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Conserved domains on  [gi|110349754|ref|NP_005093|]
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fasciculation and elongation protein zeta-2 isoform 1 [Homo sapiens]

Protein Classification

fasciculation and elongation protein zeta( domain architecture ID 10544171)

fasciculation and elongation protein zeta may be involved in axonal outgrowth as component of the network of molecules that regulate cellular morphology and axon guidance machinery

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FEZ pfam07763
FEZ-like protein; This is a family of eukaryotic proteins thought to be involved in axonal ...
52-270 3.64e-95

FEZ-like protein; This is a family of eukaryotic proteins thought to be involved in axonal outgrowth and fasciculation. The N-terminal regions of these sequences are less conserved than the C-terminal regions, and are highly acidic. The C. elegans homolog, UNC-76, may play structural and signalling roles in the control of axonal extension and adhesion (particularly in the presence of adjacent neuronal cells) and these roles have also been postulated for other FEZ family proteins. Certain homologs have been definitively found to interact with the N-terminal variable region (V1) of PKC-zeta, and this interaction causes cytoplasmic translocation of the FEZ family protein in mammalian neuronal cells. The C-terminal region probably participates in the association with the regulatory domain of PKC-zeta. The members of this family are predicted to form coiled-coil structures, which may interact with members of the RhoA family of signalling proteins, but are not thought to contain other characteriztic protein motifs. Certain members of this family are expressed almost exclusively in the brain, whereas others (such as FEZ2) are expressed in other tissues, and are thought to perform similar but unknown functions in these tissues.


:

Pssm-ID: 462257  Cd Length: 240  Bit Score: 283.06  E-value: 3.64e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110349754   52 CSLEEKLSLCFRPSDPGAEPpRTAVRPITERSLLQGDEIWNALTDNYGNVMPVDWKSSHTRTLHLLTLNLSEKGVSDSLL 131
Cdd:pfam07763   7 NEFDEKLTVCFRNYEAKTEG-LAPVQIRTQEEILNDCEVWWALTDNFGNILPVDWSKSYTRKLHLPTLNLNENNSSDPNL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110349754  132 fDTSDDEELREQLDMHSIIVSCVNDEPLFTADQVIEEIEEMMQESPDPEDDETPTQSDrLSMLSQEIQTLKRSSTG--SY 209
Cdd:pfam07763  86 -DESDDEELREQLDMHSLIVSCLNEEPLFTAEQVIEEIEEMMQESPDPEEEETPSSSD-LSILSQELHELSRASNNspSY 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110349754  210 EERVKRLSVSELNEILEEIETAIKEYSEELVQQLALRDELEFEKEVKNSFISVLIEVQNKQ 270
Cdd:pfam07763 164 EERLRLLSVSQLNELLEEMETLIREYSEELIQQLALRDELEFEKEVKNSFISLLLAVQNRQ 224
 
Name Accession Description Interval E-value
FEZ pfam07763
FEZ-like protein; This is a family of eukaryotic proteins thought to be involved in axonal ...
52-270 3.64e-95

FEZ-like protein; This is a family of eukaryotic proteins thought to be involved in axonal outgrowth and fasciculation. The N-terminal regions of these sequences are less conserved than the C-terminal regions, and are highly acidic. The C. elegans homolog, UNC-76, may play structural and signalling roles in the control of axonal extension and adhesion (particularly in the presence of adjacent neuronal cells) and these roles have also been postulated for other FEZ family proteins. Certain homologs have been definitively found to interact with the N-terminal variable region (V1) of PKC-zeta, and this interaction causes cytoplasmic translocation of the FEZ family protein in mammalian neuronal cells. The C-terminal region probably participates in the association with the regulatory domain of PKC-zeta. The members of this family are predicted to form coiled-coil structures, which may interact with members of the RhoA family of signalling proteins, but are not thought to contain other characteriztic protein motifs. Certain members of this family are expressed almost exclusively in the brain, whereas others (such as FEZ2) are expressed in other tissues, and are thought to perform similar but unknown functions in these tissues.


