|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10673 |
PRK10673 |
esterase; |
31-297 |
4.44e-53 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 174.15 E-value: 4.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 31 PMTYASYSSPELDRNSPLVIVHGLFGQKQNWNSVGKALHKklEAPVYAVDVRNHGSSPHTETMSYTEMAEDLVLFIDKVK 110
Cdd:PRK10673 2 KLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVN--DHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 111 EEtkktRVNLLGHSMGGKIVMrlAIDSKWSDRIEKLIVEDVSPKGYS-RRHLEFRELIKTMRNVDLcRTRKEILKDLESA 189
Cdd:PRK10673 80 IE----KATFIGHSMGGKAVM--ALTALAPDRIDKLVAIDIAPVDYHvRRHDEIFAAINAVSEAGA-TTRQQAAAIMRQH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 190 IPDLAMRQFILTNLQpssenegQMEWKININTIDSHVDEILGYTlPVGSFRGPTLFLHGANSGYVPDDHKPDIKCLFPQV 269
Cdd:PRK10673 153 LNEEGVIQFLLKSFV-------DGEWRFNVPVLWDQYPHIVGWE-KIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQA 224
|
250 260
....*....|....*....|....*...
gi 17508535 270 QFDAIPDSGHWVHAEKPQLFINSVYKFL 297
Cdd:PRK10673 225 RAHVIAGAGHWVHAEKPDAVLRAIRRYL 252
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
47-298 |
5.17e-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: 120.88 E-value: 5.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 47 PLVIVHGLFGQKQNWNSVGKALHKKLEapVYAVDVRNHGSSPHTET-MSYTEMAEDLVLFIDKVKEEtkktRVNLLGHSM 125
Cdd:COG0596 25 PVVLLHGLPGSSYEWRPLIPALAAGYR--VIAPDLRGHGRSDKPAGgYTLDDLADDLAALLDALGLE----RVVLVGHSM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 126 GGKIVMRLAIdsKWSDRIEKLIVEDvspkgysrrhlefreliktmrnvdlcrtrkEILKDLESAIPDLAMRQFILTNLQP 205
Cdd:COG0596 99 GGMVALELAA--RHPERVAGLVLVD------------------------------EVLAALAEPLRRPGLAPEALAALLR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 206 SSENEGQMEWkinintidshvdeilgytlpVGSFRGPTLFLHGANSGYVPDDHKPDIKCLFPQVQFDAIPDSGHWVHAEK 285
Cdd:COG0596 147 ALARTDLRER--------------------LARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQ 206
|
250
....*....|...
gi 17508535 286 PQLFINSVYKFLK 298
Cdd:COG0596 207 PEAFAAALRDFLA 219
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
47-286 |
7.92e-30 |
|
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: 113.37 E-value: 7.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 47 PLVIVHGLFGQKQNWNSVGKALHKKlEAPVYAVDVRNHG-SSPHTETMSYTemAEDLVLFIDKVKEETKKTRVNLLGHSM 125
Cdd:pfam00561 2 PVLLLHGLPGSSDLWRKLAPALARD-GFRVIALDLRGFGkSSRPKAQDDYR--TDDLAEDLEYILEALGLEKVNLVGHSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 126 GGKIVMRLAidSKWSDRIEKLIVedVSPKGYsrrHLEFRELIKTMRNVDLCRTRKEILKDLESAIPDL--AMRQFILTNL 203
Cdd:pfam00561 79 GGLIALAYA--AKYPDRVKALVL--LGALDP---PHELDEADRFILALFPGFFDGFVADFAPNPLGRLvaKLLALLLLRL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 204 QPSSENEG------QMEWKININTIDSHVDEILGYTL-----PVGSFRGPTLFLHGANSGYVPDDHKPDIKCLFPQVQFD 272
Cdd:pfam00561 152 RLLKALPLlnkrfpSGDYALAKSLVTGALLFIETWSTelrakFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLV 231
|
250
....*....|....
gi 17508535 273 AIPDSGHWVHAEKP 286
Cdd:pfam00561 232 VIPDAGHFAFLEGP 245
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
47-147 |
3.20e-16 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 72.94 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 47 PLVIVHGLFGQKQNWNSVGKALhKKLEAPVYAVDVrnhgsspHTETMSYTEMAEDLVLFIDKVKEETKKTRVNLLGHSMG 126
Cdd:COG1075 7 PVVLVHGLGGSAASWAPLAPRL-RAAGYPVYALNY-------PSTNGSIEDSAEQLAAFVDAVLAATGAEKVDLVGHSMG 78
|
90 100
....*....|....*....|..
