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Conserved domains on  [gi|937914749|dbj|BAS89668|]
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Os04g0473900 [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 591-1151 0e+00

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: 590.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  591 YTWINEEGKLMNRRTYQELHGNASYIAQKLLTSTKPvikpGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPmqsg 670
Cdd:cd05931    12 YTFLDDEGGREETLTYAELDRRARAIAARLQAVGKP----GDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTP---- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  671 GQALLKVENISKMCNAVAILSTSSYHAAVRAgyiknivTLAKRVQKCSAQWPDIPWIHTDSwiknyrrssdsfnSDTVLF 750
Cdd:cd05931    84 GRHAERLAAILADAGPRVVLTTAAALAAVRA-------FAASRPAAGTPRLLVVDLLPDTS-------------AADWPP 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  751 TKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFS 830
Cdd:cd05931   144 PSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  831 PMIFIRNPLLWLQTINDYHGTHSAGPNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEG 910
Cdd:cd05931   224 PAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPE 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  911 VLAPGYGLAENCVYVTCAFGECKPVFI-------------------DWQGRVCCGYVeqdDTDTLIRIVDPDSLTEhQED 971
Cdd:cd05931   304 AFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpAARELVSCGRP---LPDQEVRIVDPETGRE-LPD 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  972 GVEGEIWISSPSSGVGYWGNSEMSQRTFFNqLKNHPNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTV 1051
Cdd:cd05931   380 GEVGEIWVRGPSVASGYWGRPEATAETFGA-LAATDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATA 458

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1052 ESSSEVLRPGCCAVVGIPEEvlaqkgisipdssDQVGLVVIAEV--REGKAVSKEVVNNIKARVVEEHGVAVASVKLIKP 1129
Cdd:cd05931   459 EEAHPALRPGCVAAFSVPDD-------------GEERLVVVAEVerGADPADLAAIAAAIRAAVAREHGVAPADVVLVRP 525

                         570       580
                  ....*....|....*....|..
gi 937914749 1130 RTICKTTSGKIRRFECMRQFVD 1151
Cdd:cd05931   526 GSIPRTSSGKIQRRACRAAYLD 547
AOS cd08151
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ...
 1897-2226 4.82e-155

Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene oxide, which is an unstable epoxide. In corals, the enzyme is part of a eiconaosid synthesis pathway that is initiated by a lipoxygenase, which generates the fatty acid hydroperoxides in the first step. The structure of allene oxide synthase closely resembles that of catalase, but allene oxide synthase does not have catalase activity.


:

Pssm-ID: 163707  Cd Length: 328  Bit Score: 483.08  E-value: 4.82e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1897 EEMDQAYKKIVGNLAANLAITTMNVKSRYFHRIGVSGRGVLRMYEEIPsFPRHKIFASGKSFPVIVRHSNSLSADDDARL 1976
Cdd:cd08151     1 EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESD-FPEHAFFTAGKRFPVILRHANIVGGDDDASL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1977 DARGAAVRILSDNDGEAPLLDLTLKSGKAFYARTIADFATWLVCGLPAREEQVKRS-PHIRDAVWGSL-RSTDSYTVLHY 2054
Cdd:cd08151    80 DGRGAALRFLNAGDDDAGPLDLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRgPLARYAVWASLrRAPDSYTDLHY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 2055 YSNICRLLRFDDGREMYAKFKLRPADPDVPEDSGKVVPRGILPPETGAIPRDEDDTRPLLFLADDFRRRVGSPdGVRYVF 2134
Cdd:cd08151   160 YSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYLRNEFRQRLQSP-GVRYRL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 2135 QLQLREVPTDaaARDVALDCTRPWDEAEFPYIDVGEVSIGRNLPTEETEKLEFNPfLRCPEVDVIPATSCAQ-SASIDHG 2213
Cdd:cd08151   239 QIQLREVSDD--ATAVALDCCRPWDEDEHPWLDLAVVRLGAPLPNDELEKLAFNP-GNTPESLGLPLAYCADdYASLGHL 315

                         330
                  ....*....|...
gi 937914749 2214 RSLVYEICQRLRN 2226
Cdd:cd08151   316 RSLVYEISQRLRK 328
NRPS_term_dom super family cl37094
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 1493-1892 2.14e-28

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


The actual alignment was detected with superfamily member TIGR02353:

Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 124.09  E-value: 2.14e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1493 IWSVDFVKWWAlnkAQALAAKMLAVHLKGTIFLNYWFKMQGARIGSSVVIDTV--DITDpsLLTVADGAVLAEGALVQGH 1570
Cdd:TIGR02353   75 IWGSTYLRFWT---VKRLVDAAPTVLLSGSPLYSLYLRALGAKIGKGVDIGSLppVCTD--LLTIGAGTIVRKEVMLLGY 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1571 EVCNEVLSFRPIWIGCEASIGPYAVLQKGTVVEDGAVVPPLQKTGAGKSTRRTSR--TSVSIKKEAAKANMILEHLV-SI 1647
Cdd:TIGR02353  150 RAERGRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIPDGERwhGSPAQKTGADYRKVQPARPYtVR 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1648 YAVGILGALSgaIVYTLYTHLSGKAASPLhfsfaciAGAFhWLPAAITAYAVIvqetptsALSFALFTAFADLSYGVILS 1727
Cdd:TIGR02353  230 RRLYVAGALF--VVFVLLPPLAFLFAIPV-------AITF-DEIDWTLGPDMV-------GFILALVLTFVALAGFIAYT 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1728 ILTSITSRAL---AAKPGTK--QNGIASLIHRRITISAHVRFAKMLSG-TEAFCVYLRLLGAKIGRHCSIRAINpVANPE 1801
Cdd:TIGR02353  293 VLLLAAVRLLlnlVLKPGRYyvHSGFYYQAWTVQQLMDNSRVLLFPLYaSSYIPHWYRALGAKIGKVAEISSAQ-HEVPD 371

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1802 LISVGDGVHLGDFCNIVPGFYSKGGFTSAEIKVQENTVVGSGSLLLPGCVLQENVILGALSVAPENAVLRRGGVYVGS-- 1879
Cdd:TIGR02353  372 LTDIGEETFIADGLLMGNARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGSpp 451

                          410
                   ....*....|....
gi 937914749  1880 -QSPAMVKNTLLDE 1892
Cdd:TIGR02353  452 fELPRRVNRDDELE 465
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
105-172 1.88e-15

NAD(P)-binding Rossmann-like domain;


:

Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 72.95  E-value: 1.88e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937914749   105 IVGAGPSGLSAAYALAKLGYRnVTLFEKCHTVSGMCESIDIEGRIYDLGGQVIAANSAPVITHLAEEL 172
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLLDEL 67
YobN super family cl34196
Monoamine oxidase [Amino acid transport and metabolism];
100-343 1.94e-15

Monoamine oxidase [Amino acid transport and metabolism];


The actual alignment was detected with superfamily member COG1231:

Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 81.51  E-value: 1.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  100 DTRIGIVGAGPSGLSAAYALAKLGYRnVTLFE-------KCHTVSGmcesiDIEGRIYDLGGQVIAANSaPVITHLAEEL 172
Cdd:COG1231     7 GKDVVIVGAGLAGLAAARELRKAGLD-VTVLEardrvggRVWTLRF-----GDDGLYAELGAMRIPPSH-TNLLALAREL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  173 G-SDFEEMDTHKLSLIDSQTGNIRDLEVAEDYVSMVSLTLKLQDEANKSGRAGLHALSGLASDPTHEFLKQNGINSMPKS 251
Cdd:COG1231    80 GlPLEPFPNENGNALLYLGGKRVRAGEIAADLRGVAELLAKLLRALAAALDPWAHPAAELDRESLAEWLRRNGASPSARR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  252 VAYGYTASGYG-------FVQDMPYAFIQEFtrtsmAGKIRRFKHGYMSMWERLSKSLPFEVFCDTQVLNVKRNscGANV 324
Cdd:COG1231   160 LLGLLGAGEYGadpdelsLLDLLRYAASAGG-----GAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIRQD--GDGV 232

                         250
                  ....*....|....*....
gi 937914749  325 TIKNNNGEkqVLEFDKIIL 343
Cdd:COG1231   233 TVTTDDGG--TVRADAVIV 249
NRPS_term_dom super family cl37094
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 2279-2489 7.94e-15

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


The actual alignment was detected with superfamily member TIGR02353:

Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 80.57  E-value: 7.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  2279 LWATLCQPLLQTLVPYSVLGLVIFLPLR--GLLAVAAATRFPLYWLLPAF-WAASGVAAMATCAAAKWALVGsRVDGDTV 2355
Cdd:TIGR02353  476 RLARKNVENLRIILPFLLVQWAMLFALVvlDLQALDDYTEWGAVALLAALiLMAVGVGAFLILVERKWLVFG-RLKPQEH 554

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  2356 HIWSPAVFL-DTVWQAVRAATAEYFAELTPGSAPFAAWMRVMGASVspGDGVYVDsmGALLnPE--MVRLERGAAVGRDA 2432
Cdd:TIGR02353  555 PLWSPFVWLhELHWKLYESVAVPNFLRPFRGTPFLPAILRLLGVKI--GRGVYID--GTDL-TErdLVTIGDDSTLNEGS 629

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 937914749  2433 LLFGHVYEGEAGKVKFgaVSVGEDGFVGSRAVAMPSVTVDDGGCLAALGLAMKGETV 2489
Cdd:TIGR02353  630 VIQTHLFEDRVMKSDT--VTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKGEEV 684
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1205-1279 4.62e-08

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


:

Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 52.16  E-value: 4.62e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749 1205 NEITEFLTQIVSEHTGISKDKISLTDSL-PSYGFDSIAVVRAAQKLSDFLGVPVGAIDIFTASCISELASFLENLV 1279
Cdd:COG0236     4 EELEERLAEIIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1300-1371 6.84e-08

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


:

Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 51.78  E-value: 6.84e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937914749 1300 IIEFLTKIVSDQTGIPKDKISPMDSL-PSYGFDSIAVVQAAQKLSDFLGVPVGAIDIFTAGCISELATFLENL 1371
Cdd:COG0236     6 LEERLAEIIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
 
Name Accession Description Interval E-value
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 591-1151 0e+00

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: 590.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  591 YTWINEEGKLMNRRTYQELHGNASYIAQKLLTSTKPvikpGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPmqsg 670
Cdd:cd05931    12 YTFLDDEGGREETLTYAELDRRARAIAARLQAVGKP----GDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTP---- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  671 GQALLKVENISKMCNAVAILSTSSYHAAVRAgyiknivTLAKRVQKCSAQWPDIPWIHTDSwiknyrrssdsfnSDTVLF 750
Cdd:cd05931    84 GRHAERLAAILADAGPRVVLTTAAALAAVRA-------FAASRPAAGTPRLLVVDLLPDTS-------------AADWPP 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  751 TKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFS 830
Cdd:cd05931   144 PSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  831 PMIFIRNPLLWLQTINDYHGTHSAGPNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEG 910
Cdd:cd05931   224 PAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPE 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  911 VLAPGYGLAENCVYVTCAFGECKPVFI-------------------DWQGRVCCGYVeqdDTDTLIRIVDPDSLTEhQED 971
Cdd:cd05931   304 AFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpAARELVSCGRP---LPDQEVRIVDPETGRE-LPD 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  972 GVEGEIWISSPSSGVGYWGNSEMSQRTFFNqLKNHPNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTV 1051
Cdd:cd05931   380 GEVGEIWVRGPSVASGYWGRPEATAETFGA-LAATDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATA 458

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1052 ESSSEVLRPGCCAVVGIPEEvlaqkgisipdssDQVGLVVIAEV--REGKAVSKEVVNNIKARVVEEHGVAVASVKLIKP 1129
Cdd:cd05931   459 EEAHPALRPGCVAAFSVPDD-------------GEERLVVVAEVerGADPADLAAIAAAIRAAVAREHGVAPADVVLVRP 525

                         570       580
                  ....*....|....*....|..
gi 937914749 1130 RTICKTTSGKIRRFECMRQFVD 1151
Cdd:cd05931   526 GSIPRTSSGKIQRRACRAAYLD 547
AOS cd08151
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ...
 1897-2226 4.82e-155

Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene oxide, which is an unstable epoxide. In corals, the enzyme is part of a eiconaosid synthesis pathway that is initiated by a lipoxygenase, which generates the fatty acid hydroperoxides in the first step. The structure of allene oxide synthase closely resembles that of catalase, but allene oxide synthase does not have catalase activity.


Pssm-ID: 163707  Cd Length: 328  Bit Score: 483.08  E-value: 4.82e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1897 EEMDQAYKKIVGNLAANLAITTMNVKSRYFHRIGVSGRGVLRMYEEIPsFPRHKIFASGKSFPVIVRHSNSLSADDDARL 1976
Cdd:cd08151     1 EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESD-FPEHAFFTAGKRFPVILRHANIVGGDDDASL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1977 DARGAAVRILSDNDGEAPLLDLTLKSGKAFYARTIADFATWLVCGLPAREEQVKRS-PHIRDAVWGSL-RSTDSYTVLHY 2054
Cdd:cd08151    80 DGRGAALRFLNAGDDDAGPLDLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRgPLARYAVWASLrRAPDSYTDLHY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 2055 YSNICRLLRFDDGREMYAKFKLRPADPDVPEDSGKVVPRGILPPETGAIPRDEDDTRPLLFLADDFRRRVGSPdGVRYVF 2134
Cdd:cd08151   160 YSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYLRNEFRQRLQSP-GVRYRL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 2135 QLQLREVPTDaaARDVALDCTRPWDEAEFPYIDVGEVSIGRNLPTEETEKLEFNPfLRCPEVDVIPATSCAQ-SASIDHG 2213
Cdd:cd08151   239 QIQLREVSDD--ATAVALDCCRPWDEDEHPWLDLAVVRLGAPLPNDELEKLAFNP-GNTPESLGLPLAYCADdYASLGHL 315

                         330
                  ....*....|...
gi 937914749 2214 RSLVYEICQRLRN 2226
Cdd:cd08151   316 RSLVYEISQRLRK 328
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 605-1155 6.11e-97

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 326.13  E-value: 6.11e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTKPvikpGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVlppdPMQSGGQALLKVENISKMC 684
Cdd:PRK05850   37 TWSQLYRRTLNVAEELRRHGST----GDRAVILAPQGLEYIVAFLGALQAGLIAVPL----SVPQGGAHDERVSAVLRDT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 NAVAILSTSSYHAAVRagyiknivtlaKRVQKCSAQwPDIPWIHTDSWIKNYRRSSDSFNSDtvlftkpqPSDLCFLQFT 764
Cdd:PRK05850  109 SPSVVLTTSAVVDDVT-----------EYVAPQPGQ-SAPPVIEVDLLDLDSPRGSDARPRD--------LPSTAYLQYT 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  765 SGSTGDAKGVMITHEGLIHNVKTMKKRY------RSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMIFIRNP 838
Cdd:PRK05850  169 SGSTRTPAGVMVSHRNVIANFEQLMSDYfgdtggVPPPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTSPVAFLQRP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  839 LLWLQTINDYHGTHSAGPNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYGL 918
Cdd:PRK05850  249 ARWMQLLASNPHAFSAAPNFAFELAVRKTSDDDMAGLDLGGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGL 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  919 AENCVYV-TCAFGEC-KPVFIDWQgRVCCGYVEQDDTDT-------------LIRIVDPDSLTEHQeDGVEGEIWISSPS 983
Cdd:PRK05850  329 AEATVYVaTREPGQPpESVRFDYE-KLSAGHAKRCETGGgtplvsygsprspTVRIVDPDTCIECP-AGTVGEIWVHGDN 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  984 SGVGYWGNSEMSQRTFFNQLKN----HPNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVEsssEVLR 1059
Cdd:PRK05850  407 VAAGYWQKPEETERTFGATLVDpspgTPEGPWLRTGDLGFISEGELFIVGRIKDLLIVDGRNHYPDDIEATIQ---EITG 483

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1060 pGCCAVVGIPEevlaqkgisipDSSDQvgLVVIAEVREGKAVSKEVVNN---IKARVV----EEHGVAVASVKLIKPRTI 1132
Cdd:PRK05850  484 -GRVAAISVPD-----------DGTEK--LVAIIELKKRGDSDEEAMDRlrtVKREVTsaisKSHGLSVADLVLVAPGSI 549

                         570       580
                  ....*....|....*....|...
gi 937914749 1133 CKTTSGKIRRFECMRQFVDNTLS 1155
Cdd:PRK05850  550 PITTSGKIRRAACVEQYRQDEFT 572
FAAL_FadD32 NF038339
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ...
 627-1154 8.75e-92

long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker enzyme for the biosynthesis of the type of mycolic acids, the very large "eumycolic acids", found in Mycobacterium.


