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Conserved domains on  [gi|2255859402|ref|WP_251864950|]
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proline iminopeptidase [Enterococcus malodoratus]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 2-289 2.38e-111

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member TIGR01250:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 289  Bit Score: 323.56  E-value: 2.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402   2 KIEEGYMPYLGHQTYYRIVGEQaGNKKPLIVMHGGPGSTHNYFEVLDEMAVD-GRQIIMYDQLGCGKSAVP--SQPDLWT 78
Cdd:TIGR01250   1 EQIEGIITVDGGYHLFTKTGGE-GEKIKLLLLHGGPGMSHEYLENLRELLKEeGREVIMYDQLGCGYSDQPddSDEELWT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  79 AETWVNELIALREHLGLDEVHLLGQSWGGMLEIIYVCDYaPKGVKSMVLSSTLPSAKLWAQEQHRMIKFMSEEDQAAIAK 158
Cdd:TIGR01250  80 IDYFVDELEEVREKLGLDKFYLLGHSWGGMLAQEYALKY-GQHLKGLIISSMLDSAPEYVKELNRLRKELPPEVRAAIKR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 159 AEETGIYDDPAYLAANDRFMvrHAAPVFTEDDPEPLRRKKVA-GTESYVTAWGPNEYSPEGTLHGYDYTNKLADVTIPTL 237
Cdd:TIGR01250 159 CEASGDYDNPEYQEAVEVFY--HHLLCRLRKWPEALKHLKSGgNTNVYNIMQGPNEFTITGNLKDWDITDKLSEIKVPTL 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2255859402 238 VTSGTNDLCTPLVAKTMYDAIPGAKWELFAYSRHMPFVEEREKYMKLLEEWL 289
Cdd:TIGR01250 237 LTVGEFDTMTPEAAREMQELIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFI 288
 
Name Accession Description Interval E-value
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 2-289 2.38e-111

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: 323.56  E-value: 2.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402   2 KIEEGYMPYLGHQTYYRIVGEQaGNKKPLIVMHGGPGSTHNYFEVLDEMAVD-GRQIIMYDQLGCGKSAVP--SQPDLWT 78
Cdd:TIGR01250   1 EQIEGIITVDGGYHLFTKTGGE-GEKIKLLLLHGGPGMSHEYLENLRELLKEeGREVIMYDQLGCGYSDQPddSDEELWT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  79 AETWVNELIALREHLGLDEVHLLGQSWGGMLEIIYVCDYaPKGVKSMVLSSTLPSAKLWAQEQHRMIKFMSEEDQAAIAK 158
Cdd:TIGR01250  80 IDYFVDELEEVREKLGLDKFYLLGHSWGGMLAQEYALKY-GQHLKGLIISSMLDSAPEYVKELNRLRKELPPEVRAAIKR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 159 AEETGIYDDPAYLAANDRFMvrHAAPVFTEDDPEPLRRKKVA-GTESYVTAWGPNEYSPEGTLHGYDYTNKLADVTIPTL 237
Cdd:TIGR01250 159 CEASGDYDNPEYQEAVEVFY--HHLLCRLRKWPEALKHLKSGgNTNVYNIMQGPNEFTITGNLKDWDITDKLSEIKVPTL 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2255859402 238 VTSGTNDLCTPLVAKTMYDAIPGAKWELFAYSRHMPFVEEREKYMKLLEEWL 289
Cdd:TIGR01250 237 LTVGEFDTMTPEAAREMQELIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFI 288
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 4-292 1.96e-39

