NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720367614|ref|XP_030102222|]
View 

F-box/LRR-repeat protein 20 isoform X3 [Mus musculus]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1563018)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 62-236 1.90e-28

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.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 108.57  E-value: 1.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614  62 CPELVTLNLQTCLQITDEGLITICrgCHKLQSLCASGCSNITDAILNALGQNCPRLRILEVARCSQLTDVGFTTLARNCH 141
Cdd:cd09293    27 HSGLEWLELYMCPISDPPLDQLSN--CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614 142 ELEKMDL---EECVQITDSTLIQLSIHCPRLQVLSLSHCElITDDGIRHLGNGaCAHdQLEVIELDNCPLITDASLEHLK 218
Cdd:cd09293   105 KLQTINLgrhRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASG-CSK-SLERLSLNNCRNLTDQSIPAIL 181

                         170       180
                  ....*....|....*....|.
gi 1720367614 219 SCHSLERI---ELYDCQQITR 236
Cdd:cd09293   182 ASNYFPNLsvlEFRGCPLITD 202
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 62-236 1.90e-28

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: 108.57  E-value: 1.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614  62 CPELVTLNLQTCLQITDEGLITICrgCHKLQSLCASGCSNITDAILNALGQNCPRLRILEVARCSQLTDVGFTTLARNCH 141
Cdd:cd09293    27 HSGLEWLELYMCPISDPPLDQLSN--CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614 142 ELEKMDL---EECVQITDSTLIQLSIHCPRLQVLSLSHCElITDDGIRHLGNGaCAHdQLEVIELDNCPLITDASLEHLK 218
Cdd:cd09293   105 KLQTINLgrhRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASG-CSK-SLERLSLNNCRNLTDQSIPAIL 181

                         170       180
                  ....*....|....*....|.
gi 1720367614 219 SCHSLERI---ELYDCQQITR 236
Cdd:cd09293   182 ASNYFPNLsvlEFRGCPLITD 202
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
12-232 4.93e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 53.40  E-value: 4.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614  12 LLEQLNISWCDQVTKDGIQALVRGCGGLKALFLKGCTQLedealkyigAHCPELVTLNLQTClQITDegLITICRGCHKL 91
Cdd:COG4886    71 LLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGN-QLTD--LPEELANLTNL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614  92 QSLCASGCsNITDaILNALGqNCPRLRILEVARCsQLTDVGFTtlARNCHELEKMDLEECvQITDstlIQLSI-HCPRLQ 170
Cdd:COG4886   139 KELDLSNN-QLTD-LPEPLG-NLTNLKSLDLSNN-QLTDLPEE--LGNLTNLKELDLSNN-QITD---LPEPLgNLTNLE 208

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720367614 171 VLSLSHCELIT-DDGIRHLGNgacahdqLEVIELDNCPLitdASLEHLKSCHSLERIELYDCQ 232
Cdd:COG4886   209 ELDLSGNQLTDlPEPLANLTN-------LETLDLSNNQL---TDLPELGNLTNLEELDLSNNQ 261
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
166-191 8.01e-04

Leucine-rich repeat - CC (cysteine-containing) subfamily;


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 35.84  E-value: 8.01e-04
                           10        20
                   ....*....|....*....|....*.
gi 1720367614  166 CPRLQVLSLSHCELITDDGIRHLGNG 191
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
 
Name Accession Description Interval E-value
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 62-236 1.90e-28

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: 108.57  E-value: 1.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614  62 CPELVTLNLQTCLQITDEGLITICrgCHKLQSLCASGCSNITDAILNALGQNCPRLRILEVARCSQLTDVGFTTLARNCH 141
Cdd:cd09293    27 HSGLEWLELYMCPISDPPLDQLSN--CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614 142 ELEKMDL---EECVQITDSTLIQLSIHCPRLQVLSLSHCElITDDGIRHLGNGaCAHdQLEVIELDNCPLITDASLEHLK 218
Cdd:cd09293   105 KLQTINLgrhRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASG-CSK-SLERLSLNNCRNLTDQSIPAIL 181

