|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
87-421 |
2.21e-68 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 222.48 E-value: 2.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 87 GKANKRSIVYMHGYGAGLGFYFRNMDGLTKgvtkDFNSYFVDWLGMGNSSRPPFDIKGQtasekvEETERFFTESLETWR 166
Cdd:PLN02894 101 SKEDAPTLVMVHGYGASQGFFFRNFDALAS----RFRVIAIDQLGWGGSSRPDFTCKST------EETEAWFIDSFEEWR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 167 IGHGIEKMILVGHSMGGYLSAVYAMQYPERVEKLLLVSPVAIPENPfasnDDAEvynsvassavhavmdepplsnvtnev 246
Cdd:PLN02894 171 KAKNLSNFILLGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSES----DDKS-------------------------- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 247 lqtqEETTGLEPSRPSKpknplprFITFLWEQNVTPFSLLRLSGPLGPKLMSFWSSRRFST------LPPETFRALHNYC 320
Cdd:PLN02894 221 ----EWLTKFRATWKGA-------VLNHLWESNFTPQKIIRGLGPWGPNLVRRYTTARFGAhstgdiLSEEESKLLTDYV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 321 YSIFRLKGSSEYALGNLLAPGAFARRCIMNRLRMLKCRTIFMYGDKDWMDDVAGLEATnrlKEMNIEAEHHIISNAGHHC 400
Cdd:PLN02894 290 YHTLAAKASGELCLKYIFSFGAFARKPLLESASEWKVPTTFIYGRHDWMNYEGAVEAR---KRMKVPCEIIRVPQGGHFV 366
|
330 340
....*....|....*....|.
gi 19115012 401 YLDNPEDFNEIVLKEIRMSLR 421
Cdd:PLN02894 367 FLDNPSGFHSAVLYACRKYLS 387
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
94-405 |
1.13e-18 |
|
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: 84.86 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 94 IVYMHGYGAGLGFYFRNMDGLTKgvtKDFNSYFVDWLGMGNSSRPPFDIKGQTASekveeTERFFTESLETwrigHGIEK 173
Cdd:pfam00561 3 VLLLHGLPGSSDLWRKLAPALAR---DGFRVIALDLRGFGKSSRPKAQDDYRTDD-----LAEDLEYILEA----LGLEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 174 MILVGHSMGGYLSAVYAMQYPERVEKLLLVSPvaiPENPFASNDDAEVYnsvassavhavmdepplsnvtNEVLQTQEET 253
Cdd:pfam00561 71 VNLVGHSMGGLIALAYAAKYPDRVKALVLLGA---LDPPHELDEADRFI---------------------LALFPGFFDG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 254 TglepsRPSKPKNPLPRFITFLWeqnVTPFSLLRLSGPLGPKLMSFWSSRRFSTLPPETFRalhnycysifrlkgsseya 333
Cdd:pfam00561 127 F-----VADFAPNPLGRLVAKLL---ALLLLRLRLLKALPLLNKRFPSGDYALAKSLVTGA------------------- 179
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115012 334 lgnLLAPGAFARRCIMNRLRMLKCRTIFMYGDKDWMDDVAGLEATNRLKEmniEAEHHIISNAGHHCYLDNP 405
Cdd:pfam00561 180 ---LLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFP---NARLVVIPDAGHFAFLEGP 245
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
94-413 |
6.15e-17 |
|
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: 79.27 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 94 IVYMHGYGAGLGFYFRNMDGLTKGvtkdFNSYFVDWLGMGNSSRPPFDIKGQTASEKVEEterfFTESLetwrighGIEK 173
Cdd:COG0596 26 VVLLHGLPGSSYEWRPLIPALAAG----YRVIAPDLRGHGRSDKPAGGYTLDDLADDLAA----LLDAL-------GLER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 174 MILVGHSMGGYLSAVYAMQYPERVEKLLLVSpvaipenpfasnddaevynsvassavhavmdepplsnvtnevlqtqeet 253
Cdd:COG0596 91 VVLVGHSMGGMVALELAARHPERVAGLVLVD------------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 254 tglepsrpskpknplprfitflweqnvtpfsllrlsgplgpklmsfwssrrfstlppETFRALHNYcysiFRLKGSSEYA 333
Cdd:COG0596 122 ---------------------------------------------------------EVLAALAEP----LRRPGLAPEA 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 334 LGNLLApgAFARRCIMNRLRMLKCRTIFMYGDKDWMDDVAGLEatnRLKEMNIEAEHHIISNAGHHCYLDNPEDFNEIVL 413
Cdd:COG0596 141 LAALLR--ALARTDLRERLARITVPTLVIWGEKDPIVPPALAR---RLAELLPNAELVVLPGAGHFPPLEQPEAFAAALR 215
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