Pssm-ID: 468483 [Multi-domain]  Cd Length: 625  Bit Score: 312.81  E-value: 8.75e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  627 VIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPD-PMQSGgqallKVENISKMCNAVAILSTSSYHAAVRAGYIK 705
Cdd:NF038339   72 VTKPGDRVAILAPQGLDYVVSFFAAIYAGNIAVPLFDPDePGHTD-----RLHAVLGDCKPSAILTATSSAEGVRKFFRS 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  706 NIVTLAKRVQKCSAqwpdIPWIHTDSWIKnyrrssdsfnsdtvlftkPQPS--DLCFLQFTSGSTGDAKGVMITHEGLIH 783
Cdd:NF038339  147 LPAKERPRVIAVDA----VPDSVGSTWVR------------------PDADldDIAYLQYTSGSTRVPAGVEITHRAVAT 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  784 NVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALvsGGTSVLF-SPMIFIRNPLLW---LQTINDYHGTHSAGPNFA 859
Cdd:NF038339  205 NVLQMVDAIELDENSRGVTWLPLFHDMGLLTVILPAL--GGKYITImSPAAFVRRPGRWireLAAVSDGAGTFAAAPNFA 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  860 FELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYGLAENCVYV--TCAFGECKPVFI 937
Cdd:NF038339  283 FEHAAARGLPKEGEPLDLSNVIGLINGSEPVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVssTPREDEAKVIYV 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  938 DW----QGR--------------VCCGYVEQDDTDTlirIVDPDSLTEhQEDGVEGEIWISSPSSGVGYWGNSEMSQRTF 999
Cdd:NF038339  363 DReelnAGRivevdpdapnavaqVSCGYVARSQWAV---IVDPETGTE-LPDGQVGEIWLHGNNIGTGYWGRPEETEETF 438

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1000 FNQLKNH-----------PNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRPGCCAVVGI 1068
Cdd:NF038339  439 HNKLKSRleegshaegapEDANWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYPQDLEYSAQEASKALRPGFVAAFSV 518

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1069 PEEVLAQKGISIP---------DSSDQvgLVVIAE--VREGKAVSKEVVNNIKARVVEEHGVAVASVKLIKPRTICKTTS 1137
Cdd:NF038339  519 PANQLPAEVFENShsglkydadDSSEQ--LVIVAEraPGAGKADPQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSS 596

                         570
                  ....*....|....*..
gi 937914749 1138 GKIRRFECMRQFVDNTL 1154
Cdd:NF038339  597 GKIARRACKAAYIDGTL 613
FadD32_Coryne NF040633
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ...
 627-1151 6.60e-88

FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus Corynebacterium, are most similar to the key mycolic acid biosynthesis protein FadD32 of any fatty acid--AMP ligase in Mycobacterium tuberculosis, and are likewise encoded next to Pks13. However, as the mycolic acids produced in Corynebacterium and in Mycobacterium differ substantially, it is not clear that assigning the same name in Corynebacterium is appropriate.


Pssm-ID: 468603 [Multi-domain]  Cd Length: 613  Bit Score: 301.18  E-value: 6.60e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  627 VIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLppDPMQSGGQALLKVenISKMCNAVAILSTSSYHAAVRAgYIKN 706
Cdd:NF040633   82 VGKPGDRVAILANNSPEYIFGFLGALYAGMVPVPLY--DPNEPGHADHLRA--VLADSGPTVVLTNKTSAPAVRA-HFAD 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  707 IVtlakrvqkcSAQWPDIPWIHT--DSWIKNYRRSSDSFNSDTVLFTKPQ-PSDL-CFLQFTSGSTGDAKGVMITHEGLI 782
Cdd:NF040633  157 LP---------AAERPRILSVDSlpDSLAESWVNPMATIEGQPLLAPAGTdPSDDtAFLQYTSGSTRTPAGVVLTNRSIV 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  783 HNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFtALVSGGTSVLFSPMIFIRNPLLWLQTIN---DYHGTHSAGPNFA 859
Cdd:NF040633  228 TNVLQIFTAAQLKTPLRLVSWLPLHHDMGIILAAF-VTILGLEFELMSPRDFIQQPKRWVDQLSrreDDVNVYTVVPNFA 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  860 FELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYGLAENCVYVTCAFGECKPVFIDW 939
Cdd:NF040633  307 LELAARYANPEEGEDLDLSAVDGIIIGSEPVTEKAVDAFLDAFGPYGLRRTALRPSYGLAEASLLVTTPQTEERPLFTYF 386

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  940 ------QGRVCCgyVEQDDTDTL-------------IRIVDPDSLTEhQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFF 1000
Cdd:NF040633  387 drealaEGRAVE--VAEDSENAVpfasngqvvrpqvLAIVDPETGQE-LPDGTVGEIWVHGDNMAAGYLDREEETAETFR 463

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1001 NQLKNH----------PNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRPGCCAVVGIPE 1070
Cdd:NF040633  464 NTLGERlaensraegaPEDNWMATGDLGVIVDGELYITGRLKDLIVIAGRNHYPQDIEATVQEASDHIRPDSVAAFAVPG 543

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1071 EvlaqkgisipdssDQVGLVVIAEVREGKAVSK--EVVNNIKARVVEEHGVAVASVKLIKPRTICKTTSGKIRRFECMRQ 1148
Cdd:NF040633  544 D-------------DVEKLVILAERDDEADESGdaEAIEAIRAAVTSAHGVVPADIRIVAPGEIARSSSGKIARRVNAKA 610


                  ...
gi 937914749 1149 FVD 1151
Cdd:NF040633  611 YLE 613
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 603-1155 1.66e-82

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: 279.77  E-value: 1.66e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPdpmqsggqalLKVENISK 682
Cdd:COG0318    24 RLTYAELDARARRLAAALRALG---VGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPR----------LTAEELAY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  683 MCNavailstssyHAAVRAgyiknIVTlakrvqkcsaqwpdipwihtdswiknyrrssdsfnsdtvlftkpqpsdlCFLQ 762
Cdd:COG0318    91 ILE----------DSGARA-----LVT-------------------------------------------------ALIL 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  763 FTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPmifiRNPLLWL 842
Cdd:COG0318   107 YTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPR----FDPERVL 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  843 QTINDYHGTHSAGPNFAFELVIRRLEAEKnkvYDLSSMVFLMIAAEPVRQKTVRRFIELTQPfglsegVLAPGYGLAENC 922
Cdd:COG0318   183 ELIERERVTVLFGVPTMLARLLRHPEFAR---YDLSSLRLVVSGGAPLPPELLERFEERFGV------RIVEGYGLTETS 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  923 VYVTCAFGECKPVFIDWQGRVCCGyVEqddtdtlIRIVDPDslTEHQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFFNQ 1002
Cdd:COG0318   254 PVVTVNPEDPGERRPGSVGRPLPG-VE-------VRIVDED--GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG 323

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1003 lknhpnkkFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEVLAQKgisip 1081
Cdd:COG0318   324 --------WLRTGDLGRlDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAE---AAVVGVPDEKWGER----- 387

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1082 dssdqvgLVVIAEVREGKAVSKEvvnNIKARVVEehgvAVASVKLikPRTIC------KTTSGKIRRFECMRQFVDNTLS 1155
Cdd:COG0318   388 -------VVAFVVLRPGAELDAE---ELRAFLRE----RLARYKV--PRRVEfvdelpRTASGKIDRRALRERYAAGALE 451
FAAL_FadD21 NF038337
fatty-acid--AMP ligase FAAL21/FadD21;
631-1149 3.42e-74

fatty-acid--AMP ligase FAAL21/FadD21;


Pssm-ID: 439631 [Multi-domain]  Cd Length: 579  Bit Score: 260.19  E-value: 3.42e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  631 GDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPmqsgGQALLKVENISKMCNAVAILSTSSYHAAVrAGYIKnivtl 710
Cdd:NF038337   62 GDRAVILAPQGLPYIVAFLGAMQAGLIAVPLSVPQP----GSHDERVSAVLADTSPSVVLTTSAAAAAV-AEYLH----- 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  711 akrvQKCSAQWPDIpwIHTDSWiknyrrSSDSFNSDTVLFTkpQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKK 790
Cdd:NF038337  132 ----RPDTGAVPAV--IEIDSL------DLDGPNSPSIRIS--DAPSIAYLQYTSGSTRLPAGVMVSHRNLQVNFQQLMA 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  791 RYRSTSK------TVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMIFIRNPLLWLQTINDYHGTHSAGPNFAFELVI 864
Cdd:NF038337  198 AYFPDTNgvaprdTTIVSWLPFYHDMGLVLGVIAPILGGYRSELTSPVAFLQRPARWIHAMANGSPVFSAAPNFAFELAV 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  865 RRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYGLAENCVYVTCAFGECKPVFIDWQ-GRV 943
Cdd:NF038337  278 RKTTDADLAGLDLGNVIGIVSGAERIHPATLDRFCKRFAPYNFREDMMQPSYGLAEATVYVASRAEGGAPEVVHFEpEKL 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  944 CCGYVEQDDTDT-------------LIRIVDPDSLTEhQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFFNQLKN----H 1006
Cdd:NF038337  358 SEGSAQRCEARTgspllsygtptspTVRIVDPDTCIE-CPAGTVGEIWVHGDNVAEGYWQKPEETRRTFGGVLANpspgT 436

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1007 PNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVEsssevlrpgccAVVGipEEVLAqkgISIP-DSSD 1085
Cdd:NF038337  437 PEGPWLRTGDLGFISEDEMFIVGRMKDLLIVYGRNHYPEDIESTVQ-----------EITG--GRVAA---ISVPvDETE 500

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937914749 1086 QvgLVVIAEVR-------EGKAVSKEVVNNIKARVVEEHGVAVASVKLIKPRTICKTTSGKIRRFECMRQF 1149
Cdd:NF038337  501 K--LVTIIELKkrgdsdeEAMRKLDAVKNNVTAAISRSHGLNVADLVLVPPGSIPTTTSGKIRRAACVEQY 569
AMP-binding pfam00501
AMP-binding enzyme;
602-1038 6.88e-67

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 233.36  E-value: 6.88e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   602 NRRTYQELHGNASYIAqKLLTSTKpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVlppDPMQSGGQallkVENIS 681
Cdd:pfam00501   20 RRLTYRELDERANRLA-AGLRALG--VGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPL---NPRLPAEE----LAYIL 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   682 KMCNAVAILstssyhaAVRAGYIKNIVTLAKRVQKCSAqwpdIPWIHTDSWIKN--YRRSSDSFNSDTVLFTKPQPSDLC 759
Cdd:pfam00501   90 EDSGAKVLI-------TDDALKLEELLEALGKLEVVKL----VLVLDRDPVLKEepLPEEAKPADVPPPPPPPPDPDDLA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   760 FLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRS----TSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMIFi 835
Cdd:pfam00501  159 YIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA- 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   836 RNPLLWLQTINDYHGTHSAGPNFAFELVirrLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELtqpFGlseGVLAPG 915
Cdd:pfam00501  238 LDPAALLELIERYKVTVLYGVPTLLNML---LEAGAPKRALLSSLRLVLSGGAPLPPELARRFREL---FG---GALVNG 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   916 YGLAENCVYVTCAF-GECKPVFIDWQGRVCCGyveqddtdTLIRIVDPDSLtEHQEDGVEGEIWISSPSSGVGYWGNSEM 994
Cdd:pfam00501  309 YGLTETTGVVTTPLpLDEDLRSLGSVGRPLPG--------TEVKIVDDETG-EPVPPGEPGELCVRGPGVMKGYLNDPEL 379

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 937914749   995 SQRTFFnqlknhpNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVA 1038
Cdd:pfam00501  380 TAEAFD-------EDGWYRTGDLGRrDEDGYLEIVGRKKDQIKLG 417
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 605-1031 7.08e-36

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: 142.79  E-value: 7.08e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   605 TYQELHGNASYIAQKLLTSTKpvIKPGDRVLlIHLP-GLEFIDAFFGCIRAGVIPVPVLPPDPMQsggqallKVENISKM 683
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGG--VGPGDRVA-VLLErSAELVVAILAVLKAGAAYVPLDPAYPAE-------RLAFILED 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   684 CNAVAILSTSSyHAAVRAGYIKNIVTLAkrvqkcsaqwPDIPWIHTDSwiknyrrssdsfNSDTVLFTKPQPSDLCFLQF 763
Cdd:TIGR01733   71 AGARLLLTDSA-LASRLAGLVLPVILLD----------PLELAALDDA------------PAPPPPDAPSGPDDLAYVIY 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   764 TSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIgGLFTALVSGGTSVLFSPMIFIRNPLLWLQ 843
Cdd:TIGR01733  128 TSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPEDEERDDAALLAA 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   844 TINDYHGTHSAGPNFAFELvirrLEAEknKVYDLSSMVFLMIAAEPVRQKTVRRFIELtqpfgLSEGVLAPGYGLAENCV 923
Cdd:TIGR01733  207 LIAEHPVTVLNLTPSLLAL----LAAA--LPPALASLRLVILGGEALTPALVDRWRAR-----GPGARLINLYGPTETTV 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   924 YVTCAfgECKPVFIDWQGRVCCGYVEqddTDTLIRIVDPDslTEHQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFFnql 1003
Cdd:TIGR01733  276 WSTAT--LVDPDDAPRESPVPIGRPL---ANTRLYVLDDD--LRPVPVGVVGELYIGGPGVARGYLNRPELTAERFV--- 345