                         170       180
                  ....*....|....*....|.
gi 1720367614 219 SCHSLERI---ELYDCQQITR 236
Cdd:cd09293   182 ASNYFPNLsvlEFRGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 23-213 1.02e-27

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: 106.64  E-value: 1.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614  23 QVTKDGIQALVRG-CGGLKALFLKGCTQLeDEALKYIGaHCPELVTLNLQTCLQITDEGLITICRGCHKLQSLCASGCSN 101
Cdd:cd09293    13 QITQSNISQLLRIlHSGLEWLELYMCPIS-DPPLDQLS-NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACEN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614 102 ITDAILNALGQNCPRLRILEVAR---CSQLTDVGFTTLARNCHELEKMDLEECvQITDSTLIQL-SIHCPRLQVLSLSHC 177
Cdd:cd09293    91 ITDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELaSGCSKSLERLSLNNC 169

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720367614 178 ELITDDGIRH-LGNGACAHdqLEVIELDNCPLITDAS 213
Cdd:cd09293   170 RNLTDQSIPAiLASNYFPN--LSVLEFRGCPLITDFS 204
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 13-182 4.21e-23

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: 94.32  E-value: 4.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614  13 LEQLNISWCDQVTKDGIQALVRGCGGLKALFLKGCTQLEDEALKYIGAHCPELVTLNLqtclqitdegliticrGCHKlq 92
Cdd:cd09293    54 LKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINL----------------GRHR-- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614  93 slcasGCSNITDAILNALGQNCPRLRILEVARCsQLTDVGFTTLARNC-HELEKMDLEECVQITDS--TLIQLSIHCPRL 169
Cdd:cd09293   116 -----NGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCsKSLERLSLNNCRNLTDQsiPAILASNYFPNL 189

                         170
                  ....*....|...
gi 1720367614 170 QVLSLSHCELITD 182
Cdd:cd09293   190 SVLEFRGCPLITD 202
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 3-131 5.11e-19

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: 83.15  E-value: 5.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614   3 LKALSEGCPLLEQLNISWCDQVTKDGIQALVRGCGGLKALFL---KGCTQLEDEALKYIGAHCPELVTLNLQTClQITDE 79
Cdd:cd09293    70 LIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDK 148

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720367614  80 GLITICRGC-HKLQSLCASGCSNITDAILNAL--GQNCPRLRILEVARCSQLTDV 131
Cdd:cd09293   149 GVWELASGCsKSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFRGCPLITDF 203
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
12-232 4.93e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 53.40  E-value: 4.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614  12 LLEQLNISWCDQVTKDGIQALVRGCGGLKALFLKGCTQLedealkyigAHCPELVTLNLQTClQITDegLITICRGCHKL 91
Cdd:COG4886    71 LLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEEL---------SNLTNLESLDLSGN-QLTD--LPEELANLTNL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614  92 QSLCASGCsNITDaILNALGqNCPRLRILEVARCsQLTDVGFTtlARNCHELEKMDLEECvQITDstlIQLSI-HCPRLQ 170
Cdd:COG4886   139 KELDLSNN-QLTD-LPEPLG-NLTNLKSLDLSNN-QLTDLPEE--LGNLTNLKELDLSNN-QITD---LPEPLgNLTNLE 208

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720367614 171 VLSLSHCELIT-DDGIRHLGNgacahdqLEVIELDNCPLitdASLEHLKSCHSLERIELYDCQ 232
Cdd:COG4886   209 ELDLSGNQLTDlPEPLANLTN-------LETLDLSNNQL---TDLPELGNLTNLEELDLSNNQ 261
FBXL3_LRR-like cd23951
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
 13-183 1.87e-05

Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part of Skp1-Cul1-F-box-protein (SCF) ubiquitin ligase complexes. They contain an F-Box, which binds to the core complex component SKP and a leucine-rich repeat (LRR) domain which gives substrate binding specificity. FBXL3 (F-box and leucine rich repeat protein 3) and FBXL21 have been shown to bind CRY1 repressors and are involved in regulation of circadian clock.


