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Conserved domains on  [gi|24655464|ref|NP_611397|]
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uncharacterized protein Dmel_CG15111, isoform A [Drosophila melanogaster]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11437497)

alpha/beta hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
165-363 1.04e-28

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


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 112.32  E-value: 1.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 165 VVLYLHGNTASRGsgHRSEVYKLLRKLNYHVFSFDYRGYADSDPVPpTEEGV--VRDAMMVFEYI---ANTTSNPIVVWG 239
Cdd:COG1073  39 AVVVAHGNGGVKE--QRALYAQRLAELGFNVLAFDYRGYGESEGEP-REEGSpeRRDARAAVDYLrtlPGVDPERIGLLG 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 240 HSLGTGVAthlcAKLASLRERaPRGVILESPFTNIRDEIRMHPFAKLYKNLPWFNF--TISQPMYTNRlRFESDVHVLEF 317
Cdd:COG1073 116 ISLGGGYA----LNAAATDPR-VKAVILDSPFTSLEDLAAQRAKEARGAYLPGVPYlpNVRLASLLND-EFDPLAKIEKI 189
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24655464 318 RQPIMIIHAEDDVVVPFNLGYRLYRialdgrsRTSGPVEFHRF-GAS 363
Cdd:COG1073 190 SRPLLFIHGEKDEAVPFYMSEDLYE-------AAAEPKELLIVpGAG 229
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
165-363 1.04e-28

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 112.32  E-value: 1.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 165 VVLYLHGNTASRGsgHRSEVYKLLRKLNYHVFSFDYRGYADSDPVPpTEEGV--VRDAMMVFEYI---ANTTSNPIVVWG 239
Cdd:COG1073  39 AVVVAHGNGGVKE--QRALYAQRLAELGFNVLAFDYRGYGESEGEP-REEGSpeRRDARAAVDYLrtlPGVDPERIGLLG 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 240 HSLGTGVAthlcAKLASLRERaPRGVILESPFTNIRDEIRMHPFAKLYKNLPWFNF--TISQPMYTNRlRFESDVHVLEF 317
Cdd:COG1073 116 ISLGGGYA----LNAAATDPR-VKAVILDSPFTSLEDLAAQRAKEARGAYLPGVPYlpNVRLASLLND-EFDPLAKIEKI 189
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24655464 318 RQPIMIIHAEDDVVVPFNLGYRLYRialdgrsRTSGPVEFHRF-GAS 363
Cdd:COG1073 190 SRPLLFIHGEKDEAVPFYMSEDLYE-------AAAEPKELLIVpGAG 229
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
161-344 1.80e-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: 66.47  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464   161 PGGTVVLyLHGntasRG--SGHRSEVYKLLRKLNYHVFSFDYRGYADSDP----VPPTEEgVVRDAMMVFEYIANTTSN- 233
Cdd:pfam12146   3 PRAVVVL-VHG----LGehSGRYAHLADALAAQGFAVYAYDHRGHGRSDGkrghVPSFDD-YVDDLDTFVDKIREEHPGl 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464   234 PIVVWGHSLGTGVATHLCAKlaslRERAPRGVILESPFTNIRDEIrMHPFAK-----LYKNLPWF---NFTISQPMYTN- 304
Cdd:pfam12146  77 PLFLLGHSMGGLIAALYALR----YPDKVDGLILSAPALKIKPYL-APPILKllaklLGKLFPRLrvpNNLLPDSLSRDp 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24655464   305 --RLRFESDVHVL-----------------------EFRQPIMIIHAEDDVVVPFNLGYRLYRIA 344
Cdd:pfam12146 152 evVAAYAADPLVHggisartlyelldagerllrraaAITVPLLLLHGGADRVVDPAGSREFYERA 216
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
193-267 3.69e-04

Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 41.44  E-value: 3.69e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24655464    193 YHVFSFDYRGYADSDPVPPTEEGVVR---DAMmvfeyIANTTSNPIVVWGHSLGTGVATHLCAKLASlRERAPRGVIL 267
Cdd:smart00824  26 RDVSALPLPGFGPGEPLPASADALVEaqaEAV-----LRAAGGRPFVLVGHSSGGLLAHAVAARLEA-RGIPPAAVVL 97
PHA02857 PHA02857
monoglyceride lipase; Provisional
175-273 2.50e-03

