NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|929773706|ref|XP_014161786|]
View 

hypothetical protein SARC_00018 [Sphaeroforma arctica JP610]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SYLF super family cl01109
The SYLF domain (also called DUF500), a novel lipid-binding module; The SYLF domain is named ...
 12-219 1.37e-32

The SYLF domain (also called DUF500), a novel lipid-binding module; The SYLF domain is named after SH3YL1, Ysc84p/Lsb4p, Lsb3p, and plant FYVE, which are proteins that contain it. It is also called DUF500 and is highly conserved from bacteria to mammals. Some members, such as SH3YL1, Ysc84p, and Lsb3p, which represent the best characterized members of the family, also contain an SH3 domain, while family members from plants and stramenopiles also contain a FYVE zinc finger domain. Other members only contain a stand-alone SYLF domain. The SYLF domain of SH3YL1 binds phosphoinositides with high affinity, while the N-terminal SYLF domains of both Ysc84p and Lsb3p have been shown to bind and bundle actin filaments, as well as bind liposomes with high affinity.


The actual alignment was detected with superfamily member cd11525:

Pssm-ID: 470077  Cd Length: 199  Bit Score: 121.60  E-value: 1.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706  12 ECDHASAILES---GSVKDTKSKVksvlntIPPKLFRSCKGVAIATLAQMSILLGGVKGGSGVVLKHDpkTDEWSDPIGF 88
Cdd:cd11525    2 ECKKAAKILREftePSNRNGPDKL------IPPHVLAKAKGLAIISVIKAGFLVSARAGSGLVVARLP--DGTWSAPSAI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706  89 GLAGGLFGFQLGIAAIDLVMILTTDNAVKAFAR-GNVTLGGEIGCAIGPHGRTLEGDIAIMNISPVVTYSFSRGLLFSMS 167
Cdd:cd11525   74 GIAGLGGGFEIGVEVTDFVIVLNSKSAVRAFSQgGSLTLGGNVSVAAGPLGRNAEAAGSASGLAAIFSYSKTRGLFAGVS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 929773706 168 VEGVGIIQRPDSNKKFYGQDVDTMDVLNGfkdlqPVKPQGATAirRLHKCLQ 219
Cdd:cd11525  154 LEGSVLIERKDANRKFYGKDISAKDLLSG-----EVPPPPEAD--PLYRILD 198
 
Name Accession Description Interval E-value
SYLF_SH3YL1_like cd11525
The SYLF domain (also called DUF500), a novel lipid-binding module, of SH3 domain containing ...
 12-219 1.37e-32

The SYLF domain (also called DUF500), a novel lipid-binding module, of SH3 domain containing Ysc84-like 1 (SH3YL1) and similar proteins; This subfamily is composed of yeast Ysc84 (also called LAS17-binding protein 4, Lsb4p) and Lsb3p proteins, vertebrate SH3YL1 (SH3 domain containing Ysc84-like 1), and similar proteins. They contain an N-terminal SYLF domain (also called DUF500) and a C-terminal SH3 domain. SH3YL1 localizes to the plasma membrane and is required for dorsal ruffle formation. Ysc84p localizes to actin patches and plays an important role in actin polymerization during endocytosis. A study of the yeast SH3 domain interactome predicts that Lsb3p and Lsb4p may function as molecular hubs for the assembly of endocytic complexes. The SYLF domain of SH3YL1 binds phosphoinositides with high affinity, while the N-terminal SYLF domains of both Ysc84p and Lsb3p have been shown to bind and bundle actin filaments, as well as bind liposomes with high affinity.