Pssm-ID: 467830 [Multi-domain]  Cd Length: 349  Bit Score: 45.45  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614  13 LEQLNISWCDQVTKDGIQALVRGCGGLKALFLKgCTQLEDE-----------ALKY--IGAHCPELVTLNLQTCLQITDE 79
Cdd:cd23951   122 LELLKMKSCPRVSPRGILAVADHCQHLRELSLN-YHLLSDDlllalsseehvRLEHlrIDVVSENDGPMPLHQISKESWD 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614  80 GLITicrgcH----------------KLQSLCAS---------GCSnITDAILNALGQNCPRLRILEVARCS-QLTDVGF 133
Cdd:cd23951   201 ALIK-----HspdvnlvmyffvledeDFDPFFRSytpvthlyfGRS-VPKAVLGRVGQHCPRLVELVVCANGnSPIDEEL 274

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720367614 134 TTLARNCHELEKMDLEECvQITDSTLIQLSIHC-PRLQVLSLSHCELITDD 183
Cdd:cd23951   275 IRIAKNCKQLSSLGLGEC-EVSCSALVEFAKLCgPRLTELYVMEEVLVEDE 324
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 39-247 2.17e-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: 41.96  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614  39 LKALFLKGCTqLEDEALKYIG---AHCPELVTLNLQT--------CLQITDEGLITICrgchKLQSLCASGCSNITD--A 105
Cdd:cd00116    25 LQVLRLEGNT-LGEEAAKALAsalRPQPSLKELCLSLnetgriprGLQSLLQGLTKGC----GLQELDLSDNALGPDgcG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614 106 ILNALGQNcPRLRILEVARCSqLTDVGFTTLAR----NCHELEKMDLEECvQITDSTLIQLS---IHCPRLQVLSLSHCE 178
Cdd:cd00116   100 VLESLLRS-SSLQELKLNNNG-LGDRGLRLLAKglkdLPPALEKLVLGRN-RLEGASCEALAkalRANRDLKELNLANNG 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720367614 179 lITDDGIRHLGNGACAHDQLEVIELDNCPL--ITDASLEH-LKSCHSLERIELYDCqQITRAGIKRLRTHLP 247
Cdd:cd00116   177 -IGDAGIRALAEGLKANCNLEVLDLNNNGLtdEGASALAEtLASLKSLEVLNLGDN-NLTDAGAAALASALL 246
FBXL3_LRR cd23957
Leucine-rich repeat domain of F-box/LRR-repeat protein 3; FBXL3 (F-box/LRR-repeat protein 3), ...
 102-183 7.17e-04

Leucine-rich repeat domain of F-box/LRR-repeat protein 3; FBXL3 (F-box/LRR-repeat protein 3), together with SKP1 (S-phase-kinase-associated protein-1) and cullin subunit CUL1, forms a Skp1-Cul1-F-box-protein (SCF) ubiquitin ligase complex that ubiquitinates CRY repressor proteins and mediates their degradation. FBXL21 also ubiquitinates the cryptochromes (CRYs) but counteracts FBXL3. This plays an important role in regulating oscillation of the circadian clock.


Pssm-ID: 467832 [Multi-domain]  Cd Length: 350  Bit Score: 40.42  E-value: 7.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367614 102 ITDAILNALGQNCPRLriLEVARCS---QLTDVGFTTLARNCHELEKMDLEECvQITDSTLIQLSIHC-PRLQVLSLSHC 177
Cdd:cd23957   241 VSKEVLGRVGMNCPRL--VELVVCAnglRPLDEELIRIAERCKNLTAIGLGEC-EVSCSAFVEFVKMCgGRLSQLSIMEE 317


                  ....*.
gi 1720367614 178 ELITDD 183
Cdd:cd23957   318 VLIPDQ 323
LRR_CC smart00367
Leucine-rich repeat - CC (cysteine-containing) subfamily;
166-191 8.01e-04

Leucine-rich repeat - CC (cysteine-containing) subfamily;


Pssm-ID: 197685 [Multi-domain]  Cd Length: 26  Bit Score: 35.84  E-value: 8.01e-04
                           10        20
                   ....*....|....*....|....*.
gi 1720367614  166 CPRLQVLSLSHCELITDDGIRHLGNG 191
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH