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Conserved domains on  [gi|518093919|ref|WP_019264127|]
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MULTISPECIES: PIN domain-containing protein [Methanobrevibacter]

Protein Classification

PIN domain-containing protein( domain architecture ID 10177438)

PIN (PilT N terminus) domain-containing protein may function as a nuclease; similar to Archaeoglobus fulgidus ribonuclease VapC9

Gene Ontology:  GO:0004540
PubMed:  21036780|17114934

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PIN_VapC_AF0591-like cd09879
VapC-like PIN domain of Archaeoglobus fulgidus AF0591 protein and other similar archaeal ...
 6-124 1.19e-41

VapC-like PIN domain of Archaeoglobus fulgidus AF0591 protein and other similar archaeal homologs; PIN (PilT N terminus) domain of Archaeoglobus fulgidus AF0591 protein and other similar uncharacterized archaeal homologs are included in this family. This subgroup belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) 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. Some members of the superfamily lack several of these key catalytic residues. PIN domains within this subgroup contain four of these highly conserved putative metal-binding, active site 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. Matelska et al. recently classified PIN-like domains and included distant subgroups, this subgroup includes some sequences belonging to one of these, PIN_14.


:

Pssm-ID: 350227 [Multi-domain]  Cd Length: 118  Bit Score: 133.74  E-value: 1.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518093919   6 VVIDTNFFMVPFQFNVDIIDELEKALPSYKLTTPSFVINELKGLKRNNKGKIRLNADLALKLANssNIEIKDISLennET 85
Cdd:cd09879    1 VILDTNFLMYPFQFGVDIFEELERLLGKYEIVVPSAVIEELERLAKKGKGKDKRAARLALKLAE--RCKVVESEG---EP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 518093919  86 VDDALLRVSE----VLATNDIELKKRAKKKGITVAYLRQKKYI 124
Cdd:cd09879   76 ADDAILELAKelgaIVATNDRELRKRLREKGIPVIYLRQKKRL 118
 
Name Accession Description Interval E-value
PIN_VapC_AF0591-like cd09879
VapC-like PIN domain of Archaeoglobus fulgidus AF0591 protein and other similar archaeal ...
 6-124 1.19e-41

VapC-like PIN domain of Archaeoglobus fulgidus AF0591 protein and other similar archaeal homologs; PIN (PilT N terminus) domain of Archaeoglobus fulgidus AF0591 protein and other similar uncharacterized archaeal homologs are included in this family. This subgroup belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) 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. Some members of the superfamily lack several of these key catalytic residues. PIN domains within this subgroup contain four of these highly conserved putative metal-binding, active site 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. Matelska et al. recently classified PIN-like domains and included distant subgroups, this subgroup includes some sequences belonging to one of these, PIN_14.


Pssm-ID: 350227 [Multi-domain]  Cd Length: 118  Bit Score: 133.74  E-value: 1.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518093919   6 VVIDTNFFMVPFQFNVDIIDELEKALPSYKLTTPSFVINELKGLKRNNKGKIRLNADLALKLANssNIEIKDISLennET 85
Cdd:cd09879    1 VILDTNFLMYPFQFGVDIFEELERLLGKYEIVVPSAVIEELERLAKKGKGKDKRAARLALKLAE--RCKVVESEG---EP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 518093919  86 VDDALLRVSE----VLATNDIELKKRAKKKGITVAYLRQKKYI 124
Cdd:cd09879   76 ADDAILELAKelgaIVATNDRELRKRLREKGIPVIYLRQKKRL 118
Fcf1 COG1412
rRNA-processing protein FCF1 [Translation, ribosomal structure and biogenesis];
4-127 1.09e-35

rRNA-processing protein FCF1 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441022 [Multi-domain]  Cd Length: 123  Bit Score: 118.78  E-value: 1.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518093919   4 KEVVIDTNFFMVPFQFNVDIIDELEKALPSYKLTTPSFVINELKGLKRNNKGKIRLNADLALKLANssNIEIKDIsleNN 83
Cdd:COG1412    1 VKVLLDTNALMMPAQFGVDVFEELDRLLGKYEFIVPEAVLEELEKLSRGAKGKEKRAARVALDLAE--RCEIVET---EG 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 518093919  84 ETVDDALLRVSE----VLATNDIELKKRAKKKGITVAYLRQKKYIAID 127
Cdd:COG1412   76 GYADDAILELAKengvIVATNDKELRRRLLEAGIPVIYLRQKKKLLIT 123
PIN_9 pfam18477
PIN like domain; This is a domain of unknown function that resembles the PIN like domains. ...
 6-121 3.43e-29

PIN like domain; This is a domain of unknown function that resembles the PIN like domains. Family members include Ribonuclease VapC9.


