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Conserved domains on  [gi|2524748491|ref|WP_286766564|]
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malonate decarboxylase subunit epsilon [Leclercia sp. UBA1284]

Protein Classification

ACP S-malonyltransferase( domain architecture ID 10001093)

ACP (Acyl-carrier-protein) S-malonyltransferase catalyzes the transfer of a malonyl moiety from malonyl-CoA to the free thiol group of the phosphopantetheine arm of acyl carrier protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FabD COG0331
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ...
1-282 3.69e-95

Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


:

Pssm-ID: 440100 [Multi-domain]  Cd Length: 306  Bit Score: 283.17  E-value: 3.69e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491   1 MKILFTFPGQGTQHEGMLQNLPGTE------LAQAREVLGAEVDTL---DSAASLSHTRAVQLSLLIAGVAWARELERRG 71
Cdd:COG0331     1 MKLAFLFPGQGSQYVGMGKDLYENFpvarevFEEASEALGYDLSALcfeGPEEELNLTENTQPAILAASVAAYRALEEEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491  72 VTPDIVSGLSIGAYPAAVIAGALDFTDALRLVALRGDVMEQAYPHG-YGLTAIMGLTLPQVEQLIE----GTGTYIANLN 146
Cdd:COG0331    81 IRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAVPAGpGGMAAVLGLDDEEVEALCAeaaqGEVVEIANYN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491 147 AETQIVIAGRDDGMAQVAERALAKGASKAKRLAVSVPSHCALLAEPAQKLVAAFENVTLSRPRLAYLSGSTGRVLWQPEK 226
Cdd:COG0331   161 SPGQIVISGEKEAVEAAAELAKEAGAKRAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAAPVTDPEE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2524748491 227 IADDLAMNMARTVRWQEAVISANERDARLAIEMPPGGILTCLTRQAAWEGESISLE 282
Cdd:COG0331   241 IRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGLVKRIDPGVEVLAVE 296
 
Name Accession Description Interval E-value
FabD COG0331
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ...
1-282 3.69e-95

Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440100 [Multi-domain]  Cd Length: 306  Bit Score: 283.17  E-value: 3.69e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491   1 MKILFTFPGQGTQHEGMLQNLPGTE------LAQAREVLGAEVDTL---DSAASLSHTRAVQLSLLIAGVAWARELERRG 71
Cdd:COG0331     1 MKLAFLFPGQGSQYVGMGKDLYENFpvarevFEEASEALGYDLSALcfeGPEEELNLTENTQPAILAASVAAYRALEEEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491  72 VTPDIVSGLSIGAYPAAVIAGALDFTDALRLVALRGDVMEQAYPHG-YGLTAIMGLTLPQVEQLIE----GTGTYIANLN 146
Cdd:COG0331    81 IRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAVPAGpGGMAAVLGLDDEEVEALCAeaaqGEVVEIANYN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491 147 AETQIVIAGRDDGMAQVAERALAKGASKAKRLAVSVPSHCALLAEPAQKLVAAFENVTLSRPRLAYLSGSTGRVLWQPEK 226
Cdd:COG0331   161 SPGQIVISGEKEAVEAAAELAKEAGAKRAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAAPVTDPEE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2524748491 227 IADDLAMNMARTVRWQEAVISANERDARLAIEMPPGGILTCLTRQAAWEGESISLE 282
Cdd:COG0331   241 IRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGLVKRIDPGVEVLAVE 296
malonate_mdcH TIGR03131
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon ...
3-283 2.36e-94

malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon subunit of malonate decarboxylase. This subunit has malonyl-CoA/dephospho-CoA acyltransferase activity. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. The epsilon subunit is closely related to the malonyl CoA-acyl carrier protein (ACP) transacylase family described by TIGR00128, but acts on an ACP subunit of malonate decarboxylase that has an unusual coenzyme A derivative as its prothetic group.


