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Conserved domains on  [gi|808354811|ref|NP_001293304|]
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AMP-dependent synthetase/ligase domain-containing protein [Caenorhabditis elegans]

Protein Classification

acyl-CoA synthetase; AMP-dependent synthetase/ligase( domain architecture ID 10147355)

acyl-CoA synthetase catalyzes the ATP-dependent activation of fatty acids in a two-step reaction to form acyl-CoA esters| AMP-dependent synthetase/ligase such as long-chain fatty acid--CoA ligase, which catalyzes the activation of long-chain fatty acids (over C12) as acyl-CoA prior to fatty acid elongation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
1070-1651 0e+00

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


:

Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 720.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1070 ILTLVTSKNAEQDTATCSTLLKRAERIAGLLTDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKPPVAS-DLN 1148
Cdd:cd05905     1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISqQLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1149 TTLGPIRMmvDMSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPSSWRRKNNNNcdtttsGSSGAASKEEIC 1228
Cdd:cd05905    81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKW------GPHPPTRDGDTA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1229 YLDFSINSSGQLQGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEVEQQPS 1308
Cdd:cd05905   153 YIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1309 LFLTTLSNLKVRDAFTTYSTINTCVTQLATSVENLRERGCNLSMLRSCVAIAEERPRIALMSSFCKLFAPLALNNRAIST 1388
Cdd:cd05905   233 LWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVST 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1389 SFSSRVNAAICMQGASGPEPSTVYVDARALRNDRISLVGKGAPHSVALIESGKLLPGVKIAIANPETRGQCADSHLGEIW 1468
Cdd:cd05905   313 EFGTRVNPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIW 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1469 VASIHNASPLNRLASVTGFGDEGTMNTdvynaRLTTGDTKTRWARTGYLGFLRQTQSITEHGELHDAVFVVGALNESLVL 1548
Cdd:cd05905   393 VNSPANASGYFLLDGETNDTFKVFPST-----RLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEV 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1549 RGMRYHPFDVESTVSKAHRFVGNSAVFTWNHLVVIAAECT-GSESDALDLVPAITSAVLEEHHLIVGVVVVVDPGSIRHG 1627
Cdd:cd05905   468 RGLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKN 547
                         570       580
                  ....*....|....*....|....
gi 808354811 1628 PGGEKLRSTIRSLFLEEKLNPIYV 1651
Cdd:cd05905   548 PLGEKQRMEIRQAFLAGKLHPIYV 571
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
401-1001 0e+00

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


:

Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 687.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  401 AAMVLDQSAKPSTQLTYGKLHSRAGKVAYMLLTKtvqvnkdgsknVMCKPGDRVALIYPNtqPLHFLAAFYGCLQAGVIP 480
Cdd:cd05905     1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKK-----------VGLKPGDRVALMYPD--PLDFVAAFYGCLYAGVVP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  481 VPVEMPSskreaGIAQLGFLLGNCGVKVALTSESCYKGLPKKVNTSstfsapsgsnsltGTSSEIVDFRGWPRLWWAVTE 560
Cdd:cd05905    68 IPIEPPD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKLLKS-------------KTAAEIAKKKGWPKILDFVKI 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  561 HMSKPS--RDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAI 638
Cdd:cd05905   130 PKSKRSklKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGC 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  639 LASIFNGMKVIFVPYSLMKMNPATWMHMVSKYQATTALVKSRDLHWAL------LATRDHKDISLASLRTLLVADGaNPW 712
Cdd:cd05905   210 LLSVYSGHHTILIPPELMKTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRP 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  713 SLSSCDAFAAAFTPSPYSLRpdamcpcAGSSETGTISIRRRG-NAQLGSQSGRGILSMSALSHCVVRVDTENSLTSLTLQ 791
Cdd:cd05905   289 RISSCDSFLKLFQTLGLSPR-------AVSTEFGTRVNPFICwQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQ 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  792 DAGQIVAGAVVVVTAIDGSNrLCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEPVGEYGKLIGAVRYVRSGLIGFMG 871
Cdd:cd05905   362 DSGKVLPGAQVAIVNPETKG-LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLR 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  872 P----------DGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPmkfvYRGRICVFSTSvlrdERIVIVAEQKPnCSE 941
Cdd:cd05905   441 PtkctdlnveeHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPP-GSE 511
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  942 EEAFDWITRVLRAIDTIHQVGIYCCALVPANHLPKTPLGGVHVSETKQRFENGDLHPSTL 1001
Cdd:cd05905   512 EEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
 
Name Accession Description Interval E-value
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
1070-1651 0e+00

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 720.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1070 ILTLVTSKNAEQDTATCSTLLKRAERIAGLLTDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKPPVAS-DLN 1148
Cdd:cd05905     1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISqQLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1149 TTLGPIRMmvDMSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPSSWRRKNNNNcdtttsGSSGAASKEEIC 1228
Cdd:cd05905    81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKW------GPHPPTRDGDTA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1229 YLDFSINSSGQLQGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEVEQQPS 1308
Cdd:cd05905   153 YIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1309 LFLTTLSNLKVRDAFTTYSTINTCVTQLATSVENLRERGCNLSMLRSCVAIAEERPRIALMSSFCKLFAPLALNNRAIST 1388
Cdd:cd05905   233 LWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVST 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1389 SFSSRVNAAICMQGASGPEPSTVYVDARALRNDRISLVGKGAPHSVALIESGKLLPGVKIAIANPETRGQCADSHLGEIW 1468
Cdd:cd05905   313 EFGTRVNPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIW 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1469 VASIHNASPLNRLASVTGFGDEGTMNTdvynaRLTTGDTKTRWARTGYLGFLRQTQSITEHGELHDAVFVVGALNESLVL 1548
Cdd:cd05905   393 VNSPANASGYFLLDGETNDTFKVFPST-----RLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEV 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1549 RGMRYHPFDVESTVSKAHRFVGNSAVFTWNHLVVIAAECT-GSESDALDLVPAITSAVLEEHHLIVGVVVVVDPGSIRHG 1627
Cdd:cd05905   468 RGLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKN 547
                         570       580
                  ....*....|....*....|....
gi 808354811 1628 PGGEKLRSTIRSLFLEEKLNPIYV 1651
Cdd:cd05905   548 PLGEKQRMEIRQAFLAGKLHPIYV 571
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
401-1001 0e+00

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 687.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  401 AAMVLDQSAKPSTQLTYGKLHSRAGKVAYMLLTKtvqvnkdgsknVMCKPGDRVALIYPNtqPLHFLAAFYGCLQAGVIP 480
Cdd:cd05905     1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKK-----------VGLKPGDRVALMYPD--PLDFVAAFYGCLYAGVVP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  481 VPVEMPSskreaGIAQLGFLLGNCGVKVALTSESCYKGLPKKVNTSstfsapsgsnsltGTSSEIVDFRGWPRLWWAVTE 560
Cdd:cd05905    68 IPIEPPD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKLLKS-------------KTAAEIAKKKGWPKILDFVKI 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  561 HMSKPS--RDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAI 638
Cdd:cd05905   130 PKSKRSklKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGC 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  639 LASIFNGMKVIFVPYSLMKMNPATWMHMVSKYQATTALVKSRDLHWAL------LATRDHKDISLASLRTLLVADGaNPW 712
Cdd:cd05905   210 LLSVYSGHHTILIPPELMKTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRP 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  713 SLSSCDAFAAAFTPSPYSLRpdamcpcAGSSETGTISIRRRG-NAQLGSQSGRGILSMSALSHCVVRVDTENSLTSLTLQ 791
Cdd:cd05905   289 RISSCDSFLKLFQTLGLSPR-------AVSTEFGTRVNPFICwQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQ 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  792 DAGQIVAGAVVVVTAIDGSNrLCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEPVGEYGKLIGAVRYVRSGLIGFMG 871
Cdd:cd05905   362 DSGKVLPGAQVAIVNPETKG-LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLR 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  872 P----------DGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPmkfvYRGRICVFSTSvlrdERIVIVAEQKPnCSE 941
Cdd:cd05905   441 PtkctdlnveeHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPP-GSE 511
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  942 EEAFDWITRVLRAIDTIHQVGIYCCALVPANHLPKTPLGGVHVSETKQRFENGDLHPSTL 1001
Cdd:cd05905   512 EEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
413-980 7.75e-33

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 134.17  E-value: 7.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  413 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREa 492
Cdd:COG0318    23 RRLTYAELDARARRLAAALRALGV------------GPGDRVALLLPNS--PEFVVAFLAALRAGAVVVPLNPRLTAEE- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  493 giaqLGFLLGNCGVKVALTsescykglpkkvntsstfsapsgsnsltgtsseivdfrgwprlwwavtehmskpsrdwtap 572
Cdd:COG0318    88 ----LAYILEDSGARALVT------------------------------------------------------------- 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  573 prladetiAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVV----DFkrevGLWHAILASIFNGMKV 648
Cdd:COG0318   103 --------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALplfhVF----GLTVGLLAPLLAGATL 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  649 IFVPyslmKMNPATWMHMVSKYQAT-TALVKSrdLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAFTPs 727
Cdd:COG0318   171 VLLP----RFDPERVLELIERERVTvLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFEERFGV- 241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  728 pyslrpdAMCPCAGSSETG---TISIRRRGNAQLGSQsGRgilsmsALSHCVVRVdtensltsltlqdagqivagavvvv 804
Cdd:COG0318   242 -------RIVEGYGLTETSpvvTVNPEDPGERRPGSV-GR------PLPGVEVRI------------------------- 282
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  805 taIDGSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFkvepvgeygkligAVRYVRSGLIGFMGPDGMVFVVARRQS 884
Cdd:COG0318   283 --VDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-------------RDGWLRTGDLGRLDEDGYLYIVGRKKD 347
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  885 LLAVSGRYHSADDIIATVLAVEPMKfvyrgRICVFS-TSVLRDERIV--IVAEQKPNCSEEEAFDWITRVLRAIDTIHQV 961
Cdd:COG0318   348 MIISGGENVYPAEVEEVLAAHPGVA-----EAAVVGvPDEKWGERVVafVVLRPGAELDAEELRAFLRERLARYKVPRRV 422
                         570
                  ....*....|....*....
gi 808354811  962 giyccALVPAnhLPKTPLG 980
Cdd:COG0318   423 -----EFVDE--LPRTASG 434
AMP-binding pfam00501
AMP-binding enzyme;
413-882 3.09e-31

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 128.58  E-value: 3.09e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   413 TQLTYGKLHSRAGKVAYMLLtktvqvnkdgSKNVmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVeMPSSKREA 492
Cdd:pfam00501   20 RRLTYRELDERANRLAAGLR----------ALGV--GKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPL-NPRLPAEE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   493 giaqLGFLLGNCGVKVALTSEScyKGLPKkvntsstfSAPSGSNSLTGTSSEIVDFRGWPRLWWAvtEHMSKPSRDWTAP 572
Cdd:pfam00501   85 ----LAYILEDSGAKVLITDDA--LKLEE--------LLEALGKLEVVKLVLVLDRDPVLKEEPL--PEEAKPADVPPPP 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   573 PRLAD-ETIAYIEYTTGNDGTVKGCCVT----RQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMK 647
Cdd:pfam00501  149 PPPPDpDDLAYIIYTSGTTGKPKGVMLThrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAT 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   648 VIFVPYSLMKMnPATWMHMVSKYQAT-TALVKSrdLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAFtp 726
Cdd:pfam00501  229 VVLPPGFPALD-PAALLELIERYKVTvLYGVPT--LLNMLLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF-- 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   727 spyslrPDAMCPCAGSSETGTISIRRRGNAQLGSQSGR-GIlsmsALSHCVVRV-Dtensltsltlqdagqivagavvvv 804
Cdd:pfam00501  302 ------GGALVNGYGLTETTGVVTTPLPLDEDLRSLGSvGR----PLPGTEVKIvD------------------------ 347
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811   805 taiDGSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEpvgeygkligavRYVRSGLIGFMGPDGMVFVVARR 882
Cdd:pfam00501  348 ---DETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------------GWYRTGDLGRRDEDGYLEIVGRK 410
PRK05691 PRK05691
peptide synthase; Validated
379-1026 9.51e-30

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 129.90  E-value: 9.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  379 MPRSLdsFSAFHRFGTTAAKNIAAMVLDQSAKPSTQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmckPGDRVALIY 458
Cdd:PRK05691    7 LPLTL--VQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARAS-------------FGDRAVLLF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  459 PNTQplHFLAAFYGCLQAGVIPVPVEMPSSKREAGIAQLGFLLGNCGVKVALTSESCYKGLpKKVNTSSTFSAPSgsnsl 538
Cdd:PRK05691   72 PSGP--DYVAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL-LQMEELAAANAPE----- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  539 tgtsseivdfrgwprlWWAVTEHMSKPSRDWTApPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTT--AMEY 616
Cdd:PRK05691  144 ----------------LLCVDTLDPALAEAWQE-PALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHgfGIDL 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  617 KEDETMVCVVDFKREVGLWHAILASIFNGmkvifVPYSLMKMN-----PATWMHMVSKYQATTAlvKSRDLHWALLATRd 691
Cdd:PRK05691  207 NPDDVIVSWLPLYHDMGLIGGLLQPIFSG-----VPCVLMSPAyflerPLRWLEAISEYGGTIS--GGPDFAYRLCSER- 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  692 hkdISLASLRTL-----LVA-DGANPWSLSSCDAFAAAFTPSPYSlrPDAMCPCAGSSEtGTISIRrrgnaqlGSQSGRG 765
Cdd:PRK05691  279 ---VSESALERLdlsrwRVAySGSEPIRQDSLERFAEKFAACGFD--PDSFFASYGLAE-ATLFVS-------GGRRGQG 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  766 I----LSMSALSHCVVRVDTENSLTSLTLQDAGQIVAGAVVVVTAIDGSNRlcqadeIGEICVSANSTAQLYWALDGQTH 841
Cdd:PRK05691  346 IpaleLDAEALARNRAEPGTGSVLMSCGRSQPGHAVLIVDPQSLEVLGDNR------VGEIWASGPSIAHGYWRNPEASA 419
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  842 HTFkVEPVGEygkligavRYVRSGLIGFMgPDGMVFVVARRQSLLAVSGRYHSADDIIATVlaVEPMKFVYRGRICVFST 921
Cdd:PRK05691  420 KTF-VEHDGR--------TWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTV--EREVEVVRKGRVAAFAV 487
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  922 SVLRDERIVIVAE-----QKPNCSEEeafdWITRVLRAIDTIHQVGIYCCALVPANHLPKTPLGGVHVSETKQRFENGDL 996
Cdd:PRK05691  488 NHQGEEGIGIAAEisrsvQKILPPQA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL 563
                         650       660       670
                  ....*....|....*....|....*....|
gi 808354811  997 hpstllmcphNCVLNLPKPRERQADVGPAA 1026
Cdd:PRK05691  564 ----------DSYALFPALQAVEAAQTAAS 583
PRK05691 PRK05691
peptide synthase; Validated
1049-1638 1.92e-25

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 115.65  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1049 EPSLPLLECLRSRAQSSPDHRILTLVTSKNAEQDTATCSTLLKRAERIAGLLTDRARLsrGDHVALIFPPSIDLVAAFFG 1128
Cdd:PRK05691    6 ELPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1129 CLSAGLVPVCIKPPVASDLNTTLGPIRMMVDmSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPS-SWRRKn 1207
Cdd:PRK05691   84 CLYAGVIAVPAYPPESARRHHQERLLSIIAD-AEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAeAWQEP- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1208 nnncdtttsgssgAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSS--ELYPSRHVVVCAPPYSGISLVLWC 1285
Cdd:PRK05691  162 -------------ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFgiDLNPDDVIVSWLPLYHDMGLIGGL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1286 LSSVYSGHHTTLIPPMEVEQQPSLFLTTLSNLKvrdafttySTIN--------TCVTQLA-TSVENLrergcNLSMLRsc 1356
Cdd:PRK05691  229 LQPIFSGVPCVLMSPAYFLERPLRWLEAISEYG--------GTISggpdfayrLCSERVSeSALERL-----DLSRWR-- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1357 VAIAEERP-RIALMSSFCKLFAPLALNNRAISTSFSSRVNAAICMQGASGPEPSTVYVDARALRNDRISLvGKGAPhsva 1435
Cdd:PRK05691  294 VAYSGSEPiRQDSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEP-GTGSV---- 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1436 LIESGKLLPGVKIAIANPETRGQCADSHLGEIWVA--SIHNASPLNRLASVTGFgdegtMNTDvynarlttGDTktrWAR 1513
Cdd:PRK05691  369 LMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASgpSIAHGYWRNPEASAKTF-----VEHD--------GRT---WLR 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1514 TGYLGFLRqtqsiteHGELhdavFVVGALNESLVLRGMRYHPFDVESTVSKAHRFV--GNSAVFTWNHL----VVIAAEC 1587
Cdd:PRK05691  433 TGDLGFLR-------DGEL----FVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVrkGRVAAFAVNHQgeegIGIAAEI 501
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 808354811 1588 TGSESDAL---DLVPAITSAVLEEHHLIVGVVVVVDPGSIRHGPGGEKLRSTIR 1638
Cdd:PRK05691  502 SRSVQKILppqALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACR 555
AMP-binding pfam00501
AMP-binding enzyme;
1058-1521 9.99e-25