Pssm-ID: 436530  Cd Length: 116  Bit Score: 102.38  E-value: 3.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518093919    6 VVIDTNFFMVPFQFNVDIIDELEKALPSYKLTTPSFVINELKGLKRNNKGKIRLNADLALKLANSSniEIKDISLENnet 85
Cdd:pfam18477   1 VIIDTNALMIPVQFGVDIFEELDRLLGYYEFVVPRAVLDELDRLVKAGRGEDATAASVGLDLADRC--ETVETEAGY--- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 518093919   86 VDDALLRV-----SEVLATNDIELKKRAKKKGITVAYLRQK 121
Cdd:pfam18477  76 ADDAIVELaraldADVVVTNDIPLKKRLLDAGVPVIYLRQR 116
 
Name Accession Description Interval E-value
PIN_VapC_AF0591-like cd09879
VapC-like PIN domain of Archaeoglobus fulgidus AF0591 protein and other similar archaeal ...
 6-124 1.19e-41

VapC-like PIN domain of Archaeoglobus fulgidus AF0591 protein and other similar archaeal homologs; PIN (PilT N terminus) domain of Archaeoglobus fulgidus AF0591 protein and other similar uncharacterized archaeal homologs are included in this family. This subgroup belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. The structural properties of the PIN (PilT N terminus) 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. Some members of the superfamily lack several of these key catalytic residues. PIN domains within this subgroup contain four of these highly conserved putative metal-binding, active site 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. Matelska et al. recently classified PIN-like domains and included distant subgroups, this subgroup includes some sequences belonging to one of these, PIN_14.


Pssm-ID: 350227 [Multi-domain]  Cd Length: 118  Bit Score: 133.74  E-value: 1.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518093919   6 VVIDTNFFMVPFQFNVDIIDELEKALPSYKLTTPSFVINELKGLKRNNKGKIRLNADLALKLANssNIEIKDISLennET 85
Cdd:cd09879    1 VILDTNFLMYPFQFGVDIFEELERLLGKYEIVVPSAVIEELERLAKKGKGKDKRAARLALKLAE--RCKVVESEG---EP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 518093919  86 VDDALLRVSE----VLATNDIELKKRAKKKGITVAYLRQKKYI 124
Cdd:cd09879   76 ADDAILELAKelgaIVATNDRELRKRLREKGIPVIYLRQKKRL 118
Fcf1 COG1412
rRNA-processing protein FCF1 [Translation, ribosomal structure and biogenesis];
4-127 1.09e-35

rRNA-processing protein FCF1 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441022 [Multi-domain]  Cd Length: 123  Bit Score: 118.78  E-value: 1.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518093919   4 KEVVIDTNFFMVPFQFNVDIIDELEKALPSYKLTTPSFVINELKGLKRNNKGKIRLNADLALKLANssNIEIKDIsleNN 83
Cdd:COG1412    1 VKVLLDTNALMMPAQFGVDVFEELDRLLGKYEFIVPEAVLEELEKLSRGAKGKEKRAARVALDLAE--RCEIVET---EG 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 518093919  84 ETVDDALLRVSE----VLATNDIELKKRAKKKGITVAYLRQKKYIAID 127
Cdd:COG1412   76 GYADDAILELAKengvIVATNDKELRRRLLEAGIPVIYLRQKKKLLIT 123
PIN_9 pfam18477
PIN like domain; This is a domain of unknown function that resembles the PIN like domains. ...
 6-121 3.43e-29

PIN like domain; This is a domain of unknown function that resembles the PIN like domains. Family members include Ribonuclease VapC9.


