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Conserved domains on  [gi|446409830|ref|WP_000487685|]
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MULTISPECIES: lysophospholipase L2 [Salmonella]

Protein Classification

lysophospholipase L2( domain architecture ID 10793464)

lysophospholipase L2 catalyzes the conversion of 1-lysophosphatidylcholine to glycerophosphocholine and can also hydrolyze 2-acyl glycerophosphoethanolamine as well as other substrates; belongs to the alpha/beta hydrolase superfamily

CATH:  3.40.50.1820
EC:  3.1.1.5
Gene Symbol:  pldB
Gene Ontology:  GO:0004622|GO:0006650
SCOP:  3000102

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK10749 PRK10749
lysophospholipase L2; Provisional
1-330 0e+00

lysophospholipase L2; Provisional


:

Pssm-ID: 182697  Cd Length: 330  Bit Score: 683.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830   1 MFQQQNDWETRENAFAAFAMGPLTDFWRQREEAEFIGVGNIPVRFVRFRNDSNDRTIVICPGRIESYVKYAELAYDLFHL 80
Cdd:PRK10749   1 MFQQQKDWLTRENAFAAFTMGPLLDFWRQREEAEFTGVDDIPIRFVRFRAPHHDRVVVICPGRIESYVKYAELAYDLFHL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  81 GFDIFIIDHRGQGRSGRMLSDPHRGHVDHFNDYVEDLAAFWQQEIEPGPWRKRYILAHSMGGAIATLFLQRHRVRCDAIA 160
Cdd:PRK10749  81 GYDVLIIDHRGQGRSGRLLDDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLFLQRHPGVFDAIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 161 LTAPMFGIVIRLPSFMVRHILDWAEGHQRIREDYAIGTGQWRALPFGMNALTHSRQRYQRNLRFYADEPQLRVGGPTWHW 240
Cdd:PRK10749 161 LCAPMFGIVLPLPSWMARRILNWAEGHPRIRDGYAIGTGRWRPLPFAINVLTHSRERYRRNLRFYADDPELRVGGPTYHW 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 241 VREGILAGEQVLAGASDDTTPTLLIQAEEERVVDNRTHDRFCEIRAAAGYPCEGGKPLVIKGAYHEILFEKDAMRSVALN 320
Cdd:PRK10749 241 VRESILAGEQVLAGAGDITTPLLLLQAEEERVVDNRMHDRFCEARTAAGHPCEGGKPLVIKGAYHEILFEKDAMRSVALN 320
                        330
                 ....*....|
gi 446409830 321 AIVEFFNKPN 330
Cdd:PRK10749 321 AIVDFFNRHN 330
 
Name Accession Description Interval E-value
PRK10749 PRK10749
lysophospholipase L2; Provisional
1-330 0e+00

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 683.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830   1 MFQQQNDWETRENAFAAFAMGPLTDFWRQREEAEFIGVGNIPVRFVRFRNDSNDRTIVICPGRIESYVKYAELAYDLFHL 80
Cdd:PRK10749   1 MFQQQKDWLTRENAFAAFTMGPLLDFWRQREEAEFTGVDDIPIRFVRFRAPHHDRVVVICPGRIESYVKYAELAYDLFHL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  81 GFDIFIIDHRGQGRSGRMLSDPHRGHVDHFNDYVEDLAAFWQQEIEPGPWRKRYILAHSMGGAIATLFLQRHRVRCDAIA 160
Cdd:PRK10749  81 GYDVLIIDHRGQGRSGRLLDDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLFLQRHPGVFDAIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 161 LTAPMFGIVIRLPSFMVRHILDWAEGHQRIREDYAIGTGQWRALPFGMNALTHSRQRYQRNLRFYADEPQLRVGGPTWHW 240
Cdd:PRK10749 161 LCAPMFGIVLPLPSWMARRILNWAEGHPRIRDGYAIGTGRWRPLPFAINVLTHSRERYRRNLRFYADDPELRVGGPTYHW 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 241 VREGILAGEQVLAGASDDTTPTLLIQAEEERVVDNRTHDRFCEIRAAAGYPCEGGKPLVIKGAYHEILFEKDAMRSVALN 320
Cdd:PRK10749 241 VRESILAGEQVLAGAGDITTPLLLLQAEEERVVDNRMHDRFCEARTAAGHPCEGGKPLVIKGAYHEILFEKDAMRSVALN 320
                        330
                 ....*....|
gi 446409830 321 AIVEFFNKPN 330
Cdd:PRK10749 321 AIVDFFNRHN 330
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
51-312 3.30e-71

