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Conserved domains on  [gi|1639925523|gb|TKT54418|]
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ACP S-malonyltransferase [Escherichia coli]

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 ...
8-287 2.93e-87

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: 263.53  E-value: 2.93e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   8 TVLLFAGQGNPVIGMGSDLWDLNASTKHIWDCASDISGLNLRRLCQKGPMNRLIQTTVQQLAVTAINVTLYTLCRErlEN 87
Cdd:COG0331     3 LAFLFPGQGSQYVGMGKDLYENFPVAREVFEEASEALGYDLSALCFEGPEEELNLTENTQPAILAASVAAYRALEE--EG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523  88 LTVVGSCGHSVGEYSALYAAGAISLETLFGMIHFRASLMHDESQRNKGAMLAVKGINREQLQTMITE--SGIALDISCDN 165
Cdd:COG0331    81 IRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAVPAGPGGMAAVLGLDDEEVEALCAEaaQGEVVEIANYN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523 166 TPRQQVIGGTQAALNEFATLLMAAG-YEPVKLGVSGAWHTRLMEDGVQAMRDYLAGLDIASPEHQVLMNVTAKSEVAPSI 244
Cdd:COG0331   161 SPGQIVISGEKEAVEAAAELAKEAGaKRAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAAPVTDPEE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1639925523 245 IKENLSLHLTHTVKWTESLDTFLNMPTSVaFLEISNKPYLGNM 287
Cdd:COG0331   241 IRELLVRQLTSPVRWDESVEALAEAGVTT-FVELGPGKVLSGL 282
 
Name Accession Description Interval E-value
FabD COG0331
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ...
8-287 2.93e-87

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: 263.53  E-value: 2.93e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   8 TVLLFAGQGNPVIGMGSDLWDLNASTKHIWDCASDISGLNLRRLCQKGPMNRLIQTTVQQLAVTAINVTLYTLCRErlEN 87
Cdd:COG0331     3 LAFLFPGQGSQYVGMGKDLYENFPVAREVFEEASEALGYDLSALCFEGPEEELNLTENTQPAILAASVAAYRALEE--EG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523  88 LTVVGSCGHSVGEYSALYAAGAISLETLFGMIHFRASLMHDESQRNKGAMLAVKGINREQLQTMITE--SGIALDISCDN 165
Cdd:COG0331    81 IRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAVPAGPGGMAAVLGLDDEEVEALCAEaaQGEVVEIANYN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523 166 TPRQQVIGGTQAALNEFATLLMAAG-YEPVKLGVSGAWHTRLMEDGVQAMRDYLAGLDIASPEHQVLMNVTAKSEVAPSI 244
Cdd:COG0331   161 SPGQIVISGEKEAVEAAAELAKEAGaKRAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAAPVTDPEE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1639925523 245 IKENLSLHLTHTVKWTESLDTFLNMPTSVaFLEISNKPYLGNM 287
Cdd:COG0331   241 IRELLVRQLTSPVRWDESVEALAEAGVTT-FVELGPGKVLSGL 282
fabD TIGR00128
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...
8-278 1.84e-54

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: 179.20  E-value: 1.84e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   8 TVLLFAGQGNPVIGMGSDLWDLNASTKHIWDCASDISGLNLRRLCQKGPMNRLIQTTVQQLAVTAINVTLYTLCRERlEN 87
Cdd:TIGR00128   3 IAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQASEALGYDLKKLCQEGPAEELNKTQYTQPALYVVSAILYLKLKEQ-GG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523  88 LTVVGSCGHSVGEYSALYAAGAISLETLFGMIHFRASLMHDESQRNKGAMLAVKGINREQLQTMITESGIAL-DISCDNT 166
Cdd:TIGR00128  82 LKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAVPEGGGAMAAVIGLDEEQLAQACEEATENDvDLANFNS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523 167 PRQQVIGGTQAALNEFATLLMAAGYE-PVKLGVSGAWHTRLMEDGVQAMRDYLAGLDIASPEHQVLMNVTAKSEVAPSII 245
Cdd:TIGR00128 162 PGQVVISGTKDGVEAAAALFKEMGAKrAVPLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVDAKPYTNGDRI 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1639925523 246 KENLSLHLTHTVKWTESLDtFLNMPTSVAFLEI 278
Cdd:TIGR00128 242 KEKLSEQLTSPVRWTDSVE-KLMARGVTEFAEV 273
PLN02752 PLN02752
[acyl-carrier protein] S-malonyltransferase
7-267 3.82e-38