Pssm-ID: 211401  Cd Length: 199  Bit Score: 121.60  E-value: 1.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706  12 ECDHASAILES---GSVKDTKSKVksvlntIPPKLFRSCKGVAIATLAQMSILLGGVKGGSGVVLKHDpkTDEWSDPIGF 88
Cdd:cd11525    2 ECKKAAKILREftePSNRNGPDKL------IPPHVLAKAKGLAIISVIKAGFLVSARAGSGLVVARLP--DGTWSAPSAI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706  89 GLAGGLFGFQLGIAAIDLVMILTTDNAVKAFAR-GNVTLGGEIGCAIGPHGRTLEGDIAIMNISPVVTYSFSRGLLFSMS 167
Cdd:cd11525   74 GIAGLGGGFEIGVEVTDFVIVLNSKSAVRAFSQgGSLTLGGNVSVAAGPLGRNAEAAGSASGLAAIFSYSKTRGLFAGVS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 929773706 168 VEGVGIIQRPDSNKKFYGQDVDTMDVLNGfkdlqPVKPQGATAirRLHKCLQ 219
Cdd:cd11525  154 LEGSVLIERKDANRKFYGKDISAKDLLSG-----EVPPPPEAD--PLYRILD 198
Ysc84 pfam04366
Las17-binding protein actin regulator; Ysc84 is a family of Las17-binding proteins found in ...
 98-196 7.29e-29

Las17-binding protein actin regulator; Ysc84 is a family of Las17-binding proteins found in metazoa. Together, Las17 and Ysc84 are essential for proper polymerization of actin; Ysc84 is able to bind to and stabilize the actin dimer presented by Las17 and thereby promote polymerization. An active actin cytoskeleton is necessary for adequate endocytosis. (pfam00018), or a FYVE zinc finger (pfam01363).


Pssm-ID: 461278  Cd Length: 127  Bit Score: 109.53  E-value: 7.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706   98 QLGIAAIDLVMILTTDNAVKAFA-RGNVTLGGEIGCAIGPHGRTLEGDIAIMNIS-PVVTYSFSRGLLFSMSVEGVGIIQ 175
Cdd:pfam04366   8 QIGVEITDCVLVLNTDEALEAFTsGGRVTLGGDVSVAAGPVGRGAEADATDAKLGaPIYSYSKSKGLFAGVSLEGSVISE 87

                          90       100
                  ....*....|....*....|..
gi 929773706  176 RPDSNKKFYG-QDVDTMDVLNG 196
Cdd:pfam04366  88 RKDANAAFYGrRGVTARDILAG 109
SYLF COG2930
Lipid-binding SYLF domain, Ysc84/FYVE family [Lipid transport and metabolism];
96-181 3.37e-14

Lipid-binding SYLF domain, Ysc84/FYVE family [Lipid transport and metabolism];


Pssm-ID: 442174  Cd Length: 188  Bit Score: 70.64  E-value: 3.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706  96 GFQLGIAAIDLVMILTTDNAVKAFARGNVTLGGEIGCAIGPHGRTLEGDIAIMNISPVVTYSFSR-GLLFSMSVEGVGII 174
Cdd:COG2930  102 GLQIGAQSYDLVLVFMTDEALDKFRKSGWTLGADASVAAGPVGAGASADTTATLKAPVYAYSRSKaGLFAGASLEGSKIT 181


                 ....*..
gi 929773706 175 QRPDSNK 181
Cdd:COG2930  182 RDDDANR 188
 
Name Accession Description Interval E-value
SYLF_SH3YL1_like cd11525
The SYLF domain (also called DUF500), a novel lipid-binding module, of SH3 domain containing ...
 12-219 1.37e-32

The SYLF domain (also called DUF500), a novel lipid-binding module, of SH3 domain containing Ysc84-like 1 (SH3YL1) and similar proteins; This subfamily is composed of yeast Ysc84 (also called LAS17-binding protein 4, Lsb4p) and Lsb3p proteins, vertebrate SH3YL1 (SH3 domain containing Ysc84-like 1), and similar proteins. They contain an N-terminal SYLF domain (also called DUF500) and a C-terminal SH3 domain. SH3YL1 localizes to the plasma membrane and is required for dorsal ruffle formation. Ysc84p localizes to actin patches and plays an important role in actin polymerization during endocytosis. A study of the yeast SH3 domain interactome predicts that Lsb3p and Lsb4p may function as molecular hubs for the assembly of endocytic complexes. The SYLF domain of SH3YL1 binds phosphoinositides with high affinity, while the N-terminal SYLF domains of both Ysc84p and Lsb3p have been shown to bind and bundle actin filaments, as well as bind liposomes with high affinity.


