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Conserved domains on  [gi|1720383935|ref|XP_030104337|]
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CYFIP-related Rac1 interactor B isoform X5 [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

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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 ...
18-320 0e+00

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: 592.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383935  18 HFFLDFENAQPTESEKEIYNQVNVVLKDAEGILEDLQSYRGAGHEIREAIQHPADEkLQEKAWGAVVPLVGKLKKFYEFS 97
Cdd:pfam07159   1 DIFLDFENAQPTEEEREIYNEVQEVLQDADNILQDLQSYKGAGEEIREAISNPSEE-NQEKAWNAVIPLVDKLKEFYEFS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383935  98 QRLEAALRGLLGALTSTPYSPTQHLEREQALAKQFAEILHFTLRFDELKMTNPAIQNDFSYYRRTLSRMRINNVPAEGEn 177
Cdd:pfam07159  80 SKLETVVPKLLGALCSGPLSPTQHLEQKQALAKQFAEILDFVLKFDDLKMKNPAIQNDFSYYRRTLSRMKMNNRDDEEE- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383935 178 EVNNELANRMSLFYAEATPMLKTLSDATTKFVSENKNLPIENTTDCLSTMASVCRVMLETPEYRSRFTNEETVSFCLRVM 257
Cdd:pfam07159 159 VVSDELANRMSLFYAYATPMLKVLSDATTKFVSENKSLPIDNTTDCLSTMANVCRVMLEKPDYRSRFQNEETVLFCLRVM 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720383935 258 VGVIILYDHVHPVGAFAKTSKIDMKGCIKVLKDQPPNSVEGLLNALRYTTKHLNDETTSKQIR 320
Cdd:pfam07159 239 VGVIILYDHVHPVGAFVKKSPIDIKGCVKVLKDQPPNSVEGLLNALRYTTKHLNDESTPKNIK 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 ...
18-320 0e+00

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: 592.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383935  18 HFFLDFENAQPTESEKEIYNQVNVVLKDAEGILEDLQSYRGAGHEIREAIQHPADEkLQEKAWGAVVPLVGKLKKFYEFS 97
Cdd:pfam07159   1 DIFLDFENAQPTEEEREIYNEVQEVLQDADNILQDLQSYKGAGEEIREAISNPSEE-NQEKAWNAVIPLVDKLKEFYEFS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383935  98 QRLEAALRGLLGALTSTPYSPTQHLEREQALAKQFAEILHFTLRFDELKMTNPAIQNDFSYYRRTLSRMRINNVPAEGEn 177
Cdd:pfam07159  80 SKLETVVPKLLGALCSGPLSPTQHLEQKQALAKQFAEILDFVLKFDDLKMKNPAIQNDFSYYRRTLSRMKMNNRDDEEE- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383935 178 EVNNELANRMSLFYAEATPMLKTLSDATTKFVSENKNLPIENTTDCLSTMASVCRVMLETPEYRSRFTNEETVSFCLRVM 257
Cdd:pfam07159 159 VVSDELANRMSLFYAYATPMLKVLSDATTKFVSENKSLPIDNTTDCLSTMANVCRVMLEKPDYRSRFQNEETVLFCLRVM 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720383935 258 VGVIILYDHVHPVGAFAKTSKIDMKGCIKVLKDQPPNSVEGLLNALRYTTKHLNDETTSKQIR 320
Cdd:pfam07159 239 VGVIILYDHVHPVGAFVKKSPIDIKGCVKVLKDQPPNSVEGLLNALRYTTKHLNDESTPKNIK 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 ...
18-320 0e+00

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: 592.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383935  18 HFFLDFENAQPTESEKEIYNQVNVVLKDAEGILEDLQSYRGAGHEIREAIQHPADEkLQEKAWGAVVPLVGKLKKFYEFS 97
Cdd:pfam07159   1 DIFLDFENAQPTEEEREIYNEVQEVLQDADNILQDLQSYKGAGEEIREAISNPSEE-NQEKAWNAVIPLVDKLKEFYEFS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383935  98 QRLEAALRGLLGALTSTPYSPTQHLEREQALAKQFAEILHFTLRFDELKMTNPAIQNDFSYYRRTLSRMRINNVPAEGEn 177
Cdd:pfam07159  80 SKLETVVPKLLGALCSGPLSPTQHLEQKQALAKQFAEILDFVLKFDDLKMKNPAIQNDFSYYRRTLSRMKMNNRDDEEE- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720383935 178 EVNNELANRMSLFYAEATPMLKTLSDATTKFVSENKNLPIENTTDCLSTMASVCRVMLETPEYRSRFTNEETVSFCLRVM 257
Cdd:pfam07159 159 VVSDELANRMSLFYAYATPMLKVLSDATTKFVSENKSLPIDNTTDCLSTMANVCRVMLEKPDYRSRFQNEETVLFCLRVM 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720383935 258 VGVIILYDHVHPVGAFAKTSKIDMKGCIKVLKDQPPNSVEGLLNALRYTTKHLNDETTSKQIR 320
Cdd:pfam07159 239 VGVIILYDHVHPVGAFVKKSPIDIKGCVKVLKDQPPNSVEGLLNALRYTTKHLNDESTPKNIK 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.
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