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: 137.44  E-value: 1.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402   4 EEGYMPYLGHQTYYRIVGEQAgnkKPLIVMHGGPGSTHNYFEVLDEMAvDGRQIIMYDQLGCGKSAVPSQPdlWTAETWV 83
Cdd:COG0596     3 TPRFVTVDGVRLHYREAGPDG---PPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAGG--YTLDDLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  84 NELIALREHLGLDEVHLLGQSWGGMLeIIYVCDYAPKGVKSMVLSStlpsaklwaqeqhrmikfmseEDQAAIAKAEETG 163
Cdd:COG0596    77 DDLAALLDALGLERVVLVGHSMGGMV-ALELAARHPERVAGLVLVD---------------------EVLAALAEPLRRP 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 164 IYDDPAYLAANDrfmvrhaapvfteddpeplrrkkvagtesyvtawgpneyspegTLHGYDYTNKLADVTIPTLVTSGTN 243
Cdd:COG0596   135 GLAPEALAALLR-------------------------------------------ALARTDLRERLARITVPTLVIWGEK 171

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2255859402 244 DLCTPL-VAKTMYDAIPGAKWELFAYSRHMPFVEEREKYMKLLEEWLAAN 292
Cdd:COG0596   172 DPIVPPaLARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 28-277 1.14e-28

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: 109.90  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  28 KPLIVMHGGPGSTHNYFEVLDEMAVDGRQIIMYDQLGCGKSAVPSQPDLWTAETWVNELIALREHLGLDEVHLLGQSWGG 107
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 108 MLEIIYVCDYaPKGVKSMVLSSTLPSAKLWAQEQHRMIKFMSEEDQAAIAKAEETGIYDDPAYLAANDRFmvRHAAPVFT 187
Cdd:pfam00561  81 LIALAYAAKY-PDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLL--RLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 188 EDDPEPLRRKKVAGTESYVTaWGPNEYSPEGTLHGYDYTNKLAdvtIPTLVTSGTNDLCTPLVAKTMYDA-IPGAKWELF 266
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSLVT-GALLFIETWSTELRAKFLGRLD---EPTLIIWGDQDPLVPPQALEKLAQlFPNARLVVI 233

                         250
                  ....*....|.
gi 2255859402 267 AYSRHMPFVEE 277
Cdd:pfam00561 234 PDAGHFAFLEG 244
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 7-109 7.72e-07

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 49.61  E-value: 7.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402   7 YMPYLGHQTYYRivgeQAGNKKPLIVMHGGPGSTHNYFEVLDEMAVDGRqIIMYDQLGCGKSavpSQPDL-WTAETWVNE 85
Cdd:PRK03592   11 RVEVLGSRMAYI----ETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGR-CLAPDLIGMGAS---DKPDIdYTFADHARY 82

                          90       100
                  ....*....|....*....|....
gi 2255859402  86 LIALREHLGLDEVHLLGQSWGGML 109
Cdd:PRK03592   83 LDAWFDALGLDDVVLVGHDWGSAL 106
 
Name Accession Description Interval E-value
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 2-289 2.38e-111

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: 323.56  E-value: 2.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402   2 KIEEGYMPYLGHQTYYRIVGEQaGNKKPLIVMHGGPGSTHNYFEVLDEMAVD-GRQIIMYDQLGCGKSAVP--SQPDLWT 78
Cdd:TIGR01250   1 EQIEGIITVDGGYHLFTKTGGE-GEKIKLLLLHGGPGMSHEYLENLRELLKEeGREVIMYDQLGCGYSDQPddSDEELWT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  79 AETWVNELIALREHLGLDEVHLLGQSWGGMLEIIYVCDYaPKGVKSMVLSSTLPSAKLWAQEQHRMIKFMSEEDQAAIAK 158
Cdd:TIGR01250  80 IDYFVDELEEVREKLGLDKFYLLGHSWGGMLAQEYALKY-GQHLKGLIISSMLDSAPEYVKELNRLRKELPPEVRAAIKR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 159 AEETGIYDDPAYLAANDRFMvrHAAPVFTEDDPEPLRRKKVA-GTESYVTAWGPNEYSPEGTLHGYDYTNKLADVTIPTL 237
Cdd:TIGR01250 159 CEASGDYDNPEYQEAVEVFY--HHLLCRLRKWPEALKHLKSGgNTNVYNIMQGPNEFTITGNLKDWDITDKLSEIKVPTL 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2255859402 238 VTSGTNDLCTPLVAKTMYDAIPGAKWELFAYSRHMPFVEEREKYMKLLEEWL 289
Cdd:TIGR01250 237 LTVGEFDTMTPEAAREMQELIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFI 288
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 4-292 1.96e-39

