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Conserved domains on  [gi|528514086|ref|XP_005161358|]
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post-GPI attachment to proteins factor 2 isoform X1 [Danio rerio]

Protein Classification

Frag1/DRAM/Sfk1 family protein( domain architecture ID 10563211)

Frag1/DRAM/Sfk1 family membrane protein such as Sfk1, which may be involved in the regulation of phospholipid asymmetry across the plasma membrane

PubMed:  29540528|10585768|25929859

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Frag1 pfam10277
Frag1/DRAM/Sfk1 family; This family includes Frag1, DRAM and Sfk1 proteins. Frag1 (FGF ...
 19-241 2.42e-47

Frag1/DRAM/Sfk1 family; This family includes Frag1, DRAM and Sfk1 proteins. Frag1 (FGF receptor activating protein 1) is a protein that is conserved from fungi to humans. There are four potential iso-prenylation sites throughout the peptide, viz CILW, CIIW and CIGL. Frag1 is a membrane-spanning protein that is ubiquitously expressed in adult tissues suggesting an important cellular function. Dram is a family of proteins conserved from nematodes to humans with six hydrophobic transmembrane regions and an Endoplasmic Reticulum signal peptide. It is a lysosomal protein that induces macro-autophagy as an effector of p53-mediated death, where p53 is the tumour-suppressor gene that is frequently mutated in cancer. Expression of Dram is stress-induced. This region is also part of a family of small plasma membrane proteins, referred to as Sfk1, that may act together with or upstream of Stt4p to generate normal levels of the essential phospholipid PI4P, thus allowing proper localization of Stt4p to the actin cytoskeleton.


:

Pssm-ID: 431193  Cd Length: 220  Bit Score: 156.65  E-value: 2.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528514086   19 PFTRLAVITVCLPLLGLVACIVLAMLYHYNDATYTHCQVPnyLPSISAAISLTPERYIWRFSIGLHSAPRFLVAAAYLSF 98
Cdd:pfam10277   1 NFSLLPLIAAILPLGGFIIVLIIAVVLGHVDPTFTHYGYN--FPYISDIGAYPPESCFFSIAINIGAFLRLAVAFLRYLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528514086   99 YRGRFSRRLTEQLLSGFTFLLALSENVGLLLLTYVSSTETYSVHKSGFILFIGSSLFHMLCTCKLwSLIVKYSISSEEMM 178
Cdd:pfam10277  79 LRPLARRSERVLRLNILALVFGLLGALGLSLVSNFQSTEDHSVHDIGAILFFVFGFIYMLLQTAL-SYRLGPHYTPKSRK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528514086  179 SYWFKLRLFLFNGGCCVLAVYFYRRHNTYCEEGIYTCFAVCEYLVVLSNMAFHMTAYWDFGGK 241
Cdd:pfam10277 158 SFRLKLVLLILAFVSAVAFIVFFIRHKKHCGYGAYSLSAIFEWLLALSFIFFFGTFAVDFKPI 220
 
Name Accession Description Interval E-value
Frag1 pfam10277
Frag1/DRAM/Sfk1 family; This family includes Frag1, DRAM and Sfk1 proteins. Frag1 (FGF ...
 19-241 2.42e-47

Frag1/DRAM/Sfk1 family; This family includes Frag1, DRAM and Sfk1 proteins. Frag1 (FGF receptor activating protein 1) is a protein that is conserved from fungi to humans. There are four potential iso-prenylation sites throughout the peptide, viz CILW, CIIW and CIGL. Frag1 is a membrane-spanning protein that is ubiquitously expressed in adult tissues suggesting an important cellular function. Dram is a family of proteins conserved from nematodes to humans with six hydrophobic transmembrane regions and an Endoplasmic Reticulum signal peptide. It is a lysosomal protein that induces macro-autophagy as an effector of p53-mediated death, where p53 is the tumour-suppressor gene that is frequently mutated in cancer. Expression of Dram is stress-induced. This region is also part of a family of small plasma membrane proteins, referred to as Sfk1, that may act together with or upstream of Stt4p to generate normal levels of the essential phospholipid PI4P, thus allowing proper localization of Stt4p to the actin cytoskeleton.


