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Conserved domains on  [gi|2217266759|ref|XP_011542475|]
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protein lin-9 homolog isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DIRP pfam06584
DIRP; DIRP (Domain in Rb-related Pathway) is postulated to be involved in the Rb-related ...
 142-247 3.36e-61

DIRP; DIRP (Domain in Rb-related Pathway) is postulated to be involved in the Rb-related pathway, which is encoded by multiple eukaryotic genomes and is present in proteins including lin-9 of Caenorhabditis elegans, aly of fruit fly and mustard weed. Studies of lin-9 and aly of fruit fly proteins containing DIRP suggest that this domain might be involved in development. Aly, lin-9, act in parallel to, or downstream of, activation of MAPK by the RTK-Ras signalling pathway.


:

Pssm-ID: 461955  Cd Length: 108  Bit Score: 192.44  E-value: 3.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266759 142 WFYSNIDKPLFEGDNDFCVCLKESFPNLKTRKLTRVEWGKIRRLMGKPRRCSSAFFEEERSALKQKRQKIRLLQQRKVA- 220
Cdd:pfam06584   1 WFYSNIDKPLFESKNDFEEYLNESFPGLKTRRLTRAEWQKIRRSMGKPRRFSAAFFEEEREELERKREKIRQLQQRKLNi 80

                          90       100
                  ....*....|....*....|....*...
gi 2217266759 221 DVSQF-KDLPDEIPLPLVIGTKVTARLR 247
Cdd:pfam06584  81 DLSGLlEDLPKDIPLPLVVGTKVTARLP 108
LIN9_C super family cl44855
LIN9 C-terminal; MuvB transcriptional regulatory complex interacts with B-Myb to form the MMB ...
 283-389 6.16e-61

LIN9 C-terminal; MuvB transcriptional regulatory complex interacts with B-Myb to form the MMB complex during S-phase of the cell cycle to activate genes required for the G2 and M phases. This is a domain found at the C-terminal of LIN9, one of the core members of the MuvB complex that functions as a scaffold protein and forms a subcomplex with the C-terminal of LIN152. This subcomplex forms a binding interface that recruits B-Myb to the MuvB complex which is arranged as a three-stranded antiparallel coiled-coil as the core of the structure. LIN9 contributes two helices (alpha1 and alpha2) that run antiparallel and are connected through a short linker.


The actual alignment was detected with superfamily member pfam19438:

Pssm-ID: 437270  Cd Length: 272  Bit Score: 197.87  E-value: 6.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266759 283 PDYEVLSNEPHETMPIAAFGQKQRPSRF-FMTPPRlhYTPPLQSPIIDNDPLLGQSPWRSKISGSDTETLGGFPVEFLIQ 361
Cdd:pfam19438   1 PDYEVLSNEPPETIPLSSFQQKFRPRPQpFLSPPR--YTPSLGSPLLDNDPLLSGSPFKSRLTGLDGGTLGGFPIKFLEL 78

                          90       100
                  ....*....|....*....|....*...
gi 2217266759 362 VTRLSKILMIKKEHIKKLREMNTEAEKL 389
Cdd:pfam19438  79 VVRLSKILNIKKDKIQQLKEMNTEAEKR 106
 
Name Accession Description Interval E-value
DIRP pfam06584
DIRP; DIRP (Domain in Rb-related Pathway) is postulated to be involved in the Rb-related ...
 142-247 3.36e-61

DIRP; DIRP (Domain in Rb-related Pathway) is postulated to be involved in the Rb-related pathway, which is encoded by multiple eukaryotic genomes and is present in proteins including lin-9 of Caenorhabditis elegans, aly of fruit fly and mustard weed. Studies of lin-9 and aly of fruit fly proteins containing DIRP suggest that this domain might be involved in development. Aly, lin-9, act in parallel to, or downstream of, activation of MAPK by the RTK-Ras signalling pathway.


Pssm-ID: 461955  Cd Length: 108  Bit Score: 192.44  E-value: 3.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266759 142 WFYSNIDKPLFEGDNDFCVCLKESFPNLKTRKLTRVEWGKIRRLMGKPRRCSSAFFEEERSALKQKRQKIRLLQQRKVA- 220
Cdd:pfam06584   1 WFYSNIDKPLFESKNDFEEYLNESFPGLKTRRLTRAEWQKIRRSMGKPRRFSAAFFEEEREELERKREKIRQLQQRKLNi 80

                          90       100
                  ....*....|....*....|....*...
gi 2217266759 221 DVSQF-KDLPDEIPLPLVIGTKVTARLR 247
Cdd:pfam06584  81 DLSGLlEDLPKDIPLPLVVGTKVTARLP 108
LIN9_C pfam19438
LIN9 C-terminal; MuvB transcriptional regulatory complex interacts with B-Myb to form the MMB ...
 283-389 6.16e-61