Pssm-ID: 132175  Cd Length: 295  Bit Score: 280.74  E-value: 2.36e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491   3 ILFTFPGQGTQHEGMLQNLPGTE-----LAQAREVLGAEVDTLDSAASLSHTRAVQLSLLIAGVAWARELERRGVTPDIV 77
Cdd:TIGR03131   1 IALLFPGQGSQRAGMLAELPDHPavaavLAEASDVLGIDPRELDDAEALASTRSAQLCILAAGVAAWRALLALLPRPSAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491  78 SGLSIGAYPAAVIAGALDFTDALRLVALRGDVMEQAYPHGYGLTAIMGLTLPQVEQLIEGTGTYIANLNAETQIVIAGRD 157
Cdd:TIGR03131  81 AGYSVGEYAAAVVAGVLTFDDALRLVALRAALMDQAVPGGYGMLAVLGLDLAAVEALIAKHGVYLAIINAPDQVVIAGSR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491 158 DGMAQVAERALAKGASKAKRLAVSVPSHCALLAEPAQKLVAAFENVTLSRPRLAYLSGSTGRVLWQPEKIADDLAMNMAR 237
Cdd:TIGR03131 161 AALRAVAELARAAGASRAKRLAVRVPSHTPLLAKAAEQFAEALAEIPLAAPRLPYLSGIDARLVRDAAQIRDDLARQIAT 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2524748491 238 TVRWQEAVISANERDARLAIEMPPGGILTCLTRQAAWEGESISLER 283
Cdd:TIGR03131 241 PVDWHDCMQAAYERGARLVIELGPGDVLTKLANEAFPELPARSADD 286
PLN02752 PLN02752
[acyl-carrier protein] S-malonyltransferase
2-277 3.20e-30

[acyl-carrier protein] S-malonyltransferase


Pssm-ID: 215401 [Multi-domain]  Cd Length: 343  Bit Score: 116.40  E-value: 3.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491   2 KILFTFPGQGTQHEGML---QNLPGTE--LAQAREVLGaeVDTLD-----SAASLSHTRAVQLSLLIAGVAWARELERRG 71
Cdd:PLN02752   39 TTAFLFPGQGAQAVGMGkeaAEVPAAKalFDKASEILG--YDLLDvcvngPKEKLDSTVVSQPAIYVASLAAVEKLRARD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491  72 VTPDIV------SGLSIGAYPAAVIAGALDFTDALRLVALRGDVMEQAYPHG-YGLTAIMGLTLPQVEQLI--------E 136
Cdd:PLN02752  117 GGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAADAGpSGMVSVIGLDSDKVQELCaaaneevgE 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491 137 GTGTYIANLNAETQIVIAGRDDGMAQVAERALAKGASKAKRLAVSVPSHCALLAEPAQKLVAAFENVTLSRPRLAYLSGS 216
Cdd:PLN02752  197 DDVVQIANYLCPGNYAVSGGKKGIDAVEAKAKSFKARMTVRLAVAGAFHTSFMEPAVDALEAALAAVEIRTPRIPVISNV 276
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524748491 217 TGRVLWQPEKIADDLAMNMARTVRWQEAVISANERDARLAIEMPPGGILTCLTRQAAWEGE 277
Cdd:PLN02752  277 DAQPHSDPATIKKILARQVTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGIVKRVDKGAK 337
Acyl_transf_1 pfam00698
Acyl transferase domain;
5-298 8.95e-24

Acyl transferase domain;