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 108.94  E-value: 9.99e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  1058 LRSRAQSSPDHRILTlvtskNAEQDTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPV 1137
Cdd:pfam00501    1 LERQAARTPDKTALE-----VGEGRRLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  1138 CIkppvasdlNTTLGP--IRMMVDMSKAVAILApQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPSSWRRKNNNNCDTTT 1215
Cdd:pfam00501   75 PL--------NPRLPAeeLAYILEDSGAKVLIT-DDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVP 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  1216 SGSSGAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSSE----LYPSRHVVVCAPPYSGISLVLWCLSSVYS 1291
Cdd:pfam00501  146 PPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLA 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  1292 GhHTTLIPPMEVEQQPSLFLTTLSNLKVRDAFTTYSTINTCvtqlatsVENLRERGCNLSMLRSCVaIAEERPRIALMSS 1371
Cdd:pfam00501  226 G-ATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRALLSSLRLVL-SGGAPLPPELARR 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  1372 FcklfapLALNNRAISTSFSSRVNAAICMQGASGPEPSTVyvdaralrndrislvgkgaPHSValiesGKLLPGVKIAIA 1451
Cdd:pfam00501  297 F------RELFGGALVNGYGLTETTGVVTTPLPLDEDLRS-------------------LGSV-----GRPLPGTEVKIV 346
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808354811  1452 NPETRGQCADSHLGEIWVASIHNASP-LNRlasvtgfgDEGTmntdvyNARLTTGdtktRWARTGYLGFLR 1521
Cdd:pfam00501  347 DDETGEPVPPGEPGELCVRGPGVMKGyLND--------PELT------AEAFDED----GWYRTGDLGRRD 399
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
1054-1575 2.89e-16

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 83.32  E-value: 2.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1054 LLECLRSRAQSSPDHRILTlvtsknAEQDTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAG 1133
Cdd:COG0318     1 LADLLRRAAARHPDRPALV------FGGRRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1134 LVPVCikppvasdLNTTLGP--IRMMVDMSKAVAILApqnvskllkskeaahsidsnAWpMILdledapsswrrknnnnc 1211
Cdd:COG0318    74 AVVVP--------LNPRLTAeeLAYILEDSGARALVT--------------------AL-ILY----------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1212 dttTSGSSGaASKeeicyldfsinssgqlqGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYS 1291
Cdd:COG0318   108 ---TSGTTG-RPK-----------------GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLA 166
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1292 GHHTTLIPPMEveqqPSLFLTTLSNLKVrdafTTYSTINTCVTQLAtsvENLRERGCNLSMLRSCVAIAeERPRIALMSS 1371
Cdd:COG0318   167 GATLVLLPRFD----PERVLELIERERV----TVLFGVPTMLARLL---RHPEFARYDLSSLRLVVSGG-APLPPELLER 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1372 FCKLFaplalnNRAISTSF-SSRVNAAICMqgasGPEpstvyvDARALRndrislvgkgaPHSValiesGKLLPGVKIAI 1450
Cdd:COG0318   235 FEERF------GVRIVEGYgLTETSPVVTV----NPE------DPGERR-----------PGSV-----GRPLPGVEVRI 282
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1451 ANPETRgQCADSHLGEIWVASihnasplnrlASVTG--FGD-EGTmntdvyNARLTTGdtktrWARTGYLGFlrqtqsIT 1527
Cdd:COG0318   283 VDEDGR-ELPPGEVGEIVVRG----------PNVMKgyWNDpEAT------AEAFRDG-----WLRTGDLGR------LD 334
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 808354811 1528 EHGELhdavFVVGALNESLVLRGMRYHPFDVESTVSkAHRFVGNSAVF 1575
Cdd:COG0318   335 EDGYL----YIVGRKKDMIISGGENVYPAEVEEVLA-AHPGVAEAAVV 377
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
416-706 3.14e-14

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 76.92  E-value: 3.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   416 TYGKLHSRAGKVAYMLLTKtvqvnkdgsknVMCKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPV--EMPSSKREag 493
Cdd:TIGR01733    1 TYRELDERANRLARHLRAA-----------GGVGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLdpAYPAERLA-- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   494 iaqlgFLLGNCGVKVALTSESCYKGLPkkvntsstfsapsgsnsltGTSSEIVDFRgwPRLWWAVTEHMSKPSRDWTAPP 573
Cdd:TIGR01733   66 -----FILEDAGARLLLTDSALASRLA-------------------GLVLPVILLD--PLELAALDDAPAPPPPDAPSGP 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   574 rladETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWhAILASIFNGMKVIFVPY 653
Cdd:TIGR01733  120 ----DDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPE 194
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 808354811   654 SLMKMNPATWMHMVSKYQATTA-LVKSrdlHWALLAtrDHKDISLASLRTLLVA 706
Cdd:TIGR01733  195 DEERDDAALLAALIAEHPVTVLnLTPS---LLALLA--AALPPALASLRLVILG 243
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1089-1220 2.08e-07

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 55.35  E-value: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  1089 LLKRAERIAGLLTDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKP--PVASdlnttlgpIRMMVDMSKAVAI 1166
Cdd:TIGR01733    5 LDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPayPAER--------LAFILEDAGARLL 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 808354811  1167 LA-PQNVSKLLKSKEAAHSIDSNAWPMI--LDLEDAPSSWRRKNNNNCDTTTSGSSG 1220
Cdd:TIGR01733   77 LTdSALASRLAGLVLPVILLDPLELAALddAPAPPPPDAPSGPDDLAYVIYTSGSTG 133
 
Name Accession Description Interval E-value
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
1070-1651 0e+00

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 720.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1070 ILTLVTSKNAEQDTATCSTLLKRAERIAGLLTDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKPPVAS-DLN 1148
Cdd:cd05905     1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISqQLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1149 TTLGPIRMmvDMSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPSSWRRKNNNNcdtttsGSSGAASKEEIC 1228
Cdd:cd05905    81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKW------GPHPPTRDGDTA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1229 YLDFSINSSGQLQGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEVEQQPS 1308
Cdd:cd05905   153 YIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1309 LFLTTLSNLKVRDAFTTYSTINTCVTQLATSVENLRERGCNLSMLRSCVAIAEERPRIALMSSFCKLFAPLALNNRAIST 1388
Cdd:cd05905   233 LWLQTLSQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVST 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1389 SFSSRVNAAICMQGASGPEPSTVYVDARALRNDRISLVGKGAPHSVALIESGKLLPGVKIAIANPETRGQCADSHLGEIW 1468
Cdd:cd05905   313 EFGTRVNPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIW 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1469 VASIHNASPLNRLASVTGFGDEGTMNTdvynaRLTTGDTKTRWARTGYLGFLRQTQSITEHGELHDAVFVVGALNESLVL 1548
Cdd:cd05905   393 VNSPANASGYFLLDGETNDTFKVFPST-----RLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEV 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1549 RGMRYHPFDVESTVSKAHRFVGNSAVFTWNHLVVIAAECT-GSESDALDLVPAITSAVLEEHHLIVGVVVVVDPGSIRHG 1627
Cdd:cd05905   468 RGLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKN 547
                         570       580
                  ....*....|....*....|....
gi 808354811 1628 PGGEKLRSTIRSLFLEEKLNPIYV 1651
Cdd:cd05905   548 PLGEKQRMEIRQAFLAGKLHPIYV 571
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
401-1001 0e+00

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 687.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  401 AAMVLDQSAKPSTQLTYGKLHSRAGKVAYMLLTKtvqvnkdgsknVMCKPGDRVALIYPNtqPLHFLAAFYGCLQAGVIP 480
Cdd:cd05905     1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKK-----------VGLKPGDRVALMYPD--PLDFVAAFYGCLYAGVVP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  481 VPVEMPSskreaGIAQLGFLLGNCGVKVALTSESCYKGLPKKVNTSstfsapsgsnsltGTSSEIVDFRGWPRLWWAVTE 560
Cdd:cd05905    68 IPIEPPD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKLLKS-------------KTAAEIAKKKGWPKILDFVKI 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  561 HMSKPS--RDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAI 638
Cdd:cd05905   130 PKSKRSklKKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGC 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  639 LASIFNGMKVIFVPYSLMKMNPATWMHMVSKYQATTALVKSRDLHWAL------LATRDHKDISLASLRTLLVADGaNPW 712
Cdd:cd05905   210 LLSVYSGHHTILIPPELMKTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRP 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  713 SLSSCDAFAAAFTPSPYSLRpdamcpcAGSSETGTISIRRRG-NAQLGSQSGRGILSMSALSHCVVRVDTENSLTSLTLQ 791
Cdd:cd05905   289 RISSCDSFLKLFQTLGLSPR-------AVSTEFGTRVNPFICwQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQ 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  792 DAGQIVAGAVVVVTAIDGSNrLCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEPVGEYGKLIGAVRYVRSGLIGFMG 871
Cdd:cd05905   362 DSGKVLPGAQVAIVNPETKG-LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLR 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  872 P----------DGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPmkfvYRGRICVFSTSvlrdERIVIVAEQKPnCSE 941
Cdd:cd05905   441 PtkctdlnveeHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPP-GSE 511
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  942 EEAFDWITRVLRAIDTIHQVGIYCCALVPANHLPKTPLGGVHVSETKQRFENGDLHPSTL 1001
Cdd:cd05905   512 EEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
401-993 5.34e-66

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 234.44  E-value: 5.34e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  401 AAMVLDQSAKPSTQLTYGKLHSRAGKVAYMLLTKTvqvnkdgsknvmcKPGDRVALIYPntQPLHFLAAFYGCLQAGVIP 480
Cdd:cd05931    11 AYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-------------KPGDRVLLLAP--PGLDFVAAFLGCLYAGAIA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  481 VPVEMPSSKREAgiAQLGFLLGNCGVKVALTSEScykglpkkvntsstfsapsgsnSLTGTSSEIVDFRGWPRLWWAVTE 560
Cdd:cd05931    76 VPLPPPTPGRHA--ERLAAILADAGPRVVLTTAA----------------------ALAAVRAFAASRPAAGTPRLLVVD 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  561 HM-SKPSRDWTaPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAIL 639
Cdd:cd05931   132 LLpDTSAADWP-PPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLL 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  640 ASIFNGMKVIFV-PYSLMKmNPATWMHMVSKYQATTALVKSRDLHWALLATRDHK--DISLASLRTLLVadGANPWSLSS 716
Cdd:cd05931   211 TPLYSGGPSVLMsPAAFLR-RPLRWLRLISRYRATISAAPNFAYDLCVRRVRDEDleGLDLSSWRVALN--GAEPVRPAT 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  717 CDAFAAAFtpSPYSLRPDAMCPCAGSSE-TGTISIRRRGNAQLGSQSGRGILSMSALshcVVRVDTENS--LTSLTLQDA 793
Cdd:cd05931   288 LRRFAEAF--APFGFRPEAFRPSYGLAEaTLFVSGGPPGTGPVVLRVDRDALAGRAV---AVAADDPAAreLVSCGRPLP 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  794 GQivagavvvVTAI--DGSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEPVGeygkliGAVRYVRSGLIGFMG 871
Cdd:cd05931   363 DQ--------EVRIvdPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAAT------DEGGWLRTGDLGFLH 428
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  872 pDGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPMkfVYRGRICVFSTSVLRDERIVIVAEQKPNCSEEEAFDWITRV 951
Cdd:cd05931   429 -DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAI 505
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|..
gi 808354811  952 LRAIDTIHQVGIYCCALVPANHLPKTPLGGVHVSETKQRFEN 993
Cdd:cd05931   506 RAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
1061-1642 4.98e-51

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 190.14  E-value: 4.98e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1061 RAQSSPDHRILTLVTSKNAEQDTATCSTLLKRAERIAGLLtdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIK 1140
Cdd:cd05931     2 RAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARL--QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1141 PPVAsdlNTTLGPIRMMVDMSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDL--EDAPSSWRRKnnnncdtttsgs 1218
Cdd:cd05931    80 PPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLlpDTSAADWPPP------------ 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1219 sgAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLI 1298
Cdd:cd05931   145 --SPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLM 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1299 PPMEVEQQPSLFLTTLSnlKVRDAFT-----TYstiNTCVTqlATSVENLRerGCNLSMLRSCVAIAEeRPRIALMSSFC 1373
Cdd:cd05931   223 SPAAFLRRPLRWLRLIS--RYRATISaapnfAY---DLCVR--RVRDEDLE--GLDLSSWRVALNGAE-PVRPATLRRFA 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1374 KLFAPLALNNRAI--------STSFSSRvnaaicmqGASGPEPSTVYVDARALRNdRISLVGKGAPHSVALIESGKLLPG 1445
Cdd:cd05931   293 EAFAPFGFRPEAFrpsyglaeATLFVSG--------GPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPD 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1446 VKIAIANPETRGQCADSHLGEIWVASIHNASP-LNRlasvtgfgDEGTMNTdvYNARLTTGDtkTRWARTGYLGFLRQtq 1524
Cdd:cd05931   364 QEVRIVDPETGRELPDGEVGEIWVRGPSVASGyWGR--------PEATAET--FGALAATDE--GGWLRTGDLGFLHD-- 429
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1525 sitehGELhdavFVVGALNESLVLRGMRYHPFDVESTVSKAHRFV--GNSAVFTWN-----HLVVIAAECTGSESDALD- 1596
Cdd:cd05931   430 -----GEL----YITGRLKDLIIVRGRNHYPQDIEATAEEAHPALrpGCVAAFSVPddgeeRLVVVAEVERGADPADLAa 500
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*..
gi 808354811 1597 LVPAITSAVLEEHHLIVGVVVVVDPGSIRHGPGGeKL-RSTIRSLFL 1642
Cdd:cd05931   501 IAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSG-KIqRRACRAAYL 546
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
413-980 7.75e-33

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 134.17  E-value: 7.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  413 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREa 492
Cdd:COG0318    23 RRLTYAELDARARRLAAALRALGV------------GPGDRVALLLPNS--PEFVVAFLAALRAGAVVVPLNPRLTAEE- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  493 giaqLGFLLGNCGVKVALTsescykglpkkvntsstfsapsgsnsltgtsseivdfrgwprlwwavtehmskpsrdwtap 572
Cdd:COG0318    88 ----LAYILEDSGARALVT------------------------------------------------------------- 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  573 prladetiAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVV----DFkrevGLWHAILASIFNGMKV 648
Cdd:COG0318   103 --------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALplfhVF----GLTVGLLAPLLAGATL 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  649 IFVPyslmKMNPATWMHMVSKYQAT-TALVKSrdLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAFTPs 727
Cdd:COG0318   171 VLLP----RFDPERVLELIERERVTvLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFEERFGV- 241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  728 pyslrpdAMCPCAGSSETG---TISIRRRGNAQLGSQsGRgilsmsALSHCVVRVdtensltsltlqdagqivagavvvv 804
Cdd:COG0318   242 -------RIVEGYGLTETSpvvTVNPEDPGERRPGSV-GR------PLPGVEVRI------------------------- 282
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  805 taIDGSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFkvepvgeygkligAVRYVRSGLIGFMGPDGMVFVVARRQS 884
Cdd:COG0318   283 --VDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-------------RDGWLRTGDLGRLDEDGYLYIVGRKKD 347
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  885 LLAVSGRYHSADDIIATVLAVEPMKfvyrgRICVFS-TSVLRDERIV--IVAEQKPNCSEEEAFDWITRVLRAIDTIHQV 961
Cdd:COG0318   348 MIISGGENVYPAEVEEVLAAHPGVA-----EAAVVGvPDEKWGERVVafVVLRPGAELDAEELRAFLRERLARYKVPRRV 422
                         570
                  ....*....|....*....
gi 808354811  962 giyccALVPAnhLPKTPLG 980
Cdd:COG0318   423 -----EFVDE--LPRTASG 434
AMP-binding pfam00501
AMP-binding enzyme;
413-882 3.09e-31

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 128.58  E-value: 3.09e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   413 TQLTYGKLHSRAGKVAYMLLtktvqvnkdgSKNVmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVeMPSSKREA 492
Cdd:pfam00501   20 RRLTYRELDERANRLAAGLR----------ALGV--GKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPL-NPRLPAEE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   493 giaqLGFLLGNCGVKVALTSEScyKGLPKkvntsstfSAPSGSNSLTGTSSEIVDFRGWPRLWWAvtEHMSKPSRDWTAP 572
Cdd:pfam00501   85 ----LAYILEDSGAKVLITDDA--LKLEE--------LLEALGKLEVVKLVLVLDRDPVLKEEPL--PEEAKPADVPPPP 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   573 PRLAD-ETIAYIEYTTGNDGTVKGCCVT----RQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMK 647
Cdd:pfam00501  149 PPPPDpDDLAYIIYTSGTTGKPKGVMLThrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAT 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   648 VIFVPYSLMKMnPATWMHMVSKYQAT-TALVKSrdLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAFtp 726
Cdd:pfam00501  229 VVLPPGFPALD-PAALLELIERYKVTvLYGVPT--LLNMLLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF-- 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   727 spyslrPDAMCPCAGSSETGTISIRRRGNAQLGSQSGR-GIlsmsALSHCVVRV-Dtensltsltlqdagqivagavvvv 804
Cdd:pfam00501  302 ------GGALVNGYGLTETTGVVTTPLPLDEDLRSLGSvGR----PLPGTEVKIvD------------------------ 347
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811   805 taiDGSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKVEpvgeygkligavRYVRSGLIGFMGPDGMVFVVARR 882
Cdd:pfam00501  348 ---DETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------------GWYRTGDLGRRDEDGYLEIVGRK 410
PRK05691 PRK05691
peptide synthase; Validated
379-1026 9.51e-30

