NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|330251200|gb|AEC06294|]
View 

proline iminopeptidase [Arabidopsis thaliana]

Protein Classification

alpha/beta hydrolase; tannase/feruloyl esterase family alpha/beta hydrolase( domain architecture ID 10796800)

uncharacterized alpha/beta hydrolase; may catalyze the cleavage and formation of ester bonds| tannase/feruloyl esterase family alpha/beta hydrolase similar to Aspergillus oryzae tannase and Aspergillus niger feruloyl esterase B

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
pro_imino_pep_1 TIGR01249
proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related ...
 19-325 0e+00

proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related families of proline iminopeptidase in the alpha/beta fold hydrolase family. The fine specificities of the various members, including both the range of short peptides from which proline can be removed and whether other amino acids such as alanine can be also removed, may vary among members.


:

Pssm-ID: 130316 [Multi-domain]  Cd Length: 306  Bit Score: 589.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200   19 IEPYSSGNLKVSDVHTLYWEQSGKPDGHPVVFLHGGPGGGTAPSNRRFFDPEFYRIVLFDQRGAGKSTPHACLEENTTWD 98
Cdd:TIGR01249   1 TKPFVSGYLNVSDNHQLYYEQSGNPDGKPVVFLHGGPGSGTDPGCRRFFDPETYRIVLFDQRGCGKSTPHACLEENTTWD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200   99 LVNDIEKLREHLKIPEWLVFGGSWGSTLALAYSQSHPDKVTGLVLRGIFLLRKKEIDWFYEGGAAAIYPDAWEEFRDLIP 178
Cdd:TIGR01249  81 LVADIEKLREKLGIKNWLVFGGSWGSTLALAYAQTHPEVVTGLVLRGIFLLREKEWSWFYEGGASMIYPDAWQRFMDSIP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  179 ENERGSSLVDAYHKRLNSDDLEIQYAAARAWTKWEmMTAYLRPNLENVQKAEDDKFSLAFARIENHYFVNKGFFPSDSHL 258
Cdd:TIGR01249 161 ENERNEQLVNAYHDRLQSGDEETKLAAAKAWVDWE-STTLLRPINEIVSTAEDFKFSLAFARLENHYFVNKGFLDVENFI 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330251200  259 LDNVDKIRHIKTTIVQGRYDVCCPMMSAWDLHKAWPEAELKIVYDAGHSANEPGISAELVVANEKMK 325
Cdd:TIGR01249 240 LDNISKIRNIPTYIVHGRYDLCCPLQSAWALHKAFPEAELKVTNNAGHSAFDPNNLAALVHALETYL 306
 
Name Accession Description Interval E-value
pro_imino_pep_1 TIGR01249
proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related ...
 19-325 0e+00

proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related families of proline iminopeptidase in the alpha/beta fold hydrolase family. The fine specificities of the various members, including both the range of short peptides from which proline can be removed and whether other amino acids such as alanine can be also removed, may vary among members.


Pssm-ID: 130316 [Multi-domain]  Cd Length: 306  Bit Score: 589.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200   19 IEPYSSGNLKVSDVHTLYWEQSGKPDGHPVVFLHGGPGGGTAPSNRRFFDPEFYRIVLFDQRGAGKSTPHACLEENTTWD 98
Cdd:TIGR01249   1 TKPFVSGYLNVSDNHQLYYEQSGNPDGKPVVFLHGGPGSGTDPGCRRFFDPETYRIVLFDQRGCGKSTPHACLEENTTWD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200   99 LVNDIEKLREHLKIPEWLVFGGSWGSTLALAYSQSHPDKVTGLVLRGIFLLRKKEIDWFYEGGAAAIYPDAWEEFRDLIP 178
Cdd:TIGR01249  81 LVADIEKLREKLGIKNWLVFGGSWGSTLALAYAQTHPEVVTGLVLRGIFLLREKEWSWFYEGGASMIYPDAWQRFMDSIP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  179 ENERGSSLVDAYHKRLNSDDLEIQYAAARAWTKWEmMTAYLRPNLENVQKAEDDKFSLAFARIENHYFVNKGFFPSDSHL 258
Cdd:TIGR01249 161 ENERNEQLVNAYHDRLQSGDEETKLAAAKAWVDWE-STTLLRPINEIVSTAEDFKFSLAFARLENHYFVNKGFLDVENFI 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330251200  259 LDNVDKIRHIKTTIVQGRYDVCCPMMSAWDLHKAWPEAELKIVYDAGHSANEPGISAELVVANEKMK 325
Cdd:TIGR01249 240 LDNISKIRNIPTYIVHGRYDLCCPLQSAWALHKAFPEAELKVTNNAGHSAFDPNNLAALVHALETYL 306
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 47-312 1.02e-31