                          410       420       430
                   ....*....|....*....|....*....|....
gi 937914749  1004 kNHP-----NKKFTRTGDLGR-TIDGNLFITGRI 1031
Cdd:TIGR01733  346 -PDPfaggdGARLYRTGDLVRyLPDGNLEFLGRI 378
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 1493-1892 2.14e-28

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 124.09  E-value: 2.14e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1493 IWSVDFVKWWAlnkAQALAAKMLAVHLKGTIFLNYWFKMQGARIGSSVVIDTV--DITDpsLLTVADGAVLAEGALVQGH 1570
Cdd:TIGR02353   75 IWGSTYLRFWT---VKRLVDAAPTVLLSGSPLYSLYLRALGAKIGKGVDIGSLppVCTD--LLTIGAGTIVRKEVMLLGY 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1571 EVCNEVLSFRPIWIGCEASIGPYAVLQKGTVVEDGAVVPPLQKTGAGKSTRRTSR--TSVSIKKEAAKANMILEHLV-SI 1647
Cdd:TIGR02353  150 RAERGRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIPDGERwhGSPAQKTGADYRKVQPARPYtVR 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1648 YAVGILGALSgaIVYTLYTHLSGKAASPLhfsfaciAGAFhWLPAAITAYAVIvqetptsALSFALFTAFADLSYGVILS 1727
Cdd:TIGR02353  230 RRLYVAGALF--VVFVLLPPLAFLFAIPV-------AITF-DEIDWTLGPDMV-------GFILALVLTFVALAGFIAYT 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1728 ILTSITSRAL---AAKPGTK--QNGIASLIHRRITISAHVRFAKMLSG-TEAFCVYLRLLGAKIGRHCSIRAINpVANPE 1801
Cdd:TIGR02353  293 VLLLAAVRLLlnlVLKPGRYyvHSGFYYQAWTVQQLMDNSRVLLFPLYaSSYIPHWYRALGAKIGKVAEISSAQ-HEVPD 371

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1802 LISVGDGVHLGDFCNIVPGFYSKGGFTSAEIKVQENTVVGSGSLLLPGCVLQENVILGALSVAPENAVLRRGGVYVGS-- 1879
Cdd:TIGR02353  372 LTDIGEETFIADGLLMGNARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGSpp 451

                          410
                   ....*....|....
gi 937914749  1880 -QSPAMVKNTLLDE 1892
Cdd:TIGR02353  452 fELPRRVNRDDELE 465
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
105-172 1.88e-15

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 72.95  E-value: 1.88e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937914749   105 IVGAGPSGLSAAYALAKLGYRnVTLFEKCHTVSGMCESIDIEGRIYDLGGQVIAANSAPVITHLAEEL 172
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLLDEL 67
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
100-343 1.94e-15

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 81.51  E-value: 1.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  100 DTRIGIVGAGPSGLSAAYALAKLGYRnVTLFE-------KCHTVSGmcesiDIEGRIYDLGGQVIAANSaPVITHLAEEL 172
Cdd:COG1231     7 GKDVVIVGAGLAGLAAARELRKAGLD-VTVLEardrvggRVWTLRF-----GDDGLYAELGAMRIPPSH-TNLLALAREL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  173 G-SDFEEMDTHKLSLIDSQTGNIRDLEVAEDYVSMVSLTLKLQDEANKSGRAGLHALSGLASDPTHEFLKQNGINSMPKS 251
Cdd:COG1231    80 GlPLEPFPNENGNALLYLGGKRVRAGEIAADLRGVAELLAKLLRALAAALDPWAHPAAELDRESLAEWLRRNGASPSARR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  252 VAYGYTASGYG-------FVQDMPYAFIQEFtrtsmAGKIRRFKHGYMSMWERLSKSLPFEVFCDTQVLNVKRNscGANV 324
Cdd:COG1231   160 LLGLLGAGEYGadpdelsLLDLLRYAASAGG-----GAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIRQD--GDGV 232

                         250
                  ....*....|....*....
gi 937914749  325 TIKNNNGEkqVLEFDKIIL 343
Cdd:COG1231   233 TVTTDDGG--TVRADAVIV 249
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 101-173 3.19e-15

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 80.65  E-value: 3.19e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937914749  101 TRIGIVGAGPSGLSAAYALAKLGYRnVTLFEKCHTVSGMCESIDIEGRIYDLGGQVIAANSaPVITHLAEELG 173
Cdd:COG1232     2 KRVAVIGGGIAGLTAAYRLAKAGHE-VTVLEASDRVGGLIRTVEVDGFRIDRGPHSFLTRD-PEVLELLRELG 72
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 2279-2489 7.94e-15

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 80.57  E-value: 7.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  2279 LWATLCQPLLQTLVPYSVLGLVIFLPLR--GLLAVAAATRFPLYWLLPAF-WAASGVAAMATCAAAKWALVGsRVDGDTV 2355
Cdd:TIGR02353  476 RLARKNVENLRIILPFLLVQWAMLFALVvlDLQALDDYTEWGAVALLAALiLMAVGVGAFLILVERKWLVFG-RLKPQEH 554

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  2356 HIWSPAVFL-DTVWQAVRAATAEYFAELTPGSAPFAAWMRVMGASVspGDGVYVDsmGALLnPE--MVRLERGAAVGRDA 2432
Cdd:TIGR02353  555 PLWSPFVWLhELHWKLYESVAVPNFLRPFRGTPFLPAILRLLGVKI--GRGVYID--GTDL-TErdLVTIGDDSTLNEGS 629

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 937914749  2433 LLFGHVYEGEAGKVKFgaVSVGEDGFVGSRAVAMPSVTVDDGGCLAALGLAMKGETV 2489
Cdd:TIGR02353  630 VIQTHLFEDRVMKSDT--VTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKGEEV 684
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1748-1894 1.20e-09

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 58.73  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1748 IASLIHRRITISAHVRFAKMlsgteafcVYLRLLGAKIGRHCSIRAINPVANPELISVGDGVHLGDFCNIVPGFY----- 1822
Cdd:COG0110     1 MKLLLLFGARIGDGVVIGPG--------VRIYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHpiddp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749 1823 SKGGFTSAEIKVQENTVVGSGSLLLPGCVLQENVILGALSVA----PENAvlrrggVYVGsqSPAMVKNTLLDEDE 1894
Cdd:COG0110    73 ATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVtkdvPPYA------IVAG--NPARVIRKRDEEER 140
PRK07233 PRK07233
hypothetical protein; Provisional
 102-173 2.56e-09

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 62.21  E-value: 2.56e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749  102 RIGIVGAGPSGLSAAYALAKLGYRnVTLFEKCHTVSGMCESIDIEG----RIYdlggQVIAANSAPVItHLAEELG 173
Cdd:PRK07233    1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAASFEFGGlpieRFY----HHIFKSDEALL-ELLDELG 70
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 1782-1903 1.48e-08

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 55.88  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1782 GAKIGRHCSIRA-INPvanpelISVGDGVHLGDFCNI--VPGFyskggftSAEI---------------KVQENTVVGSG 1843
Cdd:cd04645    23 GSSVWFGAVLRGdVNP------IRIGERTNIQDGSVLhvDPGY-------PTIIgdnvtvghgavlhgcTIGDNCLIGMG 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937914749 1844 SLLLPGCVLQENVILGALSVAPENAVLRRGGVYVGsqSPAMVKNTLLDED-ERIEEMDQAY 1903
Cdd:cd04645    90 AIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAG--SPAKVVRELTDEEiAELRESAEHY 148
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1205-1279 4.62e-08

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 52.16  E-value: 4.62e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749 1205 NEITEFLTQIVSEHTGISKDKISLTDSL-PSYGFDSIAVVRAAQKLSDFLGVPVGAIDIFTASCISELASFLENLV 1279
Cdd:COG0236     4 EELEERLAEIIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1300-1371 6.84e-08

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 51.78  E-value: 6.84e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937914749 1300 IIEFLTKIVSDQTGIPKDKISPMDSL-PSYGFDSIAVVQAAQKLSDFLGVPVGAIDIFTAGCISELATFLENL 1371
Cdd:COG0236     6 LEERLAEIIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1209-1270 1.06e-07

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 50.64  E-value: 1.06e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937914749  1209 EFLTQIVSEHTGISKDKISLTDSLPSYGFDSIAVVRAAQKLSDFLGVPVGAIDIFTASCISE 1270
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1302-1363 1.15e-07

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 50.64  E-value: 1.15e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937914749  1302 EFLTKIVSDQTGIPKDKISPMDSLPSYGFDSIAVVQAAQKLSDFLGVPVGAIDIFTAGCISE 1363
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 111-393 8.20e-06

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 50.95  E-value: 8.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   111 SGLSAAYALAKLGyRNVTLFEKCHTVSGMCESIDIEGRIYDLGGQVIaANSAPVITHLAEELG--SDFEEMDTHKLSLID 188
Cdd:pfam01593    2 AGLAAARELLRAG-HDVTVLEARDRVGGRIRTVRDDGFLIELGAMWF-HGAQPPLLALLKELGleDRLVLPDPAPFYTVL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   189 SQTGNI---------RDLEVAEDYVSMVSLTLKLQDEANKSGRAGLHALsGLASDPTHEFLKQNGINSMPKSVAYGYTAS 259
Cdd:pfam01593   80 FAGGRRypgdfrrvpAGWEGLLEFGRLLSIPEKLRLGLAALASDALDEF-DLDDFSLAESLLFLGRRGPGDVEVWDRLID 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   260 GYGFvQDMPY----------------AFIQEFTRTSMAGKIRRFKHGYMSMWERLSKSLP-FEVFCDTQVLNVKRNSCGA 322
Cdd:pfam01593  159 PELF-AALPFasgafagdpselsaglALPLLWALLGEGGSLLLPRGGLGALPDALAAQLLgGDVRLNTRVRSIDREGDGV 237

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749   323 NVTIKnnNGEkqVLEFDKIILSgavafknsktyrsssltdgesevVELNNLERELFS------KVQTID--YYTTVVKI 393
Cdd:pfam01593  238 TVTLT--DGE--VIEADAVIVT-----------------------VPLGVLKRILFTpplppeKARAIRnlGYGPVNKV 289
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
2394-2474 3.21e-05

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 46.02  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 2394 RVMGASVSPGDGVYVDSMGALLNPEMVRLERGAAVGRDALLF--GHVYEG-EAGKVKFGAVSVGEDGFVGSRAVAMPSVT 2470
Cdd:COG0110    22 RIYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILtgNHPIDDpATFPLRTGPVTIGDDVWIGAGATILPGVT 101


                  ....
gi 937914749 2471 VDDG 2474
Cdd:COG0110   102 IGDG 105
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 101-170 3.78e-04

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 45.60  E-value: 3.78e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937914749   101 TRIGIVGAGPSGLSAAYALAKLGYR---NVTLFEKCHTVSGMCESIDIEGRIYDLGGQVIAANSAPVITHLAE 170
Cdd:TIGR00562    3 KHVVIIGGGISGLCAAYYLEKEIPElpvELTLVEASDRVGGKIQTVKEDGYLIERGPDSFLERKKSAPDLVKD 75
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1206-1275 1.87e-03

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 39.54  E-value: 1.87e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937914749   1206 EITEFLTQIVSEHTGI-SKDKISLTDSLPSYGFDSIAVVRAAQKLSDFLGVPVGAIDIFTASCISELASFL 1275
Cdd:smart00823   12 LLLDLVREQVAAVLGHaAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1299-1368 2.56e-03

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 39.16  E-value: 2.56e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937914749   1299 VIIEFLTKIVSDQTGIPKDKISPMD-SLPSYGFDSIAVVQAAQKLSDFLGVPVGAIDIFTAGCISELATFL 1368
Cdd:smart00823   12 LLLDLVREQVAAVLGHAAAEAIDPDrPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
PRK10502 PRK10502
putative acyl transferase; Provisional
 1775-1888 3.01e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 41.09  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1775 CVYLRLLGAKIGRHCSIRAINPVANPELISVGD--------------GVHLGDFCNIVPGFY--------SKGGF--TSA 1830
Cdd:PRK10502   44 AFLLRLFGAKIGKGVVIRPSVRITYPWKLTIGDyawigddvwlynlgEITIGAHCVISQKSYlctgshdySDPHFdlNTA 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 937914749 1831 EIKVQENTVVGSGSLLLPGCVLQENVILGALSVAPENavLRRGGVYVGsqSPAMVKNT 1888
Cdd:PRK10502  124 PIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKS--LPANTICRG--NPAVPIRP 177
 
Name Accession Description Interval E-value
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 591-1151 0e+00

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: 590.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  591 YTWINEEGKLMNRRTYQELHGNASYIAQKLLTSTKPvikpGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPmqsg 670
Cdd:cd05931    12 YTFLDDEGGREETLTYAELDRRARAIAARLQAVGKP----GDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTP---- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  671 GQALLKVENISKMCNAVAILSTSSYHAAVRAgyiknivTLAKRVQKCSAQWPDIPWIHTDSwiknyrrssdsfnSDTVLF 750
Cdd:cd05931    84 GRHAERLAAILADAGPRVVLTTAAALAAVRA-------FAASRPAAGTPRLLVVDLLPDTS-------------AADWPP 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  751 TKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFS 830
Cdd:cd05931   144 PSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  831 PMIFIRNPLLWLQTINDYHGTHSAGPNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEG 910
Cdd:cd05931   224 PAAFLRRPLRWLRLISRYRATISAAPNFAYDLCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFAPFGFRPE 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  911 VLAPGYGLAENCVYVTCAFGECKPVFI-------------------DWQGRVCCGYVeqdDTDTLIRIVDPDSLTEhQED 971
Cdd:cd05931   304 AFRPSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpAARELVSCGRP---LPDQEVRIVDPETGRE-LPD 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  972 GVEGEIWISSPSSGVGYWGNSEMSQRTFFNqLKNHPNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTV 1051
Cdd:cd05931   380 GEVGEIWVRGPSVASGYWGRPEATAETFGA-LAATDEGGWLRTGDLGFLHDGELYITGRLKDLIIVRGRNHYPQDIEATA 458

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1052 ESSSEVLRPGCCAVVGIPEEvlaqkgisipdssDQVGLVVIAEV--REGKAVSKEVVNNIKARVVEEHGVAVASVKLIKP 1129
Cdd:cd05931   459 EEAHPALRPGCVAAFSVPDD-------------GEERLVVVAEVerGADPADLAAIAAAIRAAVAREHGVAPADVVLVRP 525

                         570       580
                  ....*....|....*....|..
gi 937914749 1130 RTICKTTSGKIRRFECMRQFVD 1151
Cdd:cd05931   526 GSIPRTSSGKIQRRACRAAYLD 547
AOS cd08151
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ...
 1897-2226 4.82e-155

Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene oxide, which is an unstable epoxide. In corals, the enzyme is part of a eiconaosid synthesis pathway that is initiated by a lipoxygenase, which generates the fatty acid hydroperoxides in the first step. The structure of allene oxide synthase closely resembles that of catalase, but allene oxide synthase does not have catalase activity.


