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Conserved domains on  [gi|609076|emb|CAA84382|]
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leucyl aminopeptidase [Lactobacillus delbrueckii]

Protein Classification

proline-specific peptidase family protein( domain architecture ID 11492157)

proline-specific peptidase family protein is an alpha/beta hydrolase that catalyzes the hydrolysis of substrates such as polyproline and prolyl-2-naphthylamide

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 4-287 1.95e-152

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: 427.95  E-value: 1.95e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076       4 TRIVTLDNGYHLFTRKVNEGP-VKLLCVHGGPGDNHEDFDNFKAGLAGKGVEVYSYDQLGSYWSDQPDFSKEEnrkYLTV 82
Cdd:TIGR01250   4 EGIITVDGGYHLFTKTGGEGEkIKLLLLHGGPGMSHEYLENLRELLKEEGREVIMYDQLGCGYSDQPDDSDEE---LWTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076      83 DYFVDELEEVRQKLGLENFYLLGHSWGGLLAQEYAVRYGQHLKAVVIESMIDNLDEYTVNINRERdEMFSPAQVEYMKEC 162
Cdd:TIGR01250  81 DYFVDELEEVREKLGLDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSMLDSAPEYVKELNRLR-KELPPEVRAAIKRC 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     163 EASENFDDAMYQELVAKLY--SVYLVRHPENATRHVVSTTNTQVYNYFQGNNEFMMVGKLTEWDFRDKLAQITLPTLLTV 240
Cdd:TIGR01250 160 EASGDYDNPEYQEAVEVFYhhLLCRLRKWPEALKHLKSGGNTNVYNIMQGPNEFTITGNLKDWDITDKLSEIKVPTLLTV 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 609076     241 GEFDTMPLDAVRRMHHSLKNSRMVVTPDGATATML-TTQMHFSL--PYIS 287
Cdd:TIGR01250 240 GEFDTMTPEAAREMQELIAGSRLVVFPDGSHMTMIeDPEVYFKLlsDFIR 289
 
Name Accession Description Interval E-value
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 4-287 1.95e-152

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: 427.95  E-value: 1.95e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076       4 TRIVTLDNGYHLFTRKVNEGP-VKLLCVHGGPGDNHEDFDNFKAGLAGKGVEVYSYDQLGSYWSDQPDFSKEEnrkYLTV 82
Cdd:TIGR01250   4 EGIITVDGGYHLFTKTGGEGEkIKLLLLHGGPGMSHEYLENLRELLKEEGREVIMYDQLGCGYSDQPDDSDEE---LWTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076      83 DYFVDELEEVRQKLGLENFYLLGHSWGGLLAQEYAVRYGQHLKAVVIESMIDNLDEYTVNINRERdEMFSPAQVEYMKEC 162
Cdd:TIGR01250  81 DYFVDELEEVREKLGLDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSMLDSAPEYVKELNRLR-KELPPEVRAAIKRC 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     163 EASENFDDAMYQELVAKLY--SVYLVRHPENATRHVVSTTNTQVYNYFQGNNEFMMVGKLTEWDFRDKLAQITLPTLLTV 240
Cdd:TIGR01250 160 EASGDYDNPEYQEAVEVFYhhLLCRLRKWPEALKHLKSGGNTNVYNIMQGPNEFTITGNLKDWDITDKLSEIKVPTLLTV 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 609076     241 GEFDTMPLDAVRRMHHSLKNSRMVVTPDGATATML-TTQMHFSL--PYIS 287
Cdd:TIGR01250 240 GEFDTMTPEAAREMQELIAGSRLVVFPDGSHMTMIeDPEVYFKLlsDFIR 289
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-269 1.19e-29

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: 112.02  E-value: 1.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     1 MDQTRIVTLDnGYHLFTRKV-NEGPVkLLCVHGGPGDnHEDFDNFKAGLAgKGVEVYSYDQLGSYWSDQPDfskeenrKY 79
Cdd:COG0596   1 MSTPRFVTVD-GVRLHYREAgPDGPP-VVLLHGLPGS-SYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPA-------GG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076    80 LTVDYFVDELEEVRQKLGLENFYLLGHSWGGLLAQEYAVRYGQHLKAVViesmidnldeytvninrerdeMFSPAQVEYM 159
Cdd:COG0596  70 YTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLV---------------------LVDEVLAALA 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076   160 KECEASENFDDAMYQELVAklysvylvrhpenatrhvvsttntqvynyfqgnnefmmvgkLTEWDFRDKLAQITLPTLLT 239
Cdd:COG0596 129 EPLRRPGLAPEALAALLRA-----------------------------------------LARTDLRERLARITVPTLVI 167