Pssm-ID: 211401  Cd Length: 199  Bit Score: 121.60  E-value: 1.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706  12 ECDHASAILES---GSVKDTKSKVksvlntIPPKLFRSCKGVAIATLAQMSILLGGVKGGSGVVLKHDpkTDEWSDPIGF 88
Cdd:cd11525    2 ECKKAAKILREftePSNRNGPDKL------IPPHVLAKAKGLAIISVIKAGFLVSARAGSGLVVARLP--DGTWSAPSAI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706  89 GLAGGLFGFQLGIAAIDLVMILTTDNAVKAFAR-GNVTLGGEIGCAIGPHGRTLEGDIAIMNISPVVTYSFSRGLLFSMS 167
Cdd:cd11525   74 GIAGLGGGFEIGVEVTDFVIVLNSKSAVRAFSQgGSLTLGGNVSVAAGPLGRNAEAAGSASGLAAIFSYSKTRGLFAGVS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 929773706 168 VEGVGIIQRPDSNKKFYGQDVDTMDVLNGfkdlqPVKPQGATAirRLHKCLQ 219
Cdd:cd11525  154 LEGSVLIERKDANRKFYGKDISAKDLLSG-----EVPPPPEAD--PLYRILD 198
SYLF cd11524
The SYLF domain (also called DUF500), a novel lipid-binding module; The SYLF domain is named ...
 11-214 2.16e-29

The SYLF domain (also called DUF500), a novel lipid-binding module; The SYLF domain is named after SH3YL1, Ysc84p/Lsb4p, Lsb3p, and plant FYVE, which are proteins that contain it. It is also called DUF500 and is highly conserved from bacteria to mammals. Some members, such as SH3YL1, Ysc84p, and Lsb3p, which represent the best characterized members of the family, also contain an SH3 domain, while family members from plants and stramenopiles also contain a FYVE zinc finger domain. Other members only contain a stand-alone SYLF domain. The SYLF domain of SH3YL1 binds phosphoinositides with high affinity, while the N-terminal SYLF domains of both Ysc84p and Lsb3p have been shown to bind and bundle actin filaments, as well as bind liposomes with high affinity.


Pssm-ID: 211400  Cd Length: 194  Bit Score: 113.07  E-value: 2.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706  11 KECDHASAILESGSVKDTKSkvksvlntIPPKLFRSCKGVAIAT------------------LAqmsillggvkggsgvv 72
Cdd:cd11524    1 ELVDDAARVLKEFTSDPDKG--------IPPSLLQNAKGIAIFPsvvkagfivggaggsgvvLA---------------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706  73 lkHDPKTdEWSDPIGFGLAGGLFGFQLGIAAIDLVMILTTDNAVKAFARGNVTLGGEIGCAIGPHGRTLEGDIAIMNISP 152
Cdd:cd11524   57 --RDPDG-TWSAPAFISLTGGSFGLQIGVQSTDLVLVFMTDRALDAFLSGKFTLGADASAAAGPVGRGAEAGTDTALGAE 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 929773706 153 VVTYSFSRGLLFSMSVEGVGIIQRPDSNKKFYGQDVDTMDVLNGfkdlQPVKPQGATAIRRL 214
Cdd:cd11524  134 IYSYSRSKGLFAGVSLEGSVISVDDDANRAYYGRPVSPEDILLG----KVAPPPEAQPLREA 191
Ysc84 pfam04366
Las17-binding protein actin regulator; Ysc84 is a family of Las17-binding proteins found in ...
 98-196 7.29e-29

Las17-binding protein actin regulator; Ysc84 is a family of Las17-binding proteins found in metazoa. Together, Las17 and Ysc84 are essential for proper polymerization of actin; Ysc84 is able to bind to and stabilize the actin dimer presented by Las17 and thereby promote polymerization. An active actin cytoskeleton is necessary for adequate endocytosis. (pfam00018), or a FYVE zinc finger (pfam01363).


