|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10673 |
PRK10673 |
esterase; |
38-305 |
1.48e-38 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 136.78 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 38 ELSFDSYTGENPETSPPLLTYHGLFGSKQNWRGISKALVRkvSRKVYAIDVRNHGESPHSSVHNSKAMSEDLRLFMEQRS 117
Cdd:PRK10673 2 KLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVN--DHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 118 HPNAACMGHSMGGRSMMYFARKYPELVERLIVVDISPIS--VPRStgemTEIFDAMVSLDLSPSMSMSEGRKIAREKLlk 195
Cdd:PRK10673 80 IEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDyhVRRH----DEIFAAINAVSEAGATTRQQAAAIMRQHL-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 196 aTEDETVDFIMLNLRKNpdtgafSWACNAHVLRefltrfDKYQS--NLEELPPYTGPTTFICGTRSPYMRREQWPQIQKM 273
Cdd:PRK10673 154 -NEEGVIQFLLKSFVDG------EWRFNVPVLW------DQYPHivGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQ 220
|
250 260 270
....*....|....*....|....*....|...
gi 114208056 274 FPNSEIHWLD-AGHLVHFEKPQEFLTIVSEFLN 305
Cdd:PRK10673 221 FPQARAHVIAgAGHWVHAEKPDAVLRAIRRYLN 253
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
53-307 |
3.56e-35 |
|
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: 126.65 E-value: 3.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 53 PPLLTYHGLFGSKQNWRGISKALVRKvsRKVYAIDVRNHGESPHSSVHNS-KAMSEDLRLFMEQRSHPNAACMGHSMGGR 131
Cdd:COG0596 24 PPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSDKPAGGYTlDDLADDLAALLDALGLERVVLVGHSMGGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 132 SMMYFARKYPELVERLIVVdispisvprstgemteifdamvsldlspsmsmsegrkiarekllkateDETVDFIMLNLRk 211
Cdd:COG0596 102 VALELAARHPERVAGLVLV------------------------------------------------DEVLAALAEPLR- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 212 npdtgafSWACNAHVLREFLTRFDKYqSNLEELPPYTGPTTFICGTRSPYMRREQWPQIQKMFPNSEIHWL-DAGHLVHF 290
Cdd:COG0596 133 -------RPGLAPEALAALLRALART-DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLpGAGHFPPL 204
|
250
....*....|....*..
gi 114208056 291 EKPQEFLTIVSEFLNRT 307
Cdd:COG0596 205 EQPEAFAAALRDFLARL 221
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
53-293 |
2.54e-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: 109.52 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 53 PPLLTYHGLFGSKQNWRGISKALVRKVsRKVYAIDVRNHGESPHSSVHNS---KAMSEDLRLFMEQRSHPNAACMGHSMG 129
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDG-FRVIALDLRGFGKSSRPKAQDDyrtDDLAEDLEYILEALGLEKVNLVGHSMG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 130 GRSMMYFARKYPELVERLIVVdiSPISVPRSTGEMTEI--------FDAMVSLDLSPSMSMSEGRKIA----REKLLKAT 197
Cdd:pfam00561 80 GLIALAYAAKYPDRVKALVLL--GALDPPHELDEADRFilalfpgfFDGFVADFAPNPLGRLVAKLLAllllRLRLLKAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 198 EDETVDFIM--LNLRKNPDTGAFSWACnahvlrefltrFDKYQSNLEELPPYTGPTTFICGTRSPYMRREQWPQIQKMFP 275
Cdd:pfam00561 158 PLLNKRFPSgdYALAKSLVTGALLFIE-----------TWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFP 226
|
250
....*....|....*....
gi 114208056 276 NS-EIHWLDAGHLVHFEKP 293
Cdd:pfam00561 227 NArLVVIPDAGHFAFLEGP 245
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10673 |
PRK10673 |
esterase; |
38-305 |
1.48e-38 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 136.78 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 38 ELSFDSYTGENPETSPPLLTYHGLFGSKQNWRGISKALVRkvSRKVYAIDVRNHGESPHSSVHNSKAMSEDLRLFMEQRS 117
Cdd:PRK10673 2 KLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVN--DHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 118 HPNAACMGHSMGGRSMMYFARKYPELVERLIVVDISPIS--VPRStgemTEIFDAMVSLDLSPSMSMSEGRKIAREKLlk 195
Cdd:PRK10673 80 IEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDyhVRRH----DEIFAAINAVSEAGATTRQQAAAIMRQHL-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 196 aTEDETVDFIMLNLRKNpdtgafSWACNAHVLRefltrfDKYQS--NLEELPPYTGPTTFICGTRSPYMRREQWPQIQKM 273
Cdd:PRK10673 154 -NEEGVIQFLLKSFVDG------EWRFNVPVLW------DQYPHivGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQ 220
|
250 260 270
....*....|....*....|....*....|...