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 119.15  E-value: 1.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200   47 PVVFLHGGPGGGTAPsnrRFFDPEF----YRIVLFDQRGAGKSTPHACLEENTTWDLVNDIEKLREHLKIPEWLVFGGSW 122
Cdd:pfam00561   2 PVLLLHGLPGSSDLW---RKLAPALardgFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  123 GSTLALAYSQSHPDKVTGLVLRGIFLLRKKEIDWFYegGAAAIYPDAWEEFRDLIPENeRGSSLVDAYHKRLNSDDLEIQ 202
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADR--FILALFPGFFDGFVADFAPN-PLGRLVAKLLALLLLRLRLLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  203 YAAARAWTKWEMmtaYLRPNLENVQKAeddkfSLAFARIENHYFvnkgffpsdSHLLDNVDKirhiKTTIVQGRYDVCCP 282
Cdd:pfam00561 156 ALPLLNKRFPSG---DYALAKSLVTGA-----LLFIETWSTELR---------AKFLGRLDE----PTLIIWGDQDPLVP 214

                         250       260       270
                  ....*....|....*....|....*....|
gi 330251200  283 MMSAWDLHKAWPEAELKIVYDAGHSANEPG 312
Cdd:pfam00561 215 PQALEKLAQLFPNARLVVIPDAGHFAFLEG 244
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 31-310 1.13e-28

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 110.09  E-value: 1.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  31 DVHTLYWEQSGkPDGHPVVFLHGGPGGGTAPsnRRFFDP--EFYRIVLFDQRGAGKSTPHAclEENTTWDLVNDIEKLRE 108
Cdd:COG0596   10 DGVRLHYREAG-PDGPPVVLLHGLPGSSYEW--RPLIPAlaAGYRVIAPDLRGHGRSDKPA--GGYTLDDLADDLAALLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200 109 HLKIPEWLVFGGSWGSTLALAYSQSHPDKVTGLVLRGifllrkkeidwfyeggaaaiypDAWEEFRDLIpenergsslvd 188
Cdd:COG0596   85 ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD----------------------EVLAALAEPL----------- 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200 189 ayhkRLNSDDLEIQYAAARAWTKWEmmtayLRPNLENVQkaeddkfslafarienhyfvnkgffpsdshlldnvdkirhI 268
Cdd:COG0596  132 ----RRPGLAPEALAALLRALARTD-----LRERLARIT----------------------------------------V 162

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 330251200 269 KTTIVQGRYDVCCPMMSAWDLHKAWPEAELKIVYDAGHSANE 310
Cdd:COG0596  163 PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPL 204
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 31-143 1.54e-05

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 46.09  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  31 DVHTLYWEQSGKPDGHPVVFLHGGPGGGtapSNRRF-FDP--EFYRIVLFDQRGAGKSTPHacLEENTTWDLVNDIEKLR 107
Cdd:PRK14875 117 GGRTVRYLRLGEGDGTPVVLIHGFGGDL---NNWLFnHAAlaAGRPVIALDLPGHGASSKA--VGAGSLDELAAAVLAFL 191

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 330251200 108 EHLKIPEWLVFGGSWGSTLALAYSQSHPDKVTGLVL 143
Cdd:PRK14875 192 DALGIERAHLVGHSMGGAVALRLAARAPQRVASLTL 227
 
Name Accession Description Interval E-value
pro_imino_pep_1 TIGR01249
proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related ...
 19-325 0e+00

proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related families of proline iminopeptidase in the alpha/beta fold hydrolase family. The fine specificities of the various members, including both the range of short peptides from which proline can be removed and whether other amino acids such as alanine can be also removed, may vary among members.


