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Conserved domains on  [gi|530365433|ref|XP_005245570|]
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acidic leucine-rich nuclear phosphoprotein 32 family member E isoform X1 [Homo sapiens]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 705725)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  11751054

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR_9 super family cl25994
Leucine-rich repeat;
34-146 7.76e-11

Leucine-rich repeat;


The actual alignment was detected with superfamily member pfam14580:

Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 59.78  E-value: 7.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433   34 IEGLNDTFKELEFLSMANVELSSLARLPSLNKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEALQNLK 113
Cdd:pfam14580  34 IENLGATLDQFDTIDFSDNEIRKLDGFPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDPLASLK 113

                          90       100       110
                  ....*....|....*....|....*....|...
gi 530365433  114 NLKSLDLFNCEITNLEDYRESIFELLQQITYLD 146
Cdd:pfam14580 114 KLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLD 146
 
Name Accession Description Interval E-value
LRR_9 pfam14580
Leucine-rich repeat;
34-146 7.76e-11

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 59.78  E-value: 7.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433   34 IEGLNDTFKELEFLSMANVELSSLARLPSLNKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEALQNLK 113
Cdd:pfam14580  34 IENLGATLDQFDTIDFSDNEIRKLDGFPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDPLASLK 113

                          90       100       110
                  ....*....|....*....|....*....|...
gi 530365433  114 NLKSLDLFNCEITNLEDYRESIFELLQQITYLD 146
Cdd:pfam14580 114 KLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLD 146
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
41-128 2.96e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 54.17  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433  41 FKELEFLSMANVELSSL-ARLPSLNKLRKLELSDNIISGGLEVLAeKCPNLTYLNLSGNKIKDLStvEALQNLKNLKSLD 119
Cdd:COG4886  112 LTNLESLDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLPEPLG-NLTNLKSLDLSNNQLTDLP--EELGNLTNLKELD 188


                 ....*....
gi 530365433 120 LFNCEITNL 128
Cdd:COG4886  189 LSNNQITDL 197
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 25-153 4.83e-06

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 46.32  E-value: 4.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433  25 DNCLCvngEIEGLNdTFKELEFLSMANVELSSLARLPSLNKLRKLELSDNIIS--GGLEvlaeKCPN------------- 89
Cdd:cd21340   33 DNKIT---KIENLE-FLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISvvEGLE----NLTNleelhienqrlpp 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433  90 -----------------LTYLNLSGNKIKDLstvEALQNLKNLKSLDLFNCEITNLEDyresIFELLQQITYLDGFDQED 152
Cdd:cd21340  105 gekltfdprslaalsnsLRVLNISGNNIDSL---EPLAPLRNLEQLDASNNQISDLEE----LLDLLSSWPSLRELDLTG 177


                 .
gi 530365433 153 N 153
Cdd:cd21340  178 N 178
 
Name Accession Description Interval E-value
LRR_9 pfam14580
Leucine-rich repeat;
34-146 7.76e-11

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 59.78  E-value: 7.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433   34 IEGLNDTFKELEFLSMANVELSSLARLPSLNKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEALQNLK 113
Cdd:pfam14580  34 IENLGATLDQFDTIDFSDNEIRKLDGFPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDPLASLK 113

                          90       100       110
                  ....*....|....*....|....*....|...
gi 530365433  114 NLKSLDLFNCEITNLEDYRESIFELLQQITYLD 146
Cdd:pfam14580 114 KLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLD 146
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
41-128 2.96e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 54.17  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433  41 FKELEFLSMANVELSSL-ARLPSLNKLRKLELSDNIISGGLEVLAeKCPNLTYLNLSGNKIKDLStvEALQNLKNLKSLD 119
Cdd:COG4886  112 LTNLESLDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLPEPLG-NLTNLKSLDLSNNQLTDLP--EELGNLTNLKELD 188