Pssm-ID: 395567  Cd Length: 319  Bit Score: 98.70  E-value: 8.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491   5 FTFPGQGTQHEGMLQNLPGTELAQAREVLGAE-----------VDTLDSA--ASLSHTRAVQLSLLIAGVAWARELERRG 71
Cdd:pfam00698   2 FVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADeafkpqygfsvSDVLRNNpeGTLDGTQFVQPALFAMQIALAALLQSYG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491  72 VTPDIVSGLSIGAYPAAVIAGALDFTDALRLVALRGDVMEQAypHGYGLTAIMGLTLPQVEQLIEgTGTYIANLNAETQI 151
Cdd:pfam00698  82 VRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQL--AGPGGMAAVELSAEEVEQRWP-DDVVGAVVNSPRSV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491 152 VIAGRDDGMAQVAERaLAKGASKAKRLAVSVPSHCALLAEPAQKLVAAFENVTLSRPRLAYLSGSTGRVLWQPEKIADDL 231
Cdd:pfam00698 159 VISGPQEAVRELVER-VSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRTLSAEYW 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524748491 232 AMNMARTVRWQEAVISANERDARLAIEMPPGGILTCLTRQAAWEGESISLERsgvevavhLAGRLKR 298
Cdd:pfam00698 238 VRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDTLKSASDGKVAT--------LVGTLIR 296
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
59-110 3.44e-03

Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase similar to Z1214 protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132848 [Multi-domain]  Cd Length: 215  Bit Score: 38.04  E-value: 3.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2524748491  59 AGVAwaRELERRGVTPDIVSGLSIGAYPAAVIAGAlDFTDALRLVAL-----RGDVM 110
Cdd:cd07209    14 AGVL--KALAEAGIEPDIISGTSIGAINGALIAGG-DPEAVERLEKLwrelsREDVF 67
 
Name Accession Description Interval E-value
FabD COG0331
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ...
1-282 3.69e-95

Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440100 [Multi-domain]  Cd Length: 306  Bit Score: 283.17  E-value: 3.69e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491   1 MKILFTFPGQGTQHEGMLQNLPGTE------LAQAREVLGAEVDTL---DSAASLSHTRAVQLSLLIAGVAWARELERRG 71
Cdd:COG0331     1 MKLAFLFPGQGSQYVGMGKDLYENFpvarevFEEASEALGYDLSALcfeGPEEELNLTENTQPAILAASVAAYRALEEEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491  72 VTPDIVSGLSIGAYPAAVIAGALDFTDALRLVALRGDVMEQAYPHG-YGLTAIMGLTLPQVEQLIE----GTGTYIANLN 146
Cdd:COG0331    81 IRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAVPAGpGGMAAVLGLDDEEVEALCAeaaqGEVVEIANYN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491 147 AETQIVIAGRDDGMAQVAERALAKGASKAKRLAVSVPSHCALLAEPAQKLVAAFENVTLSRPRLAYLSGSTGRVLWQPEK 226
Cdd:COG0331   161 SPGQIVISGEKEAVEAAAELAKEAGAKRAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAAPVTDPEE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2524748491 227 IADDLAMNMARTVRWQEAVISANERDARLAIEMPPGGILTCLTRQAAWEGESISLE 282
Cdd:COG0331   241 IRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGLVKRIDPGVEVLAVE 296
malonate_mdcH TIGR03131
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon ...
3-283 2.36e-94

malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon subunit of malonate decarboxylase. This subunit has malonyl-CoA/dephospho-CoA acyltransferase activity. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. The epsilon subunit is closely related to the malonyl CoA-acyl carrier protein (ACP) transacylase family described by TIGR00128, but acts on an ACP subunit of malonate decarboxylase that has an unusual coenzyme A derivative as its prothetic group.