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 129.90  E-value: 9.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  379 MPRSLdsFSAFHRFGTTAAKNIAAMVLDQSAKPSTQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmckPGDRVALIY 458
Cdd:PRK05691    7 LPLTL--VQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARAS-------------FGDRAVLLF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  459 PNTQplHFLAAFYGCLQAGVIPVPVEMPSSKREAGIAQLGFLLGNCGVKVALTSESCYKGLpKKVNTSSTFSAPSgsnsl 538
Cdd:PRK05691   72 PSGP--DYVAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL-LQMEELAAANAPE----- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  539 tgtsseivdfrgwprlWWAVTEHMSKPSRDWTApPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTT--AMEY 616
Cdd:PRK05691  144 ----------------LLCVDTLDPALAEAWQE-PALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHgfGIDL 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  617 KEDETMVCVVDFKREVGLWHAILASIFNGmkvifVPYSLMKMN-----PATWMHMVSKYQATTAlvKSRDLHWALLATRd 691
Cdd:PRK05691  207 NPDDVIVSWLPLYHDMGLIGGLLQPIFSG-----VPCVLMSPAyflerPLRWLEAISEYGGTIS--GGPDFAYRLCSER- 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  692 hkdISLASLRTL-----LVA-DGANPWSLSSCDAFAAAFTPSPYSlrPDAMCPCAGSSEtGTISIRrrgnaqlGSQSGRG 765
Cdd:PRK05691  279 ---VSESALERLdlsrwRVAySGSEPIRQDSLERFAEKFAACGFD--PDSFFASYGLAE-ATLFVS-------GGRRGQG 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  766 I----LSMSALSHCVVRVDTENSLTSLTLQDAGQIVAGAVVVVTAIDGSNRlcqadeIGEICVSANSTAQLYWALDGQTH 841
Cdd:PRK05691  346 IpaleLDAEALARNRAEPGTGSVLMSCGRSQPGHAVLIVDPQSLEVLGDNR------VGEIWASGPSIAHGYWRNPEASA 419
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  842 HTFkVEPVGEygkligavRYVRSGLIGFMgPDGMVFVVARRQSLLAVSGRYHSADDIIATVlaVEPMKFVYRGRICVFST 921
Cdd:PRK05691  420 KTF-VEHDGR--------TWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTV--EREVEVVRKGRVAAFAV 487
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  922 SVLRDERIVIVAE-----QKPNCSEEeafdWITRVLRAIDTIHQVGIYCCALVPANHLPKTPLGGVHVSETKQRFENGDL 996
Cdd:PRK05691  488 NHQGEEGIGIAAEisrsvQKILPPQA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL 563
                         650       660       670
                  ....*....|....*....|....*....|
gi 808354811  997 hpstllmcphNCVLNLPKPRERQADVGPAA 1026
Cdd:PRK05691  564 ----------DSYALFPALQAVEAAQTAAS 583
PRK05850 PRK05850
acyl-CoA synthetase; Validated
415-982 1.14e-28

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 123.51  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  415 LTYGKLHSRAGKVAYmlltktvQVNKDGSknvmckPGDRVALIYPntQPLHFLAAFYGCLQAGVIPVPVEMPssKREAGI 494
Cdd:PRK05850   36 LTWSQLYRRTLNVAE-------ELRRHGS------TGDRAVILAP--QGLEYIVAFLGALQAGLIAVPLSVP--QGGAHD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  495 AQLGFLLGNCGVKVALTSESCYKGLPKKVNTSSTFSAPSgsnsltgtsseIV-----DFrgwprlwwavtehmskPSRDW 569
Cdd:PRK05850   99 ERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSAPP-----------VIevdllDL----------------DSPRG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  570 TAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRAL-TTAMEYKE-----DETMVCVVDFKREVGLWHAILASIF 643
Cdd:PRK05850  152 SDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLmSDYFGDTGgvpppDTTVVSWLPFYHDMGLVLGVCAPIL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  644 NGMKVIFV-PYSLMkMNPATWMHMVSKYQATTalvkSRDLHWAL-LATRDHKDISLASL---RTLLVADGA---NPWSLS 715
Cdd:PRK05850  232 GGCPAVLTsPVAFL-QRPARWMQLLASNPHAF----SAAPNFAFeLAVRKTSDDDMAGLdlgGVLGIISGServHPATLK 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  716 S-CDAFAaaftpsPYSLRPDAMCPCAG---------SSETGTISIRRR--------GNAQL-GSQSGRGILSMSALSHCV 776
Cdd:PRK05850  307 RfADRFA------PFNLRETAIRPSYGlaeatvyvaTREPGQPPESVRfdyeklsaGHAKRcETGGGTPLVSYGSPRSPT 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  777 VR-VDTEnsltsltlqdagqivagavvvvtaidgSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKvepvgeyGKL 855
Cdd:PRK05850  381 VRiVDPD---------------------------TCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFG-------ATL 426
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  856 IGAVR------YVRSGLIGFMGpDGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEpmkfvyRGRICVFSTSVLRDERI 929
Cdd:PRK05850  427 VDPSPgtpegpWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRNHYPDDIEATIQEIT------GGRVAAISVPDDGTEKL 499
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811  930 VIVAE-QKPNCSEEEAFDWITRVLR----AIDTIHQVGIYCCALVPANHLPKTPLGGV 982
Cdd:PRK05850  500 VAIIElKKRGDSDEEAMDRLRTVKRevtsAISKSHGLSVADLVLVAPGSIPITTSGKI 557
PRK05691 PRK05691
peptide synthase; Validated
1049-1638 1.92e-25

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 115.65  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1049 EPSLPLLECLRSRAQSSPDHRILTLVTSKNAEQDTATCSTLLKRAERIAGLLTDRARLsrGDHVALIFPPSIDLVAAFFG 1128
Cdd:PRK05691    6 ELPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1129 CLSAGLVPVCIKPPVASDLNTTLGPIRMMVDmSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPS-SWRRKn 1207
Cdd:PRK05691   84 CLYAGVIAVPAYPPESARRHHQERLLSIIAD-AEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAeAWQEP- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1208 nnncdtttsgssgAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSS--ELYPSRHVVVCAPPYSGISLVLWC 1285
Cdd:PRK05691  162 -------------ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFgiDLNPDDVIVSWLPLYHDMGLIGGL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1286 LSSVYSGHHTTLIPPMEVEQQPSLFLTTLSNLKvrdafttySTIN--------TCVTQLA-TSVENLrergcNLSMLRsc 1356
Cdd:PRK05691  229 LQPIFSGVPCVLMSPAYFLERPLRWLEAISEYG--------GTISggpdfayrLCSERVSeSALERL-----DLSRWR-- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1357 VAIAEERP-RIALMSSFCKLFAPLALNNRAISTSFSSRVNAAICMQGASGPEPSTVYVDARALRNDRISLvGKGAPhsva 1435
Cdd:PRK05691  294 VAYSGSEPiRQDSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEP-GTGSV---- 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1436 LIESGKLLPGVKIAIANPETRGQCADSHLGEIWVA--SIHNASPLNRLASVTGFgdegtMNTDvynarlttGDTktrWAR 1513
Cdd:PRK05691  369 LMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASgpSIAHGYWRNPEASAKTF-----VEHD--------GRT---WLR 432
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1514 TGYLGFLRqtqsiteHGELhdavFVVGALNESLVLRGMRYHPFDVESTVSKAHRFV--GNSAVFTWNHL----VVIAAEC 1587
Cdd:PRK05691  433 TGDLGFLR-------DGEL----FVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVrkGRVAAFAVNHQgeegIGIAAEI 501
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 808354811 1588 TGSESDAL---DLVPAITSAVLEEHHLIVGVVVVVDPGSIRHGPGGEKLRSTIR 1638
Cdd:PRK05691  502 SRSVQKILppqALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACR 555
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
407-994 5.19e-25

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 111.61  E-value: 5.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  407 QSAKPSTQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQplHFLAAFYGCLQAGVIPVPVEMP 486
Cdd:cd05906    32 DADGSEEFQSYQDLLEDARRLAAGLRQLGL------------RPGDSVILQFDDNE--DFIPAFWACVLAGFVPAPLTVP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  487 S-----SKREAGIAQLGFLLGNCgvkVALTSEscykglpkkvntsstfsapsgsnSLTGTSSEIVDFRGWPRLWWAVTEH 561
Cdd:cd05906    98 PtydepNARLRKLRHIWQLLGSP---VVLTDA-----------------------ELVAEFAGLETLSGLPGIRVLSIEE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  562 MSKPSRDWTAPPRLADeTIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILAS 641
Cdd:cd05906   152 LLDTAADHDLPQSRPD-DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  642 IFNGMKVIFVPYSLMKMNPATWMHMVSKYQATT------ALVKSRDlhwaLLATRDHKDISLASLRTLLVADGANpwSLS 715
Cdd:cd05906   231 VYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLND----LLEEIEDGTWDLSSLRYLVNAGEAV--VAK 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  716 SCDAFAAAFtpSPYSLRPDAMCPCAGSSETGTISIRrrgNAQLGSQSGRGILSMSALSHCV----VR-VDTENSLTSltl 790
Cdd:cd05906   305 TIRRLLRLL--EPYGLPPDAIRPAFGMTETCSGVIY---SRSFPTYDHSQALEFVSLGRPIpgvsMRiVDDEGQLLP--- 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  791 qdagqivagavvvvtaidgsnrlcqADEIGEICVSANSTAQLYWALDGQTHHTFKvepvgEYGkligavrYVRSGLIGFM 870
Cdd:cd05906   377 -------------------------EGEVGRLQVRGPVVTKGYYNNPEANAEAFT-----EDG-------WFRTGDLGFL 419
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  871 GpDGMVFVVARRQSLLAVSGRYHSADDIIAtvlAVEPMKFVYRGRICVFSTsvlRD-----ERIVIVAeqkpnCSEEEAF 945
Cdd:cd05906   420 D-NGNLTITGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAV---RDpgaetEELAIFF-----VPEYDLQ 487
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 808354811  946 DWITRVLRAIDTI--HQVGIYCCALVPANH--LPKTPLGGVHVSETKQRFENG 994
Cdd:cd05906   488 DALSETLRAIRSVvsREVGVSPAYLIPLPKeeIPKTSLGKIQRSKLKAAFEAG 540
AMP-binding pfam00501
AMP-binding enzyme;
1058-1521 9.99e-25

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 108.94  E-value: 9.99e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  1058 LRSRAQSSPDHRILTlvtskNAEQDTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPV 1137
Cdd:pfam00501    1 LERQAARTPDKTALE-----VGEGRRLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  1138 CIkppvasdlNTTLGP--IRMMVDMSKAVAILApQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPSSWRRKNNNNCDTTT 1215
Cdd:pfam00501   75 PL--------NPRLPAeeLAYILEDSGAKVLIT-DDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVP 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  1216 SGSSGAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSSE----LYPSRHVVVCAPPYSGISLVLWCLSSVYS 1291
Cdd:pfam00501  146 PPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLA 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  1292 GhHTTLIPPMEVEQQPSLFLTTLSNLKVRDAFTTYSTINTCvtqlatsVENLRERGCNLSMLRSCVaIAEERPRIALMSS 1371
Cdd:pfam00501  226 G-ATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRALLSSLRLVL-SGGAPLPPELARR 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  1372 FcklfapLALNNRAISTSFSSRVNAAICMQGASGPEPSTVyvdaralrndrislvgkgaPHSValiesGKLLPGVKIAIA 1451
Cdd:pfam00501  297 F------RELFGGALVNGYGLTETTGVVTTPLPLDEDLRS-------------------LGSV-----GRPLPGTEVKIV 346
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808354811  1452 NPETRGQCADSHLGEIWVASIHNASP-LNRlasvtgfgDEGTmntdvyNARLTTGdtktRWARTGYLGFLR 1521
Cdd:pfam00501  347 DDETGEPVPPGEPGELCVRGPGVMKGyLND--------PELT------AEAFDED----GWYRTGDLGRRD 399
PRK09192 PRK09192
fatty acyl-AMP ligase;
414-1001 1.11e-24

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 110.87  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  414 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIyPNTQPlHFLAAFYGCLQAGVIPVPVEMPSS--KRE 491
Cdd:PRK09192   49 ALPYQTLRARAEAGARRLLALGL------------KPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPMGfgGRE 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  492 AGIAQLGFLLGNCGVKVALtsescykglpkkvntsstfsAPSGSNSLTgtsSEIVDFRgwpRLWWAVT--EHMSKPSRDW 569
Cdd:PRK09192  115 SYIAQLRGMLASAQPAAII--------------------TPDELLPWV---NEATHGN---PLLHVLShaWFKALPEADV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  570 TAPPRLADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALT-TAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKV 648
Cdd:PRK09192  169 ALPRPTPDD-IAYLQYSSGSTRFPRGVIITHRALMANLRAIShDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  649 IFVPYSLMKMNPATWMHMVSKYQATTALvkSRDLHWALLATR----DHKDISLASLRtlLVADGANPWSLSSCDAFAAAF 724
Cdd:PRK09192  248 DYLPTRDFARRPLQWLDLISRNRGTISY--SPPFGYELCARRvnskDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAF 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  725 TPSPYSlrPDAMCPCAGSSE-TGTISIrrrgnaqlgSQSGRGI----LSMSALSHCVVRVDT-ENSLTSLTLQDAGQIVA 798
Cdd:PRK09192  324 APAGFD--DKAFMPSYGLAEaTLAVSF---------SPLGSGIvveeVDRDRLEYQGKAVAPgAETRRVRTFVNCGKALP 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  799 GAVVVVTAIDGS---NRlcqadEIGEICVSANSTAQLYWALDgqthhtfkvepvgEYGKLIGAVRYVRSGLIGFMGpDGM 875
Cdd:PRK09192  393 GHEIEIRNEAGMplpER-----VVGHICVRGPSLMSGYFRDE-------------ESQDVLAADGWLDTGDLGYLL-DGY 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  876 VFVVARRQSLLAVSGRYHSADDIiatVLAVEPMKFVYRGRICVFSTSVLRDERIVIVAEQKPNCSEEEA--FDWITRVLR 953
Cdd:PRK09192  454 LYITGRAKDLIIINGRNIWPQDI---EWIAEQEPELRSGDAAAFSIAQENGEKIVLLVQCRISDEERRGqlIHALAALVR 530
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 808354811  954 AIDTIHQVgiycCALVPANHLPKTPLGGVHVSETKQRFENGDLHPSTL 1001
Cdd:PRK09192  531 SEFGVEAA----VELVPPHSLPRTSSGKLSRAKAKKRYLSGAFASLDV 574
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
449-996 5.73e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 109.05  E-value: 5.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  449 KPGDRVALIYPntQPLHFLAAFYGCLQAGVIPVPVEMPSskrEAG-IAQLGFLLGNCGVKVALTSESCYKGLPKKVNTSS 527
Cdd:PRK07769   77 KPGDRVAILAP--QNLDYLIAFFGALYAGRIAVPLFDPA---EPGhVGRLHAVLDDCTPSAILTTTDSAEGVRKFFRARP 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  528 TFSAPsgsnsltgtssEIVDFRGWPRlwwAVTEhmskpsrDWTaPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHC 607
Cdd:PRK07769  152 AKERP-----------RVIAVDAVPD---EVGA-------TWV-PPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNV 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  608 RALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPYSLMKmNPATWMHMVSKYQATTALVKSRDLHWA-- 685
Cdd:PRK07769  210 LQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVR-RPGRWIRELARKPGGTGGTFSAAPNFAfe 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  686 LLATR-----DHKDISLASLRTLLvaDGANPWSLSSCDAFAAAFtpSPYSLRPDAMCPCAGSSE-TGTISIRRRGNAQLG 759
Cdd:PRK07769  289 HAAARglpkdGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAF--APYGLPPTAIKPSYGMAEaTLFVSTTPMDEEPTV 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  760 SQSGRGILSmsalSHCVVRV--DTENSLTSLTlqdAGQIVAGAVVVVtaIDGSNRLCQAD-EIGEICVSANSTAQLYWAL 836
Cdd:PRK07769  365 IYVDRDELN----AGRFVEVpaDAPNAVAQVS---AGKVGVSEWAVI--VDPETASELPDgQIGEIWLHGNNIGTGYWGK 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  837 DGQTHHTFK------VEPVGEYGKLIGAvRYVRSGLIGFMgPDGMVFVVARRQSLLAVSGRYHSADDIIATvlAVEPMKF 910
Cdd:PRK07769  436 PEETAATFQnilksrLSESHAEGAPDDA-LWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLEYT--AQEATKA 511
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  911 VYRGRICVFS---------------TSVLRD-----ERIVIVAEQKPNCSEEEAFDWITRVLRAIDTIHQVGIYCCALVP 970
Cdd:PRK07769  512 LRTGYVAAFSvpanqlpqvvfddshAGLKFDpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVP 591
                         570       580
                  ....*....|....*....|....*.
gi 808354811  971 ANHLPKTPLGGVHVSETKQRFENGDL 996
Cdd:PRK07769  592 AGSIPRTSSGKIARRACRAAYLDGSL 617
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
1054-1648 7.25e-20

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 95.96  E-value: 7.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1054 LLECLRSRAQSSPDHRILTLVTSKNAEQDTATCSTLLKRAERIAGLLTDRARlsRGDHVALIFPPSIDLVAAFFGCLSAG 1133
Cdd:PRK12476   39 LIERNIANVGDTVAYRYLDHSHSAAGCAVELTWTQLGVRLRAVGARLQQVAG--PGDRVAILAPQGIDYVAGFFAAIKAG 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1134 LVPVCIKPPV----ASDLNTTLGPIRMMVDMSKAVAilaPQNVSKLLKSKEAAHSidsnawPMILDLEDAPSSwrrknnn 1209
Cdd:PRK12476  117 TIAVPLFAPElpghAERLDTALRDAEPTVVLTTTAA---AEAVEGFLRNLPRLRR------PRVIAIDAIPDS------- 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1210 ncdtttSGSSGAASK---EEICYLDFSINSSGQLQGSSMSEASAIT-VCKSIKVSSELYPSRHVVVCAPPYSGISLVLWC 1285
Cdd:PRK12476  181 ------AGESFVPVEldtDDVSHLQYTSGSTRPPVGVEITHRAVGTnLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIG 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1286 LSSVYSGHhTTLIPPMEVEQQPSLFLTTLSnlkvrdAFTTYSTINTCVTQLA---TSVENLRERGCNLSMLRSCVAIAEE 1362
Cdd:PRK12476  255 FPAVYGGH-STLMSPTAFVRRPQRWIKALS------EGSRTGRVVTAAPNFAyewAAQRGLPAEGDDIDLSNVVLIIGSE 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1363 RPRIALMSSFCKLFAPLALNNRAISTSFSSRVNAAICMQGASGPEPSTVYVDARALRNDRISLVGKGAPHSVALIESGKL 1442
Cdd:PRK12476  328 PVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQV 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1443 LPGVKIAIANPETRGQCADSHLGEIWVASihnasplNRLASvtGFGDEGTMNTDVYNARLTT----------GDTKTRWA 1512
Cdd:PRK12476  408 ARSQWAVIVDPDTGAELPDGEVGEIWLHG-------DNIGR--GYWGRPEETERTFGAKLQSrlaegshadgAADDGTWL 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1513 RTGYLGFLRQtqsitehGELhdavFVVGALNESLVLRGMRYHPFDVESTVSKAHRFV--GNSAVFT-----WNHLVVIAA 1585
Cdd:PRK12476  479 RTGDLGVYLD-------GEL----YITGRIADLIVIDGRNHYPQDIEATVAEASPMVrrGYVTAFTvpaedNERLVIVAE 547
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808354811 1586 ECTG-SESDALDLVPAITSAVLEEHHLIVGVVVVVDPGSIRHGPGGEKLRSTIRSLFLEEKLNP 1648
Cdd:PRK12476  548 RAAGtSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
449-994 7.73e-19