                 ....*....
gi 530365433 120 LFNCEITNL 128
Cdd:COG4886  189 LSNNQITDL 197
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
42-128 3.00e-06

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.01  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433  42 KELEFLSMANVELSSLAR-LPSLNKLRKLELSDNIISGGLEVLAeKCPNLTYLNLSGNKIKDLstvEALQNLKNLKSLDL 120
Cdd:COG4886  182 TNLKELDLSNNQITDLPEpLGNLTNLEELDLSGNQLTDLPEPLA-NLTNLETLDLSNNQLTDL---PELGNLTNLEELDL 257


                 ....*...
gi 530365433 121 FNCEITNL 128
Cdd:COG4886  258 SNNQLTDL 265
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 25-153 4.83e-06

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 46.32  E-value: 4.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433  25 DNCLCvngEIEGLNdTFKELEFLSMANVELSSLARLPSLNKLRKLELSDNIIS--GGLEvlaeKCPN------------- 89
Cdd:cd21340   33 DNKIT---KIENLE-FLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISvvEGLE----NLTNleelhienqrlpp 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433  90 -----------------LTYLNLSGNKIKDLstvEALQNLKNLKSLDLFNCEITNLEDyresIFELLQQITYLDGFDQED 152
Cdd:cd21340  105 gekltfdprslaalsnsLRVLNISGNNIDSL---EPLAPLRNLEQLDASNNQISDLEE----LLDLLSSWPSLRELDLTG 177


                 .
gi 530365433 153 N 153
Cdd:cd21340  178 N 178
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
42-129 6.27e-06

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 47.24  E-value: 6.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433  42 KELEFLSMANVELSSLAR-LPSLNKLRKLELSDNIISGgLEVLAeKCPNLTYLNLSGNKIKDLSTveaLQNLKNLKSLDL 120
Cdd:COG4886  205 TNLEELDLSGNQLTDLPEpLANLTNLETLDLSNNQLTD-LPELG-NLTNLEELDLSNNQLTDLPP---LANLTNLKTLDL 279


                 ....*....
gi 530365433 121 FNCEITNLE 129
Cdd:COG4886  280 SNNQLTDLK 288
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 53-126 2.03e-05

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 44.63  E-value: 2.03e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530365433  53 ELSSLAR-LPSLNKLrKLELSDNIISGGLEVLAEKCPNLTYLNL----SGNKIKDLSTVEALQNLKNLKSLDLFNCEIT 126
Cdd:cd09293   69 GLIALAQsCPNLQVL-DLRACENITDSGIVALATNCPKLQTINLgrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVT 146
LRR_8 pfam13855
Leucine rich repeat;
65-125 1.26e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.04  E-value: 1.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530365433   65 KLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTvEALQNLKNLKSLDLFNCEI 125
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSP-GAFSGLPSLRYLDLSGNRL 61
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
 48-128 1.35e-04

F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from F-box/LRR repeat protein 18 (also known as F-box and leucine-rich repeat protein 18, FBXL18), associated with F-box domains. This protein is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex through its F-box and the LRR motifs mediate the protein-protein interactions required for the binding of the specific substrates by SCFs complexes.


Pssm-ID: 466163 [Multi-domain]  Cd Length: 594  Bit Score: 43.19  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433   48 SMANVELSSLAR-LPSLNKLRKLElsDNIISGGLEVLAEKCPNLTYLNLSG-------NKIKDLSTVeaLQNLKNLKSLD 119
Cdd:pfam19729 261 SLVSLNLSGCVHcLLPDSLLRKAE--DDIDSSIVETLVACCPNLRHLNLSAahhhsseGLGGHLCAL--LARLKHLRSLS 336


                  ....*....
gi 530365433  120 LFNCEITNL 128
Cdd:pfam19729 337 LPVCAVADS 345
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 15-146 1.49e-04