Pssm-ID: 431193  Cd Length: 220  Bit Score: 156.65  E-value: 2.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528514086   19 PFTRLAVITVCLPLLGLVACIVLAMLYHYNDATYTHCQVPnyLPSISAAISLTPERYIWRFSIGLHSAPRFLVAAAYLSF 98
Cdd:pfam10277   1 NFSLLPLIAAILPLGGFIIVLIIAVVLGHVDPTFTHYGYN--FPYISDIGAYPPESCFFSIAINIGAFLRLAVAFLRYLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528514086   99 YRGRFSRRLTEQLLSGFTFLLALSENVGLLLLTYVSSTETYSVHKSGFILFIGSSLFHMLCTCKLwSLIVKYSISSEEMM 178
Cdd:pfam10277  79 LRPLARRSERVLRLNILALVFGLLGALGLSLVSNFQSTEDHSVHDIGAILFFVFGFIYMLLQTAL-SYRLGPHYTPKSRK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528514086  179 SYWFKLRLFLFNGGCCVLAVYFYRRHNTYCEEGIYTCFAVCEYLVVLSNMAFHMTAYWDFGGK 241
Cdd:pfam10277 158 SFRLKLVLLILAFVSAVAFIVFFIRHKKHCGYGAYSLSAIFEWLLALSFIFFFGTFAVDFKPI 220
 
Name Accession Description Interval E-value
Frag1 pfam10277
Frag1/DRAM/Sfk1 family; This family includes Frag1, DRAM and Sfk1 proteins. Frag1 (FGF ...
 19-241 2.42e-47

Frag1/DRAM/Sfk1 family; This family includes Frag1, DRAM and Sfk1 proteins. Frag1 (FGF receptor activating protein 1) is a protein that is conserved from fungi to humans. There are four potential iso-prenylation sites throughout the peptide, viz CILW, CIIW and CIGL. Frag1 is a membrane-spanning protein that is ubiquitously expressed in adult tissues suggesting an important cellular function. Dram is a family of proteins conserved from nematodes to humans with six hydrophobic transmembrane regions and an Endoplasmic Reticulum signal peptide. It is a lysosomal protein that induces macro-autophagy as an effector of p53-mediated death, where p53 is the tumour-suppressor gene that is frequently mutated in cancer. Expression of Dram is stress-induced. This region is also part of a family of small plasma membrane proteins, referred to as Sfk1, that may act together with or upstream of Stt4p to generate normal levels of the essential phospholipid PI4P, thus allowing proper localization of Stt4p to the actin cytoskeleton.


Pssm-ID: 431193  Cd Length: 220  Bit Score: 156.65  E-value: 2.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528514086   19 PFTRLAVITVCLPLLGLVACIVLAMLYHYNDATYTHCQVPnyLPSISAAISLTPERYIWRFSIGLHSAPRFLVAAAYLSF 98
Cdd:pfam10277   1 NFSLLPLIAAILPLGGFIIVLIIAVVLGHVDPTFTHYGYN--FPYISDIGAYPPESCFFSIAINIGAFLRLAVAFLRYLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528514086   99 YRGRFSRRLTEQLLSGFTFLLALSENVGLLLLTYVSSTETYSVHKSGFILFIGSSLFHMLCTCKLwSLIVKYSISSEEMM 178
Cdd:pfam10277  79 LRPLARRSERVLRLNILALVFGLLGALGLSLVSNFQSTEDHSVHDIGAILFFVFGFIYMLLQTAL-SYRLGPHYTPKSRK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528514086  179 SYWFKLRLFLFNGGCCVLAVYFYRRHNTYCEEGIYTCFAVCEYLVVLSNMAFHMTAYWDFGGK 241
Cdd:pfam10277 158 SFRLKLVLLILAFVSAVAFIVFFIRHKKHCGYGAYSLSAIFEWLLALSFIFFFGTFAVDFKPI 220
 
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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