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 91.78  E-value: 7.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  449 KPGDRValIYPNTQPLHFLAAFYGCLQAGVIPVPVEMPSSkreagiaqlgfllgncgvkvaltsESCYKGLPKKVNTSSt 528
Cdd:cd05908    38 KPGQEV--VFQITHNNKFLYLFWACLLGGMIAVPVSIGSN------------------------EEHKLKLNKVWNTLK- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  529 fsapsgsNSLTGTSSEIVDfrgwprlwwavtehmskpsrdwtappRLADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHCR 608
Cdd:cd05908    91 -------NPYLITEEEVLC--------------------------ELADE-LAFIQFSSGSTGDPKGVMLTHENLVHNMF 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  609 ALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPYSLMKMNPATWMHMVSKYQATtaLVKSRDLHWALLA 688
Cdd:cd05908   137 AILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKAT--IVSSPNFGYKYFL 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  689 TR--DHK--DISLASLRtlLVADGANPWSLSSCDAFAAAFtpSPYSLRPDAMCPCAGSSE-------------TGTISIR 751
Cdd:cd05908   215 KTlkPEKanDWDLSSIR--MILNGAEPIDYELCHEFLDHM--SKYGLKRNAILPVYGLAEasvgaslpkaqspFKTITLG 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  752 RRgnaqlGSQSGRGIlsmsalshcvVRVDTENSlTSLTLQDAGQivAGAVVVVTAIDGSNRLCQADEIGEICVSANSTAQ 831
Cdd:cd05908   291 RR-----HVTHGEPE----------PEVDKKDS-ECLTFVEVGK--PIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  832 LYWAldgqthhtfkvEPVgEYGKLIGAVRYVRSGLIGFMgPDGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPmkfV 911
Cdd:cd05908   353 GYYN-----------NPE-ATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEG---V 416
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  912 YRGR--ICVFSTSVLRDERIVIVAEQKPncSEEEAFDWITRVLRAID-----TIHQVgiyccalVPANHLPKTPLGGVHV 984
Cdd:cd05908   417 ELGRvvACGVNNSNTRNEEIFCFIEHRK--SEDDFYPLGKKIKKHLNkrggwQINEV-------LPIRRIPKTTSGKVKR 487
                         570
                  ....*....|
gi 808354811  985 SETKQRFENG 994
Cdd:cd05908   488 YELAQRYQSG 497
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
579-982 2.68e-18

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 88.11  E-value: 2.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  579 TIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKrEVGLWHAILASIFNGMKVIFVPYSlmkm 658
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLF-HIGGLFGLLGALLAGGTVVLLPKF---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  659 NPATWMHMVSKYQATTALVkSRDLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAFTPSPYSlrpdamcp 738
Cdd:cd04433    76 DPEAALELIEREKVTILLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAPGIKLVN-------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  739 CAGSSETG--TISIRRRGNAQLGSQSGRgilsmsALSHCVVRVdtensltsltlqdagqivagavvvvtaIDGSNRLCQA 816
Cdd:cd04433   145 GYGLTETGgtVATGPPDDDARKPGSVGR------PVPGVEVRI---------------------------VDPDGGELPP 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  817 DEIGEICVSANSTAQLYWALDGQTHHTFKvepvgeygklIGavrYVRSGLIGFMGPDGMVFVVARRQSLLAVSGRYHSAD 896
Cdd:cd04433   192 GEIGELVVRGPSVMKGYWNNPEATAAVDE----------DG---WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPA 258
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  897 DIIATVLAVEPMKfvyrgRICVFstsVLRDER------IVIVAEQKPNCSEEEAFDWITRVLRAIDTIHQVgiyccalVP 970
Cdd:cd04433   259 EVEAVLLGHPGVA-----EAAVV---GVPDPEwgervvAVVVLRPGADLDAEELRAHVRERLAPYKVPRRV-------VF 323
                         410
                  ....*....|..
gi 808354811  971 ANHLPKTPLGGV 982
Cdd:cd04433   324 VDALPRTASGKI 335
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
449-980 3.62e-18

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 90.57  E-value: 3.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  449 KPGDRVALIYPntQPLHFLAAFYGCLQAGVIPVPVEMPSSKREAgiAQLGFLLGNCGVKVALTsescykglpkkvntsst 528
Cdd:PRK12476   90 GPGDRVAILAP--QGIDYVAGFFAAIKAGTIAVPLFAPELPGHA--ERLDTALRDAEPTVVLT----------------- 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  529 fsapsgsnslTGTSSEIVD--FRGWPRL----WWAVTEHMSKPSRDWTAPPrLADETIAYIEYTTGNDGTVKGCCVTRQA 602
Cdd:PRK12476  149 ----------TTAAAEAVEgfLRNLPRLrrprVIAIDAIPDSAGESFVPVE-LDTDDVSHLQYTSGSTRPPVGVEITHRA 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  603 VFAHCRALTTAMEYKEDETM-VCVVDFKREVGLWHAILASIFNGMKVIFVPYSLMKmNPATWMHMVSKYQATTALVKSR- 680
Cdd:PRK12476  218 VGTNLVQMILSIDLLDRNTHgVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVR-RPQRWIKALSEGSRTGRVVTAAp 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  681 DLHWALLATR----DHKDISLaslRTLLVADGANPWSLSSCDAFAAAFtpSPYSLRPDAMCPCAG-------------SS 743
Cdd:PRK12476  297 NFAYEWAAQRglpaEGDDIDL---SNVVLIIGSEPVSIDAVTTFNKAF--APYGLPRTAFKPSYGiaeatlfvatiapDA 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  744 ETGTISIRRRgnaQLGSqsGRGILSMSALSHCVVRVDtensltsltlqdAGQIVAGAVVVVTAIDGSNRLcQADEIGEIC 823
Cdd:PRK12476  372 EPSVVYLDRE---QLGA--GRAVRVAADAPNAVAHVS------------CGQVARSQWAVIVDPDTGAEL-PDGEVGEIW 433
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  824 VSANSTAQLYWALDGQTHHTFKVE-----PVGEY--GKLIGAvRYVRSGLIGFMgPDGMVFVVARRQSLLAVSGRYHSAD 896
Cdd:PRK12476  434 LHGDNIGRGYWGRPEETERTFGAKlqsrlAEGSHadGAADDG-TWLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQ 511
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  897 DIIATVLAVEPMkfVYRGRICVFSTSVLRDERIVIVAEQKPNCSEEEAFDWITRVLRAIDTIHQVGIYCCALVPANHLPK 976
Cdd:PRK12476  512 DIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPR 589

                  ....
gi 808354811  977 TPLG 980
Cdd:PRK12476  590 TTSG 593
PRK05850 PRK05850
acyl-CoA synthetase; Validated
1051-1624 1.23e-17

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 88.46  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1051 SLPLLecLRSRAQSSPDHRILTLVtskNAEQDTA------TCSTLLKRAERIAGLLtdRARLSRGDHVALIFPPSIDLVA 1124
Cdd:PRK05850    2 SVPSL--LRERASLQPDDAAFTFI---DYEQDPAgvaetlTWSQLYRRTLNVAEEL--RRHGSTGDRAVILAPQGLEYIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1125 AFFGCLSAGLVPVCIKPPV--ASDLNTTLgpirMMVDmSKAVAILAPQNVSKLLKSKEAAHSIDSNAWPMILDLEDAPSS 1202
Cdd:PRK05850   75 AFLGALQAGLIAVPLSVPQggAHDERVSA----VLRD-TSPSVVLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLDLDSP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1203 wrrknnNNCDtttsgsSGAASKEEICYLDFSINSSGQLQGSSMSEASAITVCKSI---------KVSSelyPSRHVVVCA 1273
Cdd:PRK05850  150 ------RGSD------ARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLmsdyfgdtgGVPP---PDTTVVSWL 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1274 PPYSGISLVLWCLSSVYSGHHTTLIPPMEVEQQPSLFLTTLSnlKVRDAFTTYSTIntcVTQLA---TSVENLRerGCNL 1350
Cdd:PRK05850  215 PFYHDMGLVLGVCAPILGGCPAVLTSPVAFLQRPARWMQLLA--SNPHAFSAAPNF---AFELAvrkTSDDDMA--GLDL 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1351 SMLRSCVAIAEeRPRIALMSSFCKLFAPLALNNRAISTSF---SSRVNAAIcmqGASGPEPSTVYVDARALRNDRI---- 1423
Cdd:PRK05850  288 GGVLGIISGSE-RVHPATLKRFADRFAPFNLRETAIRPSYglaEATVYVAT---REPGQPPESVRFDYEKLSAGHAkrce 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1424 -----SLVGKGAPHSvaliesgkllPGVKIAiaNPETRGQCADSHLGEIWVASIHNASplnrlasvtGF--GDEGTMNTd 1496
Cdd:PRK05850  364 tgggtPLVSYGSPRS----------PTVRIV--DPDTCIECPAGTVGEIWVHGDNVAA---------GYwqKPEETERT- 421
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1497 vYNARLTT---GDTKTRWARTGYLGFlrqtqsITEhGELhdavFVVGALNESLVLRGMRYHPFDVESTVSKAHRfvGNSA 1573
Cdd:PRK05850  422 -FGATLVDpspGTPEGPWLRTGDLGF------ISE-GEL----FIVGRIKDLLIVDGRNHYPDDIEATIQEITG--GRVA 487
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354811 1574 VFT-----WNHLVVIA--AECTGSESDALDLVPA----ITSAVLEEHHLIVGVVVVVDPGSI 1624
Cdd:PRK05850  488 AISvpddgTEKLVAIIelKKRGDSDEEAMDRLRTvkreVTSAISKSHGLSVADLVLVAPGSI 549
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
1104-1652 3.81e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 87.48  E-value: 3.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1104 ARL----SRGDHVALIFPPSIDLVAAFFGCLSAGLVPVcikPPVASDLNTTLGPIRMMVDMSKAVAIL----APQNVSKL 1175
Cdd:PRK07769   70 ARLqqvtKPGDRVAILAPQNLDYLIAFFGALYAGRIAV---PLFDPAEPGHVGRLHAVLDDCTPSAILtttdSAEGVRKF 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1176 LKSKEAAHSidsnawPMILDLEDAP----SSWRRKNNNNCDTT----TSGSSGAASKEEICYLDFSINssgqlqgssmse 1247
Cdd:PRK07769  147 FRARPAKER------PRVIAVDAVPdevgATWVPPEANEDTIAylqyTSGSTRIPAGVQITHLNLPTN------------ 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1248 asAITVCKSIkvssELYPSRHVVVCAPPYSGISLVLWCLSSVySGHHTTLIPPMEVEQQPSLFLTTLSNlKVRDAFTTYS 1327
Cdd:PRK07769  209 --VLQVIDAL----EGQEGDRGVSWLPFFHDMGLITVLLPAL-LGHYITFMSPAAFVRRPGRWIRELAR-KPGGTGGTFS 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1328 TINTCVTQLATS--VENLRERGCNLSMLRSCVAiAEERPRIALMSSFCKLFAPLALNNRAISTSFSSrvnAAICMQGASG 1405
Cdd:PRK07769  281 AAPNFAFEHAAArgLPKDGEPPLDLSNVKGLLN-GSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGM---AEATLFVSTT 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1406 P---EPSTVYVDARALRNDRISLVGKGAPHSVALIESGKLLPGVKIAIANPETRGQCADSHLGEIWVASIHNASPLNRLA 1482
Cdd:PRK07769  357 PmdeEPTVIYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKP 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1483 SVTGFGDEGTMNTDVYNARLTTGDTKTRWARTGYLGflrqtqsITEHGELhdavFVVGALNESLVLRGMRYHPFDVESTV 1562
Cdd:PRK07769  437 EETAATFQNILKSRLSESHAEGAPDDALWVRTGDYG-------VYFDGEL----YITGRVKDLVIIDGRNHYPQDLEYTA 505
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1563 ---SKAHR--FVG---------NSAVFTWNH-------------LVVIAAECTGS-ESDALDLVPAITSAVLEEHHLIVG 1614
Cdd:PRK07769  506 qeaTKALRtgYVAafsvpanqlPQVVFDDSHaglkfdpedtseqLVIVAERAPGAhKLDPQPIADDIRAAIAVRHGVTVR 585
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 808354811 1615 VVVVVDPGSIRHGPGGEKLRSTIRSLFLEEKLNPIYVA 1652
Cdd:PRK07769  586 DVLLVPAGSIPRTSSGKIARRACRAAYLDGSLRSGYGQ 623
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
408-890 2.38e-16

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 84.19  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  408 SAKPSTQLTYGKLHSRAGKVAYMLltktvqvNKDGSKnvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPS 487
Cdd:cd05911     4 DADTGKELTYAQLRTLSRRLAAGL-------RKLGLK-----KGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAANPIY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  488 SKREagiaqLGFLLGNCGVKVALTSESCYKglpkKVNTSSTFSAPSGSNSLTGTSSEIVDFRGwpRLWWAVTEhmskpSR 567
Cdd:cd05911    70 TADE-----LAHQLKISKPKVIFTDPDGLE----KVKEAAKELGPKDKIIVLDDKPDGVLSIE--DLLSPTLG-----EE 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  568 DWTAPPRL--ADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCR--ALTTAMEYKEDETMVCVVDFKREVGLWhAILASIF 643
Cdd:cd05911   134 DEDLPPPLkdGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSqvQTFLYGNDGSNDVILGFLPLYHIYGLF-TTLASLL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  644 NGMKVIFVPyslmKMNPATWMHMVSKYQATTALVKSRdlHWALLATR-DHKDISLASLRTLLVadGANPWSLSSCDAFAA 722
Cdd:cd05911   213 NGATVIIMP----KFDSELFLDLIEKYKITFLYLVPP--IAAALAKSpLLDKYDLSSLRVILS--GGAPLSKELQELLAK 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  723 aftpspysLRPDAMCPCA-GSSETG-TISIRRRGNAQLGSqSGRGILSMSALshcVVRVDTENSLTSltlqdagqivaga 800
Cdd:cd05911   285 --------RFPNATIKQGyGMTETGgILTVNPDGDDKPGS-VGRLLPNVEAK---IVDDDGKDSLGP------------- 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  801 vvvvtaidgsnrlcqaDEIGEICVSANSTAQLYWALDGQTHHTFKVEpvgeygkligavRYVRSGLIGFMGPDGMVFVVA 880
Cdd:cd05911   340 ----------------NEPGEICVRGPQVMKGYYNNPEATKETFDED------------GWLHTGDIGYFDEDGYLYIVD 391
                         490
                  ....*....|
gi 808354811  881 RRQSLLAVSG 890
Cdd:cd05911   392 RKKELIKYKG 401
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
1054-1575 2.89e-16

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 83.32  E-value: 2.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1054 LLECLRSRAQSSPDHRILTlvtsknAEQDTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAG 1133
Cdd:COG0318     1 LADLLRRAAARHPDRPALV------FGGRRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1134 LVPVCikppvasdLNTTLGP--IRMMVDMSKAVAILApqnvskllkskeaahsidsnAWpMILdledapsswrrknnnnc 1211
Cdd:COG0318    74 AVVVP--------LNPRLTAeeLAYILEDSGARALVT--------------------AL-ILY----------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1212 dttTSGSSGaASKeeicyldfsinssgqlqGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYS 1291
Cdd:COG0318   108 ---TSGTTG-RPK-----------------GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLA 166
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1292 GHHTTLIPPMEveqqPSLFLTTLSNLKVrdafTTYSTINTCVTQLAtsvENLRERGCNLSMLRSCVAIAeERPRIALMSS 1371
Cdd:COG0318   167 GATLVLLPRFD----PERVLELIERERV----TVLFGVPTMLARLL---RHPEFARYDLSSLRLVVSGG-APLPPELLER 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1372 FCKLFaplalnNRAISTSF-SSRVNAAICMqgasGPEpstvyvDARALRndrislvgkgaPHSValiesGKLLPGVKIAI 1450
Cdd:COG0318   235 FEERF------GVRIVEGYgLTETSPVVTV----NPE------DPGERR-----------PGSV-----GRPLPGVEVRI 282
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1451 ANPETRgQCADSHLGEIWVASihnasplnrlASVTG--FGD-EGTmntdvyNARLTTGdtktrWARTGYLGFlrqtqsIT 1527
Cdd:COG0318   283 VDEDGR-ELPPGEVGEIVVRG----------PNVMKgyWNDpEAT------AEAFRDG-----WLRTGDLGR------LD 334
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 808354811 1528 EHGELhdavFVVGALNESLVLRGMRYHPFDVESTVSkAHRFVGNSAVF 1575
Cdd:COG0318   335 EDGYL----YIVGRKKDMIISGGENVYPAEVEEVLA-AHPGVAEAAVV 377
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
412-706 1.26e-15