Pssm-ID: 436530  Cd Length: 116  Bit Score: 102.38  E-value: 3.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518093919    6 VVIDTNFFMVPFQFNVDIIDELEKALPSYKLTTPSFVINELKGLKRNNKGKIRLNADLALKLANSSniEIKDISLENnet 85
Cdd:pfam18477   1 VIIDTNALMIPVQFGVDIFEELDRLLGYYEFVVPRAVLDELDRLVKAGRGEDATAASVGLDLADRC--ETVETEAGY--- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 518093919   86 VDDALLRV-----SEVLATNDIELKKRAKKKGITVAYLRQK 121
Cdd:pfam18477  76 ADDAIVELaraldADVVVTNDIPLKKRLLDAGVPVIYLRQR 116
PIN_Fcf1-like cd09864
VapC-like PIN domain of rRNA-processing protein, Fcf1 (Utp24, YDR339C), and other eukaryotic ...
 6-123 3.60e-06

VapC-like PIN domain of rRNA-processing protein, Fcf1 (Utp24, YDR339C), and other eukaryotic homologs; Fcf1/Utp24 (FAF1-copurifying factor 1/U three-associated protein 24) is an essential protein involved in pre-rRNA processing and 40S ribosomal subunit assembly. Component of the small subunit (SSU) processome, Fcf1 is an essential nucleolar protein that is required for processing of the 18S pre-rRNA at sites A0-A2. The Fcf1 protein was reported to interact with Pmc1p (vacuolar Ca2+ ATPase) and Cor1p (core subunit of the ubiquinol-cytochrome c reductase complex). 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. Most members of the Fcf1 PIN domain subfamily have four of these conserved residues and the Fcf1-Utp23 homolog PIN domain subfamily has three. Point mutation studies of the conserved acidic residues in the putative active site of Saccharomyces cerevisiae Fcf1 determined they were essential for pre-rRNA processing at sites A1 and A2, whereas the presence of the Fcf1 protein itself is also required for cleavage at site A0.


Pssm-ID: 350212  Cd Length: 131  Bit Score: 43.29  E-value: 3.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518093919   6 VVIDTNFFMVPFQFNVDIIDELEKAL-PSYKLTTPSFVINELKGLKRnnkgKIRLnadlALKLANSSNIEikdiSLENNE 84
Cdd:cd09864   13 VLLDTNFINFSIQNKLDIVKGMMDCLyAKCIPCITDCVMAELEKLGR----KYRV----ALRIAKDPRFE----RLKCDH 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 518093919  85 TV---DDALL-RVSE----VLATNDIELKKRAKKK-GITVAYLRQKKY 123
Cdd:cd09864   81 KGtyaDDCIVnRVTQhrcyIVATCDRDLKRRIRKIpGVPIMYIKGHKY 128
PIN_YacL-like cd09877
VapC-like PIN domain of Thermus Thermophilus Hb8, uncharacterized Bacillus subtilis YacL, and ...
 23-115 1.20e-05

VapC-like PIN domain of Thermus Thermophilus Hb8, uncharacterized Bacillus subtilis YacL, and other bacterial homologs; PIN (PilT N terminus) domain of the conserved membrane protein of unknown function of Thermus Thermophilus Hb8, Bacillus subtilis YacL and other similar homologs are included in this family. This subgroup belongs to the VapC (virulence-associated protein C)-like family of the PIN domain nuclease superfamily. VapC is the PIN-domain ribonuclease toxin from prokaryotic VapBC toxin-antitoxin (TA) systems. VapB is a transcription factor-like protein antitoxin acting as an inhibitor. Other members of the VapC-like nuclease family include FitB toxin of the FitAB TA system, eukaryotic ribonucleases such as Smg6, ribosome assembly factor NOB1, exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1. 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. Proteins in this group have a C-terminal TRAM domain whose function is unknown but predicted to be a RNA-binding domain common to tRNA uracil methylation and adenine thiolation enzymes.


Pssm-ID: 350225 [Multi-domain]  Cd Length: 127  Bit Score: 41.63  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518093919  23 IIDELEKALPSYKLTTPSFVINELKGL-------KRnNKGKIRLNADLALKLANSSNIEIKDISLENNETVDDALLRVSE 95
Cdd:cd09877   13 IADIAKTGFLDGTLVVPRFVLDELQLLadssdplKR-ARGRRGLDVLKKLQKLPGLDVRIVDTDFPEIKEVDAKLVRLAK 91

                         90       100
                 ....*....|....*....|....
gi 518093919  96 V----LATNDIELKKRAKKKGITV 115
Cdd:cd09877   92 ElgakLLTNDFNLNKVAKLQGVKV 115
PIN_4 pfam13638
PIN domain; Members of this family of bacterial domains are predicted to be RNases (from ...
 7-115 5.14e-04

PIN domain; Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases).