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: 137.44  E-value: 1.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402   4 EEGYMPYLGHQTYYRIVGEQAgnkKPLIVMHGGPGSTHNYFEVLDEMAvDGRQIIMYDQLGCGKSAVPSQPdlWTAETWV 83
Cdd:COG0596     3 TPRFVTVDGVRLHYREAGPDG---PPVVLLHGLPGSSYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPAGG--YTLDDLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  84 NELIALREHLGLDEVHLLGQSWGGMLeIIYVCDYAPKGVKSMVLSStlpsaklwaqeqhrmikfmseEDQAAIAKAEETG 163
Cdd:COG0596    77 DDLAALLDALGLERVVLVGHSMGGMV-ALELAARHPERVAGLVLVD---------------------EVLAALAEPLRRP 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 164 IYDDPAYLAANDrfmvrhaapvfteddpeplrrkkvagtesyvtawgpneyspegTLHGYDYTNKLADVTIPTLVTSGTN 243
Cdd:COG0596   135 GLAPEALAALLR-------------------------------------------ALARTDLRERLARITVPTLVIWGEK 171

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2255859402 244 DLCTPL-VAKTMYDAIPGAKWELFAYSRHMPFVEEREKYMKLLEEWLAAN 292
Cdd:COG0596   172 DPIVPPaLARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 28-277 1.14e-28

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: 109.90  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  28 KPLIVMHGGPGSTHNYFEVLDEMAVDGRQIIMYDQLGCGKSAVPSQPDLWTAETWVNELIALREHLGLDEVHLLGQSWGG 107
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 108 MLEIIYVCDYaPKGVKSMVLSSTLPSAKLWAQEQHRMIKFMSEEDQAAIAKAEETGIYDDPAYLAANDRFmvRHAAPVFT 187
Cdd:pfam00561  81 LIALAYAAKY-PDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLL--RLRLLKAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 188 EDDPEPLRRKKVAGTESYVTaWGPNEYSPEGTLHGYDYTNKLAdvtIPTLVTSGTNDLCTPLVAKTMYDA-IPGAKWELF 266
Cdd:pfam00561 158 PLLNKRFPSGDYALAKSLVT-GALLFIETWSTELRAKFLGRLD---EPTLIIWGDQDPLVPPQALEKLAQlFPNARLVVI 233

                         250
                  ....*....|.
gi 2255859402 267 AYSRHMPFVEE 277
Cdd:pfam00561 234 PDAGHFAFLEG 244
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
1-291 5.68e-14

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 69.65  E-value: 5.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402   1 MKIEEGYMPYLGHQT-YYRIVGEQAGNKKPLIVMHGGPGSTHNYFEVLDEMAVDGRQIIMYDQLGCGKSAVPsQPDLWTA 79
Cdd:COG2267     1 MTRRLVTLPTRDGLRlRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGP-RGHVDSF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  80 ETWVNELIALREHLGLD---EVHLLGQSWGGMLEIIYVCDYaPKGVKSMVLSStlpsaklwaqeqhrmikfmseedqaai 156
Cdd:COG2267    80 DDYVDDLRAALDALRARpglPVVLLGHSMGGLIALLYAARY-PDRVAGLVLLA--------------------------- 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 157 akaeetgiyddPAYLAandrfmvrhaapvftedDPEplrrkkVAGTESYVTAWGPNEYspegtlhgydytnkLADVTIPT 236
Cdd:COG2267   132 -----------PAYRA-----------------DPL------LGPSARWLRALRLAEA--------------LARIDVPV 163