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 82.08  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  412 STQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVeMPSSKRE 491
Cdd:COG0365    37 ERTLTYAELRREVNRFANALRALGV------------KKGDRVAIYLPNI--PEAVIAMLACARIGAVHSPV-FPGFGAE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  492 AgiaqLGFLLGNCGVKVALTSESCYKGlPKKVNTSSTFS-APSGSNSLT-----GTSSEIVDFRGWprLWWAvtEHMSKP 565
Cdd:COG0365   102 A----LADRIEDAEAKVLITADGGLRG-GKVIDLKEKVDeALEELPSLEhvivvGRTGADVPMEGD--LDWD--ELLAAA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  566 SRDWTAPPRLADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHcrALTTAM---EYKEDETMVCVVDFKREVGLWHAILASI 642
Cdd:COG0365   173 SAEFEPEPTDADD-PLFILYTSGTTGKPKGVVHTHGGYLVH--AATTAKyvlDLKPGDVFWCTADIGWATGHSYIVYGPL 249
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354811  643 FNGMKVIFVPYSLMKMNPATWMHMVSKYQAT------TALvksRdlhwALLATRDH--KDISLASLRTLLVA 706
Cdd:COG0365   250 LNGATVVLYEGRPDFPDPGRLWELIEKYGVTvfftapTAI---R----ALMKAGDEplKKYDLSSLRLLGSA 314
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
402-890 2.96e-15

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 80.30  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  402 AMVLDQSA-----KPSTQ-----LTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFY 471
Cdd:cd05936     2 ADLLEEAArrfpdKTALIfmgrkLTYRELDALAEAFAAGLQNLGVQ------------PGDRVALMLPNC--PQFPIAYF 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  472 GCLQAGVIPVPVEMPSSKREagiaqLGFLLGNCGVKValtsescykglpkkvntsstfsapsgsnsltgtsseIVDFRGW 551
Cdd:cd05936    68 GALKAGAVVVPLNPLYTPRE-----LEHILNDSGAKA------------------------------------LIVAVSF 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  552 prlwwavtEHMSKPSRDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAH---CRALTTAMEyKEDETMVCVVDF 628
Cdd:cd05936   107 --------TDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANalqIKAWLEDLL-EGDDVVLAALPL 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  629 KREVGLWHAILASIFNGMKVIFVPyslmKMNPATWMHMVSKYQATT-ALVKSrdLHWALLATRDHKDISLASLRtlLVAD 707
Cdd:cd05936   178 FHVFGLTVALLLPLALGATIVLIP----RFRPIGVLKEIRKHRVTIfPGVPT--MYIALLNAPEFKKRDFSSLR--LCIS 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  708 GANPWSLSSCDAFAAAF-TP----------SPYSlrpdAMCPCAGSSETGTIsirrrgnaqlgsqsGRGILSMSALshcV 776
Cdd:cd05936   250 GGAPLPVEVAERFEELTgVPivegygltetSPVV----AVNPLDGPRKPGSI--------------GIPLPGTEVK---I 308
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  777 VRVDTEnsltslTLQDagqivagavvvvtaidgsnrlcqaDEIGEICVSANSTAQLYWALDGQTHHTFKVEpvgeygkli 856
Cdd:cd05936   309 VDDDGE------ELPP------------------------GEVGELWVRGPQVMKGYWNRPEETAEAFVDG--------- 349
                         490       500       510
                  ....*....|....*....|....*....|....
gi 808354811  857 gavrYVRSGLIGFMGPDGMVFVVARRQSLLAVSG 890
Cdd:cd05936   350 ----WLRTGDIGYMDEDGYFFIVDRKKDMIIVGG 379
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
412-701 5.97e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 79.95  E-value: 5.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  412 STQLTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKRE 491
Cdd:PRK07656   28 DQRLTYAELNARVRRAAAALAALGIG------------KGDRVAIWAPNS--PHWVIAALGALKAGAVVVPLNTRYTADE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  492 AgiaqlGFLLGNCGVKVAL-------TSESCYKGLPK-KVNTSSTFSAPSGSNSLTGTSSEIVdfrgwprlwwavtehmS 563
Cdd:PRK07656   94 A-----AYILARGDAKALFvlglflgVDYSATTRLPAlEHVVICETEEDDPHTEKMKTFTDFL----------------A 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  564 KPSRDWTAPPrLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIF 643
Cdd:PRK07656  153 AGDPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLM 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811  644 NGMKVIFVPyslmKMNPATWMHMVSKYQATTaLVKSRDLHWALLATRDHKDISLASLR 701
Cdd:PRK07656  232 RGATILPLP----VFDPDEVFRLIETERITV-LPGPPTMYNSLLQHPDRSAEDLSSLR 284
PRK09192 PRK09192
fatty acyl-AMP ligase;
1087-1609 1.59e-14

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 78.51  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1087 STLLKRAERIAGLLTdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVcikpPVAsdLNTTLG-------PIRMMVD 1159
Cdd:PRK09192   53 QTLRARAEAGARRLL-ALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPV----PLP--LPMGFGgresyiaQLRGMLA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1160 MSKAVAILAPQNVSKLLksKEAAHSID-----SNAWpmiLDLEDAPsswrrknnnNCDTTTsgssgaASKEEICYLDFSI 1234
Cdd:PRK09192  126 SAQPAAIITPDELLPWV--NEATHGNPllhvlSHAW---FKALPEA---------DVALPR------PTPDDIAYLQYSS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1235 NSS----GQL--QGSSMSEASAITvCKSIKVsselYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEVEQQPS 1308
Cdd:PRK09192  186 GSTrfprGVIitHRALMANLRAIS-HDGLKV----RPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPL 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1309 LFLTTLSnlkvRDAFT-TYST---INTCvtqlATSVENLRERGCNLSMLRScVAIAEERPRIALMSSFCKLFAPLALNNR 1384
Cdd:PRK09192  261 QWLDLIS----RNRGTiSYSPpfgYELC----ARRVNSKDLAELDLSCWRV-AGIGADMIRPDVLHQFAEAFAPAGFDDK 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1385 AISTSFSSRVNA-AICM----QGAsgpepSTVYVDARALRNDRISLVGKGAPHSV-ALIESGKLLPGVKIAIANpETRGQ 1458
Cdd:PRK09192  332 AFMPSYGLAEATlAVSFsplgSGI-----VVEEVDRDRLEYQGKAVAPGAETRRVrTFVNCGKALPGHEIEIRN-EAGMP 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1459 CADSHLGEIWVA--SIHNASplnrlasvtgFGDEGTmnTDVYNArlttgdtkTRWARTGYLGFLrqtqsitEHGELhdav 1536
Cdd:PRK09192  406 LPERVVGHICVRgpSLMSGY----------FRDEES--QDVLAA--------DGWLDTGDLGYL-------LDGYL---- 454
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808354811 1537 FVVGALNESLVLRGMRYHPFDVESTVSKAHRF-VGNSAVF---TWNH-LVVIAAECTGSESDA-LDLVPAITSAVLEEH 1609
Cdd:PRK09192  455 YITGRAKDLIIINGRNIWPQDIEWIAEQEPELrSGDAAAFsiaQENGeKIVLLVQCRISDEERrGQLIHALAALVRSEF 533
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
416-706 3.14e-14

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 76.92  E-value: 3.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   416 TYGKLHSRAGKVAYMLLTKtvqvnkdgsknVMCKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPV--EMPSSKREag 493
Cdd:TIGR01733    1 TYRELDERANRLARHLRAA-----------GGVGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLdpAYPAERLA-- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   494 iaqlgFLLGNCGVKVALTSESCYKGLPkkvntsstfsapsgsnsltGTSSEIVDFRgwPRLWWAVTEHMSKPSRDWTAPP 573
Cdd:TIGR01733   66 -----FILEDAGARLLLTDSALASRLA-------------------GLVLPVILLD--PLELAALDDAPAPPPPDAPSGP 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811   574 rladETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWhAILASIFNGMKVIFVPY 653
Cdd:TIGR01733  120 ----DDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPE 194
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 808354811   654 SLMKMNPATWMHMVSKYQATTA-LVKSrdlHWALLAtrDHKDISLASLRTLLVA 706
Cdd:TIGR01733  195 DEERDDAALLAALIAEHPVTVLnLTPS---LLALLA--AALPPALASLRLVILG 243
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
1264-1596 3.35e-13

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 72.70  E-value: 3.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1264 YPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPmeveQQPSLFLTTLSNLKVRDAFTTYSTINTCVtqlatsvENL 1343
Cdd:cd04433    38 LTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK----FDPEAALELIEREKVTILLGVPTLLARLL-------KAP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1344 RERGCNLSMLRSCVAIAEERPrIALMSSFcklfapLALNNRAISTSFssrvnaaicmqGAS--GPEPSTVYVDARALRnd 1421
Cdd:cd04433   107 ESAGYDLSSLRALVSGGAPLP-PELLERF------EEAPGIKLVNGY-----------GLTetGGTVATGPPDDDARK-- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1422 rislvgkgaPHSValiesGKLLPGVKIAIANPETRGqCADSHLGEIWVASIHNasplnrlasvtgfgdegtMNTDVYNAR 1501
Cdd:cd04433   167 ---------PGSV-----GRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSV------------------MKGYWNNPE 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1502 LTTGDTKTRWARTGYLGFLRqtqsitEHGELHdavfVVGALNESLVLRGMRYHPFDVESTVsKAHRFVGNSAVF-----T 1576
Cdd:cd04433   214 ATAAVDEDGWYRTGDLGRLD------EDGYLY----IVGRLKDMIKSGGENVYPAEVEAVL-LGHPGVAEAAVVgvpdpE 282
                         330       340
                  ....*....|....*....|
gi 808354811 1577 WNHLVVIAAECTGSESDALD 1596
Cdd:cd04433   283 WGERVVAVVVLRPGADLDAE 302
PRK12316 PRK12316
peptide synthase; Provisional
344-871 7.01e-12

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 71.14  E-value: 7.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  344 LEAMAKirDPDAPRPEGTIMNP---VRGEAAHSNTNNTMPRSLDSFSAFHRFGTTAAKNIAAMVLDQsakpstQLTYGKL 420
Cdd:PRK12316 1963 LEQMAE--DAQAALGELALLDAgerQRILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQ------HLSYAEL 2034
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  421 HSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLhfLAAFYGCLQAGVIPVPVEmPSSKREagiaQLGFL 500
Cdd:PRK12316 2035 DSRANRLAHRLRARGV------------GPEVRVAIAAERSFEL--VVALLAVLKAGGAYVPLD-PNYPAE----RLAYM 2095
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  501 LGNCGVKVALTSESCYKGLPkkvntsstfsAPSGSNSLTGTSSEivDFRGWPRlwwavtehmskpsrdwTAP-PRLADET 579
Cdd:PRK12316 2096 LEDSGAALLLTQRHLLERLP----------LPAGVARLPLDRDA--EWADYPD----------------TAPaVQLAGEN 2147
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  580 IAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHaILASIFNGMKVIFVPYSLmkMN 659
Cdd:PRK12316 2148 LAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARVLIRDDEL--WD 2224
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  660 PATWMHMVSKYQATTALVKSrdLHWALLATRDHKDISLASLRTLLVadGANPWSLSSCDAFAAAftpspysLRPDAMCPC 739
Cdd:PRK12316 2225 PEQLYDEMERHGVTILDFPP--VYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRLAWEA-------LRPVYLFNG 2293
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  740 AGSSETGTISIRRRGNAQLGSQS-----GRGIlsmSALSHCVvrvdtensltsltlqdagqivagavvvvtaIDGSNRLC 814
Cdd:PRK12316 2294 YGPTEAVVTPLLWKCRPQDPCGAayvpiGRAL---GNRRAYI------------------------------LDADLNLL 2340
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808354811  815 QADEIGEICVSANSTAQLYWALDGQTHHTFKVEPVGEYGKLI----GAVRYVRSGLIGFMG 871
Cdd:PRK12316 2341 APGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLyrtgDLARYRADGVVEYLG 2401
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
448-982 8.74e-11

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 66.31  E-value: 8.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  448 CKPGDRVALIYPNTQPLHFLAA--FYGCLQAGVIPVPVEmPSSKReagiAQLGFLLGNCGVKVALTSEScYKGLPKKVNT 525
Cdd:cd05922    15 GVRGERVVLILPNRFTYIELSFavAYAGGRLGLVFVPLN-PTLKE----SVLRYLVADAGGRIVLADAG-AADRLRDALP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  526 SStfsapsgsnsltGTSSEIVDFRGWprlwWAvtehmskpSRDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFA 605
Cdd:cd05922    89 AS------------PDPGTVLDADGI----RA--------ARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  606 HCRALTTAMEYKEDETMVCVVDFKREVGLwHAILASIFNGMKVIFVPYSLMkmnPATWMHMVSKYQATT-ALVKSrdlHW 684
Cdd:cd05922   145 NARSIAEYLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVL---DDAFWEDLREHGATGlAGVPS---TY 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  685 ALLATRDHKDISLASLRTLLVADGANPwslsscDAFAAAFTpspySLRPDAMcpcagssetgtisirrrgnaqlgsqsgr 764
Cdd:cd05922   218 AMLTRLGFDPAKLPSLRYLTQAGGRLP------QETIARLR----ELLPGAQ---------------------------- 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  765 gILSMSALSHCVVR---VDTENSLTSLTlqDAGQIVAGAVVVVTAIDGSnrLCQADEIGEICVSANSTAQLYWalDGQTH 841
Cdd:cd05922   260 -VYVMYGQTEATRRmtyLPPERILEKPG--SIGLAIPGGEFEILDDDGT--PTPPGEPGEIVHRGPNVMKGYW--NDPPY 332
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  842 HTFKVEPVGeygkligavrYVRSGLIGFMGPDGMVFVVARRQSLLAVSGRYHSADDIIATVLAVEPMkfvyrGRICVFST 921
Cdd:cd05922   333 RRKEGRGGG----------VLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI-----IEAAAVGL 397
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808354811  922 SVLRDERIVIVAEQKPNCSEEEafdwITRVLRAIDTIHQVGIYCcalVPANHLPKTPLGGV 982
Cdd:cd05922   398 PDPLGEKLALFVTAPDKIDPKD----VLRSLAERLPPYKVPATV---RVVDELPLTASGKV 451
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
570-993 1.52e-10

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 65.79  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  570 TAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYK-EDETMVCVVDFKREVGLWHAILASIFNGMKV 648
Cdd:PRK07768  144 IDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMYFGAEL 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  649 IFV-PYSLMKmNPATWMHMVSKYQAT-TAlvkSRDLHWALLATR-----DHKDISLASLRTLLvaDGANPWSLSSCDAFA 721
Cdd:PRK07768  224 VKVtPMDFLR-DPLLWAELISKYRGTmTA---APNFAYALLARRlrrqaKPGAFDLSSLRFAL--NGAEPIDPADVEDLL 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  722 AAftPSPYSLRPDAMCPCAGSSETG-TISIRRRGN--------AQLGSQSGRGILSMSA-----------LSHCVVRVdt 781
Cdd:PRK07768  298 DA--GARFGLRPEAILPAYGMAEATlAVSFSPCGAglvvdevdADLLAALRRAVPATKGntrrlatlgppLPGLEVRV-- 373
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  782 ensltsltlqdagqivagavvvvtaIDGSNRLCQADEIGEICVSANSTAQLYWALDGQthhtfkVEPVGEYGKLigavry 861
Cdd:PRK07768  374 -------------------------VDEDGQVLPPRGVGVIELRGESVTPGYLTMDGF------IPAQDADGWL------ 416
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  862 vRSGLIGFMGPDGMVFVVARRQSLLAVSGRYHSADDI---IATVLAVEPmkfvyRGRICVFSTSVLRDERIVIVAEQKPN 938
Cdd:PRK07768  417 -DTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIeraAARVEGVRP-----GNAVAVRLDAGHSREGFAVAVESNAF 490
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 808354811  939 CSEEEafdwITRVLRAI--DTIHQVGI--YCCALVPANHLPKTPLGGVHVSETKQRFEN 993
Cdd:PRK07768  491 EDPAE----VRRIRHQVahEVVAEVGVrpRNVVVLGPGSIPKTPSGKLRRANAAELVTP 545
PRK12467 PRK12467
peptide synthase; Provisional
350-675 2.94e-10

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 65.57  E-value: 2.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  350 IRDPDAPRPEGTIMNPVRGEAAhsntnntmprsLDSFSAFHRfGTTAAKNIAAMVLDQSAKP---------STQLTYGKL 420
Cdd:PRK12467 1538 VADPERRLGELDLLDEAERRQI-----------LEGWNATHT-GYPLARLVHQLIEDQAAATpeavalvfgEQELTYGEL 1605
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  421 HSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEmPSSKREagiaQLGFL 500
Cdd:PRK12467 1606 NRRANRLAHRLIALGV------------GPEVLVGIAVERS--LEMVVGLLAILKAGGAYVPLD-PEYPRE----RLAYM 1666
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  501 LGNCGVKVALTSESCYKGLPkkvntsstfsAPSGSNSLtgtsseIVDfrgwPRLWWAVTEHMSKPSRdwtappRLADETI 580
Cdd:PRK12467 1667 IEDSGIELLLTQSHLQARLP----------LPDGLRSL------VLD----QEDDWLEGYSDSNPAV------NLAPQNL 1720
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  581 AYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHaILASIFNGMKVIFVPYSLMKmNP 660
Cdd:PRK12467 1721 AYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWE-LFWPLINGARLVIAPPGAHR-DP 1798
                         330
                  ....*....|....*
gi 808354811  661 ATWMHMVSKYQATTA 675
Cdd:PRK12467 1799 EQLIQLIERQQVTTL 1813
PRK08316 PRK08316
acyl-CoA synthetase; Validated
413-623 2.90e-09