                       250       260       270
                ....*....|....*....|....*....|.
gi 609076   240 VGEFDTM-PLDAVRRMHHSLKNSRMVVTPDG 269
Cdd:COG0596 168 WGEKDPIvPPALARRLAELLPNAELVVLPGA 198
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 27-269 1.97e-23

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: 96.03  E-value: 1.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076      27 LLCVHGGPGdNHEDFDNFKAGLAGKGVEVYSYDQLGSYWSDQPdfskeENRKYLTVDYFVDELEEVRQKLGLENFYLLGH 106
Cdd:pfam00561   3 VLLLHGLPG-SSDLWRKLAPALARDGFRVIALDLRGFGKSSRP-----KAQDDYRTDDLAEDLEYILEALGLEKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     107 SWGGLLAQEYAVRYGQHLKAVVIESMIDNLDEYtvNINRERDEMFSPAQVEYMKecEASENFDDAMyqeLVAKLYSVYLV 186
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGALDPPHEL--DEADRFILALFPGFFDGFV--ADFAPNPLGR---LVAKLLALLLL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     187 RHpenATRHVVSTTNTQVYNYFQGNNEFMMVGKLTEW------DFRDKLAQITLPTLLTVGEFD-TMPLDAVRRMHHSLK 259
Cdd:pfam00561 150 RL---RLLKALPLLNKRFPSGDYALAKSLVTGALLFIetwsteLRAKFLGRLDEPTLIIWGDQDpLVPPQALEKLAQLFP 226

                         250
                  ....*....|
gi 609076     260 NSRMVVTPDG 269
Cdd:pfam00561 227 NARLVVIPDA 236
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 27-129 1.83e-15

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 76.10  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     27 LLCVHGGPGDNHEDFDNFKAgLAGKgVEVYSYDQLGSYWSDQPDF---SKEEnrkylTVDYFVDELEEVRQKLGLENFYL 103
Cdd:PLN02894 108 LVMVHGYGASQGFFFRNFDA-LASR-FRVIAIDQLGWGGSSRPDFtckSTEE-----TEAWFIDSFEEWRKAKNLSNFIL 180

                         90       100
                 ....*....|....*....|....*.
gi 609076    104 LGHSWGGLLAQEYAVRYGQHLKAVVI 129
Cdd:PLN02894 181 LGHSFGGYVAAKYALKHPEHVQHLIL 206
 
Name Accession Description Interval E-value
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 4-287 1.95e-152

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: 427.95  E-value: 1.95e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076       4 TRIVTLDNGYHLFTRKVNEGP-VKLLCVHGGPGDNHEDFDNFKAGLAGKGVEVYSYDQLGSYWSDQPDFSKEEnrkYLTV 82
Cdd:TIGR01250   4 EGIITVDGGYHLFTKTGGEGEkIKLLLLHGGPGMSHEYLENLRELLKEEGREVIMYDQLGCGYSDQPDDSDEE---LWTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076      83 DYFVDELEEVRQKLGLENFYLLGHSWGGLLAQEYAVRYGQHLKAVVIESMIDNLDEYTVNINRERdEMFSPAQVEYMKEC 162
Cdd:TIGR01250  81 DYFVDELEEVREKLGLDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSMLDSAPEYVKELNRLR-KELPPEVRAAIKRC 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     163 EASENFDDAMYQELVAKLY--SVYLVRHPENATRHVVSTTNTQVYNYFQGNNEFMMVGKLTEWDFRDKLAQITLPTLLTV 240
Cdd:TIGR01250 160 EASGDYDNPEYQEAVEVFYhhLLCRLRKWPEALKHLKSGGNTNVYNIMQGPNEFTITGNLKDWDITDKLSEIKVPTLLTV 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 609076     241 GEFDTMPLDAVRRMHHSLKNSRMVVTPDGATATML-TTQMHFSL--PYIS 287
Cdd:TIGR01250 240 GEFDTMTPEAAREMQELIAGSRLVVFPDGSHMTMIeDPEVYFKLlsDFIR 289
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-269 1.19e-29