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2255859402 237 LVTSGTNDLCTPL--VAKTMYDAIPGAKWELFAYSRHMPFVE-EREKYMKLLEEWLAA 291
Cdd:COG2267   164 LVLHGGADRVVPPeaARRLAARLSPDVELVLLPGARHELLNEpAREEVLAAILAWLER 221
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 30-276 1.76e-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: 54.14  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  30 LIVMHGGPGSTHNYFEVLDEMAVDGRQIIMYDQLGCGKSA-----VPSQpdlwtaETWVNELIALREHLGLDEVH----L 100
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDgkrghVPSF------DDYVDDLDTFVDKIREEHPGlplfL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 101 LGQSWGGMLEIIYVCDYAPKgVKSMVLSSTL---------PSAKLWAQEQ---HRMIKFMSEEDQaaiakaeeTGIYDDP 168
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDK-VDGLILSAPAlkikpylapPILKLLAKLLgklFPRLRVPNNLLP--------DSLSRDP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 169 AYLAANDRfmvrhaapvfteddpEPLRRKKVAgtesyvTAWGpneyspEGTLHGYDYTNKLA-DVTIPTLVTSGTND-LC 246
Cdd:pfam12146 152 EVVAAYAA---------------DPLVHGGIS------ARTL------YELLDAGERLLRRAaAITVPLLLLHGGADrVV 204

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2255859402 247 TPLVAKTMYDAIPGAKWELFAY--SRHMPFVE 276
Cdd:pfam12146 205 DPAGSREFYERAGSTDKTLKLYpgLYHELLNE 236
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 7-109 7.72e-07

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 49.61  E-value: 7.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402   7 YMPYLGHQTYYRivgeQAGNKKPLIVMHGGPGSTHNYFEVLDEMAVDGRqIIMYDQLGCGKSavpSQPDL-WTAETWVNE 85
Cdd:PRK03592   11 RVEVLGSRMAYI----ETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGR-CLAPDLIGMGAS---DKPDIdYTFADHARY 82

                          90       100
                  ....*....|....*....|....
gi 2255859402  86 LIALREHLGLDEVHLLGQSWGGML 109
Cdd:PRK03592   83 LDAWFDALGLDDVVLVGHDWGSAL 106
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
12-292 1.29e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 45.39  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  12 GHQTYYRIVGEQAGNKKPLIVM-HGGPGSTHNYF-EVLDEMAVDGRQIIMYDQLGCGKSA-VPSQPDLWTAETWVNELIA 88
Cdd:COG1506     7 GTTLPGWLYLPADGKKYPVVVYvHGGPGSRDDSFlPLAQALASRGYAVLAPDYRGYGESAgDWGGDEVDDVLAAIDYLAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  89 lREHLGLDEVHLLGQSWGGMleiiyvcdyapkgvksMVLSStlpsaklwAQEQHRMIKfmseedqAAIAKAeetGIYDDP 168
Cdd:COG1506    87 -RPYVDPDRIGIYGHSYGGY----------------MALLA--------AARHPDRFK-------AAVALA---GVSDLR 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 169 AYLAANDRFMVRHAAPvfTEDDPEPLRrkkvagtesyvtawgpnEYSPegtlhgydyTNKLADVTIPTLVTSGTNDLCTP 248
Cdd:COG1506   132 SYYGTTREYTERLMGG--PWEDPEAYA-----------------ARSP---------LAYADKLKTPLLLIHGEADDRVP 183

