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Conserved domains on  [gi|496332617|ref|WP_009041795|]
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prolyl aminopeptidase [Pseudomonas chlororaphis]

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, ...
 8-311 1.93e-156

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 TIGR01249:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 306  Bit Score: 439.66  E-value: 1.93e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617    8 IKPYARHDLAVDEPHVLYVDESGSPEGLPVVFIHGGPGAGCDAQSRRYFDPNLYRIITFDQRGCGRSTPHASLENNTTWD 87
Cdd:TIGR01249   1 TKPFVSGYLNVSDNHQLYYEQSGNPDGKPVVFLHGGPGSGTDPGCRRFFDPETYRIVLFDQRGCGKSTPHACLEENTTWD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617   88 LVADLERIRLHLGIEKWVVFGGSWGSTLALAYAQTHPERVHGLILRGIFLCRPQEIEWFYQAGASRLFPDYWQDYVAPIP 167
Cdd:TIGR01249  81 LVADIEKLREKLGIKNWLVFGGSWGSTLALAYAQTHPEVVTGLVLRGIFLLREKEWSWFYEGGASMIYPDAWQRFMDSIP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  168 LDER-DDLLSAFHKRLVGNDQIAQMHAAKAWSTWEGrTATLRPNPLVVDRFSEPQRALSIARIECHYFTNHAFLEP-NQL 245
Cdd:TIGR01249 161 ENERnEQLVNAYHDRLQSGDEETKLAAAKAWVDWES-TTLLRPINEIVSTAEDFKFSLAFARLENHYFVNKGFLDVeNFI 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496332617  246 IRDMGKIAHLPGVIVHGRYDVICPLDNAWELHQAWPNSELQVIRDAGHAASEPGITDALVRAADQM 311
Cdd:TIGR01249 240 LDNISKIRNIPTYIVHGRYDLCCPLQSAWALHKAFPEAELKVTNNAGHSAFDPNNLAALVHALETY 305
 
Name Accession Description Interval E-value
pro_imino_pep_1 TIGR01249
proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related ...
 8-311 1.93e-156

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: 439.66  E-value: 1.93e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617    8 IKPYARHDLAVDEPHVLYVDESGSPEGLPVVFIHGGPGAGCDAQSRRYFDPNLYRIITFDQRGCGRSTPHASLENNTTWD 87
Cdd:TIGR01249   1 TKPFVSGYLNVSDNHQLYYEQSGNPDGKPVVFLHGGPGSGTDPGCRRFFDPETYRIVLFDQRGCGKSTPHACLEENTTWD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617   88 LVADLERIRLHLGIEKWVVFGGSWGSTLALAYAQTHPERVHGLILRGIFLCRPQEIEWFYQAGASRLFPDYWQDYVAPIP 167
Cdd:TIGR01249  81 LVADIEKLREKLGIKNWLVFGGSWGSTLALAYAQTHPEVVTGLVLRGIFLLREKEWSWFYEGGASMIYPDAWQRFMDSIP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  168 LDER-DDLLSAFHKRLVGNDQIAQMHAAKAWSTWEGrTATLRPNPLVVDRFSEPQRALSIARIECHYFTNHAFLEP-NQL 245
Cdd:TIGR01249 161 ENERnEQLVNAYHDRLQSGDEETKLAAAKAWVDWES-TTLLRPINEIVSTAEDFKFSLAFARLENHYFVNKGFLDVeNFI 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496332617  246 IRDMGKIAHLPGVIVHGRYDVICPLDNAWELHQAWPNSELQVIRDAGHAASEPGITDALVRAADQM 311
Cdd:TIGR01249 240 LDNISKIRNIPTYIVHGRYDLCCPLQSAWALHKAFPEAELKVTNNAGHSAFDPNNLAALVHALETY 305
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 36-299 6.84e-39

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: 137.64  E-value: 6.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617   36 PVVFIHGGPGAGcDAQSR--RYFDPNLYRIITFDQRGCGRSTPHASLENNTTWDLVADLERIRLHLGIEKWVVFGGSWGS 113
Cdd:pfam00561   2 PVLLLHGLPGSS-DLWRKlaPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  114 TLALAYAQTHPERVHGLILRGIFLCRPQEIEWFYQAGASrlFPDYWQDYVAPIPLDERDDLLSAFHKRLVGNDQIAQMHA 193
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILAL--FPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  194 AKAWSTWEGRtatlRPNPLVVDRFSEPQRAlsiariechYFTNHAFLEPNQLIRdmgkiahLPGVIVHGRYDVICPLDNA 273
Cdd:pfam00561 159 LLNKRFPSGD----YALAKSLVTGALLFIE---------TWSTELRAKFLGRLD-------EPTLIIWGDQDPLVPPQAL 218