gi 114208056 274 FPNSEIHWLD-AGHLVHFEKPQEFLTIVSEFLN 305
Cdd:PRK10673 221 FPQARAHVIAgAGHWVHAEKPDAVLRAIRRYLN 253
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
53-307 |
3.56e-35 |
|
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: 126.65 E-value: 3.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 53 PPLLTYHGLFGSKQNWRGISKALVRKvsRKVYAIDVRNHGESPHSSVHNS-KAMSEDLRLFMEQRSHPNAACMGHSMGGR 131
Cdd:COG0596 24 PPVVLLHGLPGSSYEWRPLIPALAAG--YRVIAPDLRGHGRSDKPAGGYTlDDLADDLAALLDALGLERVVLVGHSMGGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 132 SMMYFARKYPELVERLIVVdispisvprstgemteifdamvsldlspsmsmsegrkiarekllkateDETVDFIMLNLRk 211
Cdd:COG0596 102 VALELAARHPERVAGLVLV------------------------------------------------DEVLAALAEPLR- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 212 npdtgafSWACNAHVLREFLTRFDKYqSNLEELPPYTGPTTFICGTRSPYMRREQWPQIQKMFPNSEIHWL-DAGHLVHF 290
Cdd:COG0596 133 -------RPGLAPEALAALLRALART-DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLpGAGHFPPL 204
|
250
....*....|....*..
gi 114208056 291 EKPQEFLTIVSEFLNRT 307
Cdd:COG0596 205 EQPEAFAAALRDFLARL 221
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
53-293 |
2.54e-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: 109.52 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 53 PPLLTYHGLFGSKQNWRGISKALVRKVsRKVYAIDVRNHGESPHSSVHNS---KAMSEDLRLFMEQRSHPNAACMGHSMG 129
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDG-FRVIALDLRGFGKSSRPKAQDDyrtDDLAEDLEYILEALGLEKVNLVGHSMG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 130 GRSMMYFARKYPELVERLIVVdiSPISVPRSTGEMTEI--------FDAMVSLDLSPSMSMSEGRKIA----REKLLKAT 197
Cdd:pfam00561 80 GLIALAYAAKYPDRVKALVLL--GALDPPHELDEADRFilalfpgfFDGFVADFAPNPLGRLVAKLLAllllRLRLLKAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 198 EDETVDFIM--LNLRKNPDTGAFSWACnahvlrefltrFDKYQSNLEELPPYTGPTTFICGTRSPYMRREQWPQIQKMFP 275
Cdd:pfam00561 158 PLLNKRFPSgdYALAKSLVTGALLFIE-----------TWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFP 226
|
250
....*....|....*....
gi 114208056 276 NS-EIHWLDAGHLVHFEKP 293
Cdd:pfam00561 227 NArLVVIPDAGHFAFLEGP 245
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
49-304 |
2.00e-11 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 63.81 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 49 PETSPPLLTYHGLFGSKQNWRGISKALVRKvsRKVYAIDVRNHGESPHSSVHNS-KAMSEDLRLFMEQRSHPNAACMGHS 127
Cdd:PRK14875 128 EGDGTPVVLIHGFGGDLNNWLFNHAALAAG--RPVIALDLPGHGASSKAVGAGSlDELAAAVLAFLDALGIERAHLVGHS 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 128 MGGRSMMYFARKYPELVERLIVvdISPISV-PRSTGEMTEIF-DAMVSLDLSPSMSM--SEGRKIAR---EKLLKATEDE 200
Cdd:PRK14875 206 MGGAVALRLAARAPQRVASLTL--IAPAGLgPEINGDYIDGFvAAESRRELKPVLELlfADPALVTRqmvEDLLKYKRLD 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 201 TVDFIMLNLRKNpdtgAFSWACNAHVLREFLTRFDKyqsnleelppytgPTTFICGtrspymRREQ---WPQIQKMFPNS 277
Cdd:PRK14875 284 GVDDALRALADA----LFAGGRQRVDLRDRLASLAI-------------PVLVIWG------EQDRiipAAHAQGLPDGV 340
|
250 260
....*....|....*....|....*...
gi 114208056 278 EIHWLD-AGHLVHFEKPQEFLTIVSEFL 304
Cdd:PRK14875 341 AVHVLPgAGHMPQMEAAADVNRLLAEFL 368
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
59-154 |
7.89e-10 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 57.70 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 59 HGLFGSKQNWRGISKALVRK-VSrkVYAIDVRNHGESPHSSVHNS--KAMSEDLRLFMEQ-RSHPNAAC--MGHSMGGRS 132
Cdd:COG2267 35 HGLGEHSGRYAELAEALAAAgYA--VLAFDLRGHGRSDGPRGHVDsfDDYVDDLRAALDAlRARPGLPVvlLGHSMGGLI 112
|
90 100
....*....|....*....|..
