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Conserved domains on  [gi|119657520|gb|ABL86758|]
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phytase [Bacillus subtilis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Phytase super family cl17685
Phytase; Phytase is a secreted enzyme which hydrolyses phytate to release inorganic phosphate. ...
5-380 0e+00

Phytase; Phytase is a secreted enzyme which hydrolyses phytate to release inorganic phosphate. This family appears to represent a novel enzyme that shows phytase activity and has been shown to have a six- bladed propeller folding architecture.


The actual alignment was detected with superfamily member pfam02333:

Pssm-ID: 473085  Cd Length: 375  Bit Score: 583.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520    5 KTLLLTAAAGLMLTCGAvSSQAKHKLSDPYHFTVNAAAETEPVDTAGDAADDPAIWLDPKNPQNSKLITTNKKSGLVVYS 84
Cdd:pfam02333   1 KTRILSTAALSLLSPAA-AGLSVAEASALQSFRVTASAETDPVASGDDAADDPAIWVHPKDPEKSMLITTNKKSGLLVYD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520   85 LEGKMLHSYPTGKLNNVDIRYDFPLNGKKVDIAAASNRSEGKNTIEIYAIDGKNGTLQSITDPDRPIASAIDEVYGFSLY 164
Cdd:pfam02333  80 LNGKQLYSYEFGKLNNVDLRYGFPLAGQKIDIAAASNRSEGKNTIEIYAIDGSKGKLKAISGPNTPIVTSISEVYGFSLY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520  165 HSQKTGKYYAMVTGKEGEFEQYELNADKNGYISGKKVRAFKMNSQTEGMAADDEYGSLYIAEEDEAIWKFSAEPDGGSNG 244
Cdd:pfam02333 160 HSQKTGKFYALVTGKEGEFEQYELFDNGKGAVDGKKVREFKLASQTEGLVADDEYGRLYIAEEDAAIWLFGAEPGGGDKG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520  245 TVIDRADGRHLTPDIEGLTIYYAADGKGYLLASSQGNSSYAIYERQGQNKYVADFQITDGPETDGTSDTDGIDVLGFGLG 324
Cdd:pfam02333 240 ETVDRADGVHLTADIEGLTIYYAEDGEGYLIASSQGSNSYAVYDREGKNEYVASFVIADGPGIDGTSDTDGIDVLGFGLG 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119657520  325 PEYPFGFFVAQDGENIDHGQKANQNFKMVPWERIADKIGFHPQVNKQVDPRKMTDR 380
Cdd:pfam02333 320 SKYPYGIFVAQDGENLQNGQVINQNFKIVSWEAIADALGDDPDVDNQVNPRKLKYR 375
 
Name Accession Description Interval E-value
Phytase pfam02333
Phytase; Phytase is a secreted enzyme which hydrolyses phytate to release inorganic phosphate. ...
5-380 0e+00

Phytase; Phytase is a secreted enzyme which hydrolyses phytate to release inorganic phosphate. This family appears to represent a novel enzyme that shows phytase activity and has been shown to have a six- bladed propeller folding architecture.