                         250       260
                  ....*....|....*....|....*.
gi 496332617  274 WELHQAWPNSELQVIRDAGHAASEPG 299
Cdd:pfam00561 219 EKLAQLFPNARLVVIPDAGHFAFLEG 244
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 24-307 5.82e-33

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: 121.26  E-value: 5.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  24 LYVDESGsPEGLPVVFIHGGPGagcdaqSRRYFDPNL------YRIITFDQRGCGRSTPHASleNNTTWDLVADLERIRL 97
Cdd:COG0596   14 LHYREAG-PDGPPVVLLHGLPG------SSYEWRPLIpalaagYRVIAPDLRGHGRSDKPAG--GYTLDDLADDLAALLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  98 HLGIEKWVVFGGSWGSTLALAYAQTHPERVHGLILRGiflcrpqeiewfyqagasrlfpDYWQDYVAPIPLDERDDllSA 177
Cdd:COG0596   85 ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD----------------------EVLAALAEPLRRPGLAP--EA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617 178 FHkrlvgndqiAQMHAAKAWSTWEGrtatlrpnplvvdrfsepqralsIARIEChyftnhaflepnqlirdmgkiahlPG 257
Cdd:COG0596  141 LA---------ALLRALARTDLRER-----------------------LARITV------------------------PT 164

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496332617 258 VIVHGRYDVICPLDNAWELHQAWPNSELQVIRDAGHAA--SEPGITDALVRA 307
Cdd:COG0596  165 LVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPplEQPEAFAAALRD 216
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 28-132 8.47e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 46.86  E-value: 8.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  28 ESGSPEGLPVVFIHGgpgAGCDAQSRRYFDPNL---YRIITFDQRGCGRSTPhaSLENNTTWDLVADLERIRLHLGIEKW 104
Cdd:PRK14875 125 RLGEGDGTPVVLIHG---FGGDLNNWLFNHAALaagRPVIALDLPGHGASSK--AVGAGSLDELAAAVLAFLDALGIERA 199

                         90       100
                 ....*....|....*....|....*...
gi 496332617 105 VVFGGSWGSTLALAYAQTHPERVHGLIL 132
Cdd:PRK14875 200 HLVGHSMGGAVALRLAARAPQRVASLTL 227
 
Name Accession Description Interval E-value
pro_imino_pep_1 TIGR01249
proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related ...
 8-311 1.93e-156

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: 439.66  E-value: 1.93e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617    8 IKPYARHDLAVDEPHVLYVDESGSPEGLPVVFIHGGPGAGCDAQSRRYFDPNLYRIITFDQRGCGRSTPHASLENNTTWD 87
Cdd:TIGR01249   1 TKPFVSGYLNVSDNHQLYYEQSGNPDGKPVVFLHGGPGSGTDPGCRRFFDPETYRIVLFDQRGCGKSTPHACLEENTTWD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617   88 LVADLERIRLHLGIEKWVVFGGSWGSTLALAYAQTHPERVHGLILRGIFLCRPQEIEWFYQAGASRLFPDYWQDYVAPIP 167
Cdd:TIGR01249  81 LVADIEKLREKLGIKNWLVFGGSWGSTLALAYAQTHPEVVTGLVLRGIFLLREKEWSWFYEGGASMIYPDAWQRFMDSIP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  168 LDER-DDLLSAFHKRLVGNDQIAQMHAAKAWSTWEGrTATLRPNPLVVDRFSEPQRALSIARIECHYFTNHAFLEP-NQL 245
Cdd:TIGR01249 161 ENERnEQLVNAYHDRLQSGDEETKLAAAKAWVDWES-TTLLRPINEIVSTAEDFKFSLAFARLENHYFVNKGFLDVeNFI 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496332617  246 IRDMGKIAHLPGVIVHGRYDVICPLDNAWELHQAWPNSELQVIRDAGHAASEPGITDALVRAADQM 311
Cdd:TIGR01249 240 LDNISKIRNIPTYIVHGRYDLCCPLQSAWALHKAFPEAELKVTNNAGHSAFDPNNLAALVHALETY 305
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 36-299 6.84e-39

