NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|511674005|dbj|GAD00043|]
View 

hypothetical protein AALB_0123 [Agarivorans albus MKT 106]

Protein Classification

lipid-binding SYLF domain-containing protein( domain architecture ID 10789889)

lipid-binding SYLF domain-containing protein

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 COG2930
Lipid-binding SYLF domain, Ysc84/FYVE family [Lipid transport and metabolism];
1-178 5.46e-27

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


:

Pssm-ID: 442174  Cd Length: 188  Bit Score: 100.69  E-value: 5.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511674005   1 MKKWLALCVGVLVLSF--------------QAVADDYQATIQQF-KKSDRTTPFFNNAYGYAVFPTIGKGGIGIGGAYGE 65
Cdd:COG2930    1 MKRRKLLLLALLLLALaaaaaasaaaaakaAEIDARADATLQELyPDVPGPRELLEKAKGVLVFPNVIKAGFIVGGAYGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511674005  66 GKVYRGGAST-GSVNMGQVTLGFQLGGQAFSQIIFLQDKRAYDEFTSGSFEFGAQASAVALTVGASAQAGTSGTgaaage 144
Cdd:COG2930   81 GVLLVRGPSTpAYYSLAGGSVGLQIGAQSYDLVLVFMTDEALDKFRKSGWTLGADASVAAGPVGAGASADTTAT------ 154
                        170       180       190
                 ....*....|....*....|....*....|....
gi 511674005 145 tqskahYVSGYAVFTLAKGGLMYEASIGGQKFNF 178
Cdd:COG2930  155 ------LKAPVYAYSRSKAGLFAGASLEGSKITR 182
 
Name Accession Description Interval E-value
SYLF COG2930
Lipid-binding SYLF domain, Ysc84/FYVE family [Lipid transport and metabolism];
1-178 5.46e-27

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


Pssm-ID: 442174  Cd Length: 188  Bit Score: 100.69  E-value: 5.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511674005   1 MKKWLALCVGVLVLSF--------------QAVADDYQATIQQF-KKSDRTTPFFNNAYGYAVFPTIGKGGIGIGGAYGE 65
Cdd:COG2930    1 MKRRKLLLLALLLLALaaaaaasaaaaakaAEIDARADATLQELyPDVPGPRELLEKAKGVLVFPNVIKAGFIVGGAYGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511674005  66 GKVYRGGAST-GSVNMGQVTLGFQLGGQAFSQIIFLQDKRAYDEFTSGSFEFGAQASAVALTVGASAQAGTSGTgaaage 144
Cdd:COG2930   81 GVLLVRGPSTpAYYSLAGGSVGLQIGAQSYDLVLVFMTDEALDKFRKSGWTLGADASVAAGPVGAGASADTTAT------ 154
                        170       180       190
                 ....*....|....*....|....*....|....
gi 511674005 145 tqskahYVSGYAVFTLAKGGLMYEASIGGQKFNF 178
Cdd:COG2930  155 ------LKAPVYAYSRSKAGLFAGASLEGSKITR 182
SYLF cd11524
The SYLF domain (also called DUF500), a novel lipid-binding module; The SYLF domain is named ...
20-149 1.36e-19

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: 81.48  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511674005  20 ADDYQATIQQFKK-SDRTTP--FFNNAYGYAVFPTigkggigiggaygegkVYRGGA---------------STGS---- 77
Cdd:cd11524    3 VDDAARVLKEFTSdPDKGIPpsLLQNAKGIAIFPS----------------VVKAGFivggaggsgvvlardPDGTwsap 66
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511674005  78 --VNMGQVTLGFQLGGQAFSQIIFLQDKRAYDEFTSGSFEFGAQASAVALTVGASAQAGTSGTGAAAGETQSKA 149
Cdd:cd11524   67 afISLTGGSFGLQIGVQSTDLVLVFMTDRALDAFLSGKFTLGADASAAAGPVGRGAEAGTDTALGAEIYSYSRS 140
Ysc84 pfam04366
Las17-binding protein actin regulator; Ysc84 is a family of Las17-binding proteins found in ...
81-142 7.65e-06

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: 43.27  E-value: 7.65e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511674005   81 GQVTLGFQLGGQAFSQIIFLQDKRAYDEFTS-GSFEFGAQASAVALTVGASAQAGTSGTGAAA 142
Cdd:pfam04366   1 GGGGLGFQIGVEITDCVLVLNTDEALEAFTSgGRVTLGGDVSVAAGPVGRGAEADATDAKLGA 63
 
Name Accession Description Interval E-value
SYLF COG2930
Lipid-binding SYLF domain, Ysc84/FYVE family [Lipid transport and metabolism];
1-178 5.46e-27

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


Pssm-ID: 442174  Cd Length: 188  Bit Score: 100.69  E-value: 5.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511674005   1 MKKWLALCVGVLVLSF--------------QAVADDYQATIQQF-KKSDRTTPFFNNAYGYAVFPTIGKGGIGIGGAYGE 65
Cdd:COG2930    1 MKRRKLLLLALLLLALaaaaaasaaaaakaAEIDARADATLQELyPDVPGPRELLEKAKGVLVFPNVIKAGFIVGGAYGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511674005  66 GKVYRGGAST-GSVNMGQVTLGFQLGGQAFSQIIFLQDKRAYDEFTSGSFEFGAQASAVALTVGASAQAGTSGTgaaage 144
Cdd:COG2930   81 GVLLVRGPSTpAYYSLAGGSVGLQIGAQSYDLVLVFMTDEALDKFRKSGWTLGADASVAAGPVGAGASADTTAT------ 154
                        170       180       190
                 ....*....|....*....|....*....|....
gi 511674005 145 tqskahYVSGYAVFTLAKGGLMYEASIGGQKFNF 178
Cdd:COG2930  155 ------LKAPVYAYSRSKAGLFAGASLEGSKITR 182
SYLF cd11524
The SYLF domain (also called DUF500), a novel lipid-binding module; The SYLF domain is named ...
20-149 1.36e-19

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: 81.48  E-value: 1.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511674005  20 ADDYQATIQQFKK-SDRTTP--FFNNAYGYAVFPTigkggigiggaygegkVYRGGA---------------STGS---- 77
Cdd:cd11524    3 VDDAARVLKEFTSdPDKGIPpsLLQNAKGIAIFPS----------------VVKAGFivggaggsgvvlardPDGTwsap 66
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511674005  78 --VNMGQVTLGFQLGGQAFSQIIFLQDKRAYDEFTSGSFEFGAQASAVALTVGASAQAGTSGTGAAAGETQSKA 149
Cdd:cd11524   67 afISLTGGSFGLQIGVQSTDLVLVFMTDRALDAFLSGKFTLGADASAAAGPVGRGAEAGTDTALGAEIYSYSRS 140
Ysc84 pfam04366
Las17-binding protein actin regulator; Ysc84 is a family of Las17-binding proteins found in ...
81-142 7.65e-06

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: 43.27  E-value: 7.65e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511674005   81 GQVTLGFQLGGQAFSQIIFLQDKRAYDEFTS-GSFEFGAQASAVALTVGASAQAGTSGTGAAA 142
Cdd:pfam04366   1 GGGGLGFQIGVEITDCVLVLNTDEALEAFTSgGRVTLGGDVSVAAGPVGRGAEADATDAKLGA 63
 
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