91-205 |
1.40e-14 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 72.34 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 91 KRSIVYMHGYGAGLGFYFRNMDGLTKgvtKDFNSYFVDWLGMGNSSRPPFDIKGQTASekVEETERFftesLETWRIGHG 170
Cdd:COG2267 28 RGTVVLVHGLGEHSGRYAELAEALAA---AGYAVLAFDLRGHGRSDGPRGHVDSFDDY--VDDLRAA----LDALRARPG 98
|
90 100 110
....*....|....*....|....*....|....*
gi 19115012 171 iEKMILVGHSMGGYLSAVYAMQYPERVEKLLLVSP 205
Cdd:COG2267 99 -LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP 132
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
87-208 |
1.50e-08 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 56.11 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 87 GKANKRSIVYMHGYGAGLGFYFRNMDGLTKGVTkdfnSYFVDWLGMGNSSRppfDIKGQTASEKVEETERFftesLETwr 166
Cdd:PRK14875 127 GEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRP----VIALDLPGHGASSK---AVGAGSLDELAAAVLAF----LDA-- 193
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 19115012 167 igHGIEKMILVGHSMGGYLSAVYAMQYPERVEKLLLVSPVAI 208
Cdd:PRK14875 194 --LGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAGL 233
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
91-205 |
3.46e-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: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 91 KRSIVYMHGYGAGLGFYFRNMDGLTKgvtKDFNSYFVDWLGMGNSSRPPFDIKGQTASekVEETERFFTESLETwrigHG 170
Cdd:pfam12146 4 RAVVVLVHGLGEHSGRYAHLADALAA---QGFAVYAYDHRGHGRSDGKRGHVPSFDDY--VDDLDTFVDKIREE----HP 74
|
90 100 110
....*....|....*....|....*....|....*
gi 19115012 171 IEKMILVGHSMGGYLSAVYAMQYPERVEKLLLVSP 205
Cdd:pfam12146 75 GLPLFLLGHSMGGLIAALYALRYPDKVDGLILSAP 109
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
88-214 |
4.13e-08 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 53.79 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 88 KANKRSIVYMHGYGAG------LGFYFRNmdgltkgvtKDFNSYFVDWLGMGNSsrpPFDIKGQTASEKVEETERFFTES 161
Cdd:COG1647 12 EGGRKGVLLLHGFTGSpaemrpLAEALAK---------AGYTVYAPRLPGHGTS---PEDLLKTTWEDWLEDVEEAYEIL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 19115012 162 LETWrighgiEKMILVGHSMGGYLSAVYAMQYPErVEKLLLVSPVAIPENPFA 214
Cdd:COG1647 80 KAGY------DKVIVIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSA 125
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
94-309 |
2.16e-07 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 51.32 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 94 IVYMHGYGAGlgfyfrnMDGLTKGVTKDFNSYFVDWLGMGNSSRPPFDIkgqtasEKVEETERFFTESLETWRIghgiek 173
Cdd:pfam12697 1 VVLVHGAGLS-------AAPLAALLAAGVAVLAPDLPGHGSSSPPPLDL------ADLADLAALLDELGAARPV------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 174 mILVGHSMGGYLSAVYAMQYPERVeklLLVSPVAIPENPFASN---------DDAEVYNSVASSAVHAVMDEPPLSNVTN 244
Cdd:pfam12697 62 -VLVGHSLGGAVALAAAAAALVVG---VLVAPLAAPPGLLAALlallarlgaALAAPAWLAAESLARGFLDDLPADAEWA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115012 245 EVLQTQEETTGLEPSRPSKPKNPLPRFITFLWEQNvtpfsllRLSGPLGPKLMSFWSSRRFSTLP 309
Cdd:pfam12697 138 AALARLAALLAALALLPLAAWRDLPVPVLVLAEED-------RLVPELAQRLLAALAGARLVVLP 195
|
|
| PLN02578 |
PLN02578 |
hydrolase |
94-221 |
1.07e-05 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 47.14 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 94 IVYMHGYGAGLgFYFR-NMDGLTKgvtkDFNSYFVDWLGMGNSSRPPFDIKGQTASEKVEEterFFTESLEtwrighgiE 172
Cdd:PLN02578 89 IVLIHGFGASA-FHWRyNIPELAK----KYKVYALDLLGFGWSDKALIEYDAMVWRDQVAD---FVKEVVK--------E 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 19115012 173 KMILVGHSMGGYLSAVYAMQYPERVEKLLLVSPVAIPENPFASNDDAEV 221