gi 17508535 127 GkIVMRLAI-DSKWSDRIEKLI 147
Cdd:COG1075 79 G-LVARYYLkRLGGAAKVARVV 99
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
47-298 |
4.39e-15 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 72.73 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 47 PLVIVHGLFGQKQNWNSVGKALHKKlEAPVYAVDVRNHGSSPHTETM--SYTEMAEDLVLFIDKVKEETKKtRVNLLGHS 124
Cdd:COG2267 30 TVVLVHGLGEHSGRYAELAEALAAA-GYAVLAFDLRGHGRSDGPRGHvdSFDDYVDDLRAALDALRARPGL-PVVLLGHS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 125 MGGKIVMRLAidSKWSDRIEKLIVedVSPKgysrrhlefreliktMRNVDLCRTRKEILKDLEsaIPDLAMRqfiltnlq 204
Cdd:COG2267 108 MGGLIALLYA--ARYPDRVAGLVL--LAPA---------------YRADPLLGPSARWLRALR--LAEALAR-------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 205 pssenegqmewkinintidshvdeilgytlpvgsFRGPTLFLHGANSGYVP-DDHKPDIKCLFPQVQFDAIPDSGHWVHA 283
Cdd:COG2267 159 ----------------------------------IDVPVLVLHGGADRVVPpEAARRLAARLSPDVELVLLPGARHELLN 204
|
250
....*....|....*.
gi 17508535 284 EKP-QLFINSVYKFLK 298
Cdd:COG2267 205 EPArEEVLAAILAWLE 220
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
48-147 |
2.96e-12 |
|
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: 64.93 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 48 LVIVHGLfgqkqNWNSvGKALH--KKLEAP---VYAVDVRNHGSSP----HTEtmSYTEMAEDLVLFIDKVKEETKKTRV 118
Cdd:pfam12146 7 VVLVHGL-----GEHS-GRYAHlaDALAAQgfaVYAYDHRGHGRSDgkrgHVP--SFDDYVDDLDTFVDKIREEHPGLPL 78
|
90 100
....*....|....*....|....*....
gi 17508535 119 NLLGHSMGGKIVMRLAIdsKWSDRIEKLI 147
Cdd:pfam12146 79 FLLGHSMGGLIAALYAL--RYPDKVDGLI 105
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
47-289 |
4.91e-12 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 65.74 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 47 PLVIVHGLFGQKQNWNSVGKALHKKleAPVYAVDVRNHG-SSPHTETMSYTEMAEDLVLFIDKVKEEtkktRVNLLGHSM 125
Cdd:PRK14875 133 PVVLIHGFGGDLNNWLFNHAALAAG--RPVIALDLPGHGaSSKAVGAGSLDELAAAVLAFLDALGIE----RAHLVGHSM 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 126 GGKIVMRLAIDSkwSDRIEKLIVedVSPKGYSRrhlEF-RELIKTMRNVDLCRTRKEILKDLeSAIPDLAMRQFIltnlq 204
Cdd:PRK14875 207 GGAVALRLAARA--PQRVASLTL--IAPAGLGP---EInGDYIDGFVAAESRRELKPVLELL-FADPALVTRQMV----- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 205 pssenEGQMEWKiNINTIDSHVDEILGYTLPVG-----------SFRGPTLFLHGANSGYVPDDHKPDikcLFPQVQFDA 273
Cdd:PRK14875 274 -----EDLLKYK-RLDGVDDALRALADALFAGGrqrvdlrdrlaSLAIPVLVIWGEQDRIIPAAHAQG---LPDGVAVHV 344
|
250
....*....|....*.