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: 112.02  E-value: 1.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     1 MDQTRIVTLDnGYHLFTRKV-NEGPVkLLCVHGGPGDnHEDFDNFKAGLAgKGVEVYSYDQLGSYWSDQPDfskeenrKY 79
Cdd:COG0596   1 MSTPRFVTVD-GVRLHYREAgPDGPP-VVLLHGLPGS-SYEWRPLIPALA-AGYRVIAPDLRGHGRSDKPA-------GG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076    80 LTVDYFVDELEEVRQKLGLENFYLLGHSWGGLLAQEYAVRYGQHLKAVViesmidnldeytvninrerdeMFSPAQVEYM 159
Cdd:COG0596  70 YTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLV---------------------LVDEVLAALA 128

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076   160 KECEASENFDDAMYQELVAklysvylvrhpenatrhvvsttntqvynyfqgnnefmmvgkLTEWDFRDKLAQITLPTLLT 239
Cdd:COG0596 129 EPLRRPGLAPEALAALLRA-----------------------------------------LARTDLRERLARITVPTLVI 167

                       250       260       270
                ....*....|....*....|....*....|.
gi 609076   240 VGEFDTM-PLDAVRRMHHSLKNSRMVVTPDG 269
Cdd:COG0596 168 WGEKDPIvPPALARRLAELLPNAELVVLPGA 198
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 27-269 1.97e-23

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: 96.03  E-value: 1.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076      27 LLCVHGGPGdNHEDFDNFKAGLAGKGVEVYSYDQLGSYWSDQPdfskeENRKYLTVDYFVDELEEVRQKLGLENFYLLGH 106
Cdd:pfam00561   3 VLLLHGLPG-SSDLWRKLAPALARDGFRVIALDLRGFGKSSRP-----KAQDDYRTDDLAEDLEYILEALGLEKVNLVGH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     107 SWGGLLAQEYAVRYGQHLKAVVIESMIDNLDEYtvNINRERDEMFSPAQVEYMKecEASENFDDAMyqeLVAKLYSVYLV 186
Cdd:pfam00561  77 SMGGLIALAYAAKYPDRVKALVLLGALDPPHEL--DEADRFILALFPGFFDGFV--ADFAPNPLGR---LVAKLLALLLL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     187 RHpenATRHVVSTTNTQVYNYFQGNNEFMMVGKLTEW------DFRDKLAQITLPTLLTVGEFD-TMPLDAVRRMHHSLK 259
Cdd:pfam00561 150 RL---RLLKALPLLNKRFPSGDYALAKSLVTGALLFIetwsteLRAKFLGRLDEPTLIIWGDQDpLVPPQALEKLAQLFP 226

                         250
                  ....*....|
gi 609076     260 NSRMVVTPDG 269
Cdd:pfam00561 227 NARLVVIPDA 236
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 27-129 1.83e-15

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 76.10  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     27 LLCVHGGPGDNHEDFDNFKAgLAGKgVEVYSYDQLGSYWSDQPDF---SKEEnrkylTVDYFVDELEEVRQKLGLENFYL 103
Cdd:PLN02894 108 LVMVHGYGASQGFFFRNFDA-LASR-FRVIAIDQLGWGGSSRPDFtckSTEE-----TEAWFIDSFEEWRKAKNLSNFIL 180

                         90       100
                 ....*....|....*....|....*.
gi 609076    104 LGHSWGGLLAQEYAVRYGQHLKAVVI 129
Cdd:PLN02894 181 LGHSFGGYVAAKYALKHPEHVQHLIL 206
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
1-139 2.17e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 73.50  E-value: 2.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     1 MDQTRI-VTLDNGYHLFTRK-VNEGPVK--LLCVHGGpGDNHEDFDNFKAGLAGKGVEVYSYDQLGSYWSDQPdfskeeN 76
Cdd:COG2267   1 MTRRLVtLPTRDGLRLRGRRwRPAGSPRgtVVLVHGL-GEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGP------R 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 609076    77 RKYLTVDYFVDELEEVRQKLGLEN---FYLLGHSWGGLLAQEYAVRYGQHLKAVVIESMIDNLDEY 139
Cdd:COG2267  74 GHVDSFDDYVDDLRAALDALRARPglpVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPL 139
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 30-131 1.14e-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: 54.53  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076      30 VHGGpGDNHEDFDNFKAGLAGKGVEVYSYDQLGSYWSD-----QPDFskeenrkyltvDYFVDELEEVRQKLGLEN---- 100
Cdd:pfam12146  10 VHGL-GEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDgkrghVPSF-----------DDYVDDLDTFVDKIREEHpglp 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 609076     101 FYLLGHSWGGLLAQEYAVRYGQHLKAVVIES 131
Cdd:pfam12146  78 LFLLGHSMGGLIAALYALRYPDKVDGLILSA 108
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 27-269 1.38e-08

