NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720383940|ref|XP_030104338|]
View 

CYFIP-related Rac1 interactor B isoform X6 [Mus musculus]

Protein Classification

CYFIP-related Rac1 interactor family protein( domain architecture ID 10537453)

CYFIP-related Rac1 interactor (CYRI) family protein is a DUF1394 domain-containing protein; similar to Homo sapiens proteins, CYRIA and CYRIB, which may negatively regulates RAC1 signaling and RAC1-driven cytoskeletal remodeling

Gene Ontology:  GO:0031267

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CYRIA-B_Rac1-bd pfam07159
CYRIA/CYRIB Rac1 binding domain; This domain has been annotated as Rac1-binding domain. It can ...
 1-174 3.81e-129

CYRIA/CYRIB Rac1 binding domain; This domain has been annotated as Rac1-binding domain. It can be found in human CYRIA/CYRIB and at the N terminus of CYFIP1/2. CYFIP proteins are known RAC1 effectors that stimulate actin polymerization. In mice, CYRIB (also known as CYRI or FAM49B) negatively regulates RAC1-driven cytoskeletal remodelling and plays a role in restricting infection mediated by Mycobacterium tuberculosis and Listeria monocytogenes.


:

Pssm-ID: 462106  Cd Length: 301  Bit Score: 364.26  E-value: 3.81e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383940   1 MTNPAIQNDFSYYRRTLSRMRINNVPAEGEnEVNNELANRMSLFYAEATPMLKTLSDATTKFVSENKNLPIENTTDCLST 80
Cdd:pfam07159 129 MKNPAIQNDFSYYRRTLSRMKMNNRDDEEE-VVSDELANRMSLFYAYATPMLKVLSDATTKFVSENKSLPIDNTTDCLST 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383940  81 MASVCRVMLETPEYRSRFTNEETVSFCLRVMVGVIILYDHVHPVGAFAKTSKIDMKGCIKVLKDQPPNSVEGLLNALRYT 160
Cdd:pfam07159 208 MANVCRVMLEKPDYRSRFQNEETVLFCLRVMVGVIILYDHVHPVGAFVKKSPIDIKGCVKVLKDQPPNSVEGLLNALRYT 287

                         170
                  ....*....|....
gi 1720383940 161 TKHLNDETTSKQIR 174
Cdd:pfam07159 288 TKHLNDESTPKNIK 301
 
Name Accession Description Interval E-value
CYRIA-B_Rac1-bd pfam07159
CYRIA/CYRIB Rac1 binding domain; This domain has been annotated as Rac1-binding domain. It can ...
 1-174 3.81e-129

CYRIA/CYRIB Rac1 binding domain; This domain has been annotated as Rac1-binding domain. It can be found in human CYRIA/CYRIB and at the N terminus of CYFIP1/2. CYFIP proteins are known RAC1 effectors that stimulate actin polymerization. In mice, CYRIB (also known as CYRI or FAM49B) negatively regulates RAC1-driven cytoskeletal remodelling and plays a role in restricting infection mediated by Mycobacterium tuberculosis and Listeria monocytogenes.


Pssm-ID: 462106  Cd Length: 301  Bit Score: 364.26  E-value: 3.81e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383940   1 MTNPAIQNDFSYYRRTLSRMRINNVPAEGEnEVNNELANRMSLFYAEATPMLKTLSDATTKFVSENKNLPIENTTDCLST 80
Cdd:pfam07159 129 MKNPAIQNDFSYYRRTLSRMKMNNRDDEEE-VVSDELANRMSLFYAYATPMLKVLSDATTKFVSENKSLPIDNTTDCLST 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383940  81 MASVCRVMLETPEYRSRFTNEETVSFCLRVMVGVIILYDHVHPVGAFAKTSKIDMKGCIKVLKDQPPNSVEGLLNALRYT 160
Cdd:pfam07159 208 MANVCRVMLEKPDYRSRFQNEETVLFCLRVMVGVIILYDHVHPVGAFVKKSPIDIKGCVKVLKDQPPNSVEGLLNALRYT 287

                         170
                  ....*....|....
gi 1720383940 161 TKHLNDETTSKQIR 174
Cdd:pfam07159 288 TKHLNDESTPKNIK 301
 
Name Accession Description Interval E-value
CYRIA-B_Rac1-bd pfam07159
CYRIA/CYRIB Rac1 binding domain; This domain has been annotated as Rac1-binding domain. It can ...
 1-174 3.81e-129

CYRIA/CYRIB Rac1 binding domain; This domain has been annotated as Rac1-binding domain. It can be found in human CYRIA/CYRIB and at the N terminus of CYFIP1/2. CYFIP proteins are known RAC1 effectors that stimulate actin polymerization. In mice, CYRIB (also known as CYRI or FAM49B) negatively regulates RAC1-driven cytoskeletal remodelling and plays a role in restricting infection mediated by Mycobacterium tuberculosis and Listeria monocytogenes.


Pssm-ID: 462106  Cd Length: 301  Bit Score: 364.26  E-value: 3.81e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383940   1 MTNPAIQNDFSYYRRTLSRMRINNVPAEGEnEVNNELANRMSLFYAEATPMLKTLSDATTKFVSENKNLPIENTTDCLST 80
Cdd:pfam07159 129 MKNPAIQNDFSYYRRTLSRMKMNNRDDEEE-VVSDELANRMSLFYAYATPMLKVLSDATTKFVSENKSLPIDNTTDCLST 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383940  81 MASVCRVMLETPEYRSRFTNEETVSFCLRVMVGVIILYDHVHPVGAFAKTSKIDMKGCIKVLKDQPPNSVEGLLNALRYT 160
Cdd:pfam07159 208 MANVCRVMLEKPDYRSRFQNEETVLFCLRVMVGVIILYDHVHPVGAFVKKSPIDIKGCVKVLKDQPPNSVEGLLNALRYT 287

                         170
                  ....*....|....
gi 1720383940 161 TKHLNDETTSKQIR 174
Cdd:pfam07159 288 TKHLNDESTPKNIK 301
 
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