gi 17508535 274 IPDSGHWVHAEKPQLF 289
Cdd:PRK14875 345 LPGAGHMPQMEAAADV 360
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
48-290 |
1.56e-10 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 59.79 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 48 LVIVHGLFgqkQNWNSVGKALHKKLEapVYAVDVRNHGSSPHTETmSYTEmAEDLVLFIDKVKEetkKTRVNLLGHSMGG 127
Cdd:pfam12697 1 VVLVHGAG---LSAAPLAALLAAGVA--VLAPDLPGHGSSSPPPL-DLAD-LADLAALLDELGA---ARPVVLVGHSLGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 128 KIVMRLAIDskwsDRIEKLIVEDvspkgysrrhlefrelikTMRNVDLCRTRKEILKDLESAIPDLAMRQFILTNLQPSS 207
Cdd:pfam12697 71 AVALAAAAA----ALVVGVLVAP------------------LAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 208 ENEGQMEWKININTIDSHVDEILGYTLPVGSFRGPTLFLHGANSGYVPDDHKpDIKCLFPQVQFDAIPDSGHWVHaEKPQ 287
Cdd:pfam12697 129 DLPADAEWAAALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPELAQ-RLLAALAGARLVVLPGAGHLPL-DDPE 206
|
...
gi 17508535 288 LFI 290
Cdd:pfam12697 207 EVA 209
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
49-298 |
1.24e-09 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 57.64 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 49 VIVHGLFGQKQNWNSVGKALHKKlEAPVYAVDVRNHGSSPHT-ETMSYTEMAEDLVLFIDKVKEETKKtrVNLLGHSMGG 127
Cdd:COG1647 19 LLLHGFTGSPAEMRPLAEALAKA-GYTVYAPRLPGHGTSPEDlLKTTWEDWLEDVEEAYEILKAGYDK--VIVIGLSMGG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 128 KIVMRLAIDskwSDRIEKLIVedVSP-KGYSRRHLEFRELIKTMRnvdlcRTRKEILKDLES------AIPDLAMRQFI- 199
Cdd:COG1647 96 LLALLLAAR---YPDVAGLVL--LSPaLKIDDPSAPLLPLLKYLA-----RSLRGIGSDIEDpevaeyAYDRTPLRALAe 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 200 LTNLqpssenegqmewkinINTIDSHVDEIlgytlpvgsfRGPTLFLHGANSGYVPDDHKPDIKCLF--PQVQFDAIPDS 277
Cdd:COG1647 166 LQRL---------------IREVRRDLPKI----------TAPTLIIQSRKDEVVPPESARYIYERLgsPDKELVWLEDS 220
|
250 260
....*....|....*....|...
gi 17508535 278 GHWVH--AEKPQLFiNSVYKFLK 298
Cdd:COG1647 221 GHVITldKDREEVA-EEILDFLE 242
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
48-149 |
4.40e-08 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 52.92 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 48 LVIVHGLFGQKQNWNSVGKALHkklEAPVYAVDVRNHGSSPHTETMSYTEMAEdlvlFIDKVKEETKKTRVNLLGHSMGG 127
Cdd:PRK11126 5 LVFLHGLLGSGQDWQPVGEALP---DYPRLYIDLPGHGGSAAISVDGFADVSR----LLSQTLQSYNILPYWLVGYSLGG 77
|
90 100
....*....|....*....|..
gi 17508535 128 KIVMRLAIDSKwSDRIEKLIVE 149
Cdd:PRK11126 78 RIAMYYACQGL-AGGLCGLIVE 98
|
|
| Lipase_2 |
pfam01674 |
Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. ... |
45-135 |
5.32e-07 |
|
Lipase (class 2); This family consists of hypothetical C. elegans proteins and lipases. Lipases or triacylglycerol acylhydrolases hydrolyse ester bonds in triacylglycerol giving diacylglycerol, monoacylglycerol, glycerol and free fatty acids. Swiss:P37957 is an extracellular lipase from B. subtilis 168.
Pssm-ID: 396304 [Multi-domain] Cd Length: 218 Bit Score: 49.27 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 45 NSPLVIVHGLFGQKQ-NWNSVGKALHKK--LEAPVYAVdvrNHGSSPHTETMSYTEMAEDLVL---FIDKVKEETKKTRV 118
Cdd:pfam01674 1 NQPVIFVHGNSGLAAgGWSKLSQYFKERgyTLAELYAT---TWGDGNESTSLQRAEKCEYVKQirrFIEAVLGYTGAAKV 77
|
90
....*....|....*..