Pssm-ID: 280491  Cd Length: 375  Bit Score: 583.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520    5 KTLLLTAAAGLMLTCGAvSSQAKHKLSDPYHFTVNAAAETEPVDTAGDAADDPAIWLDPKNPQNSKLITTNKKSGLVVYS 84
Cdd:pfam02333   1 KTRILSTAALSLLSPAA-AGLSVAEASALQSFRVTASAETDPVASGDDAADDPAIWVHPKDPEKSMLITTNKKSGLLVYD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520   85 LEGKMLHSYPTGKLNNVDIRYDFPLNGKKVDIAAASNRSEGKNTIEIYAIDGKNGTLQSITDPDRPIASAIDEVYGFSLY 164
Cdd:pfam02333  80 LNGKQLYSYEFGKLNNVDLRYGFPLAGQKIDIAAASNRSEGKNTIEIYAIDGSKGKLKAISGPNTPIVTSISEVYGFSLY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520  165 HSQKTGKYYAMVTGKEGEFEQYELNADKNGYISGKKVRAFKMNSQTEGMAADDEYGSLYIAEEDEAIWKFSAEPDGGSNG 244
Cdd:pfam02333 160 HSQKTGKFYALVTGKEGEFEQYELFDNGKGAVDGKKVREFKLASQTEGLVADDEYGRLYIAEEDAAIWLFGAEPGGGDKG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520  245 TVIDRADGRHLTPDIEGLTIYYAADGKGYLLASSQGNSSYAIYERQGQNKYVADFQITDGPETDGTSDTDGIDVLGFGLG 324
Cdd:pfam02333 240 ETVDRADGVHLTADIEGLTIYYAEDGEGYLIASSQGSNSYAVYDREGKNEYVASFVIADGPGIDGTSDTDGIDVLGFGLG 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119657520  325 PEYPFGFFVAQDGENIDHGQKANQNFKMVPWERIADKIGFHPQVNKQVDPRKMTDR 380
Cdd:pfam02333 320 SKYPYGIFVAQDGENLQNGQVINQNFKIVSWEAIADALGDDPDVDNQVNPRKLKYR 375
Phy COG4247
3-phytase (myo-inositol-hexaphosphate 3-phosphohydrolase) [Lipid transport and metabolism];
4-363 3.37e-168

3-phytase (myo-inositol-hexaphosphate 3-phosphohydrolase) [Lipid transport and metabolism];


Pssm-ID: 443389  Cd Length: 348  Bit Score: 473.59  E-value: 3.37e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520   4 SKTLLLTAAAGLMLT-CGAVSSQAKHKlsdpyhfTVNAAAETEPVDTAGDAADDPAIWLDPKNPQNSKLITTNKKSGLVV 82
Cdd:COG4247    2 KKLLTLLALALLLLAaCAASAQPAPLP-------AVTATVETEPVAGGGDAADDPAIWVNPADPAKSLVLGTDKKGGLYV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520  83 YSLEGKMLHSYPTGKLNNVDIRYDFPLNGKKVDIAAASNRseGKNTIEIYAIDGKNGTLQSITDpdrpIASAIDEVYGFS 162
Cdd:COG4247   75 YDLDGKILQFLPVGRPNNVDVRYGFKLGGKTVDLAVASDR--TNNKLRLFRIDPDTGPLTDLGG----IPTGLREPYGLC 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520 163 LYHSQKTGKYYAMVTGKEGEFEQYELNADKNGYISGKKVRAFKMNSQTEGMAADDEYGSLYIAEEDEAIWKFSAEPDGGS 242
Cdd:COG4247  149 LYKSPKDGKLYAFVNRKDGRVAQYRLVDDGGGKVTATLVRTFGLPSQPEGCVVDDETGYLYVGEEDVGIWKYDADPDAGK 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520 243 NGTVIDRADGRHLTPDIEGLTIYYAADGKGYLLASSQGNSSYAIYERQGQNKYVADFQITDGPETDGTSDTDGIDVLGFG 322
Cdd:COG4247  229 GGELIAAVGGGGLVADVEGLAIYYGGDGTGYLLASSQGDNTFAVYDREGPNAYVGSFRIGADGGIDGVSETDGLDVTSVP 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 119657520 323 LGPEYPFGFFVAQDGENIDhgqkANQNFKMVPWERIADKIG 363
Cdd:COG4247  309 LGPGFPNGLFVVQDGRNRP----PNQNFKLVDWEDIAAALG 345
 
Name Accession Description Interval E-value
Phytase pfam02333
Phytase; Phytase is a secreted enzyme which hydrolyses phytate to release inorganic phosphate. ...
5-380 0e+00

Phytase; Phytase is a secreted enzyme which hydrolyses phytate to release inorganic phosphate. This family appears to represent a novel enzyme that shows phytase activity and has been shown to have a six- bladed propeller folding architecture.