[acyl-carrier protein] S-malonyltransferase


Pssm-ID: 215401 [Multi-domain]  Cd Length: 343  Bit Score: 137.97  E-value: 3.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   7 PTVLLFAGQGNPVIGMGSDLWDLNASTKhIWDCASDISGLNLRRLCQKGPMNRLIQTTVQQLAVTAINVTLYTLCRERLE 86
Cdd:PLN02752   39 TTAFLFPGQGAQAVGMGKEAAEVPAAKA-LFDKASEILGYDLLDVCVNGPKEKLDSTVVSQPAIYVASLAAVEKLRARDG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523  87 NLTVVGS----CGHSVGEYSALYAAGAISLETLFGMIHFRASLMHDESQRNKGAMLAVKGINREQLQTMIT----ESGIA 158
Cdd:PLN02752  118 GQAVIDSvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAADAGPSGMVSVIGLDSDKVQELCAaaneEVGED 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523 159 LDISCDN--TPRQQVIGGTQAALNEFATLLMAAG-YEPVKLGVSGAWHTRLMEDGVQAMRDYLAGLDIASPEHQVLMNVT 235
Cdd:PLN02752  198 DVVQIANylCPGNYAVSGGKKGIDAVEAKAKSFKaRMTVRLAVAGAFHTSFMEPAVDALEAALAAVEIRTPRIPVISNVD 277
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1639925523 236 AKSEVAPSIIKENLSLHLTHTVKWTESLDTFL 267
Cdd:PLN02752  278 AQPHSDPATIKKILARQVTSPVQWETTVKTLL 309
PKS_AT smart00827
Acyl transferase domain in polyketide synthase (PKS) enzymes;
11-279 1.13e-37

Acyl transferase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214838 [Multi-domain]  Cd Length: 298  Bit Score: 135.61  E-value: 1.13e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   11 LFAGQGNPVIGMGSDLWDLNASTKHIWD-CA---SDISGLNLRR-LCQKGPMNRLIQTTVQQLAVTAINVTLYTLCRERl 85
Cdd:smart00827   1 VFTGQGSQWAGMGRELYETEPVFREALDeCDaalQPLLGWSLLDvLLGEDGAASLLDTEVAQPALFAVQVALARLLRSW- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   86 eNLT---VVGscgHSVGEYSALYAAGAISLETLFGMIHFRASLMHdeSQRNKGAMLAVkGINREQLQTMITESGIALDIS 162
Cdd:smart00827  80 -GVRpdaVVG---HSSGEIAAAYVAGVLSLEDAARLVAARGRLMQ--ALPGGGAMLAV-GLSEEEVEPLLAGVPDRVSVA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523  163 CDNTPRQQVIGGTQAALNEFATLLMAAGYEPVKLGVSGAWHTRLMEDGVQAMRDYLAGLDIASPEHQVLMNVTAKSEVAP 242
Cdd:smart00827 153 AVNSPSSVVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGA 232
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1639925523  243 SIIK-ENLSLHLTHTVKWTESLDTFLNMPTSVAFLEIS 279
Cdd:smart00827 233 ELDDaDYWVRNLREPVRFADAVRALLAEGGVTVFLEVG 270
Acyl_transf_1 pfam00698
Acyl transferase domain;
9-284 7.95e-21

Acyl transferase domain;


Pssm-ID: 395567  Cd Length: 319  Bit Score: 90.61  E-value: 7.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   9 VLLFAGQGNPVIGMGSDLWDLNASTKHIWDCAS----DISGLNLRRLCQKGPMNRLIQTTVQQLAVTAINVTLY-TLCRE 83
Cdd:pfam00698   1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADeafkPQYGFSVSDVLRNNPEGTLDGTQFVQPALFAMQIALAaLLQSY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523  84 RLENLTVVGscgHSVGEYSALYAAGAISLETLFGMIHFRASLMHDESqrNKGAMLAVKGINREQLQTMITEsgiaLDISC 163
Cdd:pfam00698  81 GVRPDAVVG---HSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLA--GPGGMAAVELSAEEVEQRWPDD----VVGAV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523 164 DNTPRQQVIGGTQAALNEFATLLMAAGYEPVKLGVSGAWHTRLMEDGVQAMRDYLAGLDIASPEHQVLMNVTAKSEVAPS 243
Cdd:pfam00698 152 VNSPRSVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRT 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1639925523 244 IIKENLSLHLTHTVKWTESLdTFLNMPTSVAFLEISNKPYL 284
Cdd:pfam00698 232 LSAEYWVRNLRSPVRFAEAI-LSAAEPGPLVFIEISPHPLL 271
 