Cdd:PLN02578 153 PAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAGQFGSESREKEEAIV 201
|
|
| PRK10673 |
PRK10673 |
esterase; |
169-207 |
4.90e-05 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 44.72 E-value: 4.90e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 19115012 169 HGIEKMILVGHSMGGYLSAVYAMQYPERVEKLLL--VSPVA 207
Cdd:PRK10673 78 LQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAidIAPVD 118
|
|
| YdeN |
COG3545 |
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only]; |
175-212 |
5.33e-05 |
|
Predicted esterase of the alpha/beta hydrolase fold [General function prediction only];
Pssm-ID: 442766 [Multi-domain] Cd Length: 170 Bit Score: 43.30 E-value: 5.33e-05
10 20 30
....*....|....*....|....*....|....*...
gi 19115012 175 ILVGHSMGGYLSAVYAMQYPERVEKLLLVSPvAIPENP 212
Cdd:COG3545 57 VLVAHSLGCLAVAHWAARLPRKVAGALLVAP-PDPERP 93
|
|
| PLN03087 |
PLN03087 |
BODYGUARD 1 domain containing hydrolase; Provisional |
83-205 |
1.22e-04 |
|
BODYGUARD 1 domain containing hydrolase; Provisional
Pssm-ID: 215567 Cd Length: 481 Bit Score: 44.03 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 83 DKATGKANKRSIVYMHGYGAGLGFY----FRNMDGLTKGVTKDFNsyfVDWLGMGNSSRPPFDIkgQTASEKVEETERFF 158
Cdd:PLN03087 193 QQPKDNKAKEDVLFIHGFISSSAFWtetlFPNFSDAAKSTYRLFA---VDLLGFGRSPKPADSL--YTLREHLEMIERSV 267
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 19115012 159 TESletwrigHGIEKMILVGHSMGGYLSAVYAMQYPERVEKLLLVSP 205
Cdd:PLN03087 268 LER-------YKVKSFHIVAHSLGCILALALAVKHPGAVKSLTLLAP 307
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
87-219 |
1.93e-04 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 87 GKANKRSIVYMHGYGA---GLGFYFRNMDgltkgvTKDFNSYFVDwlgmGNSSRPP-----FDIKGQTASEK---VEETE 155
Cdd:COG0400 1 GGPAAPLVVLLHGYGGdeeDLLPLAPELA------LPGAAVLAPR----APVPEGPggrawFDLSFLEGREDeegLAAAA 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115012 156 RFFTESLETWRIGHGI--EKMILVGHSMGGYLSAVYAMQYPERVEKLLLVSPVAIPENPFASNDDA 219
Cdd:COG0400 71 EALAAFIDELEARYGIdpERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAA 136
|
|
| PLN03084 |
PLN03084 |
alpha/beta hydrolase fold protein; Provisional |
86-211 |
3.26e-04 |
|
alpha/beta hydrolase fold protein; Provisional
Pssm-ID: 178633 Cd Length: 383 Bit Score: 42.56 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 86 TGKANKRSIVYMHGYGAGlGFYFRNMDGLtkgVTKDFNSYFVDWLGMGNSSRPPFDikgqtasEKVEETERFFTESLETW 165
Cdd:PLN03084 122 SGSNNNPPVLLIHGFPSQ-AYSYRKVLPV---LSKNYHAIAFDWLGFGFSDKPQPG-------YGFNYTLDEYVSSLESL 190
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 19115012 166 RIGHGIEKMILVGHsmgGYLSAV---YAMQYPERVEKLLLVSPVAIPEN 211
Cdd:PLN03084 191 IDELKSDKVSLVVQ---GYFSPPvvkYASAHPDKIKKLILLNPPLTKEH 236
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
88-205 |
4.00e-04 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 39.43 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 88 KANKRSIVYMHGYGAGLGFYFRNMDGLTKgvtKDFNSYFVDWLGMGNSsrppfdikgqtasekVEETERFFTESLETWRI 167
Cdd:COG1075 2 AATRYPVVLVHGLGGSAASWAPLAPRLRA---AGYPVYALNYPSTNGS---------------IEDSAEQLAAFVDAVLA 63
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 19115012 168 GHGIEKMILVGHSMGGYLSAVYA--MQYPERVEKLLLVSP 205
Cdd:COG1075 64 ATGAEKVDLVGHSMGGLVARYYLkrLGGAAKVARVVTLGT 103
|
|
| PGAP1 |
pfam07819 |
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ... |
169-243 |
2.78e-03 |
|
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.