LIN9 C-terminal; MuvB transcriptional regulatory complex interacts with B-Myb to form the MMB complex during S-phase of the cell cycle to activate genes required for the G2 and M phases. This is a domain found at the C-terminal of LIN9, one of the core members of the MuvB complex that functions as a scaffold protein and forms a subcomplex with the C-terminal of LIN152. This subcomplex forms a binding interface that recruits B-Myb to the MuvB complex which is arranged as a three-stranded antiparallel coiled-coil as the core of the structure. LIN9 contributes two helices (alpha1 and alpha2) that run antiparallel and are connected through a short linker.


Pssm-ID: 437270  Cd Length: 272  Bit Score: 197.87  E-value: 6.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266759 283 PDYEVLSNEPHETMPIAAFGQKQRPSRF-FMTPPRlhYTPPLQSPIIDNDPLLGQSPWRSKISGSDTETLGGFPVEFLIQ 361
Cdd:pfam19438   1 PDYEVLSNEPPETIPLSSFQQKFRPRPQpFLSPPR--YTPSLGSPLLDNDPLLSGSPFKSRLTGLDGGTLGGFPIKFLEL 78

                          90       100
                  ....*....|....*....|....*...
gi 2217266759 362 VTRLSKILMIKKEHIKKLREMNTEAEKL 389
Cdd:pfam19438  79 VVRLSKILNIKKDKIQQLKEMNTEAEKR 106
 
Name Accession Description Interval E-value
DIRP pfam06584
DIRP; DIRP (Domain in Rb-related Pathway) is postulated to be involved in the Rb-related ...
 142-247 3.36e-61

DIRP; DIRP (Domain in Rb-related Pathway) is postulated to be involved in the Rb-related pathway, which is encoded by multiple eukaryotic genomes and is present in proteins including lin-9 of Caenorhabditis elegans, aly of fruit fly and mustard weed. Studies of lin-9 and aly of fruit fly proteins containing DIRP suggest that this domain might be involved in development. Aly, lin-9, act in parallel to, or downstream of, activation of MAPK by the RTK-Ras signalling pathway.


Pssm-ID: 461955  Cd Length: 108  Bit Score: 192.44  E-value: 3.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266759 142 WFYSNIDKPLFEGDNDFCVCLKESFPNLKTRKLTRVEWGKIRRLMGKPRRCSSAFFEEERSALKQKRQKIRLLQQRKVA- 220
Cdd:pfam06584   1 WFYSNIDKPLFESKNDFEEYLNESFPGLKTRRLTRAEWQKIRRSMGKPRRFSAAFFEEEREELERKREKIRQLQQRKLNi 80

                          90       100
                  ....*....|....*....|....*...
gi 2217266759 221 DVSQF-KDLPDEIPLPLVIGTKVTARLR 247
Cdd:pfam06584  81 DLSGLlEDLPKDIPLPLVVGTKVTARLP 108
LIN9_C pfam19438
LIN9 C-terminal; MuvB transcriptional regulatory complex interacts with B-Myb to form the MMB ...
 283-389 6.16e-61

LIN9 C-terminal; MuvB transcriptional regulatory complex interacts with B-Myb to form the MMB complex during S-phase of the cell cycle to activate genes required for the G2 and M phases. This is a domain found at the C-terminal of LIN9, one of the core members of the MuvB complex that functions as a scaffold protein and forms a subcomplex with the C-terminal of LIN152. This subcomplex forms a binding interface that recruits B-Myb to the MuvB complex which is arranged as a three-stranded antiparallel coiled-coil as the core of the structure. LIN9 contributes two helices (alpha1 and alpha2) that run antiparallel and are connected through a short linker.


Pssm-ID: 437270  Cd Length: 272  Bit Score: 197.87  E-value: 6.16e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217266759 283 PDYEVLSNEPHETMPIAAFGQKQRPSRF-FMTPPRlhYTPPLQSPIIDNDPLLGQSPWRSKISGSDTETLGGFPVEFLIQ 361
Cdd:pfam19438   1 PDYEVLSNEPPETIPLSSFQQKFRPRPQpFLSPPR--YTPSLGSPLLDNDPLLSGSPFKSRLTGLDGGTLGGFPIKFLEL 78

                          90       100
                  ....*....|....*....|....*...
gi 2217266759 362 VTRLSKILMIKKEHIKKLREMNTEAEKL 389
Cdd:pfam19438  79 VVRLSKILNIKKDKIQQLKEMNTEAEKR 106
 
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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