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 39.48  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464  175 SRGSGHRSEVYKLL----RKLNYHVFSFDYRGYADS--DPVPPTEEGV-VRDAMMVFEYIANTTSN-PIVVWGHSLGTGV 246
Cdd:PHA02857  31 SHGAGEHSGRYEELaeniSSLGILVFSHDHIGHGRSngEKMMIDDFGVyVRDVVQHVVTIKSTYPGvPVFLLGHSMGATI 110
                         90       100
                 ....*....|....*....|....*..
gi 24655464  247 ATHLCAKLASLREraprGVILESPFTN 273
Cdd:PHA02857 111 SILAAYKNPNLFT----AMILMSPLVN 133
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
165-363 1.04e-28

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 112.32  E-value: 1.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 165 VVLYLHGNTASRGsgHRSEVYKLLRKLNYHVFSFDYRGYADSDPVPpTEEGV--VRDAMMVFEYI---ANTTSNPIVVWG 239
Cdd:COG1073  39 AVVVAHGNGGVKE--QRALYAQRLAELGFNVLAFDYRGYGESEGEP-REEGSpeRRDARAAVDYLrtlPGVDPERIGLLG 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 240 HSLGTGVAthlcAKLASLRERaPRGVILESPFTNIRDEIRMHPFAKLYKNLPWFNF--TISQPMYTNRlRFESDVHVLEF 317
Cdd:COG1073 116 ISLGGGYA----LNAAATDPR-VKAVILDSPFTSLEDLAAQRAKEARGAYLPGVPYlpNVRLASLLND-EFDPLAKIEKI 189
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24655464 318 RQPIMIIHAEDDVVVPFNLGYRLYRialdgrsRTSGPVEFHRF-GAS 363
Cdd:COG1073 190 SRPLLFIHGEKDEAVPFYMSEDLYE-------AAAEPKELLIVpGAG 229
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
165-360 5.30e-22

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 93.54  E-value: 5.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 165 VVLYLHGNTASRGSGHRSEVyKLLRKLNYHVFSFDYRGYADSDPVPPTEEgvVRDAMMVFEYIANTT---SNPIVVWGHS 241
Cdd:COG1506  25 VVVYVHGGPGSRDDSFLPLA-QALASRGYAVLAPDYRGYGESAGDWGGDE--VDDVLAAIDYLAARPyvdPDRIGIYGHS 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 242 LGTGVATHLcaklASLRERAPRGVILESPFTNIRDEIR-MHPFAKLYKNLPWFNFTISQpmytnrlRFESDVHVLEFRQP 320
Cdd:COG1506 102 YGGYMALLA----AARHPDRFKAAVALAGVSDLRSYYGtTREYTERLMGGPWEDPEAYA-------ARSPLAYADKLKTP 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24655464 321 IMIIHAEDDVVVPFNLGYRLYRIALdgrsRTSGPVEFHRF 360
Cdd:COG1506 171 LLLIHGEADDRVPPEQAERLYEALK----KAGKPVELLVY 206
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
139-360 2.16e-17

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 80.43  E-value: 2.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 139 RSEFPVVLPENEQLFYERLLRMPG-GTVVLYLHGNTASRGSghrsevYK----LLRKLNYHVFSFDYRGYADSDPVP--- 210
Cdd:COG2267   3 RRLVTLPTRDGLRLRGRRWRPAGSpRGTVVLVHGLGEHSGR------YAelaeALAAAGYAVLAFDLRGHGRSDGPRghv 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 211 PTEEGVVRDAMMVFEYIANTTSNPIVVWGHSLGTGVAthlcAKLASLRERAPRGVILESPftnirdeirmhpfaklyknl 290
Cdd:COG2267  77 DSFDDYVDDLRAALDALRARPGLPVVLLGHSMGGLIA----LLYAARYPDRVAGLVLLAP-------------------- 132
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24655464 291 pwfnFTISQPMYTNRLRFESDVHVLE----FRQPIMIIHAEDDVVVPFNLGYRLYRialdgrsRTSGPVEFHRF 360
Cdd:COG2267 133 ----AYRADPLLGPSARWLRALRLAEalarIDVPVLVLHGGADRVVPPEAARRLAA-------RLSPDVELVLL 195
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
162-388 1.16e-13