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 61.49  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  413 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREa 492
Cdd:PRK08316   35 RSWTYAELDAAVNRVAAALLDLGL------------KKGDRVAALGHNS--DAYALLWLACARAGAVHVPVNFMLTGEE- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  493 giaqLGFLLGNCGVKVALTsESCYKGLPKKVNTSSTFSAPSGSNSLTGTSSE--IVDFRGWprlwwavtehmSKPSRDWT 570
Cdd:PRK08316  100 ----LAYILDHSGARAFLV-DPALAPTAEAALALLPVDTLILSLVLGGREAPggWLDFADW-----------AEAGSVAE 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 808354811  571 APPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMV 623
Cdd:PRK08316  164 PDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPL 216
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
1078-1575 1.36e-08

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 59.15  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1078 NAEQDTATCSTLLKRAERIA-GLltDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLvpvcikppVASDLNTTLGP--I 1154
Cdd:cd05911     5 ADTGKELTYAQLRTLSRRLAaGL--RKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGG--------IFSAANPIYTAdeL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1155 RMMVDMSKAVAIL-APQNVSKLLKSKEAAHSIDSnawpmILDLEDAPSswrrKNNNNCDTTTSGSSGA---------ASK 1224
Cdd:cd05911    75 AHQLKISKPKVIFtDPDGLEKVKEAAKELGPKDK-----IIVLDDKPD----GVLSIEDLLSPTLGEEdedlppplkDGK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1225 EEICYLDFSINSSGQLQGSSMSEASAITVCKSIK-VSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEV 1303
Cdd:cd05911   146 DDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQtFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1304 EqqpsLFLTTLSNLKVRDAFTTystiNTCVTQLATSVENLRErgcNLSMLRSCVAIAeerprialmssfcklfAPLAlnn 1383
Cdd:cd05911   226 E----LFLDLIEKYKITFLYLV----PPIAAALAKSPLLDKY---DLSSLRVILSGG----------------APLS--- 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1384 RAISTSFSSRVNAAICMQG----ASGPePSTVyvdaralrndrislvgkgAPHSVALIES-GKLLPGVKIAIANPETRGQ 1458
Cdd:cd05911   276 KELQELLAKRFPNATIKQGygmtETGG-ILTV------------------NPDGDDKPGSvGRLLPNVEAKIVDDDGKDS 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1459 CADSHLGEIWVASIHNASP-LNRlasvtgfgDEGTMNTdvynarlttgDTKTRWARTGYLGFLRqtqsitEHGELhdavF 1537
Cdd:cd05911   337 LGPNEPGEICVRGPQVMKGyYNN--------PEATKET----------FDEDGWLHTGDIGYFD------EDGYL----Y 388
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 808354811 1538 VVGALNESLVLRGMRYHPFDVEStVSKAHRFVGNSAVF 1575
Cdd:cd05911   389 IVDRKKELIKYKGFQVAPAELEA-VLLEHPGVADAAVI 425
PRK12316 PRK12316
peptide synthase; Provisional
344-881 1.59e-08

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 59.97  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  344 LEAMAkiRDPDAPRPEGTIMNPVRGEAAHSNTNNTMPRSLDSFSAFHRFGTTAAKNIAAMVLDQSAKpstQLTYGKLHSR 423
Cdd:PRK12316 4511 LEAMA--EDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEE---KLTYAELNRR 4585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  424 AGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEmPSSKREagiaQLGFLLGN 503
Cdd:PRK12316 4586 ANRLAHALIARGV------------GPEVLVGIAMERS--AEMMVGLLAVLKAGGAYVPLD-PEYPRE----RLAYMMED 4646
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  504 CGVKVALTSESCYKGLPkkvntsstfsAPSGSNSLTgtsseiVDfrgwprlwwavtehmskPSRDWTAPP------RLAD 577
Cdd:PRK12316 4647 SGAALLLTQSHLLQRLP----------IPDGLASLA------LD-----------------RDEDWEGFPahdpavRLHP 4693
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  578 ETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIfNGMKVIFVPYSLmk 657
Cdd:PRK12316 4694 DNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLI-NGASVVIRDDSL-- 4770
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  658 MNPATWMHMVSKYQATTALVKSrdLHWALLATRDHKDISLASLRTLLVADGANPwslssCDAFAAAFTpspySLRPDAMC 737
Cdd:PRK12316 4771 WDPERLYAEIHEHRVTVLVFPP--VYLQQLAEHAERDGEPPSLRVYCFGGEAVA-----QASYDLAWR----ALKPVYLF 4839
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  738 PCAGSSETGTISIRRRgnAQLGSQSGRGILSMSALshcvvrvdtensLTSLtlqdAGQIvagavvvvtaIDGSNRLCQAD 817
Cdd:PRK12316 4840 NGYGPTETTVTVLLWK--ARDGDACGAAYMPIGTP------------LGNR----SGYV----------LDGQLNPLPVG 4891
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808354811  818 EIGEICVSANSTAQLYWALDGQTHHTFKVEPVGEYGKligavRYVRSGLIGFMGPDGMVFVVAR 881
Cdd:PRK12316 4892 VAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGG-----RLYRTGDLARYRADGVIDYLGR 4950
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
416-881 7.48e-08

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 57.12  E-value: 7.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  416 TYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQplHFLAAFYGCLQAGVIPVPVempsSKREAGiA 495
Cdd:PRK06187   33 TYAELDERVNRLANALRALGV------------KKGDRVAVFDWNSH--EYLEAYFAVPKIGAVLHPI----NIRLKP-E 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  496 QLGFLLGNCGVKVALTSES---CYKGLPKKVNTSSTFSApSGSNSLTGTSSEIVDFRGwprlWWAVTEhmskPSRDWtap 572
Cdd:PRK06187   94 EIAYILNDAEDRVVLVDSEfvpLLAAILPQLPTVRTVIV-EGDGPAAPLAPEVGEYEE----LLAAAS----DTFDF--- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  573 PRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDET-MVCVVDFkrEVGLWHAILASIFNGMKVI-- 649
Cdd:PRK06187  162 PDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVyLVIVPMF--HVHAWGLPYLALMAGAKQVip 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  650 --FVPYSLMKM----NPaTWMHMV-SKYQattalvksrdlhwALLATRDHKDISLASLRtlLVADGANPWSLSSCDAFAA 722
Cdd:PRK06187  240 rrFDPENLLDLieteRV-TFFFAVpTIWQ-------------MLLKAPRAYFVDFSSLR--LVIYGGAALPPALLREFKE 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  723 AFTpspyslrpdamCPCA---GSSETG-TISIRR------RGNAQLGSQsGRGILSMSalshcvVRVdtensltsltlqd 792
Cdd:PRK06187  304 KFG-----------IDLVqgyGMTETSpVVSVLPpedqlpGQWTKRRSA-GRPLPGVE------ARI------------- 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  793 agqivagavvvvtaIDGSNRLCQAD--EIGEICVSANSTAQLYWALDGQTHHTFkvepVGEygkligavrYVRSGLIGFM 870
Cdd:PRK06187  353 --------------VDDDGDELPPDggEVGEIIVRGPWLMQGYWNRPEATAETI----DGG---------WLHTGDVGYI 405
                         490
                  ....*....|.
gi 808354811  871 GPDGMVFVVAR 881
Cdd:PRK06187  406 DEDGYLYITDR 416
PRK12467 PRK12467
peptide synthase; Provisional
414-728 1.12e-07

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 57.09  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  414 QLTYGKLHSRAGKVAYMLLTKtvqvnkdgskNVMCKPGDRVALiypnTQPLHFLAAFYGCLQAGVIPVPVEmPSSKREag 493
Cdd:PRK12467 3120 QLSYAELNRRANRLAHRLIAI----------GVGPDVLVGVAV----ERSVEMIVALLAVLKAGGAYVPLD-PEYPRE-- 3182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  494 iaQLGFLLGNCGVKVALTSESCYKGLPkkvntsstfsAPSGSNSLTgtsseiVDfRGwprLWWAVTEHmsKPSrdwtapP 573
Cdd:PRK12467 3183 --RLAYMIEDSGVKLLLTQAHLLEQLP----------APAGDTALT------LD-RL---DLNGYSEN--NPS------T 3232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  574 RLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHaILASIFNGMKVIFVPY 653
Cdd:PRK12467 3233 RVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQER-FLWTLICGGCLVVRDN 3311
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808354811  654 SLmkMNPATWMHMVSKYQATTALVKSRDLHwALLAtrDHKDISLASLRTLLVADGANPwslssCDAFAAAFTPSP 728
Cdd:PRK12467 3312 DL--WDPEELWQAIHAHRISIACFPPAYLQ-QFAE--DAGGADCASLDIYVFGGEAVP-----PAAFEQVKRKLK 3376
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
414-982 1.51e-07

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 55.95  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  414 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREag 493
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGV------------RKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPINPMLKERE-- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  494 iaqLGFLLGNCGVKVALtsescykglpkkvntsstfsapsgsnsltgTSSEIVDfrgwprlwwavtehmskpsrdwtapp 573
Cdd:cd05935    65 ---LEYILNDSGAKVAV------------------------------VGSELDD-------------------------- 85
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  574 rladetIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFvpy 653
Cdd:cd05935    86 ------LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--- 156
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  654 sLMKMNPATWMHMVSKYQAT------TALVKsrdlhwaLLATRDHKDISLASLRTLlvadGANPWSLsscdafaaaftps 727
Cdd:cd05935   157 -MARWDRETALELIEKYKVTfwtnipTMLVD-------LLATPEFKTRDLSSLKVL----TGGGAPM------------- 211
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  728 pyslrPDAmcpcagssetgtISIRRRGNAQLGSQSGRGILSMSALSHCvvrvdteNSLTSLTLQDAGQIVAGAVVVVTAI 807
Cdd:cd05935   212 -----PPA------------VAEKLLKLTGLRFVEGYGLTETMSQTHT-------NPPLRPKLQCLGIP*FGVDARVIDI 267
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  808 DgSNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFkVEpvgeygklIGAVRYVRSGLIGFMGPDGMVFVVARRQSLLA 887
Cdd:cd05935   268 E-TGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESF-IE--------IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMIN 337
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  888 VSGryhsaddiiATVLAVEPMKFVYRGR----ICVFSTSvlrDER--------IVIVAEQKPNCSEEEAFDWITRVLRAI 955
Cdd:cd05935   338 VSG---------FKVWPAEVEAKLYKHPai*eVCVISVP---DERvgeevkafIVLRPEYRGKVTEEDIIEWAREQMAAY 405
                         570       580
                  ....*....|....*....|....*..
gi 808354811  956 DTIHQVGIyccalvpANHLPKTPLGGV 982
Cdd:cd05935   406 KYPREVEF-------VDELPRSASGKI 425
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
1055-1612 1.62e-07

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 56.14  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1055 LECLRSRAQSSPDHRILTLVtSKNAEQDTATCSTLLKRAERIAGLLTdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGL 1134
Cdd:cd05906    12 LLELLLRAAERGPTKGITYI-DADGSEEFQSYQDLLEDARRLAAGLR-QLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1135 VPVCIKPPVASDL----NTTLGPIRMMVDmsKAVAILAPQNVSKLLKSKEAAHsidsnaWPMI--LDLEDAPSSWRRKNN 1208
Cdd:cd05906    90 VPAPLTVPPTYDEpnarLRKLRHIWQLLG--SPVVLTDAELVAEFAGLETLSG------LPGIrvLSIEELLDTAADHDL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1209 NNCDTT-------TSGSSGAAskeeicyldfsinssgqlQGSSMSEASAITVCKSIKVSSELYPSR---------HVVvc 1272
Cdd:cd05906   162 PQSRPDdlallmlTSGSTGFP------------------KAVPLTHRNILARSAGKIQHNGLTPQDvflnwvpldHVG-- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1273 appysgiSLVLWCLSSVYSGHHTTLIPPMEVEQQPSLFLTTLSNLKVRDAFTTystiNTCVTQLATSVENLRERGCNLSM 1352
Cdd:cd05906   222 -------GLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAP----NFAFALLNDLLEEIEDGTWDLSS 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1353 LRSCVAIAEerPRIALMS-SFCKLFAPLALNNRAISTSFssrvnaaicmqGASgpEPSTVYVDARALRNDRIslvgkgaP 1431
Cdd:cd05906   291 LRYLVNAGE--AVVAKTIrRLLRLLEPYGLPPDAIRPAF-----------GMT--ETCSGVIYSRSFPTYDH-------S 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1432 HSVALIESGKLLPGVKIAIANPEtrGQCAD-SHLGEIWVasihnasplnRLASVTgfgdEGTMNTDVYNARLTTGDTktr 1510
Cdd:cd05906   349 QALEFVSLGRPIPGVSMRIVDDE--GQLLPeGEVGRLQV----------RGPVVT----KGYYNNPEANAEAFTEDG--- 409
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1511 WARTGYLGFLRqtqsiteHGELHdavfVVGALNESLVLRGMRYHPFDVESTVSKA----HRFVGNSAVFTWN----HLVV 1582
Cdd:cd05906   410 WFRTGDLGFLD-------NGNLT----ITGRTKDTIIVNGVNYYSHEIEAAVEEVpgvePSFTAAFAVRDPGaeteELAI 478
                         570       580       590
                  ....*....|....*....|....*....|....*
gi 808354811 1583 IAAECTGSESDALDLVPAITSAVLEE-----HHLI 1612
Cdd:cd05906   479 FFVPEYDLQDALSETLRAIRSVVSREvgvspAYLI 513
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
415-881 1.62e-07

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 55.69  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  415 LTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREagi 494
Cdd:cd17631    21 LTYAELDERVNRLAHALRALGV------------AKGDRVAVLSKNS--PEFLELLFAAARLGAVFVPLNFRLTPPE--- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  495 aqLGFLLGNCGVKValtsescykglpkkvntsstfsapsgsnsltgtsseivdfrgwprlwwavtehmskpsrdwtappr 574
Cdd:cd17631    84 --VAYILADSGAKV------------------------------------------------------------------ 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  575 LADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPys 654
Cdd:cd17631    96 LFDD-LALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILR-- 172
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  655 lmKMNPATWMHMVSKYQATTA-LVKSrdLHWALLATRDHKDISLASLRTLLVADGANPWSL-SSCDAFAAAFtpspyslr 732
Cdd:cd17631   173 --KFDPETVLDLIERHRVTSFfLVPT--MIQALLQHPRFATTDLSSLRAVIYGGAPMPERLlRALQARGVKF-------- 240
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  733 pdamCPCAGSSETG-TISIRRRGNAQ--LGSqSGRgilsmsALSHCVVRVdtensltsltlqdagqivagavvvvtaIDG 809
Cdd:cd17631   241 ----VQGYGMTETSpGVTFLSPEDHRrkLGS-AGR------PVFFVEVRI---------------------------VDP 282
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354811  810 SNRLCQADEIGEICVSANSTAQLYWALDGQTHHTFKvepvgeYGkligavrYVRSGLIGFMGPDGMVFVVAR 881
Cdd:cd17631   283 DGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR------DG-------WFHTGDLGRLDEDGYLYIVDR 341
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
1089-1220 2.08e-07

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 55.35  E-value: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  1089 LLKRAERIAGLLTDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKP--PVASdlnttlgpIRMMVDMSKAVAI 1166
Cdd:TIGR01733    5 LDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPayPAER--------LAFILEDAGARLL 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 808354811  1167 LA-PQNVSKLLKSKEAAHSIDSNAWPMI--LDLEDAPSSWRRKNNNNCDTTTSGSSG 1220
Cdd:TIGR01733   77 LTdSALASRLAGLVLPVILLDPLELAALddAPAPPPPDAPSGPDDLAYVIYTSGSTG 133
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
414-625 2.84e-07

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 54.99  E-value: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  414 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLhfLAAFYGCLQAGVIPVPVEmPSSKREag 493
Cdd:cd12116    12 SLSYAELDERANRLAARLRARGV------------GPGDRVAVYLPRSARL--VAAMLAVLKAGAAYVPLD-PDYPAD-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  494 iaQLGFLLGNCGVKVALTSESCYKGLPkkvntsstfsapsgsnsltgtsseiVDFRGWPRLWWAVTEhmsKPSRDWTAPp 573
Cdd:cd12116    75 --RLRYILEDAEPALVLTDDALPDRLP-------------------------AGLPVLLLALAAAAA---APAAPRTPV- 123
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 808354811  574 rlADETIAYIEYTTGNDGTVKGCCVTRQAV--FAHCRALTTAMeyKEDETMVCV 625
Cdd:cd12116   124 --SPDDLAYVIYTSGSTGRPKGVVVSHRNLvnFLHSMRERLGL--GPGDRLLAV 173
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
402-667 3.20e-07

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 55.01  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  402 AMVLDQSAKpstQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPV 481
Cdd:cd05926     5 ALVVPGSTP---ALTYADLAELVDDLARQLAALGI------------KKGDRVAIALPNG--LEFVVAFLAAARAGAVVA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  482 PVEmPSSKREagiaQLGFLLGNCGVKVALTSE----SCYKGLPKKVNTSSTFSAPSGSNSLTGTSSEIVDfrgwprlwwa 557
Cdd:cd05926    68 PLN-PAYKKA----EFEFYLADLGSKLVLTPKgelgPASRAASKLGLAILELALDVGVLIRAPSAESLSN---------- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  558 vteHMSKPSRDWTAPPRLADEtIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHA 637
Cdd:cd05926   133 ---LLADKKNAKSEGVPLPDD-LALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVAS 208
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 808354811  638 ILASIFNGMKVIFVP-------YSLMKMNPATWMHMV 667
Cdd:cd05926   209 LLSTLAAGGSVVLPPrfsastfWPDVRDYNATWYTAV 245
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
402-665 4.27e-07

