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Conserved domains on  [gi|1622910476|ref|XP_028696265|]
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ran-binding protein 10 isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 323-420 1.63e-15

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


:

Pssm-ID: 214806  Cd Length: 99  Bit Score: 71.94  E-value: 1.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910476  323 ATERIILFGRELQAlseqlgrEYGN-NLAHTEMLQDAFSLLAYSDP-WSCPVGQQLDPIQREPVCAALNSAILESQ-NLP 399
Cdd:smart00757   2 KIEEALAYARELLA-------PFAKeHEKFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLhGKS 74

                           90       100
                   ....*....|....*....|.
gi 1622910476  400 KQPPLMLALGQASECLRLMAR 420
Cdd:smart00757  75 SESPLEILLSAGLAALKTLLE 95
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 107-161 1.14e-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: 67.98  E-value: 1.14e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622910476 107 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTD 161
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55
SPRY super family cl02614
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 15-35 1.14e-08

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


The actual alignment was detected with superfamily member cd12909:

Pssm-ID: 470632  Cd Length: 144  Bit Score: 53.68  E-value: 1.14e-08
                          10        20
                  ....*....|....*....|.
gi 1622910476  15 NLYPTVGLQTPGEIVDANFGQ 35
Cdd:cd12909   124 NLYPTVGLRTPGEHVEANFGQ 144
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 73-100 1.88e-03

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: 35.87  E-value: 1.88e-03
                           10        20
                   ....*....|....*....|....*...
gi 1622910476   73 LQNMVSSYLVHHGYCATATAFARMTETP 100
Cdd:smart00667   6 LNRLILEYLLRNGYEETAETLQKESGLS 33
 
Name Accession Description Interval E-value
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 323-420 1.63e-15

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 71.94  E-value: 1.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910476  323 ATERIILFGRELQAlseqlgrEYGN-NLAHTEMLQDAFSLLAYSDP-WSCPVGQQLDPIQREPVCAALNSAILESQ-NLP 399
Cdd:smart00757   2 KIEEALAYARELLA-------PFAKeHEKFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLhGKS 74

                           90       100
                   ....*....|....*....|.
gi 1622910476  400 KQPPLMLALGQASECLRLMAR 420
Cdd:smart00757  75 SESPLEILLSAGLAALKTLLE 95
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 107-161 1.14e-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: 67.98  E-value: 1.14e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622910476 107 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTD 161
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 107-163 1.67e-13

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 64.90  E-value: 1.67e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622910476  107 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTDSE 163
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 334-415 1.78e-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: 64.51  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910476 334 LQALseQLGREY--GNNLAHTEMLQDAFSLLAYSDPWSC-PVGQQLDPIQREPVCAALNSAILESQNLPKQPPLMLALGQ 410
Cdd:pfam10607  57 LEAL--EYARENlaPFNEEHLKELEKLMGLLAFPDPTDSsPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKA 134


                  ....*
gi 1622910476 411 ASECL 415
Cdd:pfam10607 135 GLSAL 139
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 15-35 1.14e-08

SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells.


Pssm-ID: 293966  Cd Length: 144  Bit Score: 53.68  E-value: 1.14e-08
                          10        20
                  ....*....|....*....|.
gi 1622910476  15 NLYPTVGLQTPGEIVDANFGQ 35
Cdd:cd12909   124 NLYPTVGLRTPGEHVEANFGQ 144
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 73-100 1.88e-03

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: 35.87  E-value: 1.88e-03
                           10        20
                   ....*....|....*....|....*...
gi 1622910476   73 LQNMVSSYLVHHGYCATATAFARMTETP 100
Cdd:smart00667   6 LNRLILEYLLRNGYEETAETLQKESGLS 33
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 73-95 2.51e-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: 34.99  E-value: 2.51e-03
                          10        20
                  ....*....|....*....|...
gi 1622910476  73 LQNMVSSYLVHHGYCATATAFAR 95
Cdd:pfam08513   2 LNRLIYDYLVKEGYEETAEAFEK 24
 
Name Accession Description Interval E-value
CRA smart00757
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ...
 323-420 1.63e-15

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


Pssm-ID: 214806  Cd Length: 99  Bit Score: 71.94  E-value: 1.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910476  323 ATERIILFGRELQAlseqlgrEYGN-NLAHTEMLQDAFSLLAYSDP-WSCPVGQQLDPIQREPVCAALNSAILESQ-NLP 399
Cdd:smart00757   2 KIEEALAYARELLA-------PFAKeHEKFLKELEKTMALLAYPDPtEPSPYKELLSPSQREKLAEELNSAILELLhGKS 74

                           90       100
                   ....*....|....*....|.
gi 1622910476  400 KQPPLMLALGQASECLRLMAR 420
Cdd:smart00757  75 SESPLEILLSAGLAALKTLLE 95
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 107-161 1.14e-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: 67.98  E-value: 1.14e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622910476 107 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTD 161
Cdd:pfam10607   1 VFKERNRILEAILNGDITEAIEWCNENKPELLKINSNLEFELRLQQFIELIRSGK 55
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 107-163 1.67e-13

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 64.90  E-value: 1.67e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622910476  107 SIKNRQKIQKLVLEGRVGEAIETTQRFYPGLLEHNPNLLFMLKCRQFVEMVNGTDSE 163
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNSKLEFELRKQKFLELVRQGKLE 57
CTLH pfam10607
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ...
 334-415 1.78e-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: 64.51  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622910476 334 LQALseQLGREY--GNNLAHTEMLQDAFSLLAYSDPWSC-PVGQQLDPIQREPVCAALNSAILESQNLPKQPPLMLALGQ 410
Cdd:pfam10607  57 LEAL--EYARENlaPFNEEHLKELEKLMGLLAFPDPTDSsPYKSLLSPSRWEKLASEFNRAILKLLGLSSESPLEILLKA 134


                  ....*
gi 1622910476 411 ASECL 415
Cdd:pfam10607 135 GLSAL 139
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 15-35 1.14e-08

SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells.


Pssm-ID: 293966  Cd Length: 144  Bit Score: 53.68  E-value: 1.14e-08
                          10        20
                  ....*....|....*....|.
gi 1622910476  15 NLYPTVGLQTPGEIVDANFGQ 35
Cdd:cd12909   124 NLYPTVGLRTPGEHVEANFGQ 144
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 73-100 1.88e-03

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: 35.87  E-value: 1.88e-03
                           10        20
                   ....*....|....*....|....*...
gi 1622910476   73 LQNMVSSYLVHHGYCATATAFARMTETP 100
Cdd:smart00667   6 LNRLILEYLLRNGYEETAETLQKESGLS 33
LisH pfam08513
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ...
 73-95 2.51e-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: 34.99  E-value: 2.51e-03
                          10        20
                  ....*....|....*....|...
gi 1622910476  73 LQNMVSSYLVHHGYCATATAFAR 95
Cdd:pfam08513   2 LNRLIYDYLVKEGYEETAEAFEK 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.
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