Name Accession Description Interval E-value
FabD COG0331
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ...
8-287 2.93e-87

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: 263.53  E-value: 2.93e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   8 TVLLFAGQGNPVIGMGSDLWDLNASTKHIWDCASDISGLNLRRLCQKGPMNRLIQTTVQQLAVTAINVTLYTLCRErlEN 87
Cdd:COG0331     3 LAFLFPGQGSQYVGMGKDLYENFPVAREVFEEASEALGYDLSALCFEGPEEELNLTENTQPAILAASVAAYRALEE--EG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523  88 LTVVGSCGHSVGEYSALYAAGAISLETLFGMIHFRASLMHDESQRNKGAMLAVKGINREQLQTMITE--SGIALDISCDN 165
Cdd:COG0331    81 IRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAVPAGPGGMAAVLGLDDEEVEALCAEaaQGEVVEIANYN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523 166 TPRQQVIGGTQAALNEFATLLMAAG-YEPVKLGVSGAWHTRLMEDGVQAMRDYLAGLDIASPEHQVLMNVTAKSEVAPSI 244
Cdd:COG0331   161 SPGQIVISGEKEAVEAAAELAKEAGaKRAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAAPVTDPEE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1639925523 245 IKENLSLHLTHTVKWTESLDTFLNMPTSVaFLEISNKPYLGNM 287
Cdd:COG0331   241 IRELLVRQLTSPVRWDESVEALAEAGVTT-FVELGPGKVLSGL 282
fabD TIGR00128
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ...
8-278 1.84e-54

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: 179.20  E-value: 1.84e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   8 TVLLFAGQGNPVIGMGSDLWDLNASTKHIWDCASDISGLNLRRLCQKGPMNRLIQTTVQQLAVTAINVTLYTLCRERlEN 87
Cdd:TIGR00128   3 IAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQASEALGYDLKKLCQEGPAEELNKTQYTQPALYVVSAILYLKLKEQ-GG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523  88 LTVVGSCGHSVGEYSALYAAGAISLETLFGMIHFRASLMHDESQRNKGAMLAVKGINREQLQTMITESGIAL-DISCDNT 166
Cdd:TIGR00128  82 LKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAVPEGGGAMAAVIGLDEEQLAQACEEATENDvDLANFNS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523 167 PRQQVIGGTQAALNEFATLLMAAGYE-PVKLGVSGAWHTRLMEDGVQAMRDYLAGLDIASPEHQVLMNVTAKSEVAPSII 245
Cdd:TIGR00128 162 PGQVVISGTKDGVEAAAALFKEMGAKrAVPLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVDAKPYTNGDRI 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1639925523 246 KENLSLHLTHTVKWTESLDtFLNMPTSVAFLEI 278
Cdd:TIGR00128 242 KEKLSEQLTSPVRWTDSVE-KLMARGVTEFAEV 273
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
4-287 2.66e-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: 164.66  E-value: 2.66e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523    4 ASQPTVLLFAGQGNPVIGMGSDLWDLNASTKHIWDCASDI----SGLNLRR-LCQKGPMNRLIQTTVQQLAVTAINVTLY 78
Cdd:COG3321    525 AAPKVAFLFPGQGSQYVGMGRELYETEPVFRAALDECDALlrphLGWSLREvLFPDEEESRLDRTEVAQPALFAVEYALA 604
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   79 TLcrerLENLTVVGSC--GHSVGEYSALYAAGAISLETLFGMIHFRASLMhdESQRNKGAMLAVkGINREQLQTMITESG 156
Cdd:COG3321    605 RL----WRSWGVRPDAviGHSVGEYAAACVAGVLSLEDALRLVAARGRLM--QALPGGGAMLAV-GLSEEEVEALLAGYD 677
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523  157 iALDISCDNTPRQQVIGGTQAALNEFATLLMAAGYEPVKLGVSGAWHTRLMEDGVQAMRDYLAGLDIASPEHQVLMNVTA 236
Cdd:COG3321    678 -GVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTG 756
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1639925523  237 KSEVAPSIIKENLSLHLTHTVKWTESLDTFLNMPTSVaFLEISNKPYLGNM 287
Cdd:COG3321    757 TWLTGEALDADYWVRHLRQPVRFADAVEALLADGVRV-FLEVGPGPVLTGL 806
PLN02752 PLN02752
[acyl-carrier protein] S-malonyltransferase
7-267 3.82e-38