Pssm-ID: 461278  Cd Length: 127  Bit Score: 109.53  E-value: 7.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706   98 QLGIAAIDLVMILTTDNAVKAFA-RGNVTLGGEIGCAIGPHGRTLEGDIAIMNIS-PVVTYSFSRGLLFSMSVEGVGIIQ 175
Cdd:pfam04366   8 QIGVEITDCVLVLNTDEALEAFTsGGRVTLGGDVSVAAGPVGRGAEADATDAKLGaPIYSYSKSKGLFAGVSLEGSVISE 87

                          90       100
                  ....*....|....*....|..
gi 929773706  176 RPDSNKKFYG-QDVDTMDVLNG 196
Cdd:pfam04366  88 RKDANAAFYGrRGVTARDILAG 109
SYLF_FYVE cd11526
The SYLF domain (also called DUF500), a novel lipid-binding module, of FYVE zinc finger domain ...
 37-196 8.09e-22

The SYLF domain (also called DUF500), a novel lipid-binding module, of FYVE zinc finger domain containing proteins; This subfamily is composed of uncharacterized proteins from plants and stramenopiles containing a FYVE zinc finger domain followed by a SYLF domain (also called DUF500). The SYLF domain of the related protein, SH3YL1, binds phosphoinositides with high affinity, while the N-terminal SYLF domains of both Ysc84p and Lsb3p have been shown to bind and bundle actin filaments, as well as bind liposomes with high affinity.


Pssm-ID: 211402  Cd Length: 201  Bit Score: 92.28  E-value: 8.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706  37 NTIPPKLFRSCKGVAIATLAQMSILLGGVKGGSGVVLKHDpkTDEWSDPIGFGLAGGLFGFQLGIAAIDLVMILTTDNAV 116
Cdd:cd11526   23 QSIPHALLRGAKGLAFLTVAKAGFIVSGKVGTGLVVARLP--DGSWSAPSAIGTAGLGWGAQVGGELTDFVIVLRTRSAV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706 117 KAF-ARGNVTLGGEIGCAIGPHGRTLEGDIAI--MNISPVVTYSFSRGLLFSMSVEGVGIIQRPDSNKKFYGQDVDTMDV 193
Cdd:cd11526  101 KAFcGRGQVSLGAELSVAVGPLGRAAEADLRAgdGGVAACYSYSHSKGLFAGVSLEGSVVATRKDVNHKFYGRPVTPTEI 180


                 ...
gi 929773706 194 LNG 196
Cdd:cd11526  181 LLG 183
SYLF COG2930
Lipid-binding SYLF domain, Ysc84/FYVE family [Lipid transport and metabolism];
96-181 3.37e-14

Lipid-binding SYLF domain, Ysc84/FYVE family [Lipid transport and metabolism];


Pssm-ID: 442174  Cd Length: 188  Bit Score: 70.64  E-value: 3.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929773706  96 GFQLGIAAIDLVMILTTDNAVKAFARGNVTLGGEIGCAIGPHGRTLEGDIAIMNISPVVTYSFSR-GLLFSMSVEGVGII 174
Cdd:COG2930  102 GLQIGAQSYDLVLVFMTDEALDKFRKSGWTLGADASVAAGPVGAGASADTTATLKAPVYAYSRSKaGLFAGASLEGSKIT 181


                 ....*..
gi 929773706 175 QRPDSNK 181
Cdd:COG2930  182 RDDDANR 188
 
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