NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|578829102|ref|XP_006721301|]
View 

ran-binding protein 10 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 381-478 2.78e-15

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


:

Pssm-ID: 214806  Cd Length: 99  Bit Score: 71.56  E-value: 2.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829102   381 ATERIILFGRELQAlseQLGREYGKNLahtEMLQDAFSLLAYSDP-WSCPVGQQLDPIQREPVCAALNSAILESQ-NLPK 458
Cdd:smart00757   2 KIEEALAYARELLA---PFAKEHEKFL---KELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLhGKSS 75

                           90       100
                   ....*....|....*....|
gi 578829102   459 QPPLMLALGQASECLRLMAR 478
Cdd:smart00757  76 ESPLEILLSAGLAALKTLLE 95
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 135-191 1.91e-13

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


:

Pssm-ID: 128914  Cd Length: 58  Bit Score: 64.90  E-value: 1.91e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829102   135 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTDSE 191
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 103-123 5.32e-03

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


:

Pssm-ID: 462501  Cd Length: 25  Bit Score: 34.21  E-value: 5.32e-03
                          10        20
                  ....*....|....*....|.
gi 578829102  103 SMVSSYLVHHGYCATATAFAR 123
Cdd:pfam08513   4 RLIYDYLVKEGYEETAEAFEK 24
 
Name Accession Description Interval E-value
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 381-478 2.78e-15

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 71.56  E-value: 2.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829102   381 ATERIILFGRELQAlseQLGREYGKNLahtEMLQDAFSLLAYSDP-WSCPVGQQLDPIQREPVCAALNSAILESQ-NLPK 458
Cdd:smart00757   2 KIEEALAYARELLA---PFAKEHEKFL---KELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLhGKSS 75

                           90       100
                   ....*....|....*....|
gi 578829102   459 QPPLMLALGQASECLRLMAR 478
Cdd:smart00757  76 ESPLEILLSAGLAALKTLLE 95
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 135-191 1.91e-13

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 64.90  E-value: 1.91e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829102   135 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTDSE 191
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 135-189 2.47e-13

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: 67.21  E-value: 2.47e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829102  135 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTD 189
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 402-473 8.09e-12

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: 62.97  E-value: 8.09e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578829102  402 EYGK------NLAHTEMLQDAFSLLAYSDPWSC-PVGQQLDPIQREPVCAALNSAILESQNLPKQPPLMLALGQASECL 473
Cdd:pfam10607  61 EYARenlapfNEEHLKELEKLMGLLAFPDPTDSsPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSAL 139
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 103-123 5.32e-03

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 34.21  E-value: 5.32e-03
                          10        20
                  ....*....|....*....|.
gi 578829102  103 SMVSSYLVHHGYCATATAFAR 123
Cdd:pfam08513   4 RLIYDYLVKEGYEETAEAFEK 24
 
Name Accession Description Interval E-value
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 381-478 2.78e-15

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 71.56  E-value: 2.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578829102   381 ATERIILFGRELQAlseQLGREYGKNLahtEMLQDAFSLLAYSDP-WSCPVGQQLDPIQREPVCAALNSAILESQ-NLPK 458
Cdd:smart00757   2 KIEEALAYARELLA---PFAKEHEKFL---KELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLhGKSS 75

                           90       100
                   ....*....|....*....|
gi 578829102   459 QPPLMLALGQASECLRLMAR 478
Cdd:smart00757  76 ESPLEILLSAGLAALKTLLE 95
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 135-191 1.91e-13

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 64.90  E-value: 1.91e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 578829102   135 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTDSE 191
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 135-189 2.47e-13

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: 67.21  E-value: 2.47e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578829102  135 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTD 189
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 402-473 8.09e-12

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: 62.97  E-value: 8.09e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578829102  402 EYGK------NLAHTEMLQDAFSLLAYSDPWSC-PVGQQLDPIQREPVCAALNSAILESQNLPKQPPLMLALGQASECL 473
Cdd:pfam10607  61 EYARenlapfNEEHLKELEKLMGLLAFPDPTDSsPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKAGLSAL 139
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 103-123 5.32e-03

LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex.


Pssm-ID: 462501  Cd Length: 25  Bit Score: 34.21  E-value: 5.32e-03
                          10        20
                  ....*....|....*....|.
gi 578829102  103 SMVSSYLVHHGYCATATAFAR 123
Cdd:pfam08513   4 RLIYDYLVKEGYEETAEAFEK 24
 
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