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: 137.64  E-value: 6.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617   36 PVVFIHGGPGAGcDAQSR--RYFDPNLYRIITFDQRGCGRSTPHASLENNTTWDLVADLERIRLHLGIEKWVVFGGSWGS 113
Cdd:pfam00561   2 PVLLLHGLPGSS-DLWRKlaPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  114 TLALAYAQTHPERVHGLILRGIFLCRPQEIEWFYQAGASrlFPDYWQDYVAPIPLDERDDLLSAFHKRLVGNDQIAQMHA 193
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILAL--FPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKALP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  194 AKAWSTWEGRtatlRPNPLVVDRFSEPQRAlsiariechYFTNHAFLEPNQLIRdmgkiahLPGVIVHGRYDVICPLDNA 273
Cdd:pfam00561 159 LLNKRFPSGD----YALAKSLVTGALLFIE---------TWSTELRAKFLGRLD-------EPTLIIWGDQDPLVPPQAL 218

                         250       260
                  ....*....|....*....|....*.
gi 496332617  274 WELHQAWPNSELQVIRDAGHAASEPG 299
Cdd:pfam00561 219 EKLAQLFPNARLVVIPDAGHFAFLEG 244
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 24-307 5.82e-33

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: 121.26  E-value: 5.82e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  24 LYVDESGsPEGLPVVFIHGGPGagcdaqSRRYFDPNL------YRIITFDQRGCGRSTPHASleNNTTWDLVADLERIRL 97
Cdd:COG0596   14 LHYREAG-PDGPPVVLLHGLPG------SSYEWRPLIpalaagYRVIAPDLRGHGRSDKPAG--GYTLDDLADDLAALLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  98 HLGIEKWVVFGGSWGSTLALAYAQTHPERVHGLILRGiflcrpqeiewfyqagasrlfpDYWQDYVAPIPLDERDDllSA 177
Cdd:COG0596   85 ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD----------------------EVLAALAEPLRRPGLAP--EA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617 178 FHkrlvgndqiAQMHAAKAWSTWEGrtatlrpnplvvdrfsepqralsIARIEChyftnhaflepnqlirdmgkiahlPG 257
Cdd:COG0596  141 LA---------ALLRALARTDLRER-----------------------LARITV------------------------PT 164

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496332617 258 VIVHGRYDVICPLDNAWELHQAWPNSELQVIRDAGHAA--SEPGITDALVRA 307
Cdd:COG0596  165 LVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPplEQPEAFAAALRD 216
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 16-295 1.61e-23

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: 97.84  E-value: 1.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617   16 LAVDEPHVLYVDESGSPEGLPVVFIHGGPGAGCD--AQSRRYFDPNLYRIITFDQRGCGRST-PHASLENNTTWD-LVAD 91
Cdd:TIGR01250   7 ITVDGGYHLFTKTGGEGEKIKLLLLHGGPGMSHEylENLRELLKEEGREVIMYDQLGCGYSDqPDDSDEELWTIDyFVDE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617   92 LERIRLHLGIEKWVVFGGSWGSTLALAYAQTHPERVHGLILRGIFLCRPQeiewfYQAGASRLfpdywQDYVAPiplder 171
Cdd:TIGR01250  87 LEEVREKLGLDKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSMLDSAPE-----YVKELNRL-----RKELPP------ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  172 ddllsafhkrlvgnDQIAQMHAAKAWSTWEGR--TATLRP-NPLVVDRFSEPQRALSiaRIECHYFTN--HAFLEPNQL- 245
Cdd:TIGR01250 151 --------------EVRAAIKRCEASGDYDNPeyQEAVEVfYHHLLCRLRKWPEALK--HLKSGGNTNvyNIMQGPNEFt 214

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  246 ---------IRD-MGKIAhLPGVIVHGRYDViCPLDNAWELHQAWPNSELQVIRDAGHAA 295
Cdd:TIGR01250 215 itgnlkdwdITDkLSEIK-VPTLLTVGEFDT-MTPEAAREMQELIAGSRLVVFPDGSHMT 272
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
36-132 1.02e-09

