4-binding protein 1 and the bacterial YacP-like proteins (Nedd4-BP1, YacP nucleases; NYN domains). The NYN domain shares a common protein fold with two other previously characterized groups of nucleases, namely the PIN (PilT N-terminal) and FLAP/5' --> 3' exonuclease superfamilies. These proteins share a common set of 4 acidic conserved residues that are predicted to constitute their active site. Based on the conservation of the acidic residues and structural elements Aravind and colleagues suggest that PIN and NYN domains are likely to bind only a single metal ion, unlike the FLAP/5' --> 3' exonuclease superfamily, which binds two metal ions. Based on conserved gene neighborhoods Aravind and colleagues infer that the bacterial members are likely to be components of the processome/degradsome that process tRNAs or ribosomal RNAs.


Pssm-ID: 426520  Cd Length: 137  Bit Score: 95.04  E-value: 3.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26330860   122 PIGVFWDIENCSVPSGRSATTVVQRIREkffrgHREA-EFICVCDISKEN-KEVIQELNNCQVTVAHINAT-AKNAADDK 198
Cdd:pfam01936   1 RVAVFIDGENCPLPDGVDYRKVLEEIRS-----GGEVvRARAYGNWGDPDlRKFPDALSSTGIPVQHKPLTkGKNAVDVG 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26330860   199 LRQSLRRFANTHTaPATVVLVSTDVNFALELSDLRHRHGF-HIILVHKNQASEALLHHANQLI 260
Cdd:pfam01936  76 LAVDALELAYDNN-PDTFVLVSGDGDFAPLLERLRERGKRvEVLGAEEPSTSDALINAADRFI 137
MARF1_RRM1 pfam11608
MARF1, RNA recognition motif 1; MARF1 (also known as Limkain-b1) is an essential protein for ...
 281-357 7.49e-21

MARF1, RNA recognition motif 1; MARF1 (also known as Limkain-b1) is an essential protein for controlling meiosis and retrotransposon surveillance in mouse oocytes, first described as a human autoantigen localized to a subset of ABCD3 and PXF marked peroxisomes. It may function both as an adaptor to recruit specific RNA targets and an effector to catalyze the specific cleavages of target RNAs. MARF1 contains an N-terminal NYN domain, two central RRMs, and C-terminal OST-HTH/LOTUS domains. This domain represents the RNA recognition motif 1 (RRM1) of MARF1.


Pssm-ID: 463307  Cd Length: 89  Bit Score: 87.10  E-value: 7.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26330860   281 TLLYVYNLPANKDgKSISN----RLRRLSDNCGGKVLSITGCSAILRFINQDSAERAQKRMENEDVFGNRIIVSFTPKHR 356
Cdd:pfam11608   3 NLLFVRNLPVNCD-KSLQNavkhRLRRLSDNCGGKVLGISQGTAVLRFGSPEAASRACKRMENEDVYGHRISLSFSLGPR 81


                  .
gi 26330860   357 E 357
Cdd:pfam11608  82 D 82
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 283-350 1.06e-04

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


Pssm-ID: 409669 [Multi-domain]  Cd Length: 72  Bit Score: 40.73  E-value: 1.06e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26330860 283 LYVYNLPANKDGKSISNRLRRLsdncgGKVLSIT---------GCSAILRFINQDSAERAQKRMENEDVFGNRIIVS 350
Cdd:cd00590   1 LFVGNLPPDTTEEDLRELFSKF-----GEVVSVRivrdrdgksKGFAFVEFESPEDAEKALEALNGTELGGRPLKVS 72
 
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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