Pssm-ID: 163707  Cd Length: 328  Bit Score: 483.08  E-value: 4.82e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1897 EEMDQAYKKIVGNLAANLAITTMNVKSRYFHRIGVSGRGVLRMYEEIPsFPRHKIFASGKSFPVIVRHSNSLSADDDARL 1976
Cdd:cd08151     1 EFLDSELKKIELNLATMFAAATLKTGRRGTHTIGVGAKGVLTVLAESD-FPEHAFFTAGKRFPVILRHANIVGGDDDASL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1977 DARGAAVRILSDNDGEAPLLDLTLKSGKAFYARTIADFATWLVCGLPAREEQVKRS-PHIRDAVWGSL-RSTDSYTVLHY 2054
Cdd:cd08151    80 DGRGAALRFLNAGDDDAGPLDLVMNTGESFGFWTAASFADFAGAGLPFREKAAKLRgPLARYAVWASLrRAPDSYTDLHY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 2055 YSNICRLLRFDDGREMYAKFKLRPADPDVPEDSGKVVPRGILPPETGAIPRDEDDTRPLLFLADDFRRRVGSPdGVRYVF 2134
Cdd:cd08151   160 YSQICYEFVALDGKSRYARFRLLPPDADTEWDLGEDVLETIFQRPRLYLPRLPGDTRPKDYLRNEFRQRLQSP-GVRYRL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 2135 QLQLREVPTDaaARDVALDCTRPWDEAEFPYIDVGEVSIGRNLPTEETEKLEFNPfLRCPEVDVIPATSCAQ-SASIDHG 2213
Cdd:cd08151   239 QIQLREVSDD--ATAVALDCCRPWDEDEHPWLDLAVVRLGAPLPNDELEKLAFNP-GNTPESLGLPLAYCADdYASLGHL 315

                         330
                  ....*....|...
gi 937914749 2214 RSLVYEICQRLRN 2226
Cdd:cd08151   316 RSLVYEISQRLRK 328
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 605-1155 6.11e-97

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 326.13  E-value: 6.11e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTKPvikpGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVlppdPMQSGGQALLKVENISKMC 684
Cdd:PRK05850   37 TWSQLYRRTLNVAEELRRHGST----GDRAVILAPQGLEYIVAFLGALQAGLIAVPL----SVPQGGAHDERVSAVLRDT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 NAVAILSTSSYHAAVRagyiknivtlaKRVQKCSAQwPDIPWIHTDSWIKNYRRSSDSFNSDtvlftkpqPSDLCFLQFT 764
Cdd:PRK05850  109 SPSVVLTTSAVVDDVT-----------EYVAPQPGQ-SAPPVIEVDLLDLDSPRGSDARPRD--------LPSTAYLQYT 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  765 SGSTGDAKGVMITHEGLIHNVKTMKKRY------RSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMIFIRNP 838
Cdd:PRK05850  169 SGSTRTPAGVMVSHRNVIANFEQLMSDYfgdtggVPPPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTSPVAFLQRP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  839 LLWLQTINDYHGTHSAGPNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYGL 918
Cdd:PRK05850  249 ARWMQLLASNPHAFSAAPNFAFELAVRKTSDDDMAGLDLGGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGL 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  919 AENCVYV-TCAFGEC-KPVFIDWQgRVCCGYVEQDDTDT-------------LIRIVDPDSLTEHQeDGVEGEIWISSPS 983
Cdd:PRK05850  329 AEATVYVaTREPGQPpESVRFDYE-KLSAGHAKRCETGGgtplvsygsprspTVRIVDPDTCIECP-AGTVGEIWVHGDN 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  984 SGVGYWGNSEMSQRTFFNQLKN----HPNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVEsssEVLR 1059
Cdd:PRK05850  407 VAAGYWQKPEETERTFGATLVDpspgTPEGPWLRTGDLGFISEGELFIVGRIKDLLIVDGRNHYPDDIEATIQ---EITG 483

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1060 pGCCAVVGIPEevlaqkgisipDSSDQvgLVVIAEVREGKAVSKEVVNN---IKARVV----EEHGVAVASVKLIKPRTI 1132
Cdd:PRK05850  484 -GRVAAISVPD-----------DGTEK--LVAIIELKKRGDSDEEAMDRlrtVKREVTsaisKSHGLSVADLVLVAPGSI 549

                         570       580
                  ....*....|....*....|...
gi 937914749 1133 CKTTSGKIRRFECMRQFVDNTLS 1155
Cdd:PRK05850  550 PITTSGKIRRAACVEQYRQDEFT 572
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 564-1154 9.92e-95

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 321.68  E-value: 9.92e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  564 VEFPDLPSLDGYLQYWGthKVTEKNVIYTWIN---EEGKLMNRRTYQELHGNASYIAQKLltstKPVIKPGDRVLLIHLP 640
Cdd:PRK07769   15 IRFPPNTNLVRHVERWA--KVRGDKLAYRFLDfstERDGVARDLTWSQFGARNRAVGARL----QQVTKPGDRVAILAPQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  641 GLEFIDAFFGCIRAGVIPVPVLPPD-PMQSGgqallKVENISKMCNAVAILSTSSYHAAVRAgYIKNIVtlakrvqkcSA 719
Cdd:PRK07769   89 NLDYLIAFFGALYAGRIAVPLFDPAePGHVG-----RLHAVLDDCTPSAILTTTDSAEGVRK-FFRARP---------AK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  720 QWPDIpwIHTDSwiknyrrSSDSFNSdtvLFTKPQPS--DLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSK 797
Cdd:PRK07769  154 ERPRV--IAVDA-------VPDEVGA---TWVPPEANedTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEG 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  798 TVLVSWLPQYHDMGLIGGLFTALVsGGTSVLFSPMIFIRNPLLWLQTI----NDYHGTHSAGPNFAFEL-VIRRLEAEKN 872
Cdd:PRK07769  222 DRGVSWLPFFHDMGLITVLLPALL-GHYITFMSPAAFVRRPGRWIRELarkpGGTGGTFSAAPNFAFEHaAARGLPKDGE 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  873 KVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYGLAENCVYV--TCAFGECKPVFIDWQ----GR---- 942
Cdd:PRK07769  301 PPLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVstTPMDEEPTVIYVDRDelnaGRfvev 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  943 ----------VCCGYVEQDDTDTlirIVDPDSLTEhQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFFNQLKN-----H- 1006
Cdd:PRK07769  381 padapnavaqVSAGKVGVSEWAV---IVDPETASE-LPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNILKSrlsesHa 456

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1007 ----PNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRPGCCAVVGIPEEVLAQKGISIP- 1081
Cdd:PRK07769  457 egapDDALWVRTGDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRTGYVAAFSVPANQLPQVVFDDSh 536

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1082 --------DSSDQvgLVVIAEVREG--KAVSKEVVNNIKARVVEEHGVAVASVKLIKPRTICKTTSGKIRRFECMRQFVD 1151
Cdd:PRK07769  537 aglkfdpeDTSEQ--LVIVAERAPGahKLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLD 614


                  ...
gi 937914749 1152 NTL 1154
Cdd:PRK07769  615 GSL 617
FAAL_FadD32 NF038339
long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker ...
 627-1154 8.75e-92

long-chain-fatty-acid--AMP ligase FAAL32/FadD32; FadD32, also called FAAL32, is a marker enzyme for the biosynthesis of the type of mycolic acids, the very large "eumycolic acids", found in Mycobacterium.


Pssm-ID: 468483 [Multi-domain]  Cd Length: 625  Bit Score: 312.81  E-value: 8.75e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  627 VIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPD-PMQSGgqallKVENISKMCNAVAILSTSSYHAAVRAGYIK 705
Cdd:NF038339   72 VTKPGDRVAILAPQGLDYVVSFFAAIYAGNIAVPLFDPDePGHTD-----RLHAVLGDCKPSAILTATSSAEGVRKFFRS 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  706 NIVTLAKRVQKCSAqwpdIPWIHTDSWIKnyrrssdsfnsdtvlftkPQPS--DLCFLQFTSGSTGDAKGVMITHEGLIH 783
Cdd:NF038339  147 LPAKERPRVIAVDA----VPDSVGSTWVR------------------PDADldDIAYLQYTSGSTRVPAGVEITHRAVAT 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  784 NVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALvsGGTSVLF-SPMIFIRNPLLW---LQTINDYHGTHSAGPNFA 859
Cdd:NF038339  205 NVLQMVDAIELDENSRGVTWLPLFHDMGLLTVILPAL--GGKYITImSPAAFVRRPGRWireLAAVSDGAGTFAAAPNFA 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  860 FELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYGLAENCVYV--TCAFGECKPVFI 937
Cdd:NF038339  283 FEHAAARGLPKEGEPLDLSNVIGLINGSEPVTTSSMRKFNEAFAPYGLPKTAIKPSYGMAEATLFVssTPREDEAKVIYV 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  938 DW----QGR--------------VCCGYVEQDDTDTlirIVDPDSLTEhQEDGVEGEIWISSPSSGVGYWGNSEMSQRTF 999
Cdd:NF038339  363 DReelnAGRivevdpdapnavaqVSCGYVARSQWAV---IVDPETGTE-LPDGQVGEIWLHGNNIGTGYWGRPEETEETF 438

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1000 FNQLKNH-----------PNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRPGCCAVVGI 1068
Cdd:NF038339  439 HNKLKSRleegshaegapEDANWMRTGDYGVYYDGELYITGRVKDLVIVDGRNHYPQDLEYSAQEASKALRPGFVAAFSV 518

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1069 PEEVLAQKGISIP---------DSSDQvgLVVIAE--VREGKAVSKEVVNNIKARVVEEHGVAVASVKLIKPRTICKTTS 1137
Cdd:NF038339  519 PANQLPAEVFENShsglkydadDSSEQ--LVIVAEraPGAGKADPQPIADAVRAAIAVRHGVTVRDVLLVPAGSIPRTSS 596

                         570
                  ....*....|....*..
gi 937914749 1138 GKIRRFECMRQFVDNTL 1154
Cdd:NF038339  597 GKIARRACKAAYIDGTL 613
FadD32_Coryne NF040633
FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus ...
 627-1151 6.60e-88

FadD32-like long-chain-fatty-acid--AMP ligase; Members of this family are found in the genus Corynebacterium, are most similar to the key mycolic acid biosynthesis protein FadD32 of any fatty acid--AMP ligase in Mycobacterium tuberculosis, and are likewise encoded next to Pks13. However, as the mycolic acids produced in Corynebacterium and in Mycobacterium differ substantially, it is not clear that assigning the same name in Corynebacterium is appropriate.


Pssm-ID: 468603 [Multi-domain]  Cd Length: 613  Bit Score: 301.18  E-value: 6.60e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  627 VIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLppDPMQSGGQALLKVenISKMCNAVAILSTSSYHAAVRAgYIKN 706
Cdd:NF040633   82 VGKPGDRVAILANNSPEYIFGFLGALYAGMVPVPLY--DPNEPGHADHLRA--VLADSGPTVVLTNKTSAPAVRA-HFAD 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  707 IVtlakrvqkcSAQWPDIPWIHT--DSWIKNYRRSSDSFNSDTVLFTKPQ-PSDL-CFLQFTSGSTGDAKGVMITHEGLI 782
Cdd:NF040633  157 LP---------AAERPRILSVDSlpDSLAESWVNPMATIEGQPLLAPAGTdPSDDtAFLQYTSGSTRTPAGVVLTNRSIV 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  783 HNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFtALVSGGTSVLFSPMIFIRNPLLWLQTIN---DYHGTHSAGPNFA 859
Cdd:NF040633  228 TNVLQIFTAAQLKTPLRLVSWLPLHHDMGIILAAF-VTILGLEFELMSPRDFIQQPKRWVDQLSrreDDVNVYTVVPNFA 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  860 FELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYGLAENCVYVTCAFGECKPVFIDW 939
Cdd:NF040633  307 LELAARYANPEEGEDLDLSAVDGIIIGSEPVTEKAVDAFLDAFGPYGLRRTALRPSYGLAEASLLVTTPQTEERPLFTYF 386

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  940 ------QGRVCCgyVEQDDTDTL-------------IRIVDPDSLTEhQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFF 1000
Cdd:NF040633  387 drealaEGRAVE--VAEDSENAVpfasngqvvrpqvLAIVDPETGQE-LPDGTVGEIWVHGDNMAAGYLDREEETAETFR 463

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1001 NQLKNH----------PNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRPGCCAVVGIPE 1070
Cdd:NF040633  464 NTLGERlaensraegaPEDNWMATGDLGVIVDGELYITGRLKDLIVIAGRNHYPQDIEATVQEASDHIRPDSVAAFAVPG 543

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1071 EvlaqkgisipdssDQVGLVVIAEVREGKAVSK--EVVNNIKARVVEEHGVAVASVKLIKPRTICKTTSGKIRRFECMRQ 1148
Cdd:NF040633  544 D-------------DVEKLVILAERDDEADESGdaEAIEAIRAAVTSAHGVVPADIRIVAPGEIARSSSGKIARRVNAKA 610


                  ...
gi 937914749 1149 FVD 1151
Cdd:NF040633  611 YLE 613
PRK05691 PRK05691
peptide synthase; Validated
 605-1154 1.15e-82

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 305.55  E-value: 1.15e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTKPvikpGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPMQSGGQALLkvenISKMC 684
Cdd:PRK05691   42 SYRDLDLRARTIAAALQARASF----GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARRHHQERL----LSIIA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 NAVA--ILSTSSYHAAvragyiknivtLAKRVQKCSAQWPdiPWIHTDSWiknyrrssDSFNSDTVLFTKPQPSDLCFLQ 762
Cdd:PRK05691  114 DAEPrlLLTVADLRDS-----------LLQMEELAAANAP--ELLCVDTL--------DPALAEAWQEPALQPDDIAFLQ 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  763 FTSGSTGDAKGVMITHEGLIHNVKTMKKRYR--STSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMIFIRNPLL 840
Cdd:PRK05691  173 YTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPAYFLERPLR 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  841 WLQTINDYHGTHSAGPNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYGLAE 920
Cdd:PRK05691  253 WLEAISEYGGTISGGPDFAYRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGFDPDSFFASYGLAE 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  921 NCVYVTC---------------AFGECKPVFIDWQGRVCCGYVEQDDTdtlIRIVDPDSLTEhQEDGVEGEIWISSPSSG 985
Cdd:PRK05691  333 ATLFVSGgrrgqgipaleldaeALARNRAEPGTGSVLMSCGRSQPGHA---VLIVDPQSLEV-LGDNRVGEIWASGPSIA 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  986 VGYWGNSEMSQRTFFNqlknHPNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRPGCCAV 1065
Cdd:PRK05691  409 HGYWRNPEASAKTFVE----HDGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKGRVAA 484