gi 17508535 119 NLLGHSMGGKIvMRLAI 135
Cdd:pfam01674 78 DIVAHSMGVPI-ARKAI 93
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
40-298 |
1.02e-06 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 48.86 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 40 PELDRNSPLVI-VHGLFGQKQN-WNSVGKALHKKLEApVYAVDVRNHGSSPHTETmsyTEMAEDLVLFIDKVKEETK--K 115
Cdd:COG1506 17 PADGKKYPVVVyVHGGPGSRDDsFLPLAQALASRGYA-VLAPDYRGYGESAGDWG---GDEVDDVLAAIDYLAARPYvdP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 116 TRVNLLGHSMGGKIVMRLAidSKWSDRIEKLIvedvspkgysrrhlefreliktmrnvdlcrtrkeilkdLESAIPDLAM 195
Cdd:COG1506 93 DRIGIYGHSYGGYMALLAA--ARHPDRFKAAV--------------------------------------ALAGVSDLRS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 196 rQFILTNLQPSSENEGQMEWKININTID--SHVDEIlgytlpvgsfRGPTLFLHGANSGYVPDDH------------KPd 261
Cdd:COG1506 133 -YYGTTREYTERLMGGPWEDPEAYAARSplAYADKL----------KTPLLLIHGEADDRVPPEQaerlyealkkagKP- 200
|
250 260 270
....*....|....*....|....*....|....*..
gi 17508535 262 ikclfpqVQFDAIPDSGHWVHAEKPQLFINSVYKFLK 298
Cdd:COG1506 201 -------VELLVYPGEGHGFSGAGAPDYLERILDFLD 230
|
|
| PLN02652 |
PLN02652 |
hydrolase; alpha/beta fold family protein |
24-148 |
3.72e-06 |
|
hydrolase; alpha/beta fold family protein
Pssm-ID: 215352 [Multi-domain] Cd Length: 395 Bit Score: 47.97 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 24 CRKFAPVpmtyasysSPELdrNSPLVIVHGLfgqkqNWNSvGKALH--KKLEAP---VYAVDVRNHGSSP--HTETMSYT 96
Cdd:PLN02652 125 CRSWAPA--------AGEM--RGILIIIHGL-----NEHS-GRYLHfaKQLTSCgfgVYAMDWIGHGGSDglHGYVPSLD 188
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 17508535 97 EMAEDLVLFIDKVKEETKKTRVNLLGHSMGGKIVMRLAIDSKWSDRIEKLIV 148
Cdd:PLN02652 189 YVVEDTEAFLEKIRSENPGVPCFLFGHSTGGAVVLKAASYPSIEDKLEGIVL 240
|
|
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
43-299 |
5.73e-06 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 47.21 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 43 DRNSP-LVIVHGlFGQKQ-----NWNSVGKALHkkleapVYAVDVRNHGSSPHTE-TMSYTEMAEDLvlFIDKVKEETKK 115
Cdd:PLN02894 102 KEDAPtLVMVHG-YGASQgfffrNFDALASRFR------VIAIDQLGWGGSSRPDfTCKSTEETEAW--FIDSFEEWRKA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 116 TRVN---LLGHSMGGKIVMRLAIdsKWSDRIEKLIVedVSPKGYS-------RRHLEFRELIKTM-------RNVdlcrT 178
Cdd:PLN02894 173 KNLSnfiLLGHSFGGYVAAKYAL--KHPEHVQHLIL--VGPAGFSsesddksEWLTKFRATWKGAvlnhlweSNF----T 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 179 RKEILKDLESAIPDLAMRqfiLTNLQPSSENEGQMEWKININTIDSHVDEI----------LGYTLPVGSF--------- 239
Cdd:PLN02894 245 PQKIIRGLGPWGPNLVRR---YTTARFGAHSTGDILSEEESKLLTDYVYHTlaakasgelcLKYIFSFGAFarkpllesa 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17508535 240 ---RGPTLFLHGANSGYVPDDHKPDIKCLFPQVQFDAIPDSGHWVHAEKPQLF----INSVYKFLKP 299
Cdd:PLN02894 322 sewKVPTTFIYGRHDWMNYEGAVEARKRMKVPCEIIRVPQGGHFVFLDNPSGFhsavLYACRKYLSP 388
|
|
| Palm_thioest |
pfam02089 |
Palmitoyl protein thioesterase; |
47-132 |
1.02e-05 |
|
Palmitoyl protein thioesterase;
Pssm-ID: 460441 [Multi-domain] Cd Length: 248 Bit Score: 46.08 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 47 PLVIVHGLFGQKQN--WNSVGKALHKKL-EAPVYAVDVRNHGSSPHTETmSYTEMAEDLVLFIDKVKEETKKTRVNLLGH 123
Cdd:pfam02089 1 PVVIWHGLGDSCASpgMQSLAELIKEAHpGTYVHSIDIGDGPSEDRKAS-FFGNMNEQVEAVCEQLKPELPANGFNAIGF 79
|
....*....