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: 221.32  E-value: 3.30e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830   51 DSNDRTIVICPGRIESYVKYAELAYDLFHLGFDIFIIDHRGQGRSgrmlsDPHRGHVDHFNDYVEDLAAFWQQEIEPGPW 130
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRS-----DGKRGHVPSFDDYVDDLDTFVDKIREEHPG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  131 RKRYILAHSMGGAIATLFLQRHRVRCDAIALTAPMFGIVIRLPSFMVRHILDWAeghQRIredyaigtgqWRALPFGMNA 210
Cdd:pfam12146  76 LPLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLL---GKL----------FPRLRVPNNL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  211 LTHSRQRYQRNLRFYADEPqLRVGGPTWHWVREGILAGEQVLAGASDDTTPTLLIQAEEERVVDNRTHDRFceIRAAagy 290
Cdd:pfam12146 143 LPDSLSRDPEVVAAYAADP-LVHGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREF--YERA--- 216
                         250       260
                  ....*....|....*....|..
gi 446409830  291 PCEGGKPLVIKGAYHEILFEKD 312
Cdd:pfam12146 217 GSTDKTLKLYPGLYHELLNEPD 238
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
29-328 4.23e-40

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 140.52  E-value: 4.23e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  29 QREEAEFIGVGNIPVRFVRFRNDSNDR-TIVICPGRIESYVKYAELAYDLFHLGFDIFIIDHRGQGRSGRMlsdphRGHV 107
Cdd:COG2267    2 TRRLVTLPTRDGLRLRGRRWRPAGSPRgTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGP-----RGHV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 108 DHFNDYVEDLAAFWQQeIEPGPWRKRYILAHSMGGAIATLFLQRHRVRCDAIALTAPmfgivirlpsfmvrhildwaegh 187
Cdd:COG2267   77 DSFDDYVDDLRAALDA-LRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP----------------------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 188 qriredyaigtgqwralpfgmnalthsrqryqrnlrFYADEPQLrvgGPTWHWVREGilageQVLAGASDDTTPTLLIQA 267
Cdd:COG2267  133 ------------------------------------AYRADPLL---GPSARWLRAL-----RLAEALARIDVPVLVLHG 168
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446409830 268 EEERVVDNRTHDRFCEIRAAagypceGGKPLVIKGAYHEILFEKDamRSVALNAIVEFFNK 328
Cdd:COG2267  169 GADRVVPPEAARRLAARLSP------DVELVLLPGARHELLNEPA--REEVLAAILAWLER 221
 
Name Accession Description Interval E-value
PRK10749 PRK10749
lysophospholipase L2; Provisional
1-330 0e+00

lysophospholipase L2; Provisional


Pssm-ID: 182697  Cd Length: 330  Bit Score: 683.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830   1 MFQQQNDWETRENAFAAFAMGPLTDFWRQREEAEFIGVGNIPVRFVRFRNDSNDRTIVICPGRIESYVKYAELAYDLFHL 80
Cdd:PRK10749   1 MFQQQKDWLTRENAFAAFTMGPLLDFWRQREEAEFTGVDDIPIRFVRFRAPHHDRVVVICPGRIESYVKYAELAYDLFHL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  81 GFDIFIIDHRGQGRSGRMLSDPHRGHVDHFNDYVEDLAAFWQQEIEPGPWRKRYILAHSMGGAIATLFLQRHRVRCDAIA 160
Cdd:PRK10749  81 GYDVLIIDHRGQGRSGRLLDDPHRGHVERFNDYVDDLAAFWQQEIQPGPYRKRYALAHSMGGAILTLFLQRHPGVFDAIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 161 LTAPMFGIVIRLPSFMVRHILDWAEGHQRIREDYAIGTGQWRALPFGMNALTHSRQRYQRNLRFYADEPQLRVGGPTWHW 240
Cdd:PRK10749 161 LCAPMFGIVLPLPSWMARRILNWAEGHPRIRDGYAIGTGRWRPLPFAINVLTHSRERYRRNLRFYADDPELRVGGPTYHW 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 241 VREGILAGEQVLAGASDDTTPTLLIQAEEERVVDNRTHDRFCEIRAAAGYPCEGGKPLVIKGAYHEILFEKDAMRSVALN 320
Cdd:PRK10749 241 VRESILAGEQVLAGAGDITTPLLLLQAEEERVVDNRMHDRFCEARTAAGHPCEGGKPLVIKGAYHEILFEKDAMRSVALN 320
                        330
                 ....*....|
gi 446409830 321 AIVEFFNKPN 330
Cdd:PRK10749 321 AIVDFFNRHN 330
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
51-312 3.30e-71