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1066 VGIPEEvlAQKGISIPdssdqvglvviAEVREG--KAVSKEV-VNNIKARVVEEHGVAVASVKLIKPRTICKTTSGKIRR 1142
Cdd:PRK05691  485 FAVNHQ--GEEGIGIA-----------AEISRSvqKILPPQAlIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQR 551

                         570
                  ....*....|..
gi 937914749 1143 FECMRQFVDNTL 1154
Cdd:PRK05691  552 SACRLRLADGSL 563
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 627-1154 1.63e-82

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 285.48  E-value: 1.63e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  627 VIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPD-PmqsgGQALlKVENISKMCNAVAILSTSSYHAAVRaGYIK 705
Cdd:PRK12476   88 VAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPElP----GHAE-RLDTALRDAEPTVVLTTTAAAEAVE-GFLR 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  706 NIVTLAK-RVQKCSaqwpDIPwihtdswiknyrrssdsfNSDTVLFTKPQP--SDLCFLQFTSGSTGDAKGVMITHEGLI 782
Cdd:PRK12476  162 NLPRLRRpRVIAID----AIP------------------DSAGESFVPVELdtDDVSHLQYTSGSTRPPVGVEITHRAVG 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  783 HNVKTMkkryrSTSKTVL------VSWLPQYHDMGLIGGLFTAlVSGGTSVLFSPMIFIRNPLLWLQTIND---YHGTHS 853
Cdd:PRK12476  220 TNLVQM-----ILSIDLLdrnthgVSWLPLYHDMGLSMIGFPA-VYGGHSTLMSPTAFVRRPQRWIKALSEgsrTGRVVT 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  854 AGPNFAFELVIRR-LEAEKNKVyDLSSMVfLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYGLAENCVYVTCAFGEC 932
Cdd:PRK12476  294 AAPNFAYEWAAQRgLPAEGDDI-DLSNVV-LIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATLFVATIAPDA 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  933 KP--VFIDWQ----GR--------------VCCGYVEQDDTDTlirIVDPDSLTEhQEDGVEGEIWISSPSSGVGYWGNS 992
Cdd:PRK12476  372 EPsvVYLDREqlgaGRavrvaadapnavahVSCGQVARSQWAV---IVDPDTGAE-LPDGEVGEIWLHGDNIGRGYWGRP 447

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  993 EMSQRTFFNQLK------NH-----PNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRPG 1061
Cdd:PRK12476  448 EETERTFGAKLQsrlaegSHadgaaDDGTWLRTGDLGVYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRG 527

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1062 CCAVVGIPEEvlaqkgisipdssDQVGLVVIAE--VREGKAVSKEVVNNIKARVVEEHGVAVASVKLIKPRTICKTTSGK 1139
Cdd:PRK12476  528 YVTAFTVPAE-------------DNERLVIVAEraAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGK 594

                         570
                  ....*....|....*
gi 937914749 1140 IRRFECMRQFVDNTL 1154
Cdd:PRK12476  595 LARRACRAQYLDGRL 609
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 603-1155 1.66e-82

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: 279.77  E-value: 1.66e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPdpmqsggqalLKVENISK 682
Cdd:COG0318    24 RLTYAELDARARRLAAALRALG---VGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPR----------LTAEELAY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  683 MCNavailstssyHAAVRAgyiknIVTlakrvqkcsaqwpdipwihtdswiknyrrssdsfnsdtvlftkpqpsdlCFLQ 762
Cdd:COG0318    91 ILE----------DSGARA-----LVT-------------------------------------------------ALIL 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  763 FTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPmifiRNPLLWL 842
Cdd:COG0318   107 YTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPR----FDPERVL 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  843 QTINDYHGTHSAGPNFAFELVIRRLEAEKnkvYDLSSMVFLMIAAEPVRQKTVRRFIELTQPfglsegVLAPGYGLAENC 922
Cdd:COG0318   183 ELIERERVTVLFGVPTMLARLLRHPEFAR---YDLSSLRLVVSGGAPLPPELLERFEERFGV------RIVEGYGLTETS 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  923 VYVTCAFGECKPVFIDWQGRVCCGyVEqddtdtlIRIVDPDslTEHQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFFNQ 1002
Cdd:COG0318   254 PVVTVNPEDPGERRPGSVGRPLPG-VE-------VRIVDED--GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG 323

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1003 lknhpnkkFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEVLAQKgisip 1081
Cdd:COG0318   324 --------WLRTGDLGRlDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAE---AAVVGVPDEKWGER----- 387

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1082 dssdqvgLVVIAEVREGKAVSKEvvnNIKARVVEehgvAVASVKLikPRTIC------KTTSGKIRRFECMRQFVDNTLS 1155
Cdd:COG0318   388 -------VVAFVVLRPGAELDAE---ELRAFLRE----RLARYKV--PRRVEfvdelpRTASGKIDRRALRERYAAGALE 451
PRK09192 PRK09192
fatty acyl-AMP ligase;
598-1144 3.22e-75

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 263.02  E-value: 3.22e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  598 GKLMNRRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVlpPDPMQSGGQALLkV 677
Cdd:PRK09192   44 GQLEEALPYQTLRARAEAGARRLLALG---LKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL--PLPMGFGGRESY-I 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  678 ENISKM---CNAVAILSTSSYhaavrAGYIKNIVTLAKRVQKCSAQWPDIPwihtdswiknyrrssdsfNSDTVLFTKPQ 754
Cdd:PRK09192  118 AQLRGMlasAQPAAIITPDEL-----LPWVNEATHGNPLLHVLSHAWFKAL------------------PEADVALPRPT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVK-----TMKKRY--RStsktvlVSWLPQYHDMGLIGGLFTALVSGGTSV 827
Cdd:PRK09192  175 PDDIAYLQYSSGSTRFPRGVIITHRALMANLRaishdGLKVRPgdRC------VSWLPFYHDMGLVGFLLTPVATQLSVD 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  828 LFSPMIFIRNPLLWLQTINDYHGTHSAGPNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGL 907
Cdd:PRK09192  249 YLPTRDFARRPLQWLDLISRNRGTISYSPPFGYELCARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGF 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  908 SEGVLAPGYGLAENCVYVTCA----------------FGECKPVFIDWQGR-----VCCGYVEQDDTdtlIRIVDPDS-- 964
Cdd:PRK09192  329 DDKAFMPSYGLAEATLAVSFSplgsgivveevdrdrlEYQGKAVAPGAETRrvrtfVNCGKALPGHE---IEIRNEAGmp 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  965 LTEHQEdgveGEIWISSPSSGVGYWGNSEmSQRTFF--NQLKnhpnkkftrTGDLGRTIDGNLFITGRIKDLIIVAGRNI 1042
Cdd:PRK09192  406 LPERVV----GHICVRGPSLMSGYFRDEE-SQDVLAadGWLD---------TGDLGYLLDGYLYITGRAKDLIIINGRNI 471

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1043 YSADVEKTVESSSEvLRPGCCAVVGIPEEvlaqkgisipdssDQVGLVVIAEVREGKAVSKE-VVNNIKARVVEEHGVAV 1121
Cdd:PRK09192  472 WPQDIEWIAEQEPE-LRSGDAAAFSIAQE-------------NGEKIVLLVQCRISDEERRGqLIHALAALVRSEFGVEA 537

                         570       580
                  ....*....|....*....|...
gi 937914749 1122 aSVKLIKPRTICKTTSGKIRRFE 1144
Cdd:PRK09192  538 -AVELVPPHSLPRTSSGKLSRAK 559
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 603-1151 1.59e-74

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: 259.91  E-value: 1.59e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPMQSGGQALLKVENISK 682
Cdd:cd05906    39 FQSYQDLLEDARRLAAGLRQLG---LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRKLRHIWQ 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  683 MCNAVAILSTSSYHAAVRAgyiknivtlakrvQKCSAQWPDIPwIHTDSWIKNYRRSSDSFNSdtvlftkpQPSDLCFLQ 762
Cdd:cd05906   116 LLGSPVVLTDAELVAEFAG-------------LETLSGLPGIR-VLSIEELLDTAADHDLPQS--------RPDDLALLM 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  763 FTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMIFIRNPLLWL 842
Cdd:cd05906   174 LTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWL 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  843 QTINDYHGTHSAGPNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYGLAENC 922
Cdd:cd05906   254 DLIDRYRVTITWAPNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETC 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  923 ----VYVTCAFGEC--KPVFidwqgrVCCGY----VEqddtdtlIRIVDPDslTEHQEDGVEGEIWISSPSSGVGYWGNS 992
Cdd:cd05906   334 sgviYSRSFPTYDHsqALEF------VSLGRpipgVS-------MRIVDDE--GQLLPEGEVGRLQVRGPVVTKGYYNNP 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  993 EMSQRTF-----FnqlknhpnkkftRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRPGCCAVVG 1067
Cdd:cd05906   399 EANAEAFtedgwF------------RTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAV 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1068 IPEevlaqkgisiPDSSDQVGLV-VIAEVREGKAVskEVVNNIKARVVEEHGVAVASVKLIKPRTICKTTSGKIRRFECM 1146
Cdd:cd05906   467 RDP----------GAETEELAIFfVPEYDLQDALS--ETLRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQRSKLK 534


                  ....*
gi 937914749 1147 RQFVD 1151
Cdd:cd05906   535 AAFEA 539
FAAL_FadD21 NF038337
fatty-acid--AMP ligase FAAL21/FadD21;
631-1149 3.42e-74

fatty-acid--AMP ligase FAAL21/FadD21;


Pssm-ID: 439631 [Multi-domain]  Cd Length: 579  Bit Score: 260.19  E-value: 3.42e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  631 GDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPmqsgGQALLKVENISKMCNAVAILSTSSYHAAVrAGYIKnivtl 710
Cdd:NF038337   62 GDRAVILAPQGLPYIVAFLGAMQAGLIAVPLSVPQP----GSHDERVSAVLADTSPSVVLTTSAAAAAV-AEYLH----- 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  711 akrvQKCSAQWPDIpwIHTDSWiknyrrSSDSFNSDTVLFTkpQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKK 790
Cdd:NF038337  132 ----RPDTGAVPAV--IEIDSL------DLDGPNSPSIRIS--DAPSIAYLQYTSGSTRLPAGVMVSHRNLQVNFQQLMA 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  791 RYRSTSK------TVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMIFIRNPLLWLQTINDYHGTHSAGPNFAFELVI 864
Cdd:NF038337  198 AYFPDTNgvaprdTTIVSWLPFYHDMGLVLGVIAPILGGYRSELTSPVAFLQRPARWIHAMANGSPVFSAAPNFAFELAV 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  865 RRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYGLAENCVYVTCAFGECKPVFIDWQ-GRV 943
Cdd:NF038337  278 RKTTDADLAGLDLGNVIGIVSGAERIHPATLDRFCKRFAPYNFREDMMQPSYGLAEATVYVASRAEGGAPEVVHFEpEKL 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  944 CCGYVEQDDTDT-------------LIRIVDPDSLTEhQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFFNQLKN----H 1006
Cdd:NF038337  358 SEGSAQRCEARTgspllsygtptspTVRIVDPDTCIE-CPAGTVGEIWVHGDNVAEGYWQKPEETRRTFGGVLANpspgT 436

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1007 PNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVEsssevlrpgccAVVGipEEVLAqkgISIP-DSSD 1085
Cdd:NF038337  437 PEGPWLRTGDLGFISEDEMFIVGRMKDLLIVYGRNHYPEDIESTVQ-----------EITG--GRVAA---ISVPvDETE 500

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937914749 1086 QvgLVVIAEVR-------EGKAVSKEVVNNIKARVVEEHGVAVASVKLIKPRTICKTTSGKIRRFECMRQF 1149
Cdd:NF038337  501 K--LVTIIELKkrgdsdeEAMRKLDAVKNNVTAAISRSHGLNVADLVLVPPGSIPTTTSGKIRRAACVEQY 569
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 755-1142 1.77e-70

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 247.99  E-value: 1.77e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKT-VLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMI 833
Cdd:PRK07768  151 EDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETdVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTPMD 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  834 FIRNPLLWLQTINDYHGTHSAGPNFAFELVIRRLE-AEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVL 912
Cdd:PRK07768  231 FLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRrQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAGARFGLRPEAI 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  913 APGYGLAENCVYVTcaFGEC-KPVFIDwqgRVCCGYVEQ---------DDTDTL-----------IRIVDpDSLTEHQED 971
Cdd:PRK07768  311 LPAYGMAEATLAVS--FSPCgAGLVVD---EVDADLLAAlrravpatkGNTRRLatlgpplpgleVRVVD-EDGQVLPPR 384

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  972 GVeGEIWISSPSSGVGYwgnsemsqRTFFNQLKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKT 1050
Cdd:PRK07768  385 GV-GVIELRGESVTPGY--------LTMDGFIPAQDADGWLDTGDLGYlTEEGEVVVCGRVKDVIIMAGRNIYPTDIERA 455

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1051 VESSSEVlRPGCCAVVGIPEevlaqkgisiPDSSDqvGLVVIAEVREGK--AVSKEVVNNIKARVVEEHGVAVASVKLIK 1128
Cdd:PRK07768  456 AARVEGV-RPGNAVAVRLDA----------GHSRE--GFAVAVESNAFEdpAEVRRIRHQVAHEVVAEVGVRPRNVVVLG 522

                         410
                  ....*....|....
gi 937914749 1129 PRTICKTTSGKIRR 1142
Cdd:PRK07768  523 PGSIPKTPSGKLRR 536
AMP-binding pfam00501
AMP-binding enzyme;
602-1038 6.88e-67

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 233.36  E-value: 6.88e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   602 NRRTYQELHGNASYIAqKLLTSTKpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVlppDPMQSGGQallkVENIS 681
Cdd:pfam00501   20 RRLTYRELDERANRLA-AGLRALG--VGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPL---NPRLPAEE----LAYIL 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   682 KMCNAVAILstssyhaAVRAGYIKNIVTLAKRVQKCSAqwpdIPWIHTDSWIKN--YRRSSDSFNSDTVLFTKPQPSDLC 759
Cdd:pfam00501   90 EDSGAKVLI-------TDDALKLEELLEALGKLEVVKL----VLVLDRDPVLKEepLPEEAKPADVPPPPPPPPDPDDLA 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   760 FLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRS----TSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMIFi 835
Cdd:pfam00501  159 YIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA- 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   836 RNPLLWLQTINDYHGTHSAGPNFAFELVirrLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELtqpFGlseGVLAPG 915
Cdd:pfam00501  238 LDPAALLELIERYKVTVLYGVPTLLNML---LEAGAPKRALLSSLRLVLSGGAPLPPELARRFREL---FG---GALVNG 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   916 YGLAENCVYVTCAF-GECKPVFIDWQGRVCCGyveqddtdTLIRIVDPDSLtEHQEDGVEGEIWISSPSSGVGYWGNSEM 994
Cdd:pfam00501  309 YGLTETTGVVTTPLpLDEDLRSLGSVGRPLPG--------TEVKIVDDETG-EPVPPGEPGELCVRGPGVMKGYLNDPEL 379