Pssm-ID: 132175  Cd Length: 295  Bit Score: 280.74  E-value: 2.36e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491   3 ILFTFPGQGTQHEGMLQNLPGTE-----LAQAREVLGAEVDTLDSAASLSHTRAVQLSLLIAGVAWARELERRGVTPDIV 77
Cdd:TIGR03131   1 IALLFPGQGSQRAGMLAELPDHPavaavLAEASDVLGIDPRELDDAEALASTRSAQLCILAAGVAAWRALLALLPRPSAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491  78 SGLSIGAYPAAVIAGALDFTDALRLVALRGDVMEQAYPHGYGLTAIMGLTLPQVEQLIEGTGTYIANLNAETQIVIAGRD 157
Cdd:TIGR03131  81 AGYSVGEYAAAVVAGVLTFDDALRLVALRAALMDQAVPGGYGMLAVLGLDLAAVEALIAKHGVYLAIINAPDQVVIAGSR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491 158 DGMAQVAERALAKGASKAKRLAVSVPSHCALLAEPAQKLVAAFENVTLSRPRLAYLSGSTGRVLWQPEKIADDLAMNMAR 237
Cdd:TIGR03131 161 AALRAVAELARAAGASRAKRLAVRVPSHTPLLAKAAEQFAEALAEIPLAAPRLPYLSGIDARLVRDAAQIRDDLARQIAT 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2524748491 238 TVRWQEAVISANERDARLAIEMPPGGILTCLTRQAAWEGESISLER 283
Cdd:TIGR03131 241 PVDWHDCMQAAYERGARLVIELGPGDVLTKLANEAFPELPARSADD 286
fabD TIGR00128
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...
1-271 1.28e-56

malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 272922 [Multi-domain]  Cd Length: 290  Bit Score: 184.21  E-value: 1.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491   1 MKILFTFPGQGTQHEGMLQNLPGT-----EL-AQAREVLGAEVDTL---DSAASLSHTRAVQLSLLIAGVAWARELERRG 71
Cdd:TIGR00128   1 MKIAYVFPGQGSQTVGMGKDLYEQypiakELfDQASEALGYDLKKLcqeGPAEELNKTQYTQPALYVVSAILYLKLKEQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491  72 -VTPDIVSGLSIGAYPAAVIAGALDFTDALRLVALRGDVMEQAYPHGYG-LTAIMGLTLPQVEQLIEGTGTY---IANLN 146
Cdd:TIGR00128  81 gLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAVPEGGGaMAAVIGLDEEQLAQACEEATENdvdLANFN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491 147 AETQIVIAGRDDGMAQVAERALAKGASKAKRLAVSVPSHCALLAEPAQKLVAAFENVTLSRPRLAYLSGSTGRVLWQPEK 226
Cdd:TIGR00128 161 SPGQVVISGTKDGVEAAAALFKEMGAKRAVPLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVDAKPYTNGDR 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2524748491 227 IADDLAMNMARTVRWQEAVISANERDARLAIEMPPGGILTCLTRQ 271
Cdd:TIGR00128 241 IKEKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGLIKR 285
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
2-278 4.13e-45

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 163.50  E-value: 4.13e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491    2 KILFTFPGQGTQHEGMLQNLPGTE------LAQAREVLGAEVDT--------LDSAASLSHTRAVQLSLLIAGVAWAREL 67
Cdd:COG3321    528 KVAFLFPGQGSQYVGMGRELYETEpvfraaLDECDALLRPHLGWslrevlfpDEEESRLDRTEVAQPALFAVEYALARLW 607
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491   68 ERRGVTPDIVSGLSIGAYPAAVIAGALDFTDALRLVALRGDVMEQAYPHGyGLTAIMgLTLPQVEQLIEGTGT-YIANLN 146
Cdd:COG3321    608 RSWGVRPDAVIGHSVGEYAAACVAGVLSLEDALRLVAARGRLMQALPGGG-AMLAVG-LSEEEVEALLAGYDGvSIAAVN 685
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491  147 AETQIVIAGRDDGMAQVAERALAKGAsKAKRLAVSVPSHCALLAEPAQKLVAAFENVTLSRPRLAYLSGSTGRVLWQPEK 226
Cdd:COG3321    686 GPRSTVVSGPAEAVEALAARLEARGI-RARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGEAL 764
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2524748491  227 IADDLAMNMARTVRWQEAVISANERDARLAIEMPPGGILTCLTRQAAWEGES 278
Cdd:COG3321    765 DADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQCLAAAGD 816
PLN02752 PLN02752
[acyl-carrier protein] S-malonyltransferase
2-277 3.20e-30

