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Conserved domains on  [gi|75516947|gb|AAI01523|]
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Leucine rich repeat containing 41 [Homo sapiens]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1006001)

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, ...
599-757 5.49e-04

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: 43.24  E-value: 5.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75516947 599 GAQPAPLLCSILKASGSLQQLSLDSATFASPQDFGLVlQTLKEyNLALKRLSFHDMNLADCQSEVLF--LLQNLTLQEIT 676
Cdd:COG5238 193 GDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILA-EALKG-NKSLTTLDLSNNQIGDEGVIALAeaLKNNTTVETLY 270
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75516947 677 FSfCRLFEKRPAQFLPEMVaamKGNSTLKGLRLPGNRLGNAGLLALADVFSEdsSSSLCQLDISSNCIKPDGLLEFAKRL 756
Cdd:COG5238 271 LS-GNQIGAEGAIALAKAL---QGNTTLTSLDLSVNRIGDEGAIALAEGLQG--NKTLHTLNLAYNGIGAQGAIALAKAL 344

                .
gi 75516947 757 E 757
Cdd:COG5238 345 Q 345
 
Name Accession Description Interval E-value
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
599-757 5.49e-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: 43.24  E-value: 5.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75516947 599 GAQPAPLLCSILKASGSLQQLSLDSATFASPQDFGLVlQTLKEyNLALKRLSFHDMNLADCQSEVLF--LLQNLTLQEIT 676
Cdd:COG5238 193 GDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILA-EALKG-NKSLTTLDLSNNQIGDEGVIALAeaLKNNTTVETLY 270
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75516947 677 FSfCRLFEKRPAQFLPEMVaamKGNSTLKGLRLPGNRLGNAGLLALADVFSEdsSSSLCQLDISSNCIKPDGLLEFAKRL 756
Cdd:COG5238 271 LS-GNQIGAEGAIALAKAL---QGNTTLTSLDLSVNRIGDEGAIALAEGLQG--NKTLHTLNLAYNGIGAQGAIALAKAL 344

                .
gi 75516947 757 E 757
Cdd:COG5238 345 Q 345
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
442-757 4.12e-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: 40.03  E-value: 4.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75516947 442 GSDPSCLGLpALEASQRFRSISTLELFTVPLSTEAALTLCHLLSSWvSLESLTLSYNGLGSNIFRLL-DSLRALSgqagC 520
Cdd:cd00116  64 GRIPRGLQS-LLQGLTKGCGLQELDLSDNALGPDGCGVLESLLRSS-SLQELKLNNNGLGDRGLRLLaKGLKDLP----P 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75516947 521 RLRALHLSD--LFSplpilELTRAIVRALPLLRVLsirvdhpsqrdnpgvpgnagppsHIIgdeEIPENCLeqlemgfpr 598
Cdd:cd00116 138 ALEKLVLGRnrLEG-----ASCEALAKALRANRDL-----------------------KEL---NLANNGI--------- 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75516947 599 GAQPAPLLCSILKASGSLQQLSLDSATFaspQDFGLVLqtlkeynlalkrlsfhdmnLADCqsevlfLLQNLTLQEITFS 678
Cdd:cd00116 178 GDAGIRALAEGLKANCNLEVLDLNNNGL---TDEGASA-------------------LAET------LASLKSLEVLNLG 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75516947 679 FCRLFEKRPAQFLPEMvaaMKGNSTLKGLRLPGNRLGNAGLLALADVFSEdsSSSLCQLDISSNCIKPDGLLEFAKRLE 757
Cdd:cd00116 230 DNNLTDAGAAALASAL---LSPNISLLTLSLSCNDITDDGAKDLAEVLAE--KESLLELDLRGNKFGEEGAQLLAESLL 303
 
Name Accession Description Interval E-value
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
599-757 5.49e-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: 43.24  E-value: 5.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75516947 599 GAQPAPLLCSILKASGSLQQLSLDSATFASPQDFGLVlQTLKEyNLALKRLSFHDMNLADCQSEVLF--LLQNLTLQEIT 676
Cdd:COG5238 193 GDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILA-EALKG-NKSLTTLDLSNNQIGDEGVIALAeaLKNNTTVETLY 270
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75516947 677 FSfCRLFEKRPAQFLPEMVaamKGNSTLKGLRLPGNRLGNAGLLALADVFSEdsSSSLCQLDISSNCIKPDGLLEFAKRL 756
Cdd:COG5238 271 LS-GNQIGAEGAIALAKAL---QGNTTLTSLDLSVNRIGDEGAIALAEGLQG--NKTLHTLNLAYNGIGAQGAIALAKAL 344

                .
gi 75516947 757 E 757
Cdd:COG5238 345 Q 345
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
442-757 4.12e-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: 40.03  E-value: 4.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75516947 442 GSDPSCLGLpALEASQRFRSISTLELFTVPLSTEAALTLCHLLSSWvSLESLTLSYNGLGSNIFRLL-DSLRALSgqagC 520
Cdd:cd00116  64 GRIPRGLQS-LLQGLTKGCGLQELDLSDNALGPDGCGVLESLLRSS-SLQELKLNNNGLGDRGLRLLaKGLKDLP----P 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75516947 521 RLRALHLSD--LFSplpilELTRAIVRALPLLRVLsirvdhpsqrdnpgvpgnagppsHIIgdeEIPENCLeqlemgfpr 598
Cdd:cd00116 138 ALEKLVLGRnrLEG-----ASCEALAKALRANRDL-----------------------KEL---NLANNGI--------- 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75516947 599 GAQPAPLLCSILKASGSLQQLSLDSATFaspQDFGLVLqtlkeynlalkrlsfhdmnLADCqsevlfLLQNLTLQEITFS 678
Cdd:cd00116 178 GDAGIRALAEGLKANCNLEVLDLNNNGL---TDEGASA-------------------LAET------LASLKSLEVLNLG 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75516947 679 FCRLFEKRPAQFLPEMvaaMKGNSTLKGLRLPGNRLGNAGLLALADVFSEdsSSSLCQLDISSNCIKPDGLLEFAKRLE 757
Cdd:cd00116 230 DNNLTDAGAAALASAL---LSPNISLLTLSLSCNDITDDGAKDLAEVLAE--KESLLELDLRGNKFGEEGAQLLAESLL 303
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
666-757 5.61e-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: 40.16  E-value: 5.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75516947 666 LLQNLTLQEITFSFCRLFEKRpAQFLpemVAAMKGNSTLKGLRLPGNRLGNAGLLALADvfSEDSSSSLCQLDISSNCIK 745
Cdd:COG5238 316 LQGNKTLHTLNLAYNGIGAQG-AIAL---AKALQENTTLHSLDLSDNQIGDEGAIALAK--YLEGNTTLRELNLGKNNIG 389
                        90
                ....*....|..
gi 75516947 746 PDGLLEFAKRLE 757
Cdd:COG5238 390 KQGAEALIDALQ 401
 
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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