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 937914749   995 SQRTFFnqlknhpNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVA 1038
Cdd:pfam00501  380 TAEAFD-------EDGWYRTGDLGRrDEDGYLEIVGRKKDQIKLG 417
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 757-1141 9.04e-67

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: 230.25  E-value: 9.04e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  757 DLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHdMGLIGGLFTALVSGGTSVLFSPmifiR 836
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFH-IGGLFGLLGALLAGGTVVLLPK----F 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  837 NPLLWLQTINDYHGTHSAGPNFAFELVIRRLEAEKnkvYDLSSMVFLMIAAEPVRQKTVRRFIELTQPfglsegVLAPGY 916
Cdd:cd04433    76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAG---YDLSSLRALVSGGAPLPPELLERFEEAPGI------KLVNGY 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  917 GLAENCVYVTCAFGECKPVFIDWQGRVCCGyVEqddtdtlIRIVDPDslTEHQEDGVEGEIWISSPSSGVGYWGNSEMSQ 996
Cdd:cd04433   147 GLTETGGTVATGPPDDDARKPGSVGRPVPG-VE-------VRIVDPD--GGELPPGEIGELVVRGPSVMKGYWNNPEATA 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  997 RTFFNqlknhpnkKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEVLAQ 1075
Cdd:cd04433   217 AVDED--------GWYRTGDLGRlDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAE---AAVVGVPDPEWGE 285

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749 1076 KgisipdssdqVGLVViaEVREGKAVSKEVVNNIKARVVEEHGVAvasVKLIKPRTICKTTSGKIR 1141
Cdd:cd04433   286 R----------VVAVV--VLRPGADLDAEELRAHVRERLAPYKVP---RRVVFVDALPRTASGKID 336
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 605-1149 7.19e-64

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: 227.37  E-value: 7.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNAS---YIAQKLltstkpVIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVlPPDPMQSGGQALLKVENIs 681
Cdd:cd05908    17 SYRHLREEALgylGALQEL------GIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPV-SIGSNEEHKLKLNKVWNT- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  682 kmcnavailstssyhaavragyIKNIVTLAkrvqkcsaqwpdipwihtdswiknyrrssdsfnSDTVLftKPQPSDLCFL 761
Cdd:cd05908    89 ----------------------LKNPYLIT---------------------------------EEEVL--CELADELAFI 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  762 QFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMIFIRNPLLW 841
Cdd:cd05908   112 QFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILW 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  842 LQTINDYHGTHSAGPNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYGLAEN 921
Cdd:cd05908   192 LKKASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  922 CVYVTC--AFGECKPVFIDWQG-RVCCGYVEQDDTD---------------TLIRIVDPDSltEHQEDGVEGEIWISSPS 983
Cdd:cd05908   272 SVGASLpkAQSPFKTITLGRRHvTHGEPEPEVDKKDsecltfvevgkpideTDIRICDEDN--KILPDGYIGHIQIRGKN 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  984 SGVGYWGNSEMSQRTFfnqlknhPNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpGCC 1063
Cdd:cd05908   350 VTPGYYNNPEATAKVF-------TDDGWLKTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVEL-GRV 421

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1064 AVVGIPEEVLAQKGIsipdssdqvglVVIAEVREGKAVSKEVVNNIKARVVEEHGVAVASVKLIkpRTICKTTSGKIRRF 1143
Cdd:cd05908   422 VACGVNNSNTRNEEI-----------FCFIEHRKSEDDFYPLGKKIKKHLNKRGGWQINEVLPI--RRIPKTTSGKVKRY 488


                  ....*.
gi 937914749 1144 ECMRQF 1149
Cdd:cd05908   489 ELAQRY 494
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
 590-1154 1.52e-57

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: 211.05  E-value: 1.52e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  590 IYTWINEEGKLMNRRTYQELHGNASYIAQKLLTSTKpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPMQS 669
Cdd:cd05905     1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG--LKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  670 ggqaLLKVENISKMcnAVAIlstssyhaAVRAGYIKNIVTLAKRVQKC-SAQ---WPDIPWIHTDSwiknyrrssdSFNS 745
Cdd:cd05905    79 ----LGFLLGTCKV--RVAL--------TVEACLKGLPKKLLKSKTAAeIAKkkgWPKILDFVKIP----------KSKR 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  746 DTVLFTKPQP----SDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALV 821
Cdd:cd05905   135 SKLKKWGPHPptrdGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVY 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  822 SGGTSVLFSPMIFIRNPLLWLQTINDYHGTHSAGP----NFAFELVIRRLEAEKNKVYDLSSMVFLMIAAE-PVRQKTVR 896
Cdd:cd05905   215 SGHHTILIPPELMKTNPLLWLQTLSQYKVRDAYVKlrtlHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCEnRPRISSCD 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  897 RFIELTQPFGLSegvlapgyglaenCVYVTCAFGECKPVFIDWQG----------------RVCCGYVEQDDT------- 953
Cdd:cd05905   295 SFLKLFQTLGLS-------------PRAVSTEFGTRVNPFICWQGtsgpepsrvyldmralRHGVVRLDERDKpnslplq 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  954 -------DTLIRIVDPDSLtEHQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFFNQLKNHP-----NKKFTRTGDLG--- 1018
Cdd:cd05905   362 dsgkvlpGAQVAIVNPETK-GLCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLstgitNNSYARTGLLGflr 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1019 --RTIDGN------LFITGRIKDLIIVAGRNIYSADVEKTVESS-SEVlrpGCCAVVGIPEEVlaqkgisipdssdqvgl 1089
Cdd:cd05905   441 ptKCTDLNveehdlLFVVGSIDETLEVRGLRHHPSDIEATVMRVhPYR---GRCAVFSITGLV----------------- 500

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749 1090 VVIAEVREGkavSKEVVNNIKARVV----EEHGVAVASVKLIKPRTICKTTSGKIRRFECMRQFVDNTL 1154
Cdd:cd05905   501 VVVAEQPPG---SEEEALDLVPLVLnailEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKL 566
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
603-1148 3.26e-57

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


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 208.85  E-value: 3.26e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTKPVIkpgdrVLLIHLPGLEFIDAFFGCIRAG----VIPVPVLPPDPMQSGGQALLKVE 678
Cdd:PRK05851   31 RHPWPEVHGRAENVAARLLDRDRPGA-----VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  679 NISkmcnAVAILSTSSYHAAVRAgyiknivtLAKRVQkcsaqwpdipwIHTDSWIKNYRRSSDsfnsdtvlFTKPQPSDL 758
Cdd:PRK05851  106 GIG----VRTVLSHGSHLERLRA--------VDSSVT-----------VHDLATAAHTNRSAS--------LTPPDSGGP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  759 CFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKT-VLVSWLPQYHDMGLIGgLFTALVSGGTSVLFSPMIFIRN 837
Cdd:PRK05851  155 AVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATdVGCSWLPLYHDMGLAF-LLTAALAGAPLWLAPTTAFSAS 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  838 PLLWLQTINDYHGTHSAGPNFAFELVIRRleAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGVLAPGYG 917
Cdd:PRK05851  234 PFRWLSWLSDSRATLTAAPNFAYNLIGKY--ARRVSDVDLGALRVALNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYG 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  918 LAENcvyvTCAFGECKP---VFIDwqgrvccgYVEQDDTDTL--------------IRIVDPDSLTEHQEDGVeGEIWIS 980
Cdd:PRK05851  312 LAES----TCAVTVPVPgigLRVD--------EVTTDDGSGArrhavlgnpipgmeVRISPGDGAAGVAGREI-GEIEIR 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  981 SPSSGVGYWGNSEMSQRTFFnqlknhpnkkftRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKtVESSSEVLRP 1060
Cdd:PRK05851  379 GASMMSGYLGQAPIDPDDWF------------PTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIER-VAAQVRGVRE 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1061 GCCAVVGIPEevlaqkgisipdSSDQVGLVVIAEVR---EGKAVSkEVVNnikaRVVEEHGVAVASVKLIKPRTICKTTS 1137
Cdd:PRK05851  446 GAVVAVGTGE------------GSARPGLVIAAEFRgpdEAGARS-EVVQ----RVASECGVVPSDVVFVAPGSLPRTSS 508

                         570
                  ....*....|.
gi 937914749 1138 GKIRRFECMRQ 1148
Cdd:PRK05851  509 GKLRRLAVKRS 519
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 603-1142 1.57e-46

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: 175.44  E-value: 1.57e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIhLP-GLEFIDAFFGCIRAGVIPVPVLPpdpmQSGGQALlkvENIS 681
Cdd:cd05936    24 KLTYRELDALAEAFAAGLQNLG---VQPGDRVALM-LPnCPQFPIAYFGALKAGAVVVPLNP----LYTPREL---EHIL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  682 KMCNAVAILSTSSYHAAVRAGYiknivTLAKRVQkcsaqwpdipwihtdswiknyrrssdsfnsdtvlftkPQPSDLCFL 761
Cdd:cd05936    93 NDSGAKALIVAVSFTDLLAAGA-----PLGERVA-------------------------------------LTPEDVAVL 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  762 QFTSGSTGDAKGVMITHEGLIHNVKTMKKRY--RSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLF-SPMifirnP 838
Cdd:cd05936   131 QYTSGTTGVPKGAMLTHRNLVANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIpRFR-----P 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  839 LLWLQTINDYHGTHSAGPNfafELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQpfglseGVLAPGYGL 918
Cdd:cd05936   206 IGVLKEIRKHRVTIFPGVP---TMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTG------VPIVEGYGL 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  919 AEnCVYVTCA---FGECKPvfidwqgrvccGYVEQDDTDTLIRIVDPDslTEHQEDGVEGEIWISSPSSGVGYWGNSEMS 995
Cdd:cd05936   277 TE-TSPVVAVnplDGPRKP-----------GSIGIPLPGTEVKIVDDD--GEELPPGEVGELWVRGPQVMKGYWNRPEET 342

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  996 QRTFFNqlknhpnkKFTRTGDLGRtID--GNLFITGRIKDLIIVAGRNIYSADVEktvesssEVL--RPGC--CAVVGIP 1069
Cdd:cd05936   343 AEAFVD--------GWLRTGDIGY-MDedGYFFIVDRKKDMIIVGGFNVYPREVE-------EVLyeHPAVaeAAVVGVP 406

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1070 EevlaqkgisiPDSSDQVGLVVIaeVREGKAVSK-EVVNNIKARvveehgvaVASVKLikPRTIC------KTTSGKIRR 1142
Cdd:cd05936   407 D----------PYSGEAVKAFVV--LKEGASLTEeEIIAFCREQ--------LAGYKV--PRQVEfrdelpKSAVGKILR 464
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
593-1148 1.20e-45

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 175.30  E-value: 1.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  593 WINEEGKLMnRRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLlIHLP-GLEFIDAFFGCIRAGVIPVPVlppdpmqSGG 671
Cdd:COG0365    30 WEGEDGEER-TLTYAELRREVNRFANALRALG---VKKGDRVA-IYLPnIPEAVIAMLACARIGAVHSPV-------FPG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  672 qalLKVENIS---KMCNAVAILSTSSYHAAVRAGYIKNIVTLAKR----VQKC--------SAQWP-DIPWihtDSWIKN 735
Cdd:COG0365    98 ---FGAEALAdriEDAEAKVLITADGGLRGGKVIDLKEKVDEALEelpsLEHVivvgrtgaDVPMEgDLDW---DELLAA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  736 yrrssdsfNSDTVLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEG-LIHNVKTMKK--------RYRSTSKtvlVSWLpq 806
Cdd:COG0365   172 --------ASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYvldlkpgdVFWCTAD---IGWA-- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  807 yhdMGLIGGLFTALVSGGTSVLFSPMIFIRNPLLWLQTINDYHGTH-SAGPNFafelvIRRLEAEKNKV---YDLSSMVF 882
Cdd:COG0365   239 ---TGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVfFTAPTA-----IRALMKAGDEPlkkYDLSSLRL 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  883 LMIAAEPVRQKTVRRFIELTqpfglseGV-LAPGYGLAE-NCVYVTCAFG-ECKPVFIdwqGRVCCGYVeqddtdtlIRI 959
Cdd:COG0365   311 LGSAGEPLNPEVWEWWYEAV-------GVpIVDGWGQTEtGGIFISNLPGlPVKPGSM---GKPVPGYD--------VAV 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  960 VDPDSltEHQEDGVEGEIWISSPSSG--VGYWGNSEMSQRTFFNQLKNhpnkkFTRTGDLG-RTIDGNLFITGRIKDLII 1036
Cdd:COG0365   373 VDEDG--NPVPPGEEGELVIKGPWPGmfRGYWNDPERYRETYFGRFPG-----WYRTGDGArRDEDGYFWILGRSDDVIN 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1037 VAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEVlaqKGISIpdssdqVGLVVIaevREGKAVSKEVVNNIKARVVEE 1116
Cdd:COG0365   446 VSGHRIGTAEIESALVSHPAVAE---AAVVGVPDEI---RGQVV------KAFVVL---KPGVEPSDELAKELQAHVREE 510

                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 937914749 1117 HGvAVAsvkliKPRTIC------KTTSGKIRRFEcMRQ 1148
Cdd:COG0365   511 LG-PYA-----YPREIEfvdelpKTRSGKIMRRL-LRK 541
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 605-1072 8.98e-42

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: 162.00  E-value: 8.98e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLtstKPVIKPGDRVLLIHLPGLEFIDAFFGCIRAGVI--PV-PVLPPDPMQsggqALLKvenIS 681
Cdd:cd05911    12 TYAQLRTLSRRLAAGLR---KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIfsAAnPIYTADELA----HQLK---IS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  682 KmcnAVAILSTSSYHAAVRA-----GYIKNIVTLAKRVQKCSAQwpdipwihTDSWiknyrrSSDSFNSDTVLFTKPQ-- 754
Cdd:cd05911    82 K---PKVIFTDPDGLEKVKEaakelGPKDKIIVLDDKPDGVLSI--------EDLL------SPTLGEEDEDLPPPLKdg 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRST--SKTVLVSWLPQYHDMGLIgGLFTALVSGGTSVLFSPM 832
Cdd:cd05911   145 KDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNdgSNDVILGFLPLYHIYGLF-TTLASLLNGATVIIMPKF 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  833 ifirNPLLWLQTINDYHGTHSagpNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELtqpfgLSEGVL 912
Cdd:cd05911   224 ----DSELFLDLIEKYKITFL---YLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKR-----FPNATI 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  913 APGYGLAENCVYVTCAFGeckpvFIDWQGrvCCGYVeqdDTDTLIRIVDPDSlTEHQEDGVEGEIWISSPSSGVGYWGNS 992
Cdd:cd05911   292 KQGYGMTETGGILTVNPD-----GDDKPG--SVGRL---LPNVEAKIVDDDG-KDSLGPNEPGEICVRGPQVMKGYYNNP 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  993 EMSQRTFFNQlknhpnkKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEktvesssEVLR--PGC--CAVVG 1067
Cdd:cd05911   361 EATKETFDED-------GWLHTGDIGYfDEDGYLYIVDRKKELIKYKGFQVAPAELE-------AVLLehPGVadAAVIG 426