Pssm-ID: 369540 Cd Length: 233 Bit Score: 39.27 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 169 HGIEKMILVGHSMGGYLS---AVYAMQYPERVEKLL-LVSPVAIPENPFaSNDDAEVYNSVAS--SAVHAVMDEPPLSNV 242
Cdd:pfam07819 88 PGPTSVILIGHSMGGIVAraaLTLPNYIPQSVNTIItLSSPHAKPPLTF-DGDILKFYERLNAfwRKLYNDGDSNNLSNV 166
|
.
gi 19115012 243 T 243
Cdd:pfam07819 167 L 167
|
|
| PLN02679 |
PLN02679 |
hydrolase, alpha/beta fold family protein |
81-182 |
3.55e-03 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178283 [Multi-domain] Cd Length: 360 Bit Score: 39.44 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 81 VSDKATGKANKRSIVYMHGYGAGLGFYFRNMDGLTKGVTkdfnSYFVDWLGMGNSSRPPfdikgqtasekveeterFFTE 160
Cdd:PLN02679 78 VKGSPEVTSSGPPVLLVHGFGASIPHWRRNIGVLAKNYT----VYAIDLLGFGASDKPP-----------------GFSY 136
|
90 100
....*....|....*....|....*....
gi 19115012 161 SLETWR------IGHGIEK-MILVGHSMG 182
Cdd:PLN02679 137 TMETWAelildfLEEVVQKpTVLIGNSVG 165
|
|
| PHA02857 |
PHA02857 |
monoglyceride lipase; Provisional |
174-250 |
4.26e-03 |
|
monoglyceride lipase; Provisional
Pssm-ID: 165193 [Multi-domain] Cd Length: 276 Bit Score: 38.71 E-value: 4.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115012 174 MILVGHSMGGYLSAVYAMQYPERVEKLLLVSPVAIPEN-PFASNDDAEVYNSVASSAVHAVMDEPPLSNVTNEVLQTQ 250
Cdd:PHA02857 99 VFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNAEAvPRLNLLAAKLMGIFYPNKIVGKLCPESVSRDMDEVYKYQ 176
|
|
| Esterase |
pfam00756 |
Putative esterase; This family contains Esterase D. However it is not clear if all members of ... |
176-213 |
4.28e-03 |
|
Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.
Pssm-ID: 395613 [Multi-domain] Cd Length: 246 Bit Score: 38.60 E-value: 4.28e-03
10 20 30
....*....|....*....|....*....|....*...
gi 19115012 176 LVGHSMGGYLSAVYAMQYPERVEKLLLVSPVAIPENPF 213
Cdd:pfam00756 114 LAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNSM 151
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
94-207 |
4.43e-03 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 38.46 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115012 94 IVYMHGYGAG-LGFYFRNMDGLTKgvtKDFNSYFVDWLGMGNSSrppfdikGQTASEKVEETERFFTesletWRIGHGI- 171
Cdd:COG1506 26 VVYVHGGPGSrDDSFLPLAQALAS---RGYAVLAPDYRGYGESA-------GDWGGDEVDDVLAAID-----YLAARPYv 90
|
90 100 110
....*....|....*....|....*....|....*...
gi 19115012 172 --EKMILVGHSMGGYLSAVYAMQYPERVEKLLLVSPVA 207
Cdd:COG1506 91 dpDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS 128
|
|
| |