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: 221.32  E-value: 3.30e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830   51 DSNDRTIVICPGRIESYVKYAELAYDLFHLGFDIFIIDHRGQGRSgrmlsDPHRGHVDHFNDYVEDLAAFWQQEIEPGPW 130
Cdd:pfam12146   1 GEPRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRS-----DGKRGHVPSFDDYVDDLDTFVDKIREEHPG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  131 RKRYILAHSMGGAIATLFLQRHRVRCDAIALTAPMFGIVIRLPSFMVRHILDWAeghQRIredyaigtgqWRALPFGMNA 210
Cdd:pfam12146  76 LPLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPYLAPPILKLLAKLL---GKL----------FPRLRVPNNL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  211 LTHSRQRYQRNLRFYADEPqLRVGGPTWHWVREGILAGEQVLAGASDDTTPTLLIQAEEERVVDNRTHDRFceIRAAagy 290
Cdd:pfam12146 143 LPDSLSRDPEVVAAYAADP-LVHGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREF--YERA--- 216
                         250       260
                  ....*....|....*....|..
gi 446409830  291 PCEGGKPLVIKGAYHEILFEKD 312
Cdd:pfam12146 217 GSTDKTLKLYPGLYHELLNEPD 238
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
29-328 4.23e-40

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 140.52  E-value: 4.23e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  29 QREEAEFIGVGNIPVRFVRFRNDSNDR-TIVICPGRIESYVKYAELAYDLFHLGFDIFIIDHRGQGRSGRMlsdphRGHV 107
Cdd:COG2267    2 TRRLVTLPTRDGLRLRGRRWRPAGSPRgTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGP-----RGHV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 108 DHFNDYVEDLAAFWQQeIEPGPWRKRYILAHSMGGAIATLFLQRHRVRCDAIALTAPmfgivirlpsfmvrhildwaegh 187
Cdd:COG2267   77 DSFDDYVDDLRAALDA-LRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP----------------------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 188 qriredyaigtgqwralpfgmnalthsrqryqrnlrFYADEPQLrvgGPTWHWVREGilageQVLAGASDDTTPTLLIQA 267
Cdd:COG2267  133 ------------------------------------AYRADPLL---GPSARWLRAL-----RLAEALARIDVPVLVLHG 168
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446409830 268 EEERVVDNRTHDRFCEIRAAagypceGGKPLVIKGAYHEILFEKDamRSVALNAIVEFFNK 328
Cdd:COG2267  169 GADRVVPPEAARRLAARLSP------DVELVLLPGARHELLNEPA--REEVLAAILAWLER 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
56-312 4.72e-33

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: 122.61  E-value: 4.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830   56 TIVICPGRIESYVKYAELAYDLFHLGFDIFIIDHRGQGRSGRmLSDPHRGHVDHFNDYVEDLaafwqqeIEPGPWRKRYI 135
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSR-PKAQDDYRTDDLAEDLEYI-------LEALGLEKVNL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  136 LAHSMGGAIATLFLQRHRVRCDAIALTAPMfgivirLPSFMVRHILD-WAEGHQRIREDYAIGTGQWRALPFGMNALTHS 214
Cdd:pfam00561  74 VGHSMGGLIALAYAAKYPDRVKALVLLGAL------DPPHELDEADRfILALFPGFFDGFVADFAPNPLGRLVAKLLALL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  215 RQRYQR-------NLRFYADEPQLRVGGPTWHWVREGILAGEQVLAGASDDTTPTLLIQAEEERVVDNRTHDRFCEIraa 287
Cdd:pfam00561 148 LLRLRLlkalpllNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQL--- 224
                         250       260
                  ....*....|....*....|....*
gi 446409830  288 agypCEGGKPLVIKGAYHEILFEKD 312
Cdd:pfam00561 225 ----FPNARLVVIPDAGHFAFLEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
76-172 1.97e-08