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 54.22  E-value: 4.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  402 AMVLDQSakpstQLTYGKLHSRAGKVAYMLLTKTvqvnKDGsknvmckPGDRVALIYPNTQplHFLAAFYGCLQAGVIPV 481
Cdd:cd05941     4 AIVDDGD-----SITYADLVARAARLANRLLALG----KDL-------RGDRVAFLAPPSA--EYVVAQLAIWRAGGVAV 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  482 PVEmpsskREAGIAQLGFLLGNcgvkvaltsescykglpkkvntsstfSAPSgsnsltgtssEIVDfrgwprlwwavteh 561
Cdd:cd05941    66 PLN-----PSYPLAELEYVITD--------------------------SEPS----------LVLD-------------- 90
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  562 mskpsrdwtapprladetIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILAS 641
Cdd:cd05941    91 ------------------PALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCP 152
                         250       260
                  ....*....|....*....|....
gi 808354811  642 IFNGMKVIFVPyslmKMNPATWMH 665
Cdd:cd05941   153 LFAGASVEFLP----KFDPKEVAI 172
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
413-701 5.72e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 54.20  E-value: 5.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  413 TQLTYGKLHSRAGKVAYMLltktvqVNKDGsknvmCKPGDRVALIYPNTqPlHFLAAFYGCLQAGVIPVPVEmPSSKREa 492
Cdd:PRK08314   34 RAISYRELLEEAERLAGYL------QQECG-----VRKGDRVLLYMQNS-P-QFVIAYYAILRANAVVVPVN-PMNREE- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  493 giaQLGFLLGNCGVKVALTSESCYKGLPKKVNT-----------SSTFSAPSGSN--SLTGTSSEIVDFRGWPRLWWavT 559
Cdd:PRK08314   99 ---ELAHYVTDSGARVAIVGSELAPKVAPAVGNlrlrhvivaqySDYLPAEPEIAvpAWLRAEPPLQALAPGGVVAW--K 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  560 EHMSKPSRdwtAPPRLAD-ETIAYIEYTTGNDGTVKGCCVTRQAVFAHcrALTTAMEYK--EDETMVCVVDFKREVGLWH 636
Cdd:PRK08314  174 EALAAGLA---PPPHTAGpDDLAVLPYTSGTTGVPKGCMHTHRTVMAN--AVGSVLWSNstPESVVLAVLPLFHVTGMVH 248
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808354811  637 AILASIFNGMKVIFVPyslmKMNPATWMHMVSKYQATtalvksrdlHWA--------LLATRDHKDISLASLR 701
Cdd:PRK08314  249 SMNAPIYAGATVVLMP----RWDREAAARLIERYRVT---------HWTniptmvvdFLASPGLAERDLSSLR 308
PRK06178 PRK06178
acyl-CoA synthetase; Validated
413-706 6.35e-07

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 54.28  E-value: 6.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  413 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLHflAAFYGCLQAGVIPVPVEmPSSKRea 492
Cdd:PRK06178   57 HVITYAELDELSDRFAALLRQRGV------------GAGDRVAVFLPNCPQFH--IVFFGILKLGAVHVPVS-PLFRE-- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  493 giAQLGFLLGNCGVKVALTSESCYKgLPKKV--NTS-STFSAPSGSNSLTGTSSEIVDF--RGWPRLWWAVTEHMSKPsR 567
Cdd:PRK06178  120 --HELSYELNDAGAEVLLALDQLAP-VVEQVraETSlRHVIVTSLADVLPAEPTLPLPDslRAPRLAAAGAIDLLPAL-R 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  568 DWTAPPRLAD---ETIAYIEYTTGNDGTVKGCCVT-RQAVFAHCRALTTAMEYKEDETMvcvVDFKREvgLWHA-----I 638
Cdd:PRK06178  196 ACTAPVPLPPpalDALAALNYTGGTTGMPKGCEHTqRDMVYTAAAAYAVAVVGGEDSVF---LSFLPE--FWIAgenfgL 270
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  639 LASIFNGMKVIFvpysLMKMNPATWMHMVSKYQATTA--LVKSRDlhwALLATRDHKDISLASLRTLLVA 706
Cdd:PRK06178  271 LFPLFSGATLVL----LARWDAVAFMAAVERYRVTRTvmLVDNAV---ELMDHPRFAEYDLSSLRQVRVV 333
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
413-706 8.52e-07

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 54.09  E-value: 8.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  413 TQLTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPV--EMPSskr 490
Cdd:COG1020   500 QSLTYAELNARANRLAHHLRALGVG------------PGDLVGVCLERS--LEMVVALLAVLKAGAAYVPLdpAYPA--- 562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  491 eagiAQLGFLLGNCGVKVALTSESCYKGLPKkvntsstfsapsgsnsltgtsseivdfRGWPRLWWAVTEHMSKPSRDwt 570
Cdd:COG1020   563 ----ERLAYMLEDAGARLVLTQSALAARLPE---------------------------LGVPVLALDALALAAEPATN-- 609
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  571 APPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCV--VDFkrEVGLWhAILASIFNGMKV 648
Cdd:COG1020   610 PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW-EIFGALLSGATL 686
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 808354811  649 IFVPYSLMKmNPATWMHMVSKYQATTA-LVKSrdlHWALLAtrDHKDISLASLRTLLVA 706
Cdd:COG1020   687 VLAPPEARR-DPAALAELLARHRVTVLnLTPS---LLRALL--DAAPEALPSLRLVLVG 739
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
449-624 1.11e-06

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 52.98  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  449 KPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVeMPSSKREagiaQLGFLLGNCGVKVALTSEScykglpkkvntsst 528
Cdd:cd05907    28 EPGDRVAILSRNR--PEWTIADLAILAIGAVPVPI-YPTSSAE----QIAYILNDSEAKALFVEDP-------------- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  529 fsapsgsnsltgtsseivdfrgwprlwwavtehmskpsrdwtapprladETIAYIEYTTGNDGTVKGCCVTRQAVFAHCR 608
Cdd:cd05907    87 -------------------------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNAL 117
                         170
                  ....*....|....*.
gi 808354811  609 ALTTAMEYKEDETMVC 624
Cdd:cd05907   118 ALAERLPATEGDRHLS 133
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
411-894 1.28e-06

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 53.14  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  411 PSTQLTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKr 490
Cdd:cd05959    26 DAGSLTYAELEAEARRVAGALRALGVK------------REERVLLIMLDT--VDFPTAFLGAIRAGIVPVPVNTLLTP- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  491 eagiAQLGFLLGNCGVKVALTSESCYKGLPKKVNTSST------FSAPSGSNSLTGTSSEIvdfrgwprlwWAVTEHMSK 564
Cdd:cd05959    91 ----DDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHtlvvliVSGGAGPEAGALLLAEL----------VAAEAEQLK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  565 PSRDWtapprlADEtIAYIEYTTGNDGTVKGccvtrqAVFAHCRALTTAMEY-------KEDETMVCVVDFKREVGLWHA 637
Cdd:cd05959   157 PAATH------ADD-PAFWLYSSGSTGRPKG------VVHLHADIYWTAELYarnvlgiREDDVCFSAAKLFFAYGLGNS 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  638 ILASIFNGMKVIFVPyslMKMNPATWMHMVSKYQATTaLVKSRDLHWALLATRDHKDISLASLRTLLVADGANPWSLSsc 717
Cdd:cd05959   224 LTFPLSVGATTVLMP---ERPTPAAVFKRIRRYRPTV-FFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVG-- 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  718 DAFAAAFTPSpyslrpdaMCPCAGSSETGTISIRRR-GNAQLGSqSGRGILSMSalshcVVRVDtensltsltlqDAGQI 796
Cdd:cd05959   298 ERWKARFGLD--------ILDGIGSTEMLHIFLSNRpGRVRYGT-TGKPVPGYE-----VELRD-----------EDGGD 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  797 VAgavvvvtaidgsnrlcqADEIGEICVSANSTAQLYWALDGQTHHTFKvepvGEYGKliGAVRYVRSgligfmgPDGMV 876
Cdd:cd05959   353 VA-----------------DGEPGELYVRGPSSATMYWNNRDKTRDTFQ----GEWTR--TGDKYVRD-------DDGFY 402
                         490
                  ....*....|....*...
gi 808354811  877 FVVARRQSLLAVSGRYHS 894
Cdd:cd05959   403 TYAGRADDMLKVSGIWVS 420
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
1089-1181 3.08e-06

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 51.79  E-value: 3.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1089 LLKRAERIAGLLTdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVcikppvasDLNTTLGP--IRMMVDMSKAVAI 1166
Cdd:cd05936    30 LDALAEAFAAGLQ-NLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVV--------PLNPLYTPreLEHILNDSGAKAL 100
                          90
                  ....*....|....*
gi 808354811 1167 LAPQNVSKLLKSKEA 1181
Cdd:cd05936   101 IVAVSFTDLLAAGAP 115
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
413-682 3.73e-06

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 51.54  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  413 TQLTYGKLHSRAGKVAymlltktvqvnkDGSKNVMCKPGDRVALIYPNTqPLHfLAAFYGCLQAGVIPV---PVEMPssk 489
Cdd:PRK05605   56 ATTTYAELGKQVRRAA------------AGLRALGVRPGDRVAIVLPNC-PQH-IVAFYAVLRLGAVVVehnPLYTA--- 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  490 reagiAQLGFLLGNCGVKVAL---TSESCYKGLPKK--------VNTSSTFSAP-------------SGSNSLTGTSSEI 545
Cdd:PRK05605  119 -----HELEHPFEDHGARVAIvwdKVAPTVERLRRTtpletivsVNMIAAMPLLqrlalrlpipalrKARAALTGPAPGT 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  546 VDfrgwprlWWAVTEHMSKPSRDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHC---RALTTAMEyKEDETM 622
Cdd:PRK05605  194 VP-------WETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAaqgKAWVPGLG-DGPERV 265
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811  623 VCVVDFKREVGLWHAILASIFNGMKVIFVP-------YSLMKMNPATWMHMVSK-YQATTALVKSRDL 682
Cdd:PRK05605  266 LAALPMFHAYGLTLCLTLAVSIGGELVLLPapdidliLDAMKKHPPTWLPGVPPlYEKIAEAAEERGV 333
PRK09274 PRK09274
peptide synthase; Provisional
1058-1141 2.42e-05

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 49.13  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1058 LRSRAQSSPDHRILT----LVTSKNAEQDTATCSTLLKRAERIAGLLTDrARLSRGDHVALIFPPSIDLVAAFFGCLSAG 1133
Cdd:PRK09274   12 LPRAAQERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNA-AGIGRGMRAVLMVTPSLEFFALTFALFKAG 90

                  ....*...
gi 808354811 1134 LVPVCIKP 1141
Cdd:PRK09274   91 AVPVLVDP 98
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
1081-1597 3.95e-05

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 48.13  E-value: 3.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1081 QDTATCSTLLKRAERIAGLLTdRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIkppvasdlNTTLGP--IRMMV 1158
Cdd:cd05959    27 AGSLTYAELEAEARRVAGALR-ALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPV--------NTLLTPddYAYYL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1159 DMSKAVAILAPQNVSKLLksKEAAHSIDSNAWPMIL---DLEDAPSSWRRknNNNCDTTTSGSSGAASKEEICYLDFSIN 1235
Cdd:cd05959    98 EDSRARVVVVSGELAPVL--AAALTKSEHTLVVLIVsggAGPEAGALLLA--ELVAAEAEQLKPAATHADDPAFWLYSSG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1236 SSGQLQGssmseasAITVCKSIKVSSELYPSR-------HVVVCAP----PYsGISLVLWCLSSVysGHHTTLIP----P 1300
Cdd:cd05959   174 STGRPKG-------VVHLHADIYWTAELYARNvlgiredDVCFSAAklffAY-GLGNSLTFPLSV--GATTVLMPerptP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1301 MEV-----EQQPSLFLTtlsnlkvrdAFTTYSTIntcvtqlaTSVENLRERgcNLSMLRSCVAIAEERPrialmssfckl 1375
Cdd:cd05959   244 AAVfkrirRYRPTVFFG---------VPTLYAAM--------LAAPNLPSR--DLSSLRLCVSAGEALP----------- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1376 faplalnnRAISTSFSSRVNAAIcMQGASGPEPSTVYVDARalrndrislvgkgaPHSVALIESGKLLPGVKIAIANpET 1455
Cdd:cd05959   294 --------AEVGERWKARFGLDI-LDGIGSTEMLHIFLSNR--------------PGRVRYGTTGKPVPGYEVELRD-ED 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1456 RGQCADSHLGEIWVASihnasplnrlasvtgfgdeGTMNTDVYNARLTTGDT-KTRWARTGYlGFLRQtqsitEHGELhd 1534
Cdd:cd05959   350 GGDVADGEPGELYVRG-------------------PSSATMYWNNRDKTRDTfQGEWTRTGD-KYVRD-----DDGFY-- 402
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808354811 1535 avFVVGALNESLVLRGMRYHPFDVESTVsKAHRFVGNSAVFTWNH---------LVVIAAECTGSESDALDL 1597
Cdd:cd05959   403 --TYAGRADDMLKVSGIWVSPFEVESAL-VQHPAVLEAAVVGVEDedgltkpkaFVVLRPGYEDSEALEEEL 471
PRK12316 PRK12316
peptide synthase; Provisional
413-714 4.75e-05

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 48.41  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  413 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLhfLAAFYGCLQAGVIPVPVEmPSSKREa 492
Cdd:PRK12316  535 ETLDYAELNRRANRLAHALIERGV------------GPDVLVGVAMERSIEM--VVALLAILKAGGAYVPLD-PEYPAE- 598
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  493 giaQLGFLLGNCGVKVALTSESCYKGLPkkvntsstFSApsgsnsltGTSSEIVDfrgWPRLWWavtehmskpSRDWTAP 572
Cdd:PRK12316  599 ---RLAYMLEDSGVQLLLSQSHLGRKLP--------LAA--------GVQVLDLD---RPAAWL---------EGYSEEN 647
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  573 P--RLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILAsIFNGMKVIF 650
Cdd:PRK12316  648 PgtELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVV 726
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808354811  651 VPYSLMKmNPATWMHMVSKYQATT-ALVKSrdLHWALLatRDHKDISLASLRTLLVADGANPWSL 714
Cdd:PRK12316  727 AAPGDHR-DPAKLVELINREGVDTlHFVPS--MLQAFL--QDEDVASCTSLRRIVCSGEALPADA 786
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
413-904 5.84e-05

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 47.67  E-value: 5.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  413 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEmPSSKREA 492
Cdd:cd05934     2 RRWTYAELLRESARIAAALAALGI------------RPGDRVALMLDNC--PEFLFAWFALAKLGAVLVPIN-TALRGDE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  493 giaqLGFLLGNCGVKVALTSescykglpkkvntsstfsapsgsnsltgtsseivdfrgwprlwwavtehmskpsrdwtap 572
Cdd:cd05934    67 ----LAYIIDHSGAQLVVVD------------------------------------------------------------ 82
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  573 prladetIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEYKEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVP 652
Cdd:cd05934    83 -------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP 155
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  653 yslmKMNPATWMHMVSKYQAT--TALVKSRDlhwALLAT------RDHKdislasLRTLLVAdgANPWSLSscDAFAAAF 724
Cdd:cd05934   156 ----RFSASRFWSDVRRYGATvtNYLGAMLS---YLLAQppspddRAHR------LRAAYGA--PNPPELH--EEFEERF 218
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  725 TpspyslrpdamCPCA---GSSETGTISIRRRGNAQLGSQSGRGIlsmsalSHCVVRVdtensltsltlqdagqivagav 801
Cdd:cd05934   219 G-----------VRLLegyGMTETIVGVIGPRDEPRRPGSIGRPA------PGYEVRI---------------------- 259
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  802 vvvtaIDGSNRLCQADEIGEICVSAN---STAQLYWaldGQTHHTFKVEPVGEYgkligavryvRSGLIGFMGPDGMVFV 878
Cdd:cd05934   260 -----VDDDGQELPAGEPGELVIRGLrgwGFFKGYY---NMPEATAEAMRNGWF----------HTGDLGYRDADGFFYF 321
                         490       500
                  ....*....|....*....|....*.
gi 808354811  879 VARRQSLLAVSGRYHSADDIIATVLA 904
Cdd:cd05934   322 VDRKKDMIRRRGENISSAEVERAILR 347
PRK05691 PRK05691
peptide synthase; Validated
414-603 6.19e-05

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 48.24  E-value: 6.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  414 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVAlIYPNTQPlHFLAAFYGCLQAGVIPVPVEmpsskREAG 493
Cdd:PRK05691 1156 SLDYAELHAQANRLAHYLRDKGV------------GPDVCVA-IAAERSP-QLLVGLLAILKAGGAYVPLD-----PDYP 1216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  494 IAQLGFLLGNCGVKVALTSESCYKGLPkkvntsstfsapsGSNSLTGTSSEIVDFRGWPrlwwavtehmskpsrdwTAPP 573
Cdd:PRK05691 1217 AERLAYMLADSGVELLLTQSHLLERLP-------------QAEGVSAIALDSLHLDSWP-----------------SQAP 1266
                         170       180       190
                  ....*....|....*....|....*....|..
gi 808354811  574 RLA--DETIAYIEYTTGNDGTVKGCCVTRQAV 603
Cdd:PRK05691 1267 GLHlhGDNLAYVIYTSGSTGQPKGVGNTHAAL 1298
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1052-1137 7.35e-05

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 47.45  E-value: 7.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1052 LPLLECLRSRAQSSPDHRILTlvtsknAEQDTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLS 1131
Cdd:COG1021    25 ETLGDLLRRRAERHPDRIAVV------DGERRLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALFR 97

                  ....*.
gi 808354811 1132 AGLVPV 1137
Cdd:COG1021    98 AGAIPV 103
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
414-481 1.17e-04