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 54.02  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076      27 LLCVHGGPgdnhEDFDNFkAGLAGKGVEVYSYDQLGSYWSDQPDFskeenrkylTVDYFVDELEEVRQKLGLENFYLLGH 106
Cdd:pfam12697   1 VVLVHGAG----LSAAPL-AALLAAGVAVLAPDLPGHGSSSPPPL---------DLADLADLAALLDELGAARPVVLVGH 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     107 SWGGLLAQEYAVRYgqHLKAVVIESMIDNLDEYTVNINRERDEMFSPAQVEYMKEceasENFDDAMYQELVAKLYSVYLV 186
Cdd:pfam12697  67 SLGGAVALAAAAAA--LVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAA----ESLARGFLDDLPADAEWAAAL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076     187 RHPENATRHVvsttntqvynyfqgnnefmmvgkltEWDFRDKLAQITLPTLLtVGEFDTMPLDAVRRMHHSLKNSRMVVT 266
Cdd:pfam12697 141 ARLAALLAAL-------------------------ALLPLAAWRDLPVPVLV-LAEEDRLVPELAQRLLAALAGARLVVL 194


                  ...
gi 609076     267 PDG 269
Cdd:pfam12697 195 PGA 197
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 24-128 6.24e-06

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 44.05  E-value: 6.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076    24 PVklLCVHGgPGDNHEDFDNFKAGLAGKGVEVYSYDqlgsYWSDQPDFskEENRKYLtvdyfVDELEEVRQKLGLENFYL 103
Cdd:COG1075   7 PV--VLVHG-LGGSAASWAPLAPRLRAAGYPVYALN----YPSTNGSI--EDSAEQL-----AAFVDAVLAATGAEKVDL 72

                        90       100
                ....*....|....*....|....*..
gi 609076   104 LGHSWGGLLAQEYAVRYG--QHLKAVV 128
Cdd:COG1075  73 VGHSMGGLVARYYLKRLGgaAKVARVV 99
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
27-151 6.45e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 46.55  E-value: 6.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076    27 LLCVHGGPGDNHEDFDNFKAGLAGKGVEVYSYDQLGsYWSDQPDFSKEEnrkYLTVDYFVDELEEvRQKLGLENFYLLGH 106
Cdd:COG1506  26 VVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRG-YGESAGDWGGDE---VDDVLAAIDYLAA-RPYVDPDRIGIYGH 100

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 609076   107 SWGGLLAQEYAVRYGQHLKAVVIESMIDNLDEYTVNINRERDEMF 151
Cdd:COG1506 101 SYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTERLM 145
YpfH COG0400
Predicted esterase [General function prediction only];
27-128 1.32e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 42.20  E-value: 1.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076    27 LLCVHGGpGDNHEDFDNFKAGLAGKGVEV------YSYDQLGSYWSDQPDFSKEENRKYL--TVDYFVDELEEVRQKLGL 98
Cdd:COG0400   8 VVLLHGY-GGDEEDLLPLAPELALPGAAVlaprapVPEGPGGRAWFDLSFLEGREDEEGLaaAAEALAAFIDELEARYGI 86

                        90       100       110
                ....*....|....*....|....*....|..
gi 609076    99 --ENFYLLGHSWGGLLAQEYAVRYGQHLKAVV 128
Cdd:COG0400  87 dpERIVLAGFSQGAAMALSLALRRPELLAGVV 118
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 66-137 2.53e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 41.90  E-value: 2.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 609076     66 SDQPD--FSKEENRKYLtvDYFVDELeevrqklGLENFYLLGHSWGGLLAQEYAVRYGQHLKAVV-IESMIDNLD 137
Cdd:PRK03592  67 SDKPDidYTFADHARYL--DAWFDAL-------GLDDVVLVGHDWGSALGFDWAARHPDRVRGIAfMEAIVRPMT 132
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 27-119 2.15e-03

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 39.69  E-value: 2.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 609076    27 LLCVHGGPGDNHedfdNFkAGLA---GKGVEVYSYDQLGSYWSDQPDFSKEEnrkylTVDYFVDELEEVrQKLGleNFYL 103
Cdd:COG3319 604 LFCVHPAGGNVL----CY-RPLAralGPDRPVYGLQAPGLDGGEPPPASVEE-----MAARYVEAIRAV-QPEG--PYHL 670

                        90
                ....*....|....*.
gi 609076   104 LGHSWGGLLAQEYAVR 119
Cdd:COG3319 671 LGWSFGGLVAYEMARQ 686
 
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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