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 42.73  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433  15 SPEEVTELVLDNCLCVNGEIEGLNDTFKE---LEFLSMANVELS-----SLAR-LPSLNKLRKLELSDNII----SGGLE 81
Cdd:cd00116  135 LPPALEKLVLGRNRLEGASCEALAKALRAnrdLKELNLANNGIGdagirALAEgLKANCNLEVLDLNNNGLtdegASALA 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530365433  82 VLAEKCPNLTYLNLSGNKIKDLSTVEALQNLKN----LKSLDLFNCEITNL--EDYRESIFElLQQITYLD 146
Cdd:cd00116  215 ETLASLKSLEVLNLGDNNLTDAGAAALASALLSpnisLLTLSLSCNDITDDgaKDLAEVLAE-KESLLELD 284
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 26-147 2.19e-04

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 41.70  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433  26 NCLCVngeIEGLNDTfKELEFLSMANVELS----------SLARLpsLNKLRKLELSDNIISGgLEVLAeKCPNLTYLNL 95
Cdd:cd21340   78 NRISV---VEGLENL-TNLEELHIENQRLPpgekltfdprSLAAL--SNSLRVLNISGNNIDS-LEPLA-PLRNLEQLDA 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530365433  96 SGNKIKDLSTV-EALQNLKNLKSLDLFNCEITNLEDYRESIFELLQQITYLDG 147
Cdd:cd21340  150 SNNQISDLEELlDLLSSWPSLRELDLTGNPVCKKPKYRDKIILASKSLEVLDG 202
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 88-133 3.64e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 37.61  E-value: 3.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530365433   88 PNLTYLNLSGNKIKDLstvEALQNLKNLKSLDL-FNCEITNLEDYRE 133
Cdd:pfam12799   1 PNLEVLDLSNNQITDI---PPLAKLPNLETLDLsGNNKITDLSDLAN 44
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 65-120 1.84e-03

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 39.39  E-value: 1.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530365433  65 KLRKLELSDNIIS-GGLEVLAEKCPN---LTYLNLSGNKIKD---LSTVEALQNLKNLKSLDL 120
Cdd:COG5238  237 SLTTLDLSNNQIGdEGVIALAEALKNnttVETLYLSGNQIGAegaIALAKALQGNTTLTSLDL 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 66-153 2.81e-03

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 39.00  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433  66 LRKLELSDNIISG-GLEVLAE---KCPNLTYLNLSGNKIKDLSTV---EALQNLKNLKSLDLFNCEITNLEdyRESIFEL 138
Cdd:COG5238  266 VETLYLSGNQIGAeGAIALAKalqGNTTLTSLDLSVNRIGDEGAIalaEGLQGNKTLHTLNLAYNGIGAQG--AIALAKA 343

                         90
                 ....*....|....*
gi 530365433 139 LQQITYLDGFDQEDN 153
Cdd:COG5238  344 LQENTTLHSLDLSDN 358
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 64-146 4.05e-03

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 38.23  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433  64 NKLRKLELSDNIISG-GLEVLAE---KCPNLTYLNLSGNKIKDLSTV---EALQNLKNLKSLDLFNCEITNLEdyRESIF 136
Cdd:COG5238  320 KTLHTLNLAYNGIGAqGAIALAKalqENTTLHSLDLSDNQIGDEGAIalaKYLEGNTTLRELNLGKNNIGKQG--AEALI 397

                         90
                 ....*....|..
gi 530365433 137 ELLQ--QITYLD 146
Cdd:COG5238  398 DALQtnRLHTLI 409
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 47-129 6.18e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 37.07  E-value: 6.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365433  47 LSMANVELSSLARLPSLNKLRKLELSDNIISGgLEVLaEKCPNLTYLNLSGNKIkdlSTVEALQNLKNLKSLDLFNCEIT 126
Cdd:cd21340    7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITK-IENL-EFLTNLTHLYLQNNQI---EKIENLENLVNLKKLYLGGNRIS 81


                 ...
gi 530365433 127 NLE 129
Cdd:cd21340   82 VVE 84
 
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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