[acyl-carrier protein] S-malonyltransferase


Pssm-ID: 215401 [Multi-domain]  Cd Length: 343  Bit Score: 137.97  E-value: 3.82e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   7 PTVLLFAGQGNPVIGMGSDLWDLNASTKhIWDCASDISGLNLRRLCQKGPMNRLIQTTVQQLAVTAINVTLYTLCRERLE 86
Cdd:PLN02752   39 TTAFLFPGQGAQAVGMGKEAAEVPAAKA-LFDKASEILGYDLLDVCVNGPKEKLDSTVVSQPAIYVASLAAVEKLRARDG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523  87 NLTVVGS----CGHSVGEYSALYAAGAISLETLFGMIHFRASLMHDESQRNKGAMLAVKGINREQLQTMIT----ESGIA 158
Cdd:PLN02752  118 GQAVIDSvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAADAGPSGMVSVIGLDSDKVQELCAaaneEVGED 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523 159 LDISCDN--TPRQQVIGGTQAALNEFATLLMAAG-YEPVKLGVSGAWHTRLMEDGVQAMRDYLAGLDIASPEHQVLMNVT 235
Cdd:PLN02752  198 DVVQIANylCPGNYAVSGGKKGIDAVEAKAKSFKaRMTVRLAVAGAFHTSFMEPAVDALEAALAAVEIRTPRIPVISNVD 277
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1639925523 236 AKSEVAPSIIKENLSLHLTHTVKWTESLDTFL 267
Cdd:PLN02752  278 AQPHSDPATIKKILARQVTSPVQWETTVKTLL 309
PKS_AT smart00827
Acyl transferase domain in polyketide synthase (PKS) enzymes;
11-279 1.13e-37

Acyl transferase domain in polyketide synthase (PKS) enzymes;


Pssm-ID: 214838 [Multi-domain]  Cd Length: 298  Bit Score: 135.61  E-value: 1.13e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   11 LFAGQGNPVIGMGSDLWDLNASTKHIWD-CA---SDISGLNLRR-LCQKGPMNRLIQTTVQQLAVTAINVTLYTLCRERl 85
Cdd:smart00827   1 VFTGQGSQWAGMGRELYETEPVFREALDeCDaalQPLLGWSLLDvLLGEDGAASLLDTEVAQPALFAVQVALARLLRSW- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   86 eNLT---VVGscgHSVGEYSALYAAGAISLETLFGMIHFRASLMHdeSQRNKGAMLAVkGINREQLQTMITESGIALDIS 162
Cdd:smart00827  80 -GVRpdaVVG---HSSGEIAAAYVAGVLSLEDAARLVAARGRLMQ--ALPGGGAMLAV-GLSEEEVEPLLAGVPDRVSVA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523  163 CDNTPRQQVIGGTQAALNEFATLLMAAGYEPVKLGVSGAWHTRLMEDGVQAMRDYLAGLDIASPEHQVLMNVTAKSEVAP 242
Cdd:smart00827 153 AVNSPSSVVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGA 232
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1639925523  243 SIIK-ENLSLHLTHTVKWTESLDTFLNMPTSVAFLEIS 279
Cdd:smart00827 233 ELDDaDYWVRNLREPVRFADAVRALLAEGGVTVFLEVG 270
Acyl_transf_1 pfam00698
Acyl transferase domain;
9-284 7.95e-21

Acyl transferase domain;


Pssm-ID: 395567  Cd Length: 319  Bit Score: 90.61  E-value: 7.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523   9 VLLFAGQGNPVIGMGSDLWDLNASTKHIWDCAS----DISGLNLRRLCQKGPMNRLIQTTVQQLAVTAINVTLY-TLCRE 83
Cdd:pfam00698   1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADeafkPQYGFSVSDVLRNNPEGTLDGTQFVQPALFAMQIALAaLLQSY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523  84 RLENLTVVGscgHSVGEYSALYAAGAISLETLFGMIHFRASLMHDESqrNKGAMLAVKGINREQLQTMITEsgiaLDISC 163
Cdd:pfam00698  81 GVRPDAVVG---HSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLA--GPGGMAAVELSAEEVEQRWPDD----VVGAV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1639925523 164 DNTPRQQVIGGTQAALNEFATLLMAAGYEPVKLGVSGAWHTRLMEDGVQAMRDYLAGLDIASPEHQVLMNVTAKSEVAPS 243
Cdd:pfam00698 152 VNSPRSVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRT 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1639925523 244 IIKENLSLHLTHTVKWTESLdTFLNMPTSVAFLEISNKPYL 284
Cdd:pfam00698 232 LSAEYWVRNLRSPVRFAEAI-LSAAEPGPLVFIEISPHPLL 271
 
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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