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 69.97  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 162 GGTVVLYLHGNTASRGSGHRseVYKLLRKLNYHVFSFDYRGYADS--DPVPPTEEGVVRDAMMVFEYIANTTSNPIVVwG 239
Cdd:COG1647  14 GRKGVLLLHGFTGSPAEMRP--LAEALAKAGYTVYAPRLPGHGTSpeDLLKTTWEDWLEDVEEAYEILKAGYDKVIVI-G 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 240 HSLGTGVATHLCAklaslRERAPRGVILESPFTNIRDE-IRMHPFAK-LYKNLPWFNFTISQP----MYTNRLRFESDVH 313
Cdd:COG1647  91 LSMGGLLALLLAA-----RYPDVAGLVLLSPALKIDDPsAPLLPLLKyLARSLRGIGSDIEDPevaeYAYDRTPLRALAE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 314 VLEF-----------RQPIMIIHAEDDVVVPFNLGYRLYrialdgRSRTSGPVEFHRFGASrkyGHkYLCRAPELPGLIQ 382
Cdd:COG1647 166 LQRLirevrrdlpkiTAPTLIIQSRKDEVVPPESARYIY------ERLGSPDKELVWLEDS---GH-VITLDKDREEVAE 235

                ....*....
gi 24655464 383 ---KFVENY 388
Cdd:COG1647 236 eilDFLERL 244
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
161-344 1.80e-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: 66.47  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464   161 PGGTVVLyLHGntasRG--SGHRSEVYKLLRKLNYHVFSFDYRGYADSDP----VPPTEEgVVRDAMMVFEYIANTTSN- 233
Cdd:pfam12146   3 PRAVVVL-VHG----LGehSGRYAHLADALAAQGFAVYAYDHRGHGRSDGkrghVPSFDD-YVDDLDTFVDKIREEHPGl 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464   234 PIVVWGHSLGTGVATHLCAKlaslRERAPRGVILESPFTNIRDEIrMHPFAK-----LYKNLPWF---NFTISQPMYTN- 304
Cdd:pfam12146  77 PLFLLGHSMGGLIAALYALR----YPDKVDGLILSAPALKIKPYL-APPILKllaklLGKLFPRLrvpNNLLPDSLSRDp 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24655464   305 --RLRFESDVHVL-----------------------EFRQPIMIIHAEDDVVVPFNLGYRLYRIA 344
Cdd:pfam12146 152 evVAAYAADPLVHggisartlyelldagerllrraaAITVPLLLLHGGADRVVDPAGSREFYERA 216
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
151-342 8.43e-11

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: 61.17  E-value: 8.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 151 QLFYERllRMPGGTVVLYLHGNTASRGSGHRseVYKLLRKlNYHVFSFDYRGYADSDPVPP--TEEGVVRDAMMVFEYIA 228
Cdd:COG0596  13 RLHYRE--AGPDGPPVVLLHGLPGSSYEWRP--LIPALAA-GYRVIAPDLRGHGRSDKPAGgyTLDDLADDLAALLDALG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 229 NTtsnPIVVWGHSLGTGVATHLcaklASLRERAPRGVILESPftnIRDEIR--MHPFAKLYKNLPWFNFTISQPMYTNRL 306
Cdd:COG0596  88 LE---RVVLVGHSMGGMVALEL----AARHPERVAGLVLVDE---VLAALAepLRRPGLAPEALAALLRALARTDLRERL 157
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24655464 307 RfesdvhvlEFRQPIMIIHAEDDVVVPFNLGYRLYR 342
Cdd:COG0596 158 A--------RITVPTLVIWGEKDPIVPPALARRLAE 185
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
161-360 2.47e-09

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 56.81  E-value: 2.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 161 PGGTVVLYLHG---NTASRGSgHRSEVYKLLRKLNYHVFSFDYRgYADSDPVPpteeGVVRDAMMVFEYIA------NTT 231
Cdd:COG0657  11 GPLPVVVYFHGggwVSGSKDT-HDPLARRLAARAGAAVVSVDYR-LAPEHPFP----AALEDAYAALRWLRanaaelGID 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464 232 SNPIVVWGHSLGTGVATHLCAKLASLRERAPRGVILESPFTNirdeIRMHPFAKLYKNLPwfnftisqpmytnrlrfesd 311
Cdd:COG0657  85 PDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLD----LTASPLRADLAGLP-------------------- 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24655464 312 vhvlefrqPIMIIHAEDDVVVPFNLgyRLYRiALdgrsRTSG-PVEFHRF 360
Cdd:COG0657 141 --------PTLIVTGEADPLVDESE--ALAA-AL----RAAGvPVELHVY 175
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
164-346 4.65e-09