gi 17508535 124 SMGGkIVMR 132
Cdd:pfam02089 80 SQGG-LFLR 87
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
45-297 |
6.43e-05 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 44.46 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 45 NSPLVIVHGLFGQKQNWNSVGKALHKklEAPVYAVD--------VRNHGSSPHTETMSYTEMAEDLVLfidKVKEETKKT 116
Cdd:PLN02980 1371 GSVVLFLHGFLGTGEDWIPIMKAISG--SARCISIDlpghggskIQNHAKETQTEPTLSVELVADLLY---KLIEHITPG 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 117 RVNLLGHSMGGKIVMRLAIdsKWSDRIEKLIVEDVSP-------------KGYSRRHLEFR-------------ELIKTM 170
Cdd:PLN02980 1446 KVTLVGYSMGARIALYMAL--RFSDKIEGAVIISGSPglkdevarkirsaKDDSRARMLIDhgleiflenwysgELWKSL 1523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 171 RN----VDLCRTR---KEIlKDLESAIPDLAM-RQFILTnlqpssenEGQMEWKININTIDSHVDeilgytlpvGSFR-- 240
Cdd:PLN02980 1524 RNhphfNKIVASRllhKDV-PSLAKLLSDLSIgRQPSLW--------EDLKQCDTPLLLVVGEKD---------VKFKqi 1585
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 17508535 241 GPTLFLHGANSGYVPDDHKPDIkclfpqVQFDAIPDSGHWVHAEKPQLFINSVYKFL 297
Cdd:PLN02980 1586 AQKMYREIGKSKESGNDKGKEI------IEIVEIPNCGHAVHLENPLPVIRALRKFL 1636
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
48-255 |
3.70e-04 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 41.05 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 48 LVIVHGLFGQKQNWNSVGKALHKkLEAPVYAVDVRNHGSSP--HTETMSYTemAEDLVLFIDKVKE--ETKKTRVNLLGH 123
Cdd:COG1073 40 VVVAHGNGGVKEQRALYAQRLAE-LGFNVLAFDYRGYGESEgePREEGSPE--RRDARAAVDYLRTlpGVDPERIGLLGI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 124 SMGGKIVMRLAIDSKwsdRIeKLIVEDVspkGYSRRHLEFRELIKTMRNVdlcrtrkeilkdlesAIPDLAMRqfiltnl 203
Cdd:COG1073 117 SLGGGYALNAAATDP---RV-KAVILDS---PFTSLEDLAAQRAKEARGA---------------YLPGVPYL------- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17508535 204 qPSSENEGQMEWKINintIDSHVDEIlgytlpvgsfRGPTLFLHGANSGYVP 255
Cdd:COG1073 168 -PNVRLASLLNDEFD---PLAKIEKI----------SRPLLFIHGEKDEAVP 205
|
|
| PGAP1 |
pfam07819 |
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ... |
47-153 |
1.05e-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: 39.65 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 47 PLVIVHGLFG---QKQNWNSVGKALHKKLEApvyavDVRNHG---------------SSPHTETMS-YTEMAEDLVLFID 107
Cdd:pfam07819 6 PVLFIPGNAGsykQVRSIASVAANLYQVLRK-----LLQNDNgfhldffsvdfneelSAFHGRTLLdQAEYLNDAIRYIL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 17508535 108 KVKEET--KKTRVNLLGHSMGGkIVMRLAI--DSKWSDRIEKLIVEDvSP 153
Cdd:pfam07819 81 SLYASGrpGPTSVILIGHSMGG-IVARAALtlPNYIPQSVNTIITLS-SP 128
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
40-134 |
7.87e-03 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 36.87 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508535 40 PELDRNSPLVIV-HGLFGQKQNWNSVGKALHKK--LeapVYAVDVRNHGSSPHTE--------TMSYTEMAEDLVLFIDK 108
Cdd:COG0412 23 PAGGGPRPGVVVlHEIFGLNPHIRDVARRLAAAgyV---VLAPDLYGRGGPGDDPdearalmgALDPELLAADLRAALDW 99
|
90 100
....*....|....*....|....*...
gi 17508535 109 VK--EETKKTRVNLLGHSMGGKIVMRLA 134
Cdd:COG0412 100 LKaqPEVDAGRVGVVGFCFGGGLALLAA 127
|
|
| |