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 57.70  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  36 PVVFIHGGpgagcDAQSRRYFD--PNL----YRIITFDQRGCGRSTPHASLENNTTwDLVADLERIRLHL---GIEKWVV 106
Cdd:COG2267   30 TVVLVHGL-----GEHSGRYAElaEALaaagYAVLAFDLRGHGRSDGPRGHVDSFD-DYVDDLRAALDALrarPGLPVVL 103

                         90       100
                 ....*....|....*....|....*.
gi 496332617 107 FGGSWGSTLALAYAQTHPERVHGLIL 132
Cdd:COG2267  104 LGHSMGGLIALLYAARYPDRVAGLVL 129
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 30-132 1.88e-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: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617   30 GSPEGLpVVFIHGGpgagCDaQSRRYFDP------NLYRIITFDQRGCGRSTPHASLENNTTwDLVADL----ERIRLHL 99
Cdd:pfam12146   1 GEPRAV-VVLVHGL----GE-HSGRYAHLadalaaQGFAVYAYDHRGHGRSDGKRGHVPSFD-DYVDDLdtfvDKIREEH 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 496332617  100 GIEKWVVFGGSWGSTLALAYAQTHPERVHGLIL 132
Cdd:pfam12146  74 PGLPLFLLGHSMGGLIAALYALRYPDKVDGLIL 106
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
37-134 8.15e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 52.33  E-value: 8.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  37 VVFIHGGPGAgcdaqSRRYFDPNL-------YRIITFDQRGCGRSTPHASLENntTWDLVADLERIRLHLGI--EKWVVF 107
Cdd:COG1506   26 VVYVHGGPGS-----RDDSFLPLAqalasrgYAVLAPDYRGYGESAGDWGGDE--VDDVLAAIDYLAARPYVdpDRIGIY 98

                         90       100
                 ....*....|....*....|....*..
gi 496332617 108 GGSWGSTLALAYAQTHPERVHGLILRG 134
Cdd:COG1506   99 GHSYGGYMALLAAARHPDRFKAAVALA 125
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 28-132 8.47e-06

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 46.86  E-value: 8.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  28 ESGSPEGLPVVFIHGgpgAGCDAQSRRYFDPNL---YRIITFDQRGCGRSTPhaSLENNTTWDLVADLERIRLHLGIEKW 104
Cdd:PRK14875 125 RLGEGDGTPVVLIHG---FGGDLNNWLFNHAALaagRPVIALDLPGHGASSK--AVGAGSLDELAAAVLAFLDALGIERA 199

                         90       100
                 ....*....|....*....|....*...
gi 496332617 105 VVFGGSWGSTLALAYAQTHPERVHGLIL 132
Cdd:PRK14875 200 HLVGHSMGGAVALRLAARAPQRVASLTL 227
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 17-134 5.21e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 44.52  E-value: 5.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  17 AVDEPHVL-YVDESGSPEGLPVVFIHG-GPGAGC-----DAQSRRYfdpnlyRIITFDQRGCGRST-PH---ASLENNTT 85
Cdd:PLN02894  87 ASNEPRFInTVTFDSKEDAPTLVMVHGyGASQGFffrnfDALASRF------RVIAIDQLGWGGSSrPDftcKSTEETEA 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 496332617  86 WdLVADLERIRLHLGIEKWVVFGGSWGSTLALAYAQTHPERVHGLILRG 134
Cdd:PLN02894 161 W-FIDSFEEWRKAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVG 208
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 10-131 5.61e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 44.19  E-value: 5.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  10 PYARHDLAVDEPH-----VLYVDEsGSPEGLPVVFIHGGP--------------GAGcdaqsrryfdpnlYRIITFDQRG 70
Cdd:PRK00870  18 PFAPHYVDVDDGDggplrMHYVDE-GPADGPPVLLLHGEPswsylyrkmipilaAAG-------------HRVIAPDLIG 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496332617  71 CGRSTPHASLENNTTWDLVADLERIRLHLGIEKWVVFGGSWGSTLALAYAQTHPERVHGLI 131
Cdd:PRK00870  84 FGRSDKPTRREDYTYARHVEWMRSWFEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLV 144
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 37-241 6.71e-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: 43.23  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617   37 VVFIHGGPgagcdaQSRRYFDPNL---YRIITFDQRGCGRSTPHAslennTTWDLVADLERIRLHLGIEKWVVFGG-SWG 112
Cdd:pfam12697   1 VVLVHGAG------LSAAPLAALLaagVAVLAPDLPGHGSSSPPP-----LDLADLADLAALLDELGAARPVVLVGhSLG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  113 STLALAYAqthpervHGLILRGIFLC--------RPQEIEWFYQAGASRLFPDYWQDYVAPIPLDERDDLLSAFHKRLVG 184
Cdd:pfam12697  70 GAVALAAA-------AAALVVGVLVAplaappglLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALAR 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496332617  185 NDQIAQMHAAKAWSTWEGRTATL----RPNPLVVDRFSEPQRALSIARIECHYFTNHAFLE 241
Cdd:pfam12697 143 LAALLAALALLPLAAWRDLPVPVlvlaEEDRLVPELAQRLLAALAGARLVVLPGAGHLPLD 203
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 28-132 1.72e-04

