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Conserved domains on  [gi|1063717797|ref|NP_001326481|]
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sacI homology domain-containing protein / WW domain-containing protein [Arabidopsis thaliana]

Protein Classification

SAC family polyphosphoinositide phosphatase( domain architecture ID 1025587)

SAC family polyphosphoinositide phosphatase catalyzes the hydrolysis of phosphatidylinositol (PtdIns) phosphates, such as PtdIns(3)P, PtdIns(4)P, and/or PtdIns(3,5)P2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Syja_N super family cl38069
SacI homology domain; This Pfam family represents a protein domain which shows homology to the ...
 1-189 4.78e-27

SacI homology domain; This Pfam family represents a protein domain which shows homology to the yeast protein SacI. The SacI homology domain is most notably found at the amino terminal of the inositol 5'-phosphatase synaptojanin.


The actual alignment was detected with superfamily member pfam02383:

Pssm-ID: 460545  Cd Length: 295  Bit Score: 113.05  E-value: 4.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797    1 MKGFAEYR---PFGSSGQLegivALMARRSRLHPGTRYLARGINSCSGTGNEVECEQLVWIPKRNGQSIAFnSYIWRRGT 77
Cdd:pfam02383  132 IQGFVEQGklsVFGRSVTL----TLISRRSRKRAGTRYLRRGIDDDGNVANFVETEQIVSLNTSNSEGKIF-SFVQIRGS 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797   78 IPIWWGAE--LKMTAAeaeIYVADRDPYKGSTE-YYQRLSKRYDtrnldapvgenqkkkafvPIVCVNLL-RSGegkSEC 153
Cdd:pfam02383  207 IPLFWSQDpnLKYKPK---IQITRPEATQPAFKkHFDDLIERYG------------------PVHIVNLVeKKG---RES 262

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1063717797  154 ILVQHFEESMNFIKSSgklPYTRVHLINYDWHASVK 189
Cdd:pfam02383  263 KLSEAYEEAVKYLNQF---LPDKLRYTAFDFHHECK 295
COG5329 super family cl34984
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
3-453 7.13e-19

Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5329:

Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 92.45  E-value: 7.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797    3 GFAEYRPFGSSGQLEGIvALMARRSRLHPGTRYLARGINSCSGTGNEVECEQLVWIPKRngqsiaFNSYIWRRGTIPIWW 82
Cdd:COG5329    199 GFAETVDIKVGGNTISL-TLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQY------IFSFTQVRGSIPLFW 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797   83 GAELKMTAAEAEIYVADRDPYKGSTEYYQRLSKRYDtrnldapvgenqkkkafvPIVCVNLLrsGEGKSECILVQHFEES 162
Cdd:COG5329    272 EQSNLLYGPKIKVTRSSEAAQSAFDKHFDKLREKYG------------------DVYVVNLL--KTKGYEAPLLELYEKH 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797  163 mnfIKSSGKLPytrVHLINYDWHASVKlKGEQQTIEGLWMYLKSptmaiGISEGDYLPSRQRlkdcRGEVIciddiegaf 242
Cdd:COG5329    332 ---LDLSKKPK---IHYTEFDFHKETS-QDGFDDVKKLLYLIEQ-----DLLEFGYFAYDIN----EGKSI--------- 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797  243 clrSHQNGVIRFNCADSLDRTNAASFFGGlQVFVEQCRRLGISLDTDlgyghnsvnnqggynaplPPGWEKradavtgks 322
Cdd:COG5329    387 ---SEQDGVFRTNCLDCLDRTNVIQSLIS-RVLLEQFRSEGVISDGY------------------SPFLQI--------- 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797  323 yyidHNTktttwshpcpdkpwkrldmrfeefkrstilspvseladLFLQQGDIHATLYTGSKAMHSqilnifSEESGAFK 402
Cdd:COG5329    436 ----HRE--------------------------------------LWADNGDAISRLYTGTGALKS------SFTRRGRR 467

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063717797  403 QFSAAQKNMKITLQRRYKNAMVDSSRQKQLEMFLGMrlFKHLPSIPVQPLH 453
Cdd:COG5329    468 SFAGALNDFIKSFSRYYINNFTDGQRQDAIDLLLGK--FRPQEAFSYRPLR 516
 
Name Accession Description Interval E-value
Syja_N pfam02383
SacI homology domain; This Pfam family represents a protein domain which shows homology to the ...
 1-189 4.78e-27

SacI homology domain; This Pfam family represents a protein domain which shows homology to the yeast protein SacI. The SacI homology domain is most notably found at the amino terminal of the inositol 5'-phosphatase synaptojanin.