Pssm-ID: 130316 [Multi-domain]  Cd Length: 306  Bit Score: 589.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200   19 IEPYSSGNLKVSDVHTLYWEQSGKPDGHPVVFLHGGPGGGTAPSNRRFFDPEFYRIVLFDQRGAGKSTPHACLEENTTWD 98
Cdd:TIGR01249   1 TKPFVSGYLNVSDNHQLYYEQSGNPDGKPVVFLHGGPGSGTDPGCRRFFDPETYRIVLFDQRGCGKSTPHACLEENTTWD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200   99 LVNDIEKLREHLKIPEWLVFGGSWGSTLALAYSQSHPDKVTGLVLRGIFLLRKKEIDWFYEGGAAAIYPDAWEEFRDLIP 178
Cdd:TIGR01249  81 LVADIEKLREKLGIKNWLVFGGSWGSTLALAYAQTHPEVVTGLVLRGIFLLREKEWSWFYEGGASMIYPDAWQRFMDSIP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  179 ENERGSSLVDAYHKRLNSDDLEIQYAAARAWTKWEmMTAYLRPNLENVQKAEDDKFSLAFARIENHYFVNKGFFPSDSHL 258
Cdd:TIGR01249 161 ENERNEQLVNAYHDRLQSGDEETKLAAAKAWVDWE-STTLLRPINEIVSTAEDFKFSLAFARLENHYFVNKGFLDVENFI 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330251200  259 LDNVDKIRHIKTTIVQGRYDVCCPMMSAWDLHKAWPEAELKIVYDAGHSANEPGISAELVVANEKMK 325
Cdd:TIGR01249 240 LDNISKIRNIPTYIVHGRYDLCCPLQSAWALHKAFPEAELKVTNNAGHSAFDPNNLAALVHALETYL 306
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 47-312 1.02e-31

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 119.15  E-value: 1.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200   47 PVVFLHGGPGGGTAPsnrRFFDPEF----YRIVLFDQRGAGKSTPHACLEENTTWDLVNDIEKLREHLKIPEWLVFGGSW 122
Cdd:pfam00561   2 PVLLLHGLPGSSDLW---RKLAPALardgFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  123 GSTLALAYSQSHPDKVTGLVLRGIFLLRKKEIDWFYegGAAAIYPDAWEEFRDLIPENeRGSSLVDAYHKRLNSDDLEIQ 202
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADR--FILALFPGFFDGFVADFAPN-PLGRLVAKLLALLLLRLRLLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  203 YAAARAWTKWEMmtaYLRPNLENVQKAeddkfSLAFARIENHYFvnkgffpsdSHLLDNVDKirhiKTTIVQGRYDVCCP 282
Cdd:pfam00561 156 ALPLLNKRFPSG---DYALAKSLVTGA-----LLFIETWSTELR---------AKFLGRLDE----PTLIIWGDQDPLVP 214

                         250       260       270
                  ....*....|....*....|....*....|
gi 330251200  283 MMSAWDLHKAWPEAELKIVYDAGHSANEPG 312
Cdd:pfam00561 215 PQALEKLAQLFPNARLVVIPDAGHFAFLEG 244
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 31-310 1.13e-28

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 110.09  E-value: 1.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  31 DVHTLYWEQSGkPDGHPVVFLHGGPGGGTAPsnRRFFDP--EFYRIVLFDQRGAGKSTPHAclEENTTWDLVNDIEKLRE 108
Cdd:COG0596   10 DGVRLHYREAG-PDGPPVVLLHGLPGSSYEW--RPLIPAlaAGYRVIAPDLRGHGRSDKPA--GGYTLDDLADDLAALLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200 109 HLKIPEWLVFGGSWGSTLALAYSQSHPDKVTGLVLRGifllrkkeidwfyeggaaaiypDAWEEFRDLIpenergsslvd 188
Cdd:COG0596   85 ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD----------------------EVLAALAEPL----------- 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200 189 ayhkRLNSDDLEIQYAAARAWTKWEmmtayLRPNLENVQkaeddkfslafarienhyfvnkgffpsdshlldnvdkirhI 268
Cdd:COG0596  132 ----RRPGLAPEALAALLRALARTD-----LRERLARIT----------------------------------------V 162