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 46.68  E-value: 1.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811  414 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPV 481
Cdd:COG1021    50 RLSYAELDRRADRLAAGLLALGL------------RPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
PRK07798 PRK07798
acyl-CoA synthetase; Validated
414-746 1.47e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 46.42  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  414 QLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREag 493
Cdd:PRK07798   28 RLTYAELEERANRLAHYLIAQGL------------GPGDHVGIYARNR--IEYVEAMLGAFKARAVPVNVNYRYVEDE-- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  494 iaqLGFLLGNCGVkVALTSESCYKG-----LPK--KVNTSSTFSAPSGSNSLTGTsseiVDFRGwprlwwAVTEhmSKPS 566
Cdd:PRK07798   92 ---LRYLLDDSDA-VALVYEREFAPrvaevLPRlpKLRTLVVVEDGSGNDLLPGA----VDYED------ALAA--GSPE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  567 RDwtAPPRLADETiaYIEYTTGNDGTVKGccV------TRQAVFAHCRALTTamEYKEDE-------------TMVCVVD 627
Cdd:PRK07798  156 RD--FGERSPDDL--YLLYTGGTTGMPKG--VmwrqedIFRVLLGGRDFATG--EPIEDEeelakraaagpgmRRFPAPP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  628 FKREVGLWhAILASIFNGMKVIFvpYSLMKMNPATWMHMVSKYQATTALVK----SRDLHWALLATRDHkDISlaSLRTl 703
Cdd:PRK07798  228 LMHGAGQW-AAFAALFSGQTVVL--LPDVRFDADEVWRTIEREKVNVITIVgdamARPLLDALEARGPY-DLS--SLFA- 300
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 808354811  704 lVADGANPWSLSSCDAFAAAFtpspyslrPDAMCPCA-GSSETG 746
Cdd:PRK07798  301 -IASGGALFSPSVKEALLELL--------PNVVLTDSiGSSETG 335
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
379-620 1.82e-04

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 46.29  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  379 MPRSLDSFSAfhrfgttAAKNIAAMVLDQSA----KP-----STQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcK 449
Cdd:PRK06155    9 AARAVDPLPP-------SERTLPAMLARQAErypdRPllvfgGTRWTYAEAARAAAAAAHALAAAGV------------K 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  450 PGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKreagiAQLGFLLGNCGVKVaLTSEScykGLPKKVNTsstf 529
Cdd:PRK06155   70 RGDRVALMCGNR--IEFLDVFLGCAWLGAIAVPINTALRG-----PQLEHILRNSGARL-LVVEA---ALLAALEA---- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  530 sAPSGSNSLTGTSseIVD---FRGWPRLWWAVtehmSKPSRDWTAPP---RLADetIAYIEYTTGNDGTVKGCCVTRQAV 603
Cdd:PRK06155  135 -ADPGDLPLPAVW--LLDapaSVSVPAGWSTA----PLPPLDAPAPAaavQPGD--TAAILYTSGTTGPSKGVCCPHAQF 205
                         250
                  ....*....|....*..
gi 808354811  604 FAHCRALTTAMEYKEDE 620
Cdd:PRK06155  206 YWWGRNSAEDLEIGADD 222
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
1089-1146 2.47e-04

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 45.55  E-value: 2.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811 1089 LLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKPPVASD 1146
Cdd:cd05935     7 LLEVVKKLASFLSNKG-VRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKER 63
prpE PRK10524
propionyl-CoA synthetase; Provisional
582-706 2.82e-04

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 45.71  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  582 YIEYTTGNDGTVKGccVTRQaVFAHCRALTTAMEY----KEDETMVCVVDFKREVGLWHAILASIFNGMKVIFVPYSLMK 657
Cdd:PRK10524  237 YILYTSGTTGKPKG--VQRD-TGGYAVALATSMDTifggKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTR 313
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 808354811  658 MNPATWMHMVSKYQ------ATTAL--VKSRDLhwALLATRDhkdisLASLRTLLVA 706
Cdd:PRK10524  314 PDAGIWWRIVEKYKvnrmfsAPTAIrvLKKQDP--ALLRKHD-----LSSLRALFLA 363
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
449-652 2.97e-04

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 45.48  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  449 KPGDRVALIYPNTqPLHFLAAFyGCLQAGVIPVPVEmPSSKREagiaQLGFLLGNCGVKVALTSEscyKGLPKKVNtsst 528
Cdd:COG1022    63 KPGDRVAILSDNR-PEWVIADL-AILAAGAVTVPIY-PTSSAE----EVAYILNDSGAKVLFVED---QEQLDKLL---- 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  529 fSAPSGSNSLTgtssEIV--DFRGWPRLWWAVT-EHMSKPSRDWTAPPRLAD-------ETIAYIEYTTGNDGTVKGCCV 598
Cdd:COG1022   129 -EVRDELPSLR----HIVvlDPRGLRDDPRLLSlDELLALGREVADPAELEArraavkpDDLATIIYTSGTTGRPKGVML 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 808354811  599 TRQAVFAHCRALTTAMEYKEDETMVCVVDfkrevgLWH-----AILASIFNGMKVIFVP 652
Cdd:COG1022   204 THRNLLSNARALLERLPLGPGDRTLSFLP------LAHvfertVSYYALAAGATVAFAE 256
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
1224-1562 3.14e-04

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 45.17  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1224 KEEICYLDFSINSSGQLQGSSMSEASAITVCKSIKVSSELYPSRHVVVCAPPYSGISLVLWCLSSVYSGHHTTLIPPMEV 1303
Cdd:cd05908   105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLF 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1304 EQQPSLFLTTLSNLKVRDAFTTYSTINTCVTQLATSVENlrerGCNLSMLRSCVAIAEErprIA--LMSSFCKLFAPLAL 1381
Cdd:cd05908   185 IRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKAN----DWDLSSIRMILNGAEP---IDyeLCHEFLDHMSKYGL 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1382 NNRAISTSFS-SRVNAAICMQGASGPEpSTVYVDARALR-NDRISLVGKGAPHSVALIESGKLLPGVKIAIANPETRGqC 1459
Cdd:cd05908   258 KRNAILPVYGlAEASVGASLPKAQSPF-KTITLGRRHVThGEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-L 335
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1460 ADSHLGEIWVasihnasplnRLASVTgfgdEGTMNTDVYNARLTTGDTktrWARTGYLGFLRQtqsitehGELhdavFVV 1539
Cdd:cd05908   336 PDGYIGHIQI----------RGKNVT----PGYYNNPEATAKVFTDDG---WLKTGDLGFIRN-------GRL----VIT 387
                         330       340
                  ....*....|....*....|...
gi 808354811 1540 GALNESLVLRGMRYHPFDVESTV 1562
Cdd:cd05908   388 GREKDIIFVNGQNVYPHDIERIA 410
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
1089-1141 4.43e-04

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 44.95  E-value: 4.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 808354811 1089 LLKRAERIAGLLTDRARLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKP 1141
Cdd:PRK08314   41 LLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
413-595 1.26e-03

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 43.35  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  413 TQLTYGKLHSRAGKVAYMLltktvqvnkdgsKNVMCKPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVempsSKREA 492
Cdd:PRK08276   10 EVVTYGELEARSNRLAHGL------------RALGLREGDVVAILLENN--PEFFEVYWAARRSGLYYTPI----NWHLT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  493 GiAQLGFLLGNCGVKVALTSESC---YKGLPKkvntsstfSAPSGSNSLTGTSSEIVDFRGWPRLwwavtehmskpsRDW 569
Cdd:PRK08276   72 A-AEIAYIVDDSGAKVLIVSAALadtAAELAA--------ELPAGVPLLLVVAGPVPGFRSYEEA------------LAA 130
                         170       180
                  ....*....|....*....|....*..
gi 808354811  570 TAPPRLADETIAY-IEYTTGNDGTVKG 595
Cdd:PRK08276  131 QPDTPIADETAGAdMLYSSGTTGRPKG 157
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
1089-1168 1.54e-03

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 42.97  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1089 LLKRAERIAGLLtdRAR-LSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIkppvasdlNTTLGP--IRMMVDMSKAVA 1165
Cdd:PRK08276   17 LEARSNRLAHGL--RALgLREGDVVAILLENNPEFFEVYWAARRSGLYYTPI--------NWHLTAaeIAYIVDDSGAKV 86

                  ...
gi 808354811 1166 ILA 1168
Cdd:PRK08276   87 LIV 89
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
414-890 1.80e-03

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 43.09  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  414 QLTYGKLHSRAGKVAYMLLTKTVQvnkdgsknvmckPGDRVALIYPNTqpLHFLAAFYGCLQAGVIPVPVEMPSSKREag 493
Cdd:PRK07059   48 AITYGELDELSRALAAWLQSRGLA------------KGARVAIMMPNV--LQYPVAIAAVLRAGYVVVNVNPLYTPRE-- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  494 iaqLGFLLGNCGVKVALTSESCYKGLPKKVNTSSTFSAPSGS-NSLTGTSSEIVDF--RGWPRL--WWAVTEH------M 562
Cdd:PRK07059  112 ---LEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASmGDLLGFKGHIVNFvvRRVKKMvpAWSLPGHvrfndaL 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  563 SKPSRDWTAPPRLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAME-----YKEDETMVCVVdfkrEVGLWH- 636
Cdd:PRK07059  189 AEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQpafekKPRPDQLNFVC----ALPLYHi 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  637 -AILASIFNGMKV----IFVPyslmkmNPATWMHMV---SKYQATT--ALvksRDLHWALLATRDHKDISLASLRtllVA 706
Cdd:PRK07059  265 fALTVCGLLGMRTggrnILIP------NPRDIPGFIkelKKYQVHIfpAV---NTLYNALLNNPDFDKLDFSKLI---VA 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  707 DG---------ANPWSLSSCDAFAAAFTPSPYSlrPDAMCPCAGSSE-TGTISirrrgnaqlgsqsgrgiLSMSAlSHCV 776
Cdd:PRK07059  333 NGggmavqrpvAERWLEMTGCPITEGYGLSETS--PVATCNPVDATEfSGTIG-----------------LPLPS-TEVS 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  777 VRVDTENSLTsltlqdagqivagavvvvtaidgsnrlcqADEIGEICVSANSTAQLYWALDGQThhtfkvepvgeyGKLI 856
Cdd:PRK07059  393 IRDDDGNDLP-----------------------------LGEPGEICIRGPQVMAGYWNRPDET------------AKVM 431
                         490       500       510
                  ....*....|....*....|....*....|....
gi 808354811  857 GAVRYVRSGLIGFMGPDGMVFVVARRQSLLAVSG 890
Cdd:PRK07059  432 TADGFFRTGDVGVMDERGYTKIVDRKKDMILVSG 465
PRK08316 PRK08316
acyl-CoA synthetase; Validated
1093-1204 1.83e-03

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 43.00  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1093 AERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVcikpPVasdlNTTLGP--IRMMVDMSKAVAILAPQ 1170
Cdd:PRK08316   46 VNRVAAALLDLG-LKKGDRVAALGHNSDAYALLWLACARAGAVHV----PV----NFMLTGeeLAYILDHSGARAFLVDP 116
                          90       100       110
                  ....*....|....*....|....*....|....
gi 808354811 1171 NVSKLLKSKEAAHSIDSNAWPMILDLEDAPSSWR 1204
Cdd:PRK08316  117 ALAPTAEAALALLPVDTLILSLVLGGREAPGGWL 150
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
1054-1146 1.96e-03

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 42.88  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1054 LLECLRSRAQSSPDHRILTLVtsknAEQDTATCSTLLKRAERIAGLLtDRARLSRGDHVALIFPPSIDLVAAFFGCLSAG 1133
Cdd:cd05923     3 VFEMLRRAASRAPDACAIADP----ARGLRLTYSELRARIEAVAARL-HARGLRPGQRVAVVLPNSVEAVIALLALHRLG 77
                          90
                  ....*....|...
gi 808354811 1134 LVPVCIKPPVASD 1146
Cdd:cd05923    78 AVPALINPRLKAA 90
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
1092-1559 2.79e-03

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 42.45  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1092 RAERIAGLLTDRARLSRgdhVALIFPPSIDLVAAFFGCLSAGlVPVCIKPpvasdlnttlGPIRMMVDMSKAVAIL---A 1168
Cdd:PRK05851   40 RAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAG-AAVSILP----------GPVRGADDGRWADATLtrfA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1169 PQNVSKLLKSK---EAAHSIDSNAwpMILDLedapSSWRRKNnnncdttTSGSSGAASKEEICYLDFSINSSGQLQGSSM 1245
Cdd:PRK05851  106 GIGVRTVLSHGshlERLRAVDSSV--TVHDL----ATAAHTN-------RSASLTPPDSGGPAVLQGTAGSTGTPRTAIL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1246 SEASAITVCKSIKVSSELYPSRHVVvCA--PPYSGISLVlWCLSSVYSGHHTTLIPPMEVEQQPSLFLTTLSnlkvrDAF 1323
Cdd:PRK05851  173 SPGAVLSNLRGLNARVGLDAATDVG-CSwlPLYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLS-----DSR 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1324 TTYstinTCVTQLATSV---ENLRERGCNLSMLRscVAIAEERP-RIALMSSFCKLFAPLALNNRAISTSFSsrVNAAIC 1399
Cdd:PRK05851  246 ATL----TAAPNFAYNLigkYARRVSDVDLGALR--VALNGGEPvDCDGFERFATAMAPFGFDAGAAAPSYG--LAESTC 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1400 mqGASGPEPSTvyvdarALRNDRISLVGKGAPHSVALIesGKLLPGVKIAIANPETRGQCADSHLGEIwvaSIHNASpln 1479
Cdd:PRK05851  318 --AVTVPVPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEI---EIRGAS--- 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1480 rlasvtgfgdegTMNTDVYNARLTTGDtktrWARTGYLGFLrqtqsitehgeLHDAVFVVGALNESLVLRGMRYHPFDVE 1559
Cdd:PRK05851  382 ------------MMSGYLGQAPIDPDD----WFPTGDLGYL-----------VDGGLVVCGRAKELITVAGRNIFPTEIE 434
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
1053-1137 2.91e-03

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 42.31  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1053 PLLECLRSRAQSSPDHriLTLVTSKNaeqdTATCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSA 1132
Cdd:cd05920    16 PLGDLLARSAARHPDR--IAVVDGDR----RLTYRELDRRADRLAAGLRGLG-IRPGDRVVVQLPNVAEFVVLFFALLRL 88

                  ....*
gi 808354811 1133 GLVPV 1137
Cdd:cd05920    89 GAVPV 93
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
565-745 3.04e-03

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 42.06  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  565 PSRDWTAPPrLADETIAYIEYTTGNDGTVKGCCVTRQAVFAHCRALTTAMEykedetmvcvVDFKREVG-----LWHA-- 637
Cdd:PRK05851  140 TNRSASLTP-PDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG----------LDAATDVGcswlpLYHDmg 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  638 ---ILASIFNGMKVIFVPYSLMKMNPATWMHMVSKYQATtaLVKSRDLHWALLA--TRDHKDISLASLRTLLvaDGANPW 712
Cdd:PRK05851  209 lafLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRAT--LTAAPNFAYNLIGkyARRVSDVDLGALRVAL--NGGEPV 284
                         170       180       190
                  ....*....|....*....|....*....|...
gi 808354811  713 SLSSCDAFAAAFtpSPYSLRPDAMCPCAGSSET 745
Cdd:PRK05851  285 DCDGFERFATAM--APFGFDAGAAAPSYGLAES 315
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
1092-1167 3.35e-03

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 41.91  E-value: 3.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808354811 1092 RAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAG--LVPVCIKPPVASdlnttlgpIRMMVDMSKAVAIL 1167
Cdd:cd17643    21 RANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGgaYVPIDPAYPVER--------IAFILADSGPSLLL 89
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
413-511 4.15e-03

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 41.52  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811  413 TQLTYGKLHSRAGKVAYMLLTKTVqvnkdgsknvmcKPGDRVALIYPNTQPLhfLAAFYGCLQAGVIPVPVEmpsskREA 492
Cdd:cd17643    11 RRLTYGELDARANRLARTLRAEGV------------GPGDRVALALPRSAEL--IVALLAILKAGGAYVPID-----PAY 71
                          90
                  ....*....|....*....
gi 808354811  493 GIAQLGFLLGNCGVKVALT 511
Cdd:cd17643    72 PVERIAFILADSGPSLLLT 90
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1046-1139 5.33e-03

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 41.24  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808354811 1046 IDDEPSLPllECLRSRAQSSPDhRILtLVTSKNAEQDTATCSTLLKRAERIA-GLLtdRARLSRGDHVALIFPPSIDLVA 1124
Cdd:COG1022     7 VPPADTLP--DLLRRRAARFPD-RVA-LREKEDGIWQSLTWAEFAERVRALAaGLL--ALGVKPGDRVAILSDNRPEWVI 80
                          90
                  ....*....|....*
gi 808354811 1125 AFFGCLSAGLVPVCI 1139
Cdd:COG1022    81 ADLAILAAGAVTVPI 95
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
1085-1141 5.47e-03

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 41.12  E-value: 5.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 808354811 1085 TCSTLLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKP 1141
Cdd:cd05934     5 TYAELLRESARIAAALAALG-IRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINT 60
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
1092-1141 6.04e-03

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 40.91  E-value: 6.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 808354811 1092 RAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAGLVPVCIKP 1141
Cdd:cd05919    19 GANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP 67
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1089-1137 6.97e-03

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 41.38  E-value: 6.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 808354811 1089 LLKRAERIAGLLtdRAR-LSRGDHVALIFPPSIDLVAAFFGCLSAG--LVPV 1137
Cdd:COG1020   507 LNARANRLAHHL--RALgVGPGDLVGVCLERSLEMVVALLAVLKAGaaYVPL 556
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
1089-1137 9.46e-03

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 40.66  E-value: 9.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808354811 1089 LLKRAERIAGLLTDRArLSRGDHVALIFPPSIDLVAAFFGCLSAG--LVPV 1137
Cdd:PRK07656   36 LNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGALKAGavVVPL 85
 
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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