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Conserved domains on  [gi|18390607|ref|NP_563758|]
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LisH and RanBPM domains containing protein [Arabidopsis thaliana]

Protein Classification

CLTH domain-containing protein( domain architecture ID 12107814)

CLTH domain-containing protein similar to Saccharomyces cerevisiae glucose-induced degradation protein 8 (GID8) and GID9

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 52-193 1.14e-35

CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif.


:

Pssm-ID: 402305 [Multi-domain]  Cd Length: 143  Bit Score: 122.68  E-value: 1.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390607    52 MERRKQIIHFILERKALKAFELTEQLAQDLLEKNKDLQFDLLCLHFVELICAGNCTEALKFGKTRLAPFGkvKKYVEKLE 131
Cdd:pfam10607   2 FKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGKILEALEYARENLAPFN--EEHLKELE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18390607   132 DVMALLAYEDPEK-SPMFHLLSSEYRQQVADNLNRTILEHTNHPSYTPMERIIQQVTVVRQYL 193
Cdd:pfam10607  80 KLMGLLAFPDPTDsSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTL 142
 
Name Accession Description Interval E-value
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 52-193 1.14e-35

CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif.


Pssm-ID: 402305 [Multi-domain]  Cd Length: 143  Bit Score: 122.68  E-value: 1.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390607    52 MERRKQIIHFILERKALKAFELTEQLAQDLLEKNKDLQFDLLCLHFVELICAGNCTEALKFGKTRLAPFGkvKKYVEKLE 131
Cdd:pfam10607   2 FKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGKILEALEYARENLAPFN--EEHLKELE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18390607   132 DVMALLAYEDPEK-SPMFHLLSSEYRQQVADNLNRTILEHTNHPSYTPMERIIQQVTVVRQYL 193
Cdd:pfam10607  80 KLMGLLAFPDPTDsSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTL 142
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 104-199 2.93e-24

CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi)


Pssm-ID: 214806  Cd Length: 99  Bit Score: 91.97  E-value: 2.93e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390607    104 GNCTEALKFGKTRLAPFGKVKKYVEK-LEDVMALLAYEDP-EKSPMFHLLSSEYRQQVADNLNRTILE-HTNHPSYTPME 180
Cdd:smart00757   1 GKIEEALAYARELLAPFAKEHEKFLKeLEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILElLHGKSSESPLE 80

                           90
                   ....*....|....*....
gi 18390607    181 RIIQQVTVVRQYLTEENGK 199
Cdd:smart00757  81 ILLSAGLAALKTLLEKGGV 99
 
Name Accession Description Interval E-value
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 52-193 1.14e-35

CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif.


Pssm-ID: 402305 [Multi-domain]  Cd Length: 143  Bit Score: 122.68  E-value: 1.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390607    52 MERRKQIIHFILERKALKAFELTEQLAQDLLEKNKDLQFDLLCLHFVELICAGNCTEALKFGKTRLAPFGkvKKYVEKLE 131
Cdd:pfam10607   2 FKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGKILEALEYARENLAPFN--EEHLKELE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18390607   132 DVMALLAYEDPEK-SPMFHLLSSEYRQQVADNLNRTILEHTNHPSYTPMERIIQQVTVVRQYL 193
Cdd:pfam10607  80 KLMGLLAFPDPTDsSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSALKTL 142
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 104-199 2.93e-24

CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi)


Pssm-ID: 214806  Cd Length: 99  Bit Score: 91.97  E-value: 2.93e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390607    104 GNCTEALKFGKTRLAPFGKVKKYVEK-LEDVMALLAYEDP-EKSPMFHLLSSEYRQQVADNLNRTILE-HTNHPSYTPME 180
Cdd:smart00757   1 GKIEEALAYARELLAPFAKEHEKFLKeLEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILElLHGKSSESPLE 80

                           90
                   ....*....|....*....
gi 18390607    181 RIIQQVTVVRQYLTEENGK 199
Cdd:smart00757  81 ILLSAGLAALKTLLEKGGV 99
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 52-108 4.62e-10

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 53.34  E-value: 4.62e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18390607     52 MERRKQIIHFILERKALKAFELTEQLAQDLLEKNKDLQFDLLCLHFVELICAGNCTE 108
Cdd:smart00668   2 FDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLEE 58
 
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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