[acyl-carrier protein] S-malonyltransferase


Pssm-ID: 215401 [Multi-domain]  Cd Length: 343  Bit Score: 116.40  E-value: 3.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491   2 KILFTFPGQGTQHEGML---QNLPGTE--LAQAREVLGaeVDTLD-----SAASLSHTRAVQLSLLIAGVAWARELERRG 71
Cdd:PLN02752   39 TTAFLFPGQGAQAVGMGkeaAEVPAAKalFDKASEILG--YDLLDvcvngPKEKLDSTVVSQPAIYVASLAAVEKLRARD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491  72 VTPDIV------SGLSIGAYPAAVIAGALDFTDALRLVALRGDVMEQAYPHG-YGLTAIMGLTLPQVEQLI--------E 136
Cdd:PLN02752  117 GGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAADAGpSGMVSVIGLDSDKVQELCaaaneevgE 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491 137 GTGTYIANLNAETQIVIAGRDDGMAQVAERALAKGASKAKRLAVSVPSHCALLAEPAQKLVAAFENVTLSRPRLAYLSGS 216
Cdd:PLN02752  197 DDVVQIANYLCPGNYAVSGGKKGIDAVEAKAKSFKARMTVRLAVAGAFHTSFMEPAVDALEAALAAVEIRTPRIPVISNV 276
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524748491 217 TGRVLWQPEKIADDLAMNMARTVRWQEAVISANERDARLAIEMPPGGILTCLTRQAAWEGE 277
Cdd:PLN02752  277 DAQPHSDPATIKKILARQVTSPVQWETTVKTLLEKGLEKSYELGPGKVIAGIVKRVDKGAK 337
Acyl_transf_1 pfam00698
Acyl transferase domain;
5-298 8.95e-24

Acyl transferase domain;


Pssm-ID: 395567  Cd Length: 319  Bit Score: 98.70  E-value: 8.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491   5 FTFPGQGTQHEGMLQNLPGTELAQAREVLGAE-----------VDTLDSA--ASLSHTRAVQLSLLIAGVAWARELERRG 71
Cdd:pfam00698   2 FVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADeafkpqygfsvSDVLRNNpeGTLDGTQFVQPALFAMQIALAALLQSYG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491  72 VTPDIVSGLSIGAYPAAVIAGALDFTDALRLVALRGDVMEQAypHGYGLTAIMGLTLPQVEQLIEgTGTYIANLNAETQI 151
Cdd:pfam00698  82 VRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQL--AGPGGMAAVELSAEEVEQRWP-DDVVGAVVNSPRSV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524748491 152 VIAGRDDGMAQVAERaLAKGASKAKRLAVSVPSHCALLAEPAQKLVAAFENVTLSRPRLAYLSGSTGRVLWQPEKIADDL 231
Cdd:pfam00698 159 VISGPQEAVRELVER-VSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRTLSAEYW 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524748491 232 AMNMARTVRWQEAVISANERDARLAIEMPPGGILTCLTRQAAWEGESISLERsgvevavhLAGRLKR 298
Cdd:pfam00698 238 VRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDTLKSASDGKVAT--------LVGTLIR 296
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
59-110 3.44e-03

Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase similar to Z1214 protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132848 [Multi-domain]  Cd Length: 215  Bit Score: 38.04  E-value: 3.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2524748491  59 AGVAwaRELERRGVTPDIVSGLSIGAYPAAVIAGAlDFTDALRLVAL-----RGDVM 110
Cdd:cd07209    14 AGVL--KALAEAGIEPDIISGTSIGAINGALIAGG-DPEAVERLEKLwrelsREDVF 67
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
65-107 9.39e-03

Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases.


Pssm-ID: 132844 [Multi-domain]  Cd Length: 175  Bit Score: 36.37  E-value: 9.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2524748491  65 RELERRGVTPDIVSGLSIGAYPAAVIAGALDFTDALRLVALRG 107
Cdd:cd07205    20 KALEEAGIPIDIVSGTSAGAIVGALYAAGYSPEEIEERAKLRS 62
 
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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