                  ....*
gi 937914749 1068 IPEEV 1072
Cdd:cd05911   427 IPDEV 431
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 601-1142 3.10e-41

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: 159.31  E-value: 3.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  601 MNRRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVlppdpmqsggqallkveNI 680
Cdd:cd17631    18 GRSLTYAELDERVNRLAHALRALG---VAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL-----------------NF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  681 SKMCNAVAilstssyhaavragYIknivtlakrVQKCSAqwpdipwihtdswiknyrrssdsfnsdTVLFtkpqpSDLCF 760
Cdd:cd17631    78 RLTPPEVA--------------YI---------LADSGA---------------------------KVLF-----DDLAL 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  761 LQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVL---FSPMIFirn 837
Cdd:cd17631   103 LMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVIlrkFDPETV--- 179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  838 pllwLQTINDYHGTHSAGPNFAFELVIRRLEAEKnkvYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFglsegvlAPGYG 917
Cdd:cd17631   180 ----LDLIERHRVTSFFLVPTMIQALLQHPRFAT---TDLSSLRAVIYGGAPMPERLLRALQARGVKF-------VQGYG 245

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  918 LAEnCVYVTCA---------FGEC-KPVFidwqgrvccgYVEqddtdtlIRIVDPDslTEHQEDGVEGEIWISSPSSGVG 987
Cdd:cd17631   246 MTE-TSPGVTFlspedhrrkLGSAgRPVF----------FVE-------VRIVDPD--GREVPPGEVGEIVVRGPHVMAG 305

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  988 YWGNSEMSQRTFFNqlknhpnkKFTRTGDLGRT-IDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVV 1066
Cdd:cd17631   306 YWNRPEATAAAFRD--------GWFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAE---VAVI 374

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1067 GIPEEvlaqkgisipdssdQVGLVVIAEV--REGKAVS-KEVVNNIKARvveehgvaVASVKLikPRTIC------KTTS 1137
Cdd:cd17631   375 GVPDE--------------KWGEAVVAVVvpRPGAELDeDELIAHCRER--------LARYKI--PKSVEfvdalpRNAT 430


                  ....*
gi 937914749 1138 GKIRR 1142
Cdd:cd17631   431 GKILK 435
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 605-1142 2.93e-40

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: 157.86  E-value: 2.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELhGNASYIAQKLLTSTKpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPpdpmqsggqALLKVE---NIS 681
Cdd:cd05926    16 TYADL-AELVDDLARQLAALG--IKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNP---------AYKKAEfefYLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  682 KMCNAVAILSTSSYHAAVRAG--YIKNIVTLAKRVQKCSAQWPDIPWIHTDSWIKNYRRSsdsfnsdtvlfTKPQPSDLC 759
Cdd:cd05926    84 DLGSKLVLTPKGELGPASRAAskLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSE-----------GVPLPDDLA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  760 FLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSK--TVLVswLPQYHDMGLIGGLFTALVSGGTSVL---FSPMIF 834
Cdd:cd05926   153 LILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDdrTLVV--MPLFHVHGLVASLLSTLAAGGSVVLpprFSASTF 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 irnpllWlQTINDYHGT-HSAGPNFAFELVIRrleAEKNKVYDLSSMVFLMIAAEPVRQKTvrrFIELTQPFGlsegvlA 913
Cdd:cd05926   231 ------W-PDVRDYNATwYTAVPTIHQILLNR---PEPNPESPPPKLRFIRSCSASLPPAV---LEALEATFG------A 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  914 P---GYGLAENCVYVTCafgecKPVFIDWQ--GRVCCGYVEQddtdtlIRIVDPDSltEHQEDGVEGEIWISSPSSGVGY 988
Cdd:cd05926   292 PvleAYGMTEAAHQMTS-----NPLPPGPRkpGSVGKPVGVE------VRILDEDG--EILPPGVVGEICLRGPNVTRGY 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  989 WGNSEMSQRTFFnqlKNhpnkKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVG 1067
Cdd:cd05926   359 LNNPEANAEAAF---KD----GWFRTGDLGYlDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLE---AVAFG 428

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1068 IPEEVLAQkgisipdssdQVGLVVIAevREGKAVSK-EVVNNIKARvveehgvaVASVKLikPRTIC------KTTSGKI 1140
Cdd:cd05926   429 VPDEKYGE----------EVAAAVVL--REGASVTEeELRAFCRKH--------LAAFKV--PKKVYfvdelpKTATGKI 486


                  ..
gi 937914749 1141 RR 1142
Cdd:cd05926   487 QR 488
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 587-1144 4.91e-39

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 154.57  E-value: 4.91e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  587 KNVIYTWineEGKlmnRRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPV---LP 663
Cdd:PRK06187   21 DKEAVYF---DGR---RTTYAELDERVNRLANALRALG---VKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPInirLK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  664 PDpmqsggqallKVENISKMCNAVAILSTSSYHAAVRA-----GYIKNIVTLAKrvqkCSAQWPDIPWIHTDSWIKNyrr 738
Cdd:PRK06187   92 PE----------EIAYILNDAEDRVVLVDSEFVPLLAAilpqlPTVRTVIVEGD----GPAAPLAPEVGEYEELLAA--- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  739 ssdsfNSDTVLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLigGL-F 817
Cdd:PRK06187  155 -----ASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAW--GLpY 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  818 TALVSGGTSVLfsPMIFIRNPLLWLqtindyhgTHSAGPNFAF------ELVIRRLEAEKnkvYDLSSMVFLMIAAEPVR 891
Cdd:PRK06187  228 LALMAGAKQVI--PRRFDPENLLDL--------IETERVTFFFavptiwQMLLKAPRAYF---VDFSSLRLVIYGGAALP 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  892 QKTVRRFIELtqpFGLSegvLAPGYGLAENCVYVTCAFGEcKPVFIDW-----QGRVCCGyVEqddtdtlIRIVDPDsLT 966
Cdd:PRK06187  295 PALLREFKEK---FGID---LVQGYGMTETSPVVSVLPPE-DQLPGQWtkrrsAGRPLPG-VE-------ARIVDDD-GD 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  967 EHQEDGVE-GEIWISSPSSGVGYWGNSEMSQRTFFNQlknhpnkkFTRTGDLGrTID--GNLFITGRIKDLIIVAGRNIY 1043
Cdd:PRK06187  359 ELPPDGGEvGEIIVRGPWLMQGYWNRPEATAETIDGG--------WLHTGDVG-YIDedGYLYITDRIKDVIISGGENIY 429

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1044 SADVEKTVESSSEVLRpgcCAVVGIP-----EEVLAqkgisipdssdqvgLVViaeVREGKAVS-KEVVNNIKARvveeh 1117
Cdd:PRK06187  430 PRELEDALYGHPAVAE---VAVIGVPdekwgERPVA--------------VVV---LKPGATLDaKELRAFLRGR----- 484

                         570       580       590
                  ....*....|....*....|....*....|...
gi 937914749 1118 gvaVASVKLikPRTIC------KTTSGKIRRFE 1144
Cdd:PRK06187  485 ---LAKFKL--PKRIAfvdelpRTSVGKILKRV 512
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 605-1031 7.08e-36

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: 142.79  E-value: 7.08e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   605 TYQELHGNASYIAQKLLTSTKpvIKPGDRVLlIHLP-GLEFIDAFFGCIRAGVIPVPVLPPDPMQsggqallKVENISKM 683
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGG--VGPGDRVA-VLLErSAELVVAILAVLKAGAAYVPLDPAYPAE-------RLAFILED 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   684 CNAVAILSTSSyHAAVRAGYIKNIVTLAkrvqkcsaqwPDIPWIHTDSwiknyrrssdsfNSDTVLFTKPQPSDLCFLQF 763
Cdd:TIGR01733   71 AGARLLLTDSA-LASRLAGLVLPVILLD----------PLELAALDDA------------PAPPPPDAPSGPDDLAYVIY 127

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   764 TSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIgGLFTALVSGGTSVLFSPMIFIRNPLLWLQ 843
Cdd:TIGR01733  128 TSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPEDEERDDAALLAA 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   844 TINDYHGTHSAGPNFAFELvirrLEAEknKVYDLSSMVFLMIAAEPVRQKTVRRFIELtqpfgLSEGVLAPGYGLAENCV 923
Cdd:TIGR01733  207 LIAEHPVTVLNLTPSLLAL----LAAA--LPPALASLRLVILGGEALTPALVDRWRAR-----GPGARLINLYGPTETTV 275

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   924 YVTCAfgECKPVFIDWQGRVCCGYVEqddTDTLIRIVDPDslTEHQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFFnql 1003
Cdd:TIGR01733  276 WSTAT--LVDPDDAPRESPVPIGRPL---ANTRLYVLDDD--LRPVPVGVVGELYIGGPGVARGYLNRPELTAERFV--- 345

                          410       420       430
                   ....*....|....*....|....*....|....
gi 937914749  1004 kNHP-----NKKFTRTGDLGR-TIDGNLFITGRI 1031
Cdd:TIGR01733  346 -PDPfaggdGARLYRTGDLVRyLPDGNLEFLGRI 378
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 603-1076 3.46e-35

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: 143.36  E-value: 3.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLiHLP-GLEFIDAFFGCIRAGVIPVPVLPpdpmqsggqALLKVEnIS 681
Cdd:COG1021    50 RLSYAELDRRADRLAAGLLALG---LRPGDRVVV-QLPnVAEFVIVFFALFRAGAIPVFALP---------AHRRAE-IS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  682 KMCN---AVAILStssyhAAVRAGYikNIVTLAKRVQkcsAQWPDI----------PWIHTDSWiknYRRSSDSFNSDtv 748
Cdd:COG1021   116 HFAEqseAVAYII-----PDRHRGF--DYRALARELQ---AEVPSLrhvlvvgdagEFTSLDAL---LAAPADLSEPR-- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  749 lftkPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIG-GLFTALVSGGTSV 827
Cdd:COG1021   181 ----PDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpGVLGVLYAGGTVV 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  828 L---FSPM-IFirnPLlwlqtINDYHGTHSA-GPnfafELVIRRLEAEKNKVYDLSSMVFLMIA----AEPVRQKTVRRF 898
Cdd:COG1021   257 LapdPSPDtAF---PL-----IERERVTVTAlVP----PLALLWLDAAERSRYDLSSLRVLQVGgaklSPELARRVRPAL 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  899 -IELTQPFGLSEGVLapgyglaeNC--------VYVTCafgeckpvfidwQGRVCCGYVEqddtdtlIRIVDPDSltEHQ 969
Cdd:COG1021   325 gCTLQQVFGMAEGLV--------NYtrlddpeeVILTT------------QGRPISPDDE-------VRIVDEDG--NPV 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  970 EDGVEGEIWISSPSSGVGYWGNSEMSQRTFFNQlknhpnkKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVE 1048
Cdd:COG1021   376 PPGEVGELLTRGPYTIRGYYRAPEHNARAFTPD-------GFYRTGDLVRrTPDGYLVVEGRAKDQINRGGEKIAAEEVE 448

                         490       500
                  ....*....|....*....|....*...
gi 937914749 1049 KTVESSSEVLRpgcCAVVGIPEEVLAQK 1076
Cdd:COG1021   449 NLLLAHPAVHD---AAVVAMPDEYLGER 473
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 603-1143 1.19e-34

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: 141.35  E-value: 1.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPV---LPPDPMQ-----SGGQAL 674
Cdd:cd05959    29 SLTYAELEAEARRVAGALRALG---VKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVntlLTPDDYAyyledSRARVV 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  675 LkVEniSKMCNAVAILSTSSYHAAVRAgyiknIVTLAKRVQKCSAQWPDIPWIHtdswiknyrrsSDSFNSdtvlfTKPQ 754
Cdd:cd05959   106 V-VS--GELAPVLAAALTKSEHTLVVL-----IVSGGAGPEAGALLLAELVAAE-----------AEQLKP-----AATH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKR-YRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFS--P 831
Cdd:cd05959   162 ADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPerP 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  832 mifirNPLLWLQTINDYHGTHSAG-PNFAFELvirrLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELtqpFGLSeg 910
Cdd:cd05959   242 -----TPAAVFKRIRRYRPTVFFGvPTLYAAM----LAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKAR---FGLD-- 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  911 vLAPGYGLAENC-VYVTCAFGECKPvfiDWQGRVCCGYVeqddtdtlIRIVDPDSltEHQEDGVEGEIWISSPSSGVGYW 989
Cdd:cd05959   308 -ILDGIGSTEMLhIFLSNRPGRVRY---GTTGKPVPGYE--------VELRDEDG--GDVADGEPGELYVRGPSSATMYW 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  990 GNSEMSQRTFFNQlknhpnkkFTRTGD-LGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGI 1068
Cdd:cd05959   374 NNRDKTRDTFQGE--------WTRTGDkYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLE---AAVVGV 442

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1069 PEEVlaqkGISIPdssdqVGLVVIAEVREGKAVSKEvvnNIKARVVEehgvAVASVKLikPRTIC------KTTSGKIRR 1142
Cdd:cd05959   443 EDED----GLTKP-----KAFVVLRPGYEDSEALEE---ELKEFVKD----RLAPYKY--PRWIVfvdelpKTATGKIQR 504


                  .
gi 937914749 1143 F 1143
Cdd:cd05959   505 F 505
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 755-1147 1.63e-34

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: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 137.02  E-value: 1.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPmIF 834
Cdd:cd05917     1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSP-SF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 irNPLLWLQTINDYHGTHSAGPNFAFelvIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELtqpFGLSEGVLAp 914
Cdd:cd05917    80 --DPLAVLEAIEKEKCTALHGVPTMF---IAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEV---MNMKDVTIA- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  915 gYGLAENCVYVTCAFGEcKPVFIDwqgrvcCGYVEQDDTDTLIRIVDPDSLTEHQEdGVEGEIWISSPSSGVGYWGNSEM 994
Cdd:cd05917   151 -YGMTETSPVSTQTRTD-DSIEKR------VNTVGRIMPHTEAKIVDPEGGIVPPV-GVPGELCIRGYSVMKGYWNDPEK 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  995 SQRTffnqlknHPNKKFTRTGDLGrTID--GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEV 1072
Cdd:cd05917   222 TAEA-------IDGDGWLHTGDLA-VMDedGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSD---VQVVGVPDER 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1073 LAQkgisipdssdQVGLVVIaeVREGKAVSKEvvnNIKARVVEEhgvaVASVKLikPRTIC------KTTSGKIRRFEcM 1146
Cdd:cd05917   291 YGE----------EVCAWIR--LKEGAELTEE---DIKAYCKGK----IAHYKV--PRYVFfvdefpLTVSGKIQKFK-L 348


