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Conserved domains on  [gi|922581092|ref|NP_001300116|]
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CTLH domain-containing protein [Caenorhabditis elegans]

Protein Classification

LisH and CLTH domain-containing protein( domain architecture ID 12218104)

LisH and CLTH domain-containing protein such as Gid8 (glucose-induced degradation protein 8 homolog) which is a key nuclear retention factor for beta-catenin during Wnt signaling and colorectal tumorigenesis

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 ...
 46-179 8.75e-27

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: 100.34  E-value: 8.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581092   46 MNARNEVRRLICVGEMESAIEKMTTLCPTILE-DDEINFIVRKQHLIEMVRQKLTKEPVEYFRAHLMKNGqrpcDEKMDI 124
Cdd:pfam10607   2 FKERNRILEAILNGDITEAIEWCNENKPELLKiNSNLEFELRLQQFIELIRSGKILEALEYARENLAPFN----EEHLKE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 922581092  125 IERIFTMLVF-NLEDDVEFNVYFQQSEREQTAKEVNSALLAMNGKLKSSRLDLLAK 179
Cdd:pfam10607  78 LEKLMGLLAFpDPTDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLK 133
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 5-38 6.54e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


:

Pssm-ID: 128913  Cd Length: 34  Bit Score: 38.95  E-value: 6.54e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 922581092     5 PTREELQQLVIDHFLHHGYSEVIETFSKEVNIVV 38
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
 
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 ...
 46-179 8.75e-27

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: 100.34  E-value: 8.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581092   46 MNARNEVRRLICVGEMESAIEKMTTLCPTILE-DDEINFIVRKQHLIEMVRQKLTKEPVEYFRAHLMKNGqrpcDEKMDI 124
Cdd:pfam10607   2 FKERNRILEAILNGDITEAIEWCNENKPELLKiNSNLEFELRLQQFIELIRSGKILEALEYARENLAPFN----EEHLKE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 922581092  125 IERIFTMLVF-NLEDDVEFNVYFQQSEREQTAKEVNSALLAMNGKLKSSRLDLLAK 179
Cdd:pfam10607  78 LEKLMGLLAFpDPTDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLK 133
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 97-177 6.44e-12

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 60.00  E-value: 6.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581092    97 KLTKEPVEYFRAHLMKNGQRPCDEkMDIIERIFTMLVFNLE-DDVEFNVYFQQSEREQTAKEVNSALLAM-NGKLKSSRL 174
Cdd:smart00757   1 GKIEEALAYARELLAPFAKEHEKF-LKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELlHGKSSESPL 79


                   ...
gi 922581092   175 DLL 177
Cdd:smart00757  80 EIL 82
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 5-38 6.54e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 38.95  E-value: 6.54e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 922581092     5 PTREELQQLVIDHFLHHGYSEVIETFSKEVNIVV 38
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
 
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 ...
 46-179 8.75e-27

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: 100.34  E-value: 8.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581092   46 MNARNEVRRLICVGEMESAIEKMTTLCPTILE-DDEINFIVRKQHLIEMVRQKLTKEPVEYFRAHLMKNGqrpcDEKMDI 124
Cdd:pfam10607   2 FKERNRILEAILNGDITEAIEWCNENKPELLKiNSNLEFELRLQQFIELIRSGKILEALEYARENLAPFN----EEHLKE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 922581092  125 IERIFTMLVF-NLEDDVEFNVYFQQSEREQTAKEVNSALLAMNGKLKSSRLDLLAK 179
Cdd:pfam10607  78 LEKLMGLLAFpDPTDSSPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLK 133
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 97-177 6.44e-12

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 60.00  E-value: 6.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581092    97 KLTKEPVEYFRAHLMKNGQRPCDEkMDIIERIFTMLVFNLE-DDVEFNVYFQQSEREQTAKEVNSALLAM-NGKLKSSRL 174
Cdd:smart00757   1 GKIEEALAYARELLAPFAKEHEKF-LKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELlHGKSSESPL 79


                   ...
gi 922581092   175 DLL 177
Cdd:smart00757  80 EIL 82
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 49-101 8.35e-10

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 52.96  E-value: 8.35e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 922581092    49 RNEVRRLICVGEMESAIEKMTTLCPTILEDD-EINFIVRKQHLIEMVRQKLTKE 101
Cdd:smart00668   5 RKRIRELILKGDWDEALEWLSSLKPPLLERNsKLEFELRKQKFLELVRQGKLEE 58
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 5-38 6.54e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 38.95  E-value: 6.54e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 922581092     5 PTREELQQLVIDHFLHHGYSEVIETFSKEVNIVV 38
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
 
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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