gi 114208056 133 MMYFARKYPELVERLIVvdISP 154
Cdd:COG2267 113 ALLYAARYPDRVAGLVL--LAP 132
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
83-159 |
3.71e-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: 52.99 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 83 VYAIDVRNHGESP--HSSVHNSKAMSEDLRLFME--QRSHPNA--ACMGHSMGGRSMMYFARKYPELVERLIV----VDI 152
Cdd:pfam12146 34 VYAYDHRGHGRSDgkRGHVPSFDDYVDDLDTFVDkiREEHPGLplFLLGHSMGGLIAALYALRYPDKVDGLILsapaLKI 113
|
....*..
gi 114208056 153 SPISVPR 159
Cdd:pfam12146 114 KPYLAPP 120
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
59-296 |
5.67e-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: 49.39 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 59 HGLFGSKQNWRGISKALVRkvsrkVYAIDVRNHGESPHSSVHNSKAmsEDLRLFMEQ-RSHPNAACMGHSMGGRSMMYFA 137
Cdd:pfam12697 5 HGAGLSAAPLAALLAAGVA-----VLAPDLPGHGSSSPPPLDLADL--ADLAALLDElGAARPVVLVGHSLGGAVALAAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 138 RkypelVERLIVVDISPISVPrsTGEMTEIFDAMVSLdlspsmsmsegRKIAREKLLKATEDETVDFImlnlrkNPDTGA 217
Cdd:pfam12697 78 A-----AALVVGVLVAPLAAP--PGLLAALLALLARL-----------GAALAAPAWLAAESLARGFL------DDLPAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 218 FSWACNAHVLREFLTRFDKYQsnLEELPPYTGPTTFICgTRSPYMRREqWPQIQKMFPNSEIHWL-DAGHLVHFEkPQEF 296
Cdd:pfam12697 134 AEWAAALARLAALLAALALLP--LAAWRDLPVPVLVLA-EEDRLVPEL-AQRLLAALAGARLVVLpGAGHLPLDD-PEEV 208
|
|
| PLN02578 |
PLN02578 |
hydrolase |
53-305 |
1.87e-06 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 48.68 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 53 PPLLTYHGLFGSKQNWRGISKALVRKvsRKVYAIDVRNHGESPHSSV-HNSKAMSEDLRLFMEQRSHPNAACMGHSMGGR 131
Cdd:PLN02578 87 LPIVLIHGFGASAFHWRYNIPELAKK--YKVYALDLLGFGWSDKALIeYDAMVWRDQVADFVKEVVKEPAVLVGNSLGGF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 132 SMMYFARKYPELVERLIVVDIS-PISVPRSTGEMTEIFDAMVSLDLSPSMSMSEGRKI------------AR-EKLLKAT 197
Cdd:PLN02578 165 TALSTAVGYPELVAGVALLNSAgQFGSESREKEEAIVVEETVLTRFVVKPLKEWFQRVvlgflfwqakqpSRiESVLKSV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 198 --EDETVDFIMLN--LRKNPDTGAfswacnAHVLREFLTRFDKYQSNL---EELPPYTGPTTFICGTRSPYMRREQWPQI 270
Cdd:PLN02578 245 ykDKSNVDDYLVEsiTEPAADPNA------GEVYYRLMSRFLFNQSRYtldSLLSKLSCPLLLLWGDLDPWVGPAKAEKI 318
|
250 260 270
....*....|....*....|....*....|....*
gi 114208056 271 QKMFPNSEIHWLDAGHLVHFEKPQEFLTIVSEFLN 305
Cdd:PLN02578 319 KAFYPDTTLVNLQAGHCPHDEVPEQVNKALLEWLS 353
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
51-137 |
3.61e-06 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 47.14 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 51 TSPPLLTYHGLFGSKQNWRGISKALVRkvsRKVYAIDVRNHGESPHSSVHNSKAMSEDLRLFMEQRSHPNAACMGHSMGG 130
Cdd:PRK11126 1 GLPWLVFLHGLLGSGQDWQPVGEALPD---YPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGG 77
|
....*..
gi 114208056 131 RSMMYFA 137
Cdd:PRK11126 78 RIAMYYA 84
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
59-148 |
1.82e-05 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 42.89 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 59 HGLFGSKQNWRGISKALVRKvSRKVYAIDVrnhgESPHSSVHNSkamSEDLRLFMEQ-RSHPNAACM---GHSMGGRSMM 134
Cdd:COG1075 12 HGLGGSAASWAPLAPRLRAA-GYPVYALNY----PSTNGSIEDS---AEQLAAFVDAvLAATGAEKVdlvGHSMGGLVAR 83
|
90
....*....|....*.