Pssm-ID: 460545  Cd Length: 295  Bit Score: 113.05  E-value: 4.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797    1 MKGFAEYR---PFGSSGQLegivALMARRSRLHPGTRYLARGINSCSGTGNEVECEQLVWIPKRNGQSIAFnSYIWRRGT 77
Cdd:pfam02383  132 IQGFVEQGklsVFGRSVTL----TLISRRSRKRAGTRYLRRGIDDDGNVANFVETEQIVSLNTSNSEGKIF-SFVQIRGS 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797   78 IPIWWGAE--LKMTAAeaeIYVADRDPYKGSTE-YYQRLSKRYDtrnldapvgenqkkkafvPIVCVNLL-RSGegkSEC 153
Cdd:pfam02383  207 IPLFWSQDpnLKYKPK---IQITRPEATQPAFKkHFDDLIERYG------------------PVHIVNLVeKKG---RES 262

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1063717797  154 ILVQHFEESMNFIKSSgklPYTRVHLINYDWHASVK 189
Cdd:pfam02383  263 KLSEAYEEAVKYLNQF---LPDKLRYTAFDFHHECK 295
COG5329 COG5329
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
3-453 7.13e-19

Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];


Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 92.45  E-value: 7.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797    3 GFAEYRPFGSSGQLEGIvALMARRSRLHPGTRYLARGINSCSGTGNEVECEQLVWIPKRngqsiaFNSYIWRRGTIPIWW 82
Cdd:COG5329    199 GFAETVDIKVGGNTISL-TLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQY------IFSFTQVRGSIPLFW 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797   83 GAELKMTAAEAEIYVADRDPYKGSTEYYQRLSKRYDtrnldapvgenqkkkafvPIVCVNLLrsGEGKSECILVQHFEES 162
Cdd:COG5329    272 EQSNLLYGPKIKVTRSSEAAQSAFDKHFDKLREKYG------------------DVYVVNLL--KTKGYEAPLLELYEKH 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797  163 mnfIKSSGKLPytrVHLINYDWHASVKlKGEQQTIEGLWMYLKSptmaiGISEGDYLPSRQRlkdcRGEVIciddiegaf 242
Cdd:COG5329    332 ---LDLSKKPK---IHYTEFDFHKETS-QDGFDDVKKLLYLIEQ-----DLLEFGYFAYDIN----EGKSI--------- 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797  243 clrSHQNGVIRFNCADSLDRTNAASFFGGlQVFVEQCRRLGISLDTDlgyghnsvnnqggynaplPPGWEKradavtgks 322
Cdd:COG5329    387 ---SEQDGVFRTNCLDCLDRTNVIQSLIS-RVLLEQFRSEGVISDGY------------------SPFLQI--------- 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797  323 yyidHNTktttwshpcpdkpwkrldmrfeefkrstilspvseladLFLQQGDIHATLYTGSKAMHSqilnifSEESGAFK 402
Cdd:COG5329    436 ----HRE--------------------------------------LWADNGDAISRLYTGTGALKS------SFTRRGRR 467

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063717797  403 QFSAAQKNMKITLQRRYKNAMVDSSRQKQLEMFLGMrlFKHLPSIPVQPLH 453
Cdd:COG5329    468 SFAGALNDFIKSFSRYYINNFTDGQRQDAIDLLLGK--FRPQEAFSYRPLR 516
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 306-337 2.71e-10

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 56.46  E-value: 2.71e-10
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1063717797   306 PLPPGWEKRADAvTGKSYYIDHNTKTTTWSHP 337
Cdd:smart00456    1 PLPPGWEERKDP-DGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 308-339 2.90e-10

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 56.38  E-value: 2.90e-10
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1063717797  308 PPGWEKRADAvTGKSYYIDHNTKTTTWSHPCP 339
Cdd:cd00201      1 PPGWEERWDP-DGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 307-337 5.42e-10

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 55.59  E-value: 5.42e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1063717797  307 LPPGWEKRADAvTGKSYYIDHNTKTTTWSHP 337
Cdd:pfam00397    1 LPPGWEERWDP-DGRVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
Syja_N pfam02383
SacI homology domain; This Pfam family represents a protein domain which shows homology to the ...
 1-189 4.78e-27

SacI homology domain; This Pfam family represents a protein domain which shows homology to the yeast protein SacI. The SacI homology domain is most notably found at the amino terminal of the inositol 5'-phosphatase synaptojanin.