Pssm-ID: 462257  Cd Length: 240  Bit Score: 283.06  E-value: 3.64e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110349754   52 CSLEEKLSLCFRPSDPGAEPpRTAVRPITERSLLQGDEIWNALTDNYGNVMPVDWKSSHTRTLHLLTLNLSEKGVSDSLL 131
Cdd:pfam07763   7 NEFDEKLTVCFRNYEAKTEG-LAPVQIRTQEEILNDCEVWWALTDNFGNILPVDWSKSYTRKLHLPTLNLNENNSSDPNL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110349754  132 fDTSDDEELREQLDMHSIIVSCVNDEPLFTADQVIEEIEEMMQESPDPEDDETPTQSDrLSMLSQEIQTLKRSSTG--SY 209
Cdd:pfam07763  86 -DESDDEELREQLDMHSLIVSCLNEEPLFTAEQVIEEIEEMMQESPDPEEEETPSSSD-LSILSQELHELSRASNNspSY 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110349754  210 EERVKRLSVSELNEILEEIETAIKEYSEELVQQLALRDELEFEKEVKNSFISVLIEVQNKQ 270
Cdd:pfam07763 164 EERLRLLSVSQLNELLEEMETLIREYSEELIQQLALRDELEFEKEVKNSFISLLLAVQNRQ 224
 
Name Accession Description Interval E-value
FEZ pfam07763
FEZ-like protein; This is a family of eukaryotic proteins thought to be involved in axonal ...
52-270 3.64e-95

FEZ-like protein; This is a family of eukaryotic proteins thought to be involved in axonal outgrowth and fasciculation. The N-terminal regions of these sequences are less conserved than the C-terminal regions, and are highly acidic. The C. elegans homolog, UNC-76, may play structural and signalling roles in the control of axonal extension and adhesion (particularly in the presence of adjacent neuronal cells) and these roles have also been postulated for other FEZ family proteins. Certain homologs have been definitively found to interact with the N-terminal variable region (V1) of PKC-zeta, and this interaction causes cytoplasmic translocation of the FEZ family protein in mammalian neuronal cells. The C-terminal region probably participates in the association with the regulatory domain of PKC-zeta. The members of this family are predicted to form coiled-coil structures, which may interact with members of the RhoA family of signalling proteins, but are not thought to contain other characteriztic protein motifs. Certain members of this family are expressed almost exclusively in the brain, whereas others (such as FEZ2) are expressed in other tissues, and are thought to perform similar but unknown functions in these tissues.


Pssm-ID: 462257  Cd Length: 240  Bit Score: 283.06  E-value: 3.64e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110349754   52 CSLEEKLSLCFRPSDPGAEPpRTAVRPITERSLLQGDEIWNALTDNYGNVMPVDWKSSHTRTLHLLTLNLSEKGVSDSLL 131
Cdd:pfam07763   7 NEFDEKLTVCFRNYEAKTEG-LAPVQIRTQEEILNDCEVWWALTDNFGNILPVDWSKSYTRKLHLPTLNLNENNSSDPNL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110349754  132 fDTSDDEELREQLDMHSIIVSCVNDEPLFTADQVIEEIEEMMQESPDPEDDETPTQSDrLSMLSQEIQTLKRSSTG--SY 209
Cdd:pfam07763  86 -DESDDEELREQLDMHSLIVSCLNEEPLFTAEQVIEEIEEMMQESPDPEEEETPSSSD-LSILSQELHELSRASNNspSY 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110349754  210 EERVKRLSVSELNEILEEIETAIKEYSEELVQQLALRDELEFEKEVKNSFISVLIEVQNKQ 270
Cdd:pfam07763 164 EERLRLLSVSQLNELLEEMETLIREYSEELIQQLALRDELEFEKEVKNSFISLLLAVQNRQ 224
 
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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