gi 114208056 135 YFARKY--PELVERLI 148
Cdd:COG1075 84 YYLKRLggAAKVARVV 99
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
34-172 |
7.13e-05 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 43.47 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 34 PDPVELSFDSYTGENPETSPPLLTYHGLFGSKQN-WRGISKALVRK--VsrkVYAIDVRNHGESPHssvHNSKAMSEDLR 110
Cdd:COG1506 5 ADGTTLPGWLYLPADGKKYPVVVYVHGGPGSRDDsFLPLAQALASRgyA---VLAPDYRGYGESAG---DWGGDEVDDVL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 114208056 111 LFMEQ-RSHPNA-----ACMGHSMGGRSMMYFARKYPELVERliVVDISPISVPRSTGEMTEIFDAMV 172
Cdd:COG1506 79 AAIDYlAARPYVdpdriGIYGHSYGGYMALLAAARHPDRFKA--AVALAGVSDLRSYYGTTREYTERL 144
|
|
| PLN02824 |
PLN02824 |
hydrolase, alpha/beta fold family protein |
53-153 |
1.66e-04 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178419 [Multi-domain] Cd Length: 294 Bit Score: 42.42 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 53 PPLLTYHGLFGSKQNWRGISKALVRkvSRKVYAIDVRNHGES--------PHSSVHNSKAMSEDLRLFMEQRSHPNAACM 124
Cdd:PLN02824 30 PALVLVHGFGGNADHWRKNTPVLAK--SHRVYAIDLLGYGYSdkpnprsaPPNSFYTFETWGEQLNDFCSDVVGDPAFVI 107
|
90 100
....*....|....*....|....*....
gi 114208056 125 GHSMGGRSMMYFARKYPELVERLIVVDIS 153
Cdd:PLN02824 108 CNSVGGVVGLQAAVDAPELVRGVMLINIS 136
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
46-154 |
2.04e-04 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 42.92 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 46 GENPETSPPLLtYHGLFGSKQNWRGISKALvrKVSRKVYAIDVRNHGESPHSSvHNSKAMSE---------DLRL-FMEQ 115
Cdd:PLN02980 1366 GQNAEGSVVLF-LHGFLGTGEDWIPIMKAI--SGSARCISIDLPGHGGSKIQN-HAKETQTEptlsvelvaDLLYkLIEH 1441
|
90 100 110
....*....|....*....|....*....|....*....
gi 114208056 116 RSHPNAACMGHSMGGRSMMYFARKYPELVERLIVVDISP 154
Cdd:PLN02980 1442 ITPGKVTLVGYSMGARIALYMALRFSDKIEGAVIISGSP 1480
|
|
| ABHD18 |
pfam09752 |
Alpha/beta hydrolase domain containing 18; This entry represents alpha/beta hydrolase ... |
253-287 |
6.56e-04 |
|
Alpha/beta hydrolase domain containing 18; This entry represents alpha/beta hydrolase domain-containing protein 18 (ABHD18). Its function is not clear.
Pssm-ID: 370661 [Multi-domain] Cd Length: 352 Bit Score: 40.88 E-value: 6.56e-04
10 20 30
....*....|....*....|....*....|....*
gi 114208056 253 FICGTRSPYMRREQWPQIQKMFPNSEIHWLDAGHL 287
Cdd:pfam09752 298 FVAAKDDAYVPRESVTTLQQIWPGSEVRWVDGGHV 332
|
|
| FrmB |
COG0627 |
S-formylglutathione hydrolase FrmB [Defense mechanisms]; |
122-171 |
1.66e-03 |
|
S-formylglutathione hydrolase FrmB [Defense mechanisms];
Pssm-ID: 440392 [Multi-domain] Cd Length: 249 Bit Score: 39.43 E-value: 1.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 114208056 122 ACMGHSMGGRSMMYFARKYPELVerLIVVDISPISVPRSTGEMTEIFDAM 171
Cdd:COG0627 116 AIAGLSMGGHGALTLALRHPDLF--RAVAAFSGILDPSQPPWGEKAFDAY 163
|
|
| PGAP1 |
pfam07819 |
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ... |
54-158 |
7.17e-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: 37.34 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114208056 54 PLLTYHGLFGSKQNWRGISKAL------VRKVSRKVYAIDVR----NHGESpHSSVHN----------SKAMSEDLRLFM 113
Cdd:pfam07819 6 PVLFIPGNAGSYKQVRSIASVAanlyqvLRKLLQNDNGFHLDffsvDFNEE-LSAFHGrtlldqaeylNDAIRYILSLYA 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 114208056 114 EQRSHPNA-ACMGHSMGG---RSMMYFARKYPELVERLIVVDiSPISVP 158
Cdd:pfam07819 85 SGRPGPTSvILIGHSMGGivaRAALTLPNYIPQSVNTIITLS-SPHAKP 132
|
|
| |