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 42.95  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  28 ESGSPEGLPVVFIHGGPGagcDAQSRRYFDPNL---YRIITFDQRGCGRS-TPHASLE-NNTTWDLVADLERIRLHLGIE 102
Cdd:PLN03084 121 ESGSNNNPPVLLIHGFPS---QAYSYRKVLPVLsknYHAIAFDWLGFGFSdKPQPGYGfNYTLDEYVSSLESLIDELKSD 197

                         90       100       110
                 ....*....|....*....|....*....|
gi 496332617 103 KWVVFGGSWGSTLALAYAQTHPERVHGLIL 132
Cdd:PLN03084 198 KVSLVVQGYFSPPVVKYASAHPDKIKKLIL 227
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 6-132 2.69e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 42.15  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617   6 PQIKPYARHDLAVDEPHVLYVDESGSPeglPVVFIHGGPgagcdAQSRRYFD-----PNLYRIITFDQRGCGRSTpHASL 80
Cdd:PRK03204   9 PQLYPFESRWFDSSRGRIHYIDEGTGP---PILLCHGNP-----TWSFLYRDiivalRDRFRCVAPDYLGFGLSE-RPSG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496332617  81 ENNTTWDLVADLERIRLHLGIEKWVVFGGSWGSTLALAYAQTHPERVHGLIL 132
Cdd:PRK03204  80 FGYQIDEHARVIGEFVDHLGLDRYLSMGQDWGGPISMAVAVERADRVRGVVL 131
MET2 COG2021
Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine ...
 43-132 2.71e-04

Homoserine O-acetyltransferase [Amino acid transport and metabolism]; Homoserine O-acetyltransferase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 441624 [Multi-domain]  Cd Length: 355  Bit Score: 42.00  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  43 GPGagcdaqsrRYFDPNLYRIITFDQRG-CGRSTPHASL--ENNTTW----------DLVADLERIRLHLGIEKW-VVFG 108
Cdd:COG2021   63 GPG--------KAIDTDRYFVICSNVLGgCYGSTGPASInpATGKPYgldfpvvtirDMVRAQKRLLDHLGIERLaAVIG 134

                         90       100
                 ....*....|....*....|....
gi 496332617 109 GSWGSTLALAYAQTHPERVHGLIL 132
Cdd:COG2021  135 GSMGGMQALEWAVSYPDRVRRAIV 158
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 87-158 9.21e-04

Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, and Ndr3. Their similarity was previously noted. The precise molecular and cellular function of members of this family is still unknown. Yet, they are known to be involved in cellular differentiation events. The Ndr1 group was the first to be discovered. Their expression is repressed by the proto-oncogenes N-myc and c-myc, and in line with this observation, Ndr1 protein expression is down-regulated in neoplastic cells, and is reactivated when differentiation is induced by chemicals such as retinoic acid. Ndr2 and Ndr3 expression is not under the control of N-myc or c-myc. Ndr1 expression is also activated by several chemicals: tunicamycin and homocysteine induce Ndr1 in human umbilical endothelial cells; nickel induces Ndr1 in several cell types. Members of this family are found in wide variety of multicellular eukaryotes, including an Ndr1 type protein in Helianthus annuus (sunflower), known as Sf21. Interestingly, the highest scoring matches in the noise are all alpha/beta hydrolases pfam00561, suggesting that this family may have an enzymatic function (Bateman A pers. obs.).