Pssm-ID: 433369  Cd Length: 131  Bit Score: 37.21  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518093919    7 VIDTNFFMvpfqFNVDIIDELEKalpSYKLTTPSFVINELKGLKRNNKGKIRLNADLA---------LKLANSSNIEI-- 75
Cdd:pfam13638   2 VLDTNVLL----HDPDALFNFGE---ENDVVIPITVLEELDGLKKGSDESGRELARLArqanrwldeLLENNGGRLRGqt 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 518093919   76 --KDISLENNETVDDALLRVSE-----------VLATNDIELKKRAKKKGITV 115
Cdd:pfam13638  75 ldERLPPDPFDKNDNRILAVALylkeelpdrpvILVSKDINLRIKADALGIPA 127
PIN_Fcf1-like cd08553
VapC-like PIN domain of rRNA-processing proteins, Fcf1 (Utp24, YDR339C), Utp23 (YOR004W), and ...
 6-118 2.50e-03

VapC-like PIN domain of rRNA-processing proteins, Fcf1 (Utp24, YDR339C), Utp23 (YOR004W), and other eukaryotic homologs; Fcf1 (FAF1-copurifying factor 1, also known as Utp24) and Utp23 (U three-associated protein 23) are essential proteins involved in pre-rRNA processing and 40S ribosomal subunit assembly. Components of the small subunit (SSU) processome, Fcf1 and Utp23 are essential nucleolar proteins that are required for processing of the 18S pre-rRNA at sites A0-A2. The Fcf1 protein was reported to interact with Pmc1p (vacuolar Ca2+ ATPase) and Cor1p (core subunit of the ubiquinol-cytochrome c reductase complex). 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. The subfamily of Fcf1- and Utp23-like homologs have three of the four conserved residues found in S. cerevisiae Fcf1. Some members of the superfamily, including S. cerevisiae Utp23, lack several of these key catalytic residues. Mutation of the remaining conserved putative active site residues seen in Utp23 did not interfere with rRNA maturation and cell viability. 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: 350202 [Multi-domain]  Cd Length: 123  Bit Score: 35.25  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518093919   6 VVIDTNFFMVPFQFNVDIIDELEKAL--PSYKLTTPSfVINELKGLkrnnkGKIRLNADLALKLAN-----------SSN 72
Cdd:cd08553    3 VLVDGNFIHAALQKKIDLKEALPKLLggKVKLFVTRC-VLAELRSL-----GEDFSGALLAAKRFErrrcnheegpvSAA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 518093919  73 IEIKDISLENNEtvddallrvsE--VLATNDIELKKRAKKK-GITVAYL 118
Cdd:cd08553   77 ECILDIIGKNNE----------EhyFVATQDTELRKKLRKIpGVPLLYI 115
PIN_Swt1-like cd18727
VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins; ...
 7-115 3.98e-03

VapC-like PIN domain of Saccharomyces cerevisiae Swt1p, human SWT1 and related proteins; Saccharomyces cerevisiae mRNA-processing endoribonuclease Swt1p plays an important role in quality control of nuclear mRNPs in eukaryotes. Human transcriptional protein SWT1 (RNA endoribonuclease homolog, also known as HsSwt1, C1orf26, and chromosome 1 open reading frame 26) is an RNA endonuclease that participates in quality control of nuclear mRNPs and can associate with the nuclear pore complex (NPC). This subfamily belongs to the Smg5 and Smg6-like PIN domain family. Smg5 and Smg6 are essential factors in NMD, a post-transcriptional regulatory pathway that recognizes and rapidly degrades mRNAs containing premature translation termination codons. In vivo, the Smg6 PIN domain elicits degradation of bound mRNAs, as well as, metal-ion dependent, degradation of single-stranded RNA, in vitro. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like), PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons. Point mutation studies of the conserved aspartate residues in the catalytic center of the Smg6 PIN domain revealed that Smg6 is the endonuclease involved in human NMD. However, Smg5 lacks several of these key catalytic residues and does not degrade single-stranded RNA, in vivo.


Pssm-ID: 350294  Cd Length: 141  Bit Score: 34.84  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518093919   7 VIDTNFFMVPFQFNVDIIDELEKALPSYKLTTPSFVINELKGLK-RNNKGKIRLNADLAL-----KLANSSNI------- 73
Cdd:cd18727    1 VLDTNVLISHLDLLKQLVEDVEKLSLPVVIVIPWVVLQELDGLKkSKRKSSLGWLARRAStwlleKLRSKHPRvrgqals 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 518093919  74 EIKDISLENNETVDDALL------------RVseVLATNDIELKKRAKKKGITV 115
Cdd:cd18727   81 ETLRASGDPGESNDDAILdcclyfqekygaPV--VLLSNDKNLCNKALINGIPT 132
 
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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