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Conserved domains on  [gi|30048125|gb|AAH50527|]
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NLRC5 protein, partial [Homo sapiens]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1908381)

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

CATH:  3.80.10.10
Gene Ontology:  GO:0005515
SCOP:  4003523

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
7-99 3.90e-07

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


The actual alignment was detected with superfamily member COG5238:

Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 51.71  E-value: 3.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125   7 RRMRLTHCGLQEKHLEQLCKALGGSCHLGHLHLdfSGNALGDEGAARLAQLLPGLGALQSLNLSENGLSLDAVLGLVRCF 86
Cdd:COG5238 267 ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDL--SVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKAL 344
                        90
                ....*....|...
gi 30048125  87 STLQWLFRLDISF 99
Cdd:COG5238 345 QENTTLHSLDLSD 357
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
39-366 9.28e-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.


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 37.72  E-value: 9.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125  39 LDFSGNALGDEGAArlaQLLPGLGALQSLNLSENGLSLDAVLGLVRcfstlqwlfRLDISFESQHILLRGDKTSRDMWAT 118
Cdd:cd00116   3 LSLKGELLKTERAT---ELLPKLLCLQVLRLEGNTLGEEAAKALAS---------ALRPQPSLKELCLSLNETGRIPRGL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125 119 GSLPDfpaaakflGFRQRCIPRSLCLSECPLEPPSLTRLCATLKDCPGPlELQLSCEFLSDQSL----ETLLDCLPQLPQ 194
Cdd:cd00116  71 QSLLQ--------GLTKGCGLQELDLSDNALGPDGCGVLESLLRSSSLQ-ELKLNNNGLGDRGLrllaKGLKDLPPALEK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125 195 LSLLQLSQTGLSPKSpflLANTLSLCPRVKKVDLR--SLHHATLH-----FRSNEEEEGVccGLSANLLGDSGLRCLLEC 267
Cdd:cd00116 142 LVLGRNRLEGASCEA---LAKALRANRDLKELNLAnnGIGDAGIRalaegLKANCNLEVL--DLNNNGLTDEGASALAET 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125 268 LPQVPISGLLDLSHNSISQESALYLLETLPScprvreasvnlgseqsfrihfsrEDQAGKTLRLSECSFRPEHVSRLATG 347
Cdd:cd00116 217 LASLKSLEVLNLGDNNLTDAGAAALASALLS-----------------------PNISLLTLSLSCNDITDDGAKDLAEV 273
                       330
                ....*....|....*....
gi 30048125 348 LSKSLQLTELTLTQCCLGQ 366
Cdd:cd00116 274 LAEKESLLELDLRGNKFGE 292
 
Name Accession Description Interval E-value
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
7-99 3.90e-07

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: 51.71  E-value: 3.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125   7 RRMRLTHCGLQEKHLEQLCKALGGSCHLGHLHLdfSGNALGDEGAARLAQLLPGLGALQSLNLSENGLSLDAVLGLVRCF 86
Cdd:COG5238 267 ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDL--SVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKAL 344
                        90
                ....*....|...
gi 30048125  87 STLQWLFRLDISF 99
Cdd:COG5238 345 QENTTLHSLDLSD 357
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
1-98 2.89e-05

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: 45.42  E-value: 2.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125   1 ELPLSSRRMRLTHCGLQEKHLEQLCKALGgscHLGHLH-LDFSGNALGDEGAARLAQLLPGLGALQSLNLSENGLSLDAV 79
Cdd:cd00116 134 DLPPALEKLVLGRNRLEGASCEALAKALR---ANRDLKeLNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGA 210
                        90
                ....*....|....*....
gi 30048125  80 LGLVRCFSTLQWLFRLDIS 98
Cdd:cd00116 211 SALAETLASLKSLEVLNLG 229
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
39-366 9.28e-03

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: 37.72  E-value: 9.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125  39 LDFSGNALGDEGAArlaQLLPGLGALQSLNLSENGLSLDAVLGLVRcfstlqwlfRLDISFESQHILLRGDKTSRDMWAT 118
Cdd:cd00116   3 LSLKGELLKTERAT---ELLPKLLCLQVLRLEGNTLGEEAAKALAS---------ALRPQPSLKELCLSLNETGRIPRGL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125 119 GSLPDfpaaakflGFRQRCIPRSLCLSECPLEPPSLTRLCATLKDCPGPlELQLSCEFLSDQSL----ETLLDCLPQLPQ 194
Cdd:cd00116  71 QSLLQ--------GLTKGCGLQELDLSDNALGPDGCGVLESLLRSSSLQ-ELKLNNNGLGDRGLrllaKGLKDLPPALEK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125 195 LSLLQLSQTGLSPKSpflLANTLSLCPRVKKVDLR--SLHHATLH-----FRSNEEEEGVccGLSANLLGDSGLRCLLEC 267
Cdd:cd00116 142 LVLGRNRLEGASCEA---LAKALRANRDLKELNLAnnGIGDAGIRalaegLKANCNLEVL--DLNNNGLTDEGASALAET 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125 268 LPQVPISGLLDLSHNSISQESALYLLETLPScprvreasvnlgseqsfrihfsrEDQAGKTLRLSECSFRPEHVSRLATG 347
Cdd:cd00116 217 LASLKSLEVLNLGDNNLTDAGAAALASALLS-----------------------PNISLLTLSLSCNDITDDGAKDLAEV 273
                       330
                ....*....|....*....
gi 30048125 348 LSKSLQLTELTLTQCCLGQ 366
Cdd:cd00116 274 LAEKESLLELDLRGNKFGE 292
 