Pssm-ID: 280491  Cd Length: 375  Bit Score: 583.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520    5 KTLLLTAAAGLMLTCGAvSSQAKHKLSDPYHFTVNAAAETEPVDTAGDAADDPAIWLDPKNPQNSKLITTNKKSGLVVYS 84
Cdd:pfam02333   1 KTRILSTAALSLLSPAA-AGLSVAEASALQSFRVTASAETDPVASGDDAADDPAIWVHPKDPEKSMLITTNKKSGLLVYD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520   85 LEGKMLHSYPTGKLNNVDIRYDFPLNGKKVDIAAASNRSEGKNTIEIYAIDGKNGTLQSITDPDRPIASAIDEVYGFSLY 164
Cdd:pfam02333  80 LNGKQLYSYEFGKLNNVDLRYGFPLAGQKIDIAAASNRSEGKNTIEIYAIDGSKGKLKAISGPNTPIVTSISEVYGFSLY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520  165 HSQKTGKYYAMVTGKEGEFEQYELNADKNGYISGKKVRAFKMNSQTEGMAADDEYGSLYIAEEDEAIWKFSAEPDGGSNG 244
Cdd:pfam02333 160 HSQKTGKFYALVTGKEGEFEQYELFDNGKGAVDGKKVREFKLASQTEGLVADDEYGRLYIAEEDAAIWLFGAEPGGGDKG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520  245 TVIDRADGRHLTPDIEGLTIYYAADGKGYLLASSQGNSSYAIYERQGQNKYVADFQITDGPETDGTSDTDGIDVLGFGLG 324
Cdd:pfam02333 240 ETVDRADGVHLTADIEGLTIYYAEDGEGYLIASSQGSNSYAVYDREGKNEYVASFVIADGPGIDGTSDTDGIDVLGFGLG 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119657520  325 PEYPFGFFVAQDGENIDHGQKANQNFKMVPWERIADKIGFHPQVNKQVDPRKMTDR 380
Cdd:pfam02333 320 SKYPYGIFVAQDGENLQNGQVINQNFKIVSWEAIADALGDDPDVDNQVNPRKLKYR 375
Phy COG4247
3-phytase (myo-inositol-hexaphosphate 3-phosphohydrolase) [Lipid transport and metabolism];
4-363 3.37e-168

3-phytase (myo-inositol-hexaphosphate 3-phosphohydrolase) [Lipid transport and metabolism];


Pssm-ID: 443389  Cd Length: 348  Bit Score: 473.59  E-value: 3.37e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520   4 SKTLLLTAAAGLMLT-CGAVSSQAKHKlsdpyhfTVNAAAETEPVDTAGDAADDPAIWLDPKNPQNSKLITTNKKSGLVV 82
Cdd:COG4247    2 KKLLTLLALALLLLAaCAASAQPAPLP-------AVTATVETEPVAGGGDAADDPAIWVNPADPAKSLVLGTDKKGGLYV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520  83 YSLEGKMLHSYPTGKLNNVDIRYDFPLNGKKVDIAAASNRseGKNTIEIYAIDGKNGTLQSITDpdrpIASAIDEVYGFS 162
Cdd:COG4247   75 YDLDGKILQFLPVGRPNNVDVRYGFKLGGKTVDLAVASDR--TNNKLRLFRIDPDTGPLTDLGG----IPTGLREPYGLC 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520 163 LYHSQKTGKYYAMVTGKEGEFEQYELNADKNGYISGKKVRAFKMNSQTEGMAADDEYGSLYIAEEDEAIWKFSAEPDGGS 242
Cdd:COG4247  149 LYKSPKDGKLYAFVNRKDGRVAQYRLVDDGGGKVTATLVRTFGLPSQPEGCVVDDETGYLYVGEEDVGIWKYDADPDAGK 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119657520 243 NGTVIDRADGRHLTPDIEGLTIYYAADGKGYLLASSQGNSSYAIYERQGQNKYVADFQITDGPETDGTSDTDGIDVLGFG 322
Cdd:COG4247  229 GGELIAAVGGGGLVADVEGLAIYYGGDGTGYLLASSQGDNTFAVYDREGPNAYVGSFRIGADGGIDGVSETDGLDVTSVP 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 119657520 323 LGPEYPFGFFVAQDGENIDhgqkANQNFKMVPWERIADKIG 363
Cdd:COG4247  309 LGPGFPNGLFVVQDGRNRP----PNQNFKLVDWEDIAAALG 345
 
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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