Pssm-ID: 460545  Cd Length: 295  Bit Score: 113.05  E-value: 4.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797    1 MKGFAEYR---PFGSSGQLegivALMARRSRLHPGTRYLARGINSCSGTGNEVECEQLVWIPKRNGQSIAFnSYIWRRGT 77
Cdd:pfam02383  132 IQGFVEQGklsVFGRSVTL----TLISRRSRKRAGTRYLRRGIDDDGNVANFVETEQIVSLNTSNSEGKIF-SFVQIRGS 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797   78 IPIWWGAE--LKMTAAeaeIYVADRDPYKGSTE-YYQRLSKRYDtrnldapvgenqkkkafvPIVCVNLL-RSGegkSEC 153
Cdd:pfam02383  207 IPLFWSQDpnLKYKPK---IQITRPEATQPAFKkHFDDLIERYG------------------PVHIVNLVeKKG---RES 262

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1063717797  154 ILVQHFEESMNFIKSSgklPYTRVHLINYDWHASVK 189
Cdd:pfam02383  263 KLSEAYEEAVKYLNQF---LPDKLRYTAFDFHHECK 295
COG5329 COG5329
Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];
3-453 7.13e-19

Phosphoinositide polyphosphatase (Sac family) [Signal transduction mechanisms];


Pssm-ID: 227637 [Multi-domain]  Cd Length: 570  Bit Score: 92.45  E-value: 7.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797    3 GFAEYRPFGSSGQLEGIvALMARRSRLHPGTRYLARGINSCSGTGNEVECEQLVWIPKRngqsiaFNSYIWRRGTIPIWW 82
Cdd:COG5329    199 GFAETVDIKVGGNTISL-TLISRRSSERAGTRYLSRGIDDDGNVSNFVETEQIVTDSQY------IFSFTQVRGSIPLFW 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797   83 GAELKMTAAEAEIYVADRDPYKGSTEYYQRLSKRYDtrnldapvgenqkkkafvPIVCVNLLrsGEGKSECILVQHFEES 162
Cdd:COG5329    272 EQSNLLYGPKIKVTRSSEAAQSAFDKHFDKLREKYG------------------DVYVVNLL--KTKGYEAPLLELYEKH 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797  163 mnfIKSSGKLPytrVHLINYDWHASVKlKGEQQTIEGLWMYLKSptmaiGISEGDYLPSRQRlkdcRGEVIciddiegaf 242
Cdd:COG5329    332 ---LDLSKKPK---IHYTEFDFHKETS-QDGFDDVKKLLYLIEQ-----DLLEFGYFAYDIN----EGKSI--------- 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797  243 clrSHQNGVIRFNCADSLDRTNAASFFGGlQVFVEQCRRLGISLDTDlgyghnsvnnqggynaplPPGWEKradavtgks 322
Cdd:COG5329    387 ---SEQDGVFRTNCLDCLDRTNVIQSLIS-RVLLEQFRSEGVISDGY------------------SPFLQI--------- 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717797  323 yyidHNTktttwshpcpdkpwkrldmrfeefkrstilspvseladLFLQQGDIHATLYTGSKAMHSqilnifSEESGAFK 402
Cdd:COG5329    436 ----HRE--------------------------------------LWADNGDAISRLYTGTGALKS------SFTRRGRR 467

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063717797  403 QFSAAQKNMKITLQRRYKNAMVDSSRQKQLEMFLGMrlFKHLPSIPVQPLH 453
Cdd:COG5329    468 SFAGALNDFIKSFSRYYINNFTDGQRQDAIDLLLGK--FRPQEAFSYRPLR 516
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 306-337 2.71e-10

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 56.46  E-value: 2.71e-10
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1063717797   306 PLPPGWEKRADAvTGKSYYIDHNTKTTTWSHP 337
Cdd:smart00456    1 PLPPGWEERKDP-DGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 308-339 2.90e-10

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 56.38  E-value: 2.90e-10
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1063717797  308 PPGWEKRADAvTGKSYYIDHNTKTTTWSHPCP 339
Cdd:cd00201      1 PPGWEERWDP-DGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 307-337 5.42e-10

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 55.59  E-value: 5.42e-10
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1063717797  307 LPPGWEKRADAvTGKSYYIDHNTKTTTWSHP 337
Cdd:pfam00397    1 LPPGWEERWDP-DGRVYYYNHETGETQWEKP 30
 
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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