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: 53.85  E-value: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  76 DLFHLGFDIFIIDHRGQGRSGRmlsdPHRGHvdHFNDYVEDLAAFWQQEiepgPWRKRYILAHSMGGAIATLFLQRHRVR 155
Cdd:COG0596   44 PALAAGYRVIAPDLRGHGRSDK----PAGGY--TLDDLADDLAALLDAL----GLERVVLVGHSMGGMVALELAARHPER 113
                         90
                 ....*....|....*..
gi 446409830 156 CDAIALTAPMFGIVIRL 172
Cdd:COG0596  114 VAGLVLVDEVLAALAEP 130
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
56-328 2.38e-08

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 54.15  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  56 TIVICPGR---IESYVKYAELaydLFHLGFDIFIIDHRGQGRSG---RMLSDPHRGHVDHFNDYVEDLAAFWQQEIepgp 129
Cdd:COG1073   39 AVVVAHGNggvKEQRALYAQR---LAELGFNVLAFDYRGYGESEgepREEGSPERRDARAAVDYLRTLPGVDPERI---- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 130 wrkrYILAHSMGGAIATLFLQRHRvRCDAIALTAPMFGIvirlpsfmvrhildWAEGHQRIREDYaigTGQWRALPFgmn 209
Cdd:COG1073  112 ----GLLGISLGGGYALNAAATDP-RVKAVILDSPFTSL--------------EDLAAQRAKEAR---GAYLPGVPY--- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 210 altHSRQRYQRNLRFYADepqlrvggptwhwvregilageqVLAGASDDTTPTLLIQAEEERVVdnrTHDRFCEIRAAAG 289
Cdd:COG1073  167 ---LPNVRLASLLNDEFD-----------------------PLAKIEKISRPLLFIHGEKDEAV---PFYMSEDLYEAAA 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446409830 290 YPceggKPLVI-KGAYHEILFEKDamRSVALNAIVEFFNK 328
Cdd:COG1073  218 EP----KELLIvPGAGHVDLYDRP--EEEYFDKLAEFFKK 251
PHA02857 PHA02857
monoglyceride lipase; Provisional
57-165 9.50e-08

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 52.58  E-value: 9.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  57 IVICPGRIESYVKYAELAYDLFHLGFDIFIIDHRGQGRS-GRMLSdphrghVDHFNDYVEDLAAFWQQEIEPGPWRKRYI 135
Cdd:PHA02857  28 VFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSnGEKMM------IDDFGVYVRDVVQHVVTIKSTYPGVPVFL 101
                         90       100       110
                 ....*....|....*....|....*....|
gi 446409830 136 LAHSMGGAIATLFLQRHRVRCDAIALTAPM 165
Cdd:PHA02857 102 LGHSMGATISILAAYKNPNLFTAMILMSPL 131
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
73-328 5.56e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 46.86  E-value: 5.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  73 LAYDLFHLGFDIFIIDHRGQGRSGRMLSDPHrghvdhFNDYVEDL-AAFwqQEIEPGpWRKRYILAHSMGGAIATLFLQR 151
Cdd:COG1647   34 LAEALAKAGYTVYAPRLPGHGTSPEDLLKTT------WEDWLEDVeEAY--EILKAG-YDKVIVIGLSMGGLLALLLAAR 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 152 HRvRCDAIALTAPMFGI----VIRLPsfMVRHILDWAEGHQRIREDYAIGTGQWRALPfgMNALtHSRQRYqrnlrfyad 227
Cdd:COG1647  105 YP-DVAGLVLLSPALKIddpsAPLLP--LLKYLARSLRGIGSDIEDPEVAEYAYDRTP--LRAL-AELQRL--------- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 228 epqlrvggptWHWVREGIlagEQVlagasddTTPTLLIQAEEERVVDNRTHDRFceiraAAGYPCEGGKPLVIKGAYHEI 307
Cdd:COG1647  170 ----------IREVRRDL---PKI-------TAPTLIIQSRKDEVVPPESARYI-----YERLGSPDKELVWLEDSGHVI 224
                        250       260
                 ....*....|....*....|.
gi 446409830 308 LFEKDamRSVALNAIVEFFNK 328
Cdd:COG1647  225 TLDKD--REEVAEEILDFLER 243
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
57-238 2.55e-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: 44.77  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830   57 IVICPGRIESYVKYAELAYDlfhlGFDIFIIDHRGQGRSGRMLSDPHRghvdhfndyVEDLAAFWQQEIEPGPwrkRYIL 136
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAA----GVAVLAPDLPGHGSSSPPPLDLAD---------LADLAALLDELGAARP---VVLV 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  137 AHSMGGAIATLFLQRHRVRCDAIALTAPMFGIVIRLPSFMVRHILDWAEGHQRIREDYAIGTGQWRALPFGMNALTHSRQ 216
Cdd:pfam12697  65 GHSLGGAVALAAAAAALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLA 144
                         170       180
                  ....*....|....*....|..
gi 446409830  217 RYQRNLRFYADEPQLRVGGPTW 238
Cdd:pfam12697 145 ALLAALALLPLAAWRDLPVPVL 166
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
56-328 2.37e-03