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 330251200 269 KTTIVQGRYDVCCPMMSAWDLHKAWPEAELKIVYDAGHSANE 310
Cdd:COG0596  163 PTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPL 204
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 22-143 1.15e-11

proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase


Pssm-ID: 188121 [Multi-domain]  Cd Length: 289  Bit Score: 64.32  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200   22 YSSGNLKVSDVHTLYWEQSGKPDGHPVVFLHGGPGGgtaPSN-----RRFFDPEFYRIVLFDQRGAGKST-PHACLEENT 95
Cdd:TIGR01250   2 QIEGIITVDGGYHLFTKTGGEGEKIKLLLLHGGPGM---SHEylenlRELLKEEGREVIMYDQLGCGYSDqPDDSDEELW 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 330251200   96 TWD-LVNDIEKLREHLKIPEWLVFGGSWGSTLALAYSQSHPDKVTGLVL 143
Cdd:TIGR01250  79 TIDyFVDELEEVREKLGLDKFYLLGHSWGGMLAQEYALKYGQHLKGLII 127
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
27-209 2.44e-11

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 62.33  E-value: 2.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  27 LKVSDVHTLY---WEQSGKPDGhPVVFLHGGpgggtAPSNRRFFD--PEF----YRIVLFDQRGAGKSTPHacLEENTTW 97
Cdd:COG2267    8 LPTRDGLRLRgrrWRPAGSPRG-TVVLVHGL-----GEHSGRYAElaEALaaagYAVLAFDLRGHGRSDGP--RGHVDSF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  98 -DLVNDIEKLREHLKIP---EWLVFGGSWGSTLALAYSQSHPDKVTGLVLRGIFLLRKKEI----DWFYEGGAAA----- 164
Cdd:COG2267   80 dDYVDDLRAALDALRARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLgpsaRWLRALRLAEalari 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 330251200 165 --------------IYPDAWEEFRDLIPENERGSSLVDAYHKRLNSDDLEIQYAAARAW 209
Cdd:COG2267  160 dvpvlvlhggadrvVPPEAARRLAARLSPDVELVLLPGARHELLNEPAREEVLAAILAW 218
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 41-143 1.10e-08

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 54.91  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200   41 GKPDGHpVVFLHGGP--GGGTAPSNRRFFDPEFYrIVLFDQRGAGKSTPHACLEENTTwDLVND----IEKLREHLKIPE 114
Cdd:pfam12146   1 GEPRAV-VVLVHGLGehSGRYAHLADALAAQGFA-VYAYDHRGHGRSDGKRGHVPSFD-DYVDDldtfVDKIREEHPGLP 77

                          90       100
                  ....*....|....*....|....*....
gi 330251200  115 WLVFGGSWGSTLALAYSQSHPDKVTGLVL 143
Cdd:pfam12146  78 LFLLGHSMGGLIAALYALRYPDKVDGLIL 106
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
34-192 3.54e-06

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 47.32  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  34 TLYWEQSGKPdgHP-VVFLHGGPGGGTapsnrRFFDPEF-------YRIVLFDQRGAGKSTPHacLEENTTWDLVNDIEK 105
Cdd:COG1506   13 WLYLPADGKK--YPvVVYVHGGPGSRD-----DSFLPLAqalasrgYAVLAPDYRGYGESAGD--WGGDEVDDVLAAIDY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200 106 LREHLKIPE--WLVFGGSWGSTLALAYSQSHPDKVTGLVL-RGIFllrkkeiDWFYEGGAAAIYPDAWEEFRDLIPENER 182
Cdd:COG1506   84 LAARPYVDPdrIGIYGHSYGGYMALLAAARHPDRFKAAVAlAGVS-------DLRSYYGTTREYTERLMGGPWEDPEAYA 156