Name Accession Description Interval E-value
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
7-99 3.90e-07

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: 51.71  E-value: 3.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125   7 RRMRLTHCGLQEKHLEQLCKALGGSCHLGHLHLdfSGNALGDEGAARLAQLLPGLGALQSLNLSENGLSLDAVLGLVRCF 86
Cdd:COG5238 267 ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDL--SVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKAL 344
                        90
                ....*....|...
gi 30048125  87 STLQWLFRLDISF 99
Cdd:COG5238 345 QENTTLHSLDLSD 357
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
1-98 2.89e-05

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: 45.42  E-value: 2.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125   1 ELPLSSRRMRLTHCGLQEKHLEQLCKALGgscHLGHLH-LDFSGNALGDEGAARLAQLLPGLGALQSLNLSENGLSLDAV 79
Cdd:cd00116 134 DLPPALEKLVLGRNRLEGASCEALAKALR---ANRDLKeLNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGA 210
                        90
                ....*....|....*....
gi 30048125  80 LGLVRCFSTLQWLFRLDIS 98
Cdd:cd00116 211 SALAETLASLKSLEVLNLG 229
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
11-82 4.05e-05

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: 45.55  E-value: 4.05e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30048125  11 LTHCGLQEKHLEQLCKALGGSCHLGHLHLdfSGNALGDEGAARLAQLLPGLGALQSLNLSENGLSLDAVLGL 82
Cdd:COG5238 327 LAYNGIGAQGAIALAKALQENTTLHSLDL--SDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEAL 396
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
16-82 2.82e-04

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: 42.85  E-value: 2.82e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30048125  16 LQEKHLEQLCKALGGSCHLGHLHLdfSGNALGDEGAARLAQLLPGLGALQSLNLSENGLSLDAVLGL 82
Cdd:COG5238 192 IGDEGIEELAEALTQNTTVTTLWL--KRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIAL 256
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
9-98 9.50e-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: 40.80  E-value: 9.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125   9 MRLTHCGLQEKHLEQLCKALGG-SCHLGHLHLdfSGNALGDEGAARLAQLLPGLGALQSLNLSENGLSLDAVLGLVRCFS 87
Cdd:cd00116 113 LKLNNNGLGDRGLRLLAKGLKDlPPALEKLVL--GRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLK 190
                        90
                ....*....|.
gi 30048125  88 TLQWLFRLDIS 98
Cdd:cd00116 191 ANCNLEVLDLN 201
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
15-99 5.22e-03

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: 38.49  E-value: 5.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125  15 GLQEKHLEQLCKALGGSCHLGHLHLDfsGNALGDEGAARLAQLLPGLGALQSLNLSENGLSLDAVLGLVRCF-STLQWLF 93
Cdd:cd00116 176 GIGDAGIRALAEGLKANCNLEVLDLN--NNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALlSPNISLL 253

                ....*.
gi 30048125  94 RLDISF 99
Cdd:cd00116 254 TLSLSC 259
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
39-366 9.28e-03

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: 37.72  E-value: 9.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125  39 LDFSGNALGDEGAArlaQLLPGLGALQSLNLSENGLSLDAVLGLVRcfstlqwlfRLDISFESQHILLRGDKTSRDMWAT 118
Cdd:cd00116   3 LSLKGELLKTERAT---ELLPKLLCLQVLRLEGNTLGEEAAKALAS---------ALRPQPSLKELCLSLNETGRIPRGL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125 119 GSLPDfpaaakflGFRQRCIPRSLCLSECPLEPPSLTRLCATLKDCPGPlELQLSCEFLSDQSL----ETLLDCLPQLPQ 194
Cdd:cd00116  71 QSLLQ--------GLTKGCGLQELDLSDNALGPDGCGVLESLLRSSSLQ-ELKLNNNGLGDRGLrllaKGLKDLPPALEK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125 195 LSLLQLSQTGLSPKSpflLANTLSLCPRVKKVDLR--SLHHATLH-----FRSNEEEEGVccGLSANLLGDSGLRCLLEC 267
Cdd:cd00116 142 LVLGRNRLEGASCEA---LAKALRANRDLKELNLAnnGIGDAGIRalaegLKANCNLEVL--DLNNNGLTDEGASALAET 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30048125 268 LPQVPISGLLDLSHNSISQESALYLLETLPScprvreasvnlgseqsfrihfsrEDQAGKTLRLSECSFRPEHVSRLATG 347
Cdd:cd00116 217 LASLKSLEVLNLGDNNLTDAGAAALASALLS-----------------------PNISLLTLSLSCNDITDDGAKDLAEV 273
                       330
                ....*....|....*....
gi 30048125 348 LSKSLQLTELTLTQCCLGQ 366
Cdd:cd00116 274 LAEKESLLELDLRGNKFGE 292
 
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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