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 38.84  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  56 TIVICPGRIESYVKYAELAYDLFH-LGFDIFIIDHRGQGRSGRmlsdphrghvDHFNDYVEDLAAFW-----QQEIEPgp 129
Cdd:COG1506   25 VVVYVHGGPGSRDDSFLPLAQALAsRGYAVLAPDYRGYGESAG----------DWGGDEVDDVLAAIdylaaRPYVDP-- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 130 wRKRYILAHSMGGAIATLFLQRHRVRCDAIALTAPMFgivirlpsfmvrhilDWAeghqrireDYAIGTGQWRALPFGmn 209
Cdd:COG1506   93 -DRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS---------------DLR--------SYYGTTREYTERLMG-- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830 210 ALTHSRQRY-QRNLRFYADEPQlrvggptwhwvregilageqvlagasddtTPTLLIQAEEERVVDNRTHDRFCEIRAAA 288
Cdd:COG1506  147 GPWEDPEAYaARSPLAYADKLK-----------------------------TPLLLIHGEADDRVPPEQAERLYEALKKA 197
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446409830 289 GYPCEGgkpLVIKGAYHEILfekDAMRSVALNAIVEFFNK 328
Cdd:COG1506  198 GKPVEL---LVYPGEGHGFS---GAGAPDYLERILDFLDR 231
LIDHydrolase pfam10230
Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. ...
61-155 3.45e-03

Lipid-droplet associated hydrolase; This family of proteins is conserved from plants to humans. The function is as a lipid-droplet hydrolase. Human LDAH plays a role in cholesterol homeostasis.


Pssm-ID: 370901  Cd Length: 261  Bit Score: 38.43  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830   61 PGRIESYVKYAELAYDLFHLGFDIFIIDHRGQGRSGRMLSDPHR------GHVDHFNDYVEDLaafwqQEIEPGPWRKRY 134
Cdd:pfam10230  12 PGLVGFYETFLSLLYEKLNPTFDVLGISHAGHSLEDRNDAKENGrvfslqDQIEHKIDFIRAF-----LPANSDKDVKLI 86
                          90       100
                  ....*....|....*....|.
gi 446409830  135 ILAHSMGGAIATLFLQRHRVR 155
Cdd:pfam10230  87 LIGHSIGAYIALEVLKRLSER 107
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
57-164 5.58e-03

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 38.34  E-value: 5.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  57 IVICPGRIESYVKYAELAYDLFHLGFDIFIIDHRGQGRSgrmlsDPHRGHVDHFNDYVEDLAAFWQQEIEPGPWRKRYIL 136
Cdd:PLN02652 139 LIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGS-----DGLHGYVPSLDYVVEDTEAFLEKIRSENPGVPCFLF 213
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446409830 137 AHSMGGAI---ATLFlQRHRVRCDAIALTAP 164
Cdd:PLN02652 214 GHSTGGAVvlkAASY-PSIEDKLEGIVLTSP 243
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
81-168 9.38e-03

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 37.42  E-value: 9.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446409830  81 GFDIFIIDHRGQGrsgrmLSDPHRGHVDHFNDYVEDLAAFWQQEIEPGPWRK--RYILAHSMGGAIAtlfLQRHRVRCDA 158
Cdd:PLN02385 115 GYGVFAMDYPGFG-----LSEGLHGYIPSFDDLVDDVIEHYSKIKGNPEFRGlpSFLFGQSMGGAVA---LKVHLKQPNA 186
                         90
                 ....*....|...
gi 446409830 159 ---IALTAPMFGI 168
Cdd:PLN02385 187 wdgAILVAPMCKI 199
 
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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