Pssm-ID: 397285 [Multi-domain]  Cd Length: 285  Bit Score: 40.41  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617   87 DLVADLERIRLHLGIEKWVVFGGSWGSTLALAYAQTHPERVHGLILRGIFLCRPQEIEWFYQ---------AGASRLFPD 157
Cdd:pfam03096  84 DLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNklsskllyyYGMTDSAKD 163


                  .
gi 496332617  158 Y 158
Cdd:pfam03096 164 Y 164
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 23-294 9.99e-04

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 39.90  E-value: 9.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  23 VLYVDESGSPeGLPVVfIHGGPGAGCDAQSRRYFdPNLYR----IITFDQRGCGRS--TPH--ASLENNttwDLVADLER 94
Cdd:COG1073   26 DLYLPAGASK-KYPAV-VVAHGNGGVKEQRALYA-QRLAElgfnVLAFDYRGYGESegEPReeGSPERR---DARAAVDY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  95 IRLHLGI--EKWVVFGGSWGSTLALAYAQTHPeRVHGLILrgiflcrpqeiewfyQAGASRLfpdywqdyvapiplderd 172
Cdd:COG1073  100 LRTLPGVdpERIGLLGISLGGGYALNAAATDP-RVKAVIL---------------DSPFTSL------------------ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617 173 dllsafhkrlvgnDQIAQMHAAKAWSTWEGRTAtLRPNPLVVDRFSEPQRALS-IARIEChyftnhaflepnqlirdmgk 251
Cdd:COG1073  146 -------------EDLAAQRAKEARGAYLPGVP-YLPNVRLASLLNDEFDPLAkIEKISR-------------------- 191

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 496332617 252 iahlPGVIVHGRYDVICPLDNAWELHQAWP-NSELQVIRDAGHA 294
Cdd:COG1073  192 ----PLLFIHGEKDEAVPFYMSEDLYEAAAePKELLIVPGAGHV 231
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 10-153 1.28e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 39.98  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  10 PYARHDLAVDEPHVLYVDESgspEGLPVVFIHGGPGAgcdAQSRRYFDPNLY---RIITFDQRGCGRS-TPHASLennTT 85
Cdd:PRK03592   6 PGEMRRVEVLGSRMAYIETG---EGDPIVFLHGNPTS---SYLWRNIIPHLAglgRCLAPDLIGMGASdKPDIDY---TF 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496332617  86 WDLVADLERIRLHLGIEKWVVFGGSWGSTLALAYAQTHPERVHGLILRGIFLcRPQEIEWFYQAGASR 153
Cdd:PRK03592  77 ADHARYLDAWFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFMEAIV-RPMTWDDFPPAVREL 143
PRK08775 PRK08775
homoserine O-succinyltransferase;
32-132 1.29e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 40.16  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  32 PEGLPVVFIHGGPGAGCD----------------AQSRRYFDPNLYRIITFDQRGCGRSTPHASlennTTWDLVADLERI 95
Cdd:PRK08775  55 PAGAPVVFVAGGISAHRHvaatatfpekgwweglVGSGRALDPARFRLLAFDFIGADGSLDVPI----DTADQADAIALL 130

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 496332617  96 RLHLGIEKWVVF-GGSWGSTLALAYAQTHPERVHGLIL 132
Cdd:PRK08775 131 LDALGIARLHAFvGYSYGALVGLQFASRHPARVRTLVV 168
metX PRK00175
homoserine O-acetyltransferase; Provisional
 98-132 5.55e-03

homoserine O-acetyltransferase; Provisional


Pssm-ID: 234678 [Multi-domain]  Cd Length: 379  Bit Score: 38.25  E-value: 5.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 496332617  98 HLGIEKWV-VFGGSWGSTLALAYAQTHPERV-HGLIL 132
Cdd:PRK00175 142 ALGITRLAaVVGGSMGGMQALEWAIDYPDRVrSALVI 178
PLN02578 PLN02578
hydrolase
 33-132 9.36e-03

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 37.51  E-value: 9.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496332617  33 EGLPVVFIHggpGAGCDAQSRRYFDPNL---YRIITFDQRGCGRSTPHASLENNTTW-DLVADLERirlHLGIEKWVVFG 108
Cdd:PLN02578  85 EGLPIVLIH---GFGASAFHWRYNIPELakkYKVYALDLLGFGWSDKALIEYDAMVWrDQVADFVK---EVVKEPAVLVG 158

                         90       100
                 ....*....|....*....|....
gi 496332617 109 GSWGSTLALAYAQTHPERVHGLIL 132
Cdd:PLN02578 159 NSLGGFTALSTAVGYPELVAGVAL 182
 
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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