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2255859402 249 LV-AKTMYDAIP--GAKWELFAY--SRHMPFVEEREKYMKLLEEWLAAN 292
Cdd:COG1506   184 PEqAERLYEALKkaGKPVELLVYpgEGHGFSGAGAPDYLERILDFLDRH 232
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 20-144 1.37e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 45.73  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  20 VGEQAGNKKPLIVMHGGPGSTHNYFEVLDEMAVDGRQIIMYDQLGCGKSAVPSQPDLWTAETWVNELIALREHLGLDEVH 99
Cdd:PRK00870   39 VDEGPADGPPVLLLHGEPSWSYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPTRREDYTYARHVEWMRSWFEQLDLTDVT 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2255859402 100 LLGQSWGGMLEIIYVCDYAPKGVKSMVLSSTLPSAklwaqeQHRM 144
Cdd:PRK00870  119 LVCQDWGGLIGLRLAAEHPDRFARLVVANTGLPTG------DGPM 157
PRK05855 PRK05855
SDR family oxidoreductase;
20-106 4.40e-05

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 44.59  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  20 VGEQAGNKKPLIVM-HGGPGSTHNYFEVLDEMAVDGRqIIMYDQLGCGKSAVPSQPDLWTAETWVNELIALREHLGLDE- 97
Cdd:PRK05855   17 VYEWGDPDRPTVVLvHGYPDNHEVWDGVAPLLADRFR-VVAYDVRGAGRSSAPKRTAAYTLARLADDFAAVIDAVSPDRp 95


                  ....*....
gi 2255859402  98 VHLLGQSWG 106
Cdd:PRK05855   96 VHLLAHDWG 104
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 30-279 9.29e-05

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 42.85  E-value: 9.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402  30 LIVMHGGPGSthnyFEVLDEMAVDGRQIIMYDQLGCGKSAVPSQPdlWTAETWVNELIAlrEHLGLDEVHLLGQSWGGML 109
Cdd:pfam12697   1 VVLVHGAGLS----AAPLAALLAAGVAVLAPDLPGHGSSSPPPLD--LADLADLAALLD--ELGAARPVVLVGHSLGGAV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 110 eIIYVCDYAPkgVKSMVLSSTLPSAKLwaqeqhrmikfmseEDQAAIAKAEETGIYDDPAYLAANDRfmvrhAAPVFTED 189
Cdd:pfam12697  73 -ALAAAAAAL--VVGVLVAPLAAPPGL--------------LAALLALLARLGAALAAPAWLAAESL-----ARGFLDDL 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 190 DPEPLRRKKVAGTESYVTAWGPNEYSPegtlhgydytnkLADVTIPTLVTsGTNDLCTPLVAKTMYDAIPGAKWELFAYS 269
Cdd:pfam12697 131 PADAEWAAALARLAALLAALALLPLAA------------WRDLPVPVLVL-AEEDRLVPELAQRLLAALAGARLVVLPGA 197

                         250
                  ....*....|
gi 2255859402 270 RHMPFVEERE 279
Cdd:pfam12697 198 GHLPLDDPEE 207
PhaC COG3243
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
77-127 1.16e-03

Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];


Pssm-ID: 442475 [Multi-domain]  Cd Length: 545  Bit Score: 40.32  E-value: 1.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2255859402  77 WTAETWVNELI-----ALREHLGLDEVHLLGQSWGGMLEIIYVCDYAPKG---VKSMVL 127
Cdd:COG3243   253 LGLDDYVEDGIlaavdAVREITGEDKVNLLGYCLGGTLLAIYAALLAARGpdrVASLTL 311
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
205-289 1.20e-03

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 39.54  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859402 205 YVTAWGPNEYSPEGTLHGYDYT----------------NKLADVTIPTLVTSGTND-LCTPLVAKTMYDAIPGAKWELFA 267
Cdd:COG1647   137 SLRGIGSDIEDPEVAEYAYDRTplralaelqrlirevrRDLPKITAPTLIIQSRKDeVVPPESARYIYERLGSPDKELVW 216

                          90       100
                  ....*....|....*....|....*
gi 2255859402 268 Y--SRHMPFV-EEREKYMKLLEEWL 289
Cdd:COG1647   217 LedSGHVITLdKDREEVAEEILDFL 241
 
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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