                        170
                 ....*....|
gi 330251200 183 GSSLVDAYHK 192
Cdd:COG1506  157 ARSPLAYADK 166
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 31-143 1.54e-05

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 46.09  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  31 DVHTLYWEQSGKPDGHPVVFLHGGPGGGtapSNRRF-FDP--EFYRIVLFDQRGAGKSTPHacLEENTTWDLVNDIEKLR 107
Cdd:PRK14875 117 GGRTVRYLRLGEGDGTPVVLIHGFGGDL---NNWLFnHAAlaAGRPVIALDLPGHGASSKA--VGAGSLDELAAAVLAFL 191

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 330251200 108 EHLKIPEWLVFGGSWGSTLALAYSQSHPDKVTGLVL 143
Cdd:PRK14875 192 DALGIERAHLVGHSMGGAVALRLAARAPQRVASLTL 227
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 30-143 3.08e-04

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 42.18  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  30 SDVHTLYWEQSGKPDGHPVVFLHGGPggGTAPSNRRFFD--PEFYRIVLFDQRGAGKS-TPHACLEEN-TTWDLVNDIEK 105
Cdd:PLN03084 112 SDLFRWFCVESGSNNNPPVLLIHGFP--SQAYSYRKVLPvlSKNYHAIAFDWLGFGFSdKPQPGYGFNyTLDEYVSSLES 189

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 330251200 106 LREHLKIPEWLVFGGSWGSTLALAYSQSHPDKVTGLVL 143
Cdd:PLN03084 190 LIDELKSDKVSLVVQGYFSPPVVKYASAHPDKIKKLIL 227
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 41-145 3.71e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 41.82  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  41 GKPDGHPVVFLHG-GPGGGtapsnrrFFDPEF------YRIVLFDQRGAGKST--PHAC--LEENTTWdLVNDIEKLREH 109
Cdd:PLN02894 101 SKEDAPTLVMVHGyGASQG-------FFFRNFdalasrFRVIAIDQLGWGGSSrpDFTCksTEETEAW-FIDSFEEWRKA 172

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 330251200 110 LKIPEWLVFGGSWGSTLALAYSQSHPDKVTGLVLRG 145
Cdd:PLN02894 173 KNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVG 208
PRK08775 PRK08775
homoserine O-succinyltransferase;
43-143 1.13e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 40.16  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  43 PDGHPVVFLHGG-------------PGGG---TAPSNRRFFDPEFYRIVLFDQRGAGKSTPHACleenTTWDLVNDIEKL 106
Cdd:PRK08775  55 PAGAPVVFVAGGisahrhvaatatfPEKGwweGLVGSGRALDPARFRLLAFDFIGADGSLDVPI----DTADQADAIALL 130

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 330251200 107 REHLKIPEWLVF-GGSWGSTLALAYSQSHPDKVTGLVL 143
Cdd:PRK08775 131 LDALGIARLHAFvGYSYGALVGLQFASRHPARVRTLVV 168
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 48-217 5.05e-03

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 37.84  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200   48 VVFLHGgpgggtAPSNRRFFDPEF---YRIVLFDQRGAGKSTPHAcleenTTWDLVNDIEKLREHLKIPEW-LVFGGSWG 123
Cdd:pfam12697   1 VVLVHG------AGLSAAPLAALLaagVAVLAPDLPGHGSSSPPP-----LDLADLADLAALLDELGAARPvVLVGHSLG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330251200  124 STLALAYSQSHPDKVTGLVLRGIFLLRKKEIDWFYEGGAAAIYPDAWEEFRDLIPENERGSSLVDAYHKRLNSDDLEIQY 203
Cdd:pfam12697  70 GAVALAAAAAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAA 149

                         170
                  ....*....|....
gi 330251200  204 AAARAWTKWEMMTA 217
Cdd:pfam12697 150 LALLPLAAWRDLPV 163
 
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