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: 56.36  E-value: 4.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464   164 TVVLYLHGNTASRGSGHrsEVYKLLRKLNYHVFSFDYRGYADSDPVPPTEEGVVRDAMMVFEYIANTTSN-PIVVWGHSL 242
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWR--KLAPALARDGFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILEALGLeKVNLVGHSM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464   243 GTGVATHLCAKlasLRERApRGVILESPFTNIRDEIRMHPFAKlyKNLPWFNFTISQPMYTNRLRFESDVHVLEFRQPIM 322
Cdd:pfam00561  79 GGLIALAYAAK---YPDRV-KALVLLGALDPPHELDEADRFIL--ALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLR 152
                         170       180
                  ....*....|....*....|....
gi 24655464   323 IIHAEDDVVVPFNLGYRLYRIALD 346
Cdd:pfam00561 153 LLKALPLLNKRFPSGDYALAKSLV 176
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
166-334 7.50e-06

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 46.70  E-value: 7.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464   166 VLYLHGNTAsrgsgHRSEVYKLLRKlNYHVFSFDYRGYADSDPVPPTEEGVVRDAMMVFEYIAnttSNPIVVWGHSLGTG 245
Cdd:pfam12697   1 VVLVHGAGL-----SAAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGA---ARPVVLVGHSLGGA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464   246 VATH-----------LCAKLASLRERAPRGVILESPFTNIR-------DEIRMHPFAKLYKNLPWFNFTISQPMYTNRLR 307
Cdd:pfam12697  72 VALAaaaaalvvgvlVAPLAAPPGLLAALLALLARLGAALAapawlaaESLARGFLDDLPADAEWAAALARLAALLAALA 151
                         170       180
                  ....*....|....*....|....*..
gi 24655464   308 FESDVHVLEFRQPIMIIHAEDDVVVPF 334
Cdd:pfam12697 152 LLPLAAWRDLPVPVLVLAEEDRLVPEL 178
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
149-360 1.42e-05

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 45.68  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464   149 NEQLFYERllrmpgGTVVLYLHGntasRGSGHRSEVYkllrklnYHVFSFDYRGYadsdpvppteegVVRDAMMVFEYIA 228
Cdd:pfam00326   6 NAQLLADR------GYVVAIANG----RGSGGYGEAF-------HDAGKGDLGQN------------EFDDFIAAAEYLI 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464   229 N---TTSNPIVVWGHSLGtGVATHLCAklaslrERAP---RGVILESPFTNIR--DEIRMHPFAKLYKNL--PWFNFTis 298
Cdd:pfam00326  57 EqgyTDPDRLAIWGGSYG-GYLTGAAL------NQRPdlfKAAVAHVPVVDWLayMSDTSLPFTERYMEWgnPWDNEE-- 127
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24655464   299 qpMYTNRLRFeSDVHVLEFRQPIMIIHAEDDVVVPFNLGYRLYRiALDgrsRTSGPVEFHRF 360
Cdd:pfam00326 128 --GYDYLSPY-SPADNVKVYPPLLLIHGLLDDRVPPWQSLKLVA-ALQ---RKGVPFLLLIF 182
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
193-267 3.69e-04

Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 41.44  E-value: 3.69e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24655464    193 YHVFSFDYRGYADSDPVPPTEEGVVR---DAMmvfeyIANTTSNPIVVWGHSLGTGVATHLCAKLASlRERAPRGVIL 267
Cdd:smart00824  26 RDVSALPLPGFGPGEPLPASADALVEaqaEAV-----LRAAGGRPFVLVGHSSGGLLAHAVAARLEA-RGIPPAAVVL 97
PHA02857 PHA02857
monoglyceride lipase; Provisional
175-273 2.50e-03

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 39.48  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655464  175 SRGSGHRSEVYKLL----RKLNYHVFSFDYRGYADS--DPVPPTEEGV-VRDAMMVFEYIANTTSN-PIVVWGHSLGTGV 246
Cdd:PHA02857  31 SHGAGEHSGRYEELaeniSSLGILVFSHDHIGHGRSngEKMMIDDFGVyVRDVVQHVVTIKSTYPGvPVFLLGHSMGATI 110
                         90       100
                 ....*....|....*....|....*..
gi 24655464  247 ATHLCAKLASLREraprGVILESPFTN 273
Cdd:PHA02857 111 SILAAYKNPNLFT----AMILMSPLVN 133
 
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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