                  .
gi 937914749 1147 R 1147
Cdd:cd05917   349 R 349
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 602-1048 2.81e-34

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 140.87  E-value: 2.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  602 NRRTYQELHGN----ASYIAQKLltstkpVIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVlppDPMqsggqalLKV 677
Cdd:PRK08314   34 RAISYRELLEEaerlAGYLQQEC------GVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPV---NPM-------NRE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  678 ENIS---KMCNAVAILSTSSYHA----AVRAGYIKNIVtlakrVQKCSAQWPDIPWIHTDSWIKNYRRSSDSFNSDTVLF 750
Cdd:PRK08314   98 EELAhyvTDSGARVAIVGSELAPkvapAVGNLRLRHVI-----VAQYSDYLPAEPEIAVPAWLRAEPPLQALAPGGVVAW 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  751 T------------KPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFT 818
Cdd:PRK08314  173 KealaaglappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNA 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  819 ALVSGGTSVLFSpmifiRnpllW-----LQTINDYHGTH-----------SAGPNFAfelvirrleaeknkVYDLSSMVF 882
Cdd:PRK08314  253 PIYAGATVVLMP-----R----WdreaaARLIERYRVTHwtniptmvvdfLASPGLA--------------ERDLSSLRY 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  883 LMIAAEPVRQKTVRRFIELtqpFGLSegvLAPGYGLAEncvyvTCAFGECKPVfiDWQGRVCCGyVEQDDTDTliRIVDP 962
Cdd:PRK08314  310 IGGGGAAMPEAVAERLKEL---TGLD---YVEGYGLTE-----TMAQTHSNPP--DRPKLQCLG-IPTFGVDA--RVIDP 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  963 DSLTEhQEDGVEGEIWISSPSSGVGYWGNSEMSQRTF--FNqlknhpNKKFTRTGDLGRT-IDGNLFITGRIKDLIIVAG 1039
Cdd:PRK08314  374 ETLEE-LPPGEVGEIVVHGPQVFKGYWNRPEATAEAFieID------GKRFFRTGDLGRMdEEGYFFITDRLKRMINASG 446


                  ....*....
gi 937914749 1040 RNIYSADVE 1048
Cdd:PRK08314  447 FKVWPAEVE 455
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 603-1144 7.33e-34

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 137.51  E-value: 7.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLiHLPG-LEFIDAFFGCIRAGVIPVPVLPpdpmqSGGQALLkvenis 681
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALG---VGPGDVVAF-QLPNwWEFAVLYLACLRIGAVTNPILP-----FFREHEL------ 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  682 kmcnaVAILSTSsyhaavragyiknivtlAKRVqkcsaqwpdipWIHTDSWiknyrRSSDSfnsdtvlftKPQPSDLCFL 761
Cdd:cd05903    66 -----AFILRRA-----------------KAKV-----------FVVPERF-----RQFDP---------AAMPDAVALL 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  762 QFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSpmifIRNPLLW 841
Cdd:cd05903    99 LFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD----IWDPDKA 174

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  842 LQTINDYHGTHSAG-PNFAFELvirrLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELtqpFGLsegVLAPGYGLAE 920
Cdd:cd05903   175 LALMREHGVTFMMGaTPFLTDL----LNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAEL---LGA---KVCSAYGSTE 244

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  921 NCvyvtCAFGECKPV----FIDWQGRVCCGyVEqddtdtlIRIVDPDSLTEHQedGVEGEIWISSPSSGVGYWGNSEMSq 996
Cdd:cd05903   245 CP----GAVTSITPApedrRLYTDGRPLPG-VE-------IKVVDDTGATLAP--GVEGELLSRGPSVFLGYLDRPDLT- 309

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  997 RTFFNQLknhpnkkFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEVLAQ 1075
Cdd:cd05903   310 ADAAPEG-------WFRTGDLARlDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIE---AAVVALPDERLGE 379

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937914749 1076 K--GISIPDSSDQVGLVVIAEVREGKAVSKEvvnnikarVVEEHGVAVASVklikPRtickTTSGKIRRFE 1144
Cdd:cd05903   380 RacAVVVTKSGALLTFDELVAYLDRQGVAKQ--------YWPERLVHVDDL----PR----TPSGKVQKFR 434
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 605-1144 1.92e-33

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 138.59  E-value: 1.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLltsTKPVIKPGDRVLLIhLPGL-EFIDAFFGCIRAGVIPV---PVLPPDPMQS-----GGQALL 675
Cdd:PRK05605   59 TYAELGKQVRRAAAGL---RALGVRPGDRVAIV-LPNCpQHIVAFYAVLRLGAVVVehnPLYTAHELEHpfedhGARVAI 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  676 KVENISKMCNA----------VAILSTSSYHAAVRAGYIKNIVTLAKRVQKCSAQWPD-IPWihtdswiKNYRRSSDSFN 744
Cdd:PRK05605  135 VWDKVAPTVERlrrttpletiVSVNMIAAMPLLQRLALRLPIPALRKARAALTGPAPGtVPW-------ETLVDAAIGGD 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  745 SDTVLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMK---KRYRSTSKTVLVSwLPQYHDMGLIGGLFTALV 821
Cdd:PRK05605  208 GSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKawvPGLGDGPERVLAA-LPMFHAYGLTLCLTLAVS 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  822 SGGTSVLFS----PMIFI---RNPLLWLqtindyhgthsagPnfAFELVIRRL--EAEKNKVyDLSSMVFLMIAAEPVRQ 892
Cdd:PRK05605  287 IGGELVLLPapdiDLILDamkKHPPTWL-------------P--GVPPLYEKIaeAAEERGV-DLSGVRNAFSGAMALPV 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  893 KTVRRFIELTQpfglseGVLAPGYGLAEnCVYVTCafgeCKPVFIDWQGrvccGYVEQDDTDTLIRIVDPDSLTEHQEDG 972
Cdd:PRK05605  351 STVELWEKLTG------GLLVEGYGLTE-TSPIIV----GNPMSDDRRP----GYVGVPFPDTEVRIVDPEDPDETMPDG 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  973 VEGEIWISSPSSGVGYWGNSEMSQRTFFNQlknhpnkkFTRTGDLGRT-IDGNLFITGRIKDLIIVAGRNIYSADVEktv 1051
Cdd:PRK05605  416 EEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMeEDGFIRIVDRIKELIITGGFNVYPAEVE--- 484

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1052 esssEVLR--PGC--CAVVGIPEEvlaqkgisipDSSDQVGLVVIAEvrEGKAVSKEvvnNIKARVVEEhgvaVASVKLi 1127
Cdd:PRK05605  485 ----EVLRehPGVedAAVVGLPRE----------DGSEEVVAAVVLE--PGAALDPE---GLRAYCREH----LTRYKV- 540

                         570       580
                  ....*....|....*....|...
gi 937914749 1128 kPRTIC------KTTSGKIRRFE 1144
Cdd:PRK05605  541 -PRRFYhvdelpRDQLGKVRRRE 562
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 605-1142 3.51e-33

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 136.60  E-value: 3.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLltsTKPVIKPGDrVLLIHLP-GLEFIDAFFGCIRAGVIPVPVLPpdpmqsggqaLLKVENISKM 683
Cdd:cd05904    34 TYAELERRVRRLAAGL---AKRGGRKGD-VVLLLSPnSIEFPVAFLAVLSLGAVVTTANP----------LSTPAEIAKQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  684 ---CNAVAILSTSSYHAAVRAGYIKnIVTLAKRVQKCSAQWPDIpwihtdswiknyrrssDSFNSDTVLFTKPQPSDLCF 760
Cdd:cd05904   100 vkdSGAKLAFTTAELAEKLASLALP-VVLLDSAEFDSLSFSDLL----------------FEADEAEPPVVVIKQDDVAA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  761 LQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSK--TVLVSWLPQYHDMGLiGGLFTALVSGGTSVLFSPMIFIRNp 838
Cdd:cd05904   163 LLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDseDVFLCVLPMFHIYGL-SSFALGLLRLGATVVVMPRFDLEE- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  839 llWLQTINDYHGTH-SAGPNFAFELVirrlEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIeltQPFGLSEgvLAPGYG 917
Cdd:cd05904   241 --LLAAIERYKVTHlPVVPPIVLALV----KSPIVDKYDLSSLRQIMSGAAPLGKELIEAFR---AKFPNVD--LGQGYG 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  918 LAE-NCVYVTCAFGECKPVFIDWQGRVCCGyVEqddtdtlIRIVDPDSLtEHQEDGVEGEIWISSPSSGVGYWGNSEMSQ 996
Cdd:cd05904   310 MTEsTGVVAMCFAPEKDRAKYGSVGRLVPN-VE-------AKIVDPETG-ESLPPNQTGELWIRGPSIMKGYLNNPEATA 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  997 RTFfnqlknhpNKK-FTRTGDLGRtID--GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEVL 1073
Cdd:cd05904   381 ATI--------DKEgWLHTGDLCY-IDedGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILD---AAVIPYPDEEA 448

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1074 AQkgisIPdssdqVGLVVIAevREGKAVSKEVVNNIKARVVEEHGV-AVASVKLIkPrticKTTSGKIRR 1142
Cdd:cd05904   449 GE----VP-----MAFVVRK--PGSSLTEDEIMDFVAKQVAPYKKVrKVAFVDAI-P----KSPSGKILR 502
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 605-1144 6.30e-33

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: 135.03  E-value: 6.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLtSTKpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPpdpmqsggqallkveniskmc 684
Cdd:cd05907     7 TWAEFAEEVRALAKGLI-ALG--VEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYP--------------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 navailsTSSyhaavragyiknivtlakrvqkcSAQwpdIPWIHTDSWIKnyrrssdsfnsdtVLFTkPQPSDLCFLQFT 764
Cdd:cd05907    63 -------TSS-----------------------AEQ---IAYILNDSEAK-------------ALFV-EDPDDLATIIYT 95

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  765 SGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVL-------------FSP 831
Cdd:cd05907    96 SGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFassaetllddlseVRP 175

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  832 MIFIRNPLLWlqtindyhGTHSAGpnfafelVIRRLEAE-KNKVYDL---SSMVFLMIAAEPVRQKTVRRF----IELTQ 903
Cdd:cd05907   176 TVFLAVPRVW--------EKVYAA-------IKVKAVPGlKRKLFDLavgGRLRFAASGGAPLPAELLHFFralgIPVYE 240

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  904 pfglsegvlapGYGLAENCVYVTCAFGECkpVFIDWQGRVCCGyVEqddtdtlIRIVDpdsltehqedgvEGEIWISSPS 983
Cdd:cd05907   241 -----------GYGLTETSAVVTLNPPGD--NRIGTVGKPLPG-VE-------VRIAD------------DGEILVRGPN 287

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  984 SGVGYWGNSEMSQRTFFNQLKNHpnkkftrTGDLGRtID--GNLFITGRIKDLIIVA-GRNIYSADVEKTVESS---SEV 1057
Cdd:cd05907   288 VMLGYYKNPEATAEALDADGWLH-------TGDLGE-IDedGFLHITGRKKDLIITSgGKNISPEPIENALKASpliSQA 359

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1058 L-----RPGCCAVVGIPEEVL----AQKGISIPDSSDqvgLVVIAEVREgkAVSKEV--VNnikarvveeHGVA-VASVK 1125
Cdd:cd05907   360 VvigdgRPFLVALIVPDPEALeawaEEHGIAYTDVAE---LAANPAVRA--EIEAAVeaAN---------ARLSrYEQIK 425

                         570       580
                  ....*....|....*....|....*.
gi 937914749 1126 ----LIKPRTI---CKTTSGKIRRFE 1144
Cdd:cd05907   426 kfllLPEPFTIengELTPTLKLKRPV 451
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 605-1071 7.56e-33

The adenylation domain of nonribosomal peptide synthetases (NRPS); 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: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 134.58  E-value: 7.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTStkpVIKPGDRV-LLIHlPGLEFIDAFFGCIRAGVIPVPVLPPDPmqsggqallkVENISkm 683
Cdd:cd05930    14 TYAELDARANRLARYLRER---GVGPGDLVaVLLE-RSLEMVVAILAVLKAGAAYVPLDPSYP----------AERLA-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  684 cnavAILSTSsyHAAVragyiknIVTlakrvqkcsaqwpdipwihtdswiknyrrssdsfnsdtvlftkpQPSDLCFLQF 763
Cdd:cd05930    78 ----YILEDS--GAKL-------VLT--------------------------------------------DPDDLAYVIY 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  764 TSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGlIGGLFTALVSGGTSVLFSPMiFIRNPLLWLQ 843
Cdd:cd05930   101 TSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVS-VWEIFGALLAGATLVVLPEE-VRKDPEALAD 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  844 TINDYHGTHSAGPNFAFELVIRRLEAEknkvyDLSSMVFLMIAAEPVRQKTVRRFIELtqpfgLSEGVLAPGYGLAENCV 923
Cdd:cd05930   179 LLAEEGITVLHLTPSLLRLLLQELELA-----ALPSLRLVLVGGEALPPDLVRRWREL-----LPGARLVNLYGPTEATV 248

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  924 YVTcaFGECKPVFIDWQ----GRVCCGYVeqddtdtlIRIVDPDSltEHQEDGVEGEIWISSPSSGVGYWGNSEMSQRtF 999
Cdd:cd05930   249 DAT--YYRVPPDDEEDGrvpiGRPIPNTR--------VYVLDENL--RPVPPGVPGELYIGGAGLARGYLNRPELTAE-R 315

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937914749 1000 FNQLKNHPNKKFTRTGDLGRTI-DGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEE 1071
Cdd:cd05930   316 FVPNPFGPGERMYRTGDLVRWLpDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVRE---AAVVAREDG 385
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 747-1071 3.94e-31

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: 129.14  E-value: 3.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  747 TVLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTS 826
Cdd:cd05935    75 KVAVVGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTY 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  827 VLFSpmIFIRNPLlwLQTINDYHGTHSagpNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFG 906
Cdd:cd05935   155 VLMA--RWDRETA--LELIEKYKVTFW---TNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRF 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  907 LSegvlapGYGLAEncvyvTCAFGECKPVFIdwQGRVCCGyVEQDDTDTliRIVDPDSLTEhQEDGVEGEIWISSPSSGV 986
Cdd:cd05935   228 VE------GYGLTE-----TMSQTHTNPPLR--PKLQCLG-IP*FGVDA--RVIDIETGRE-LPPNEVGEIVVRGPQIFK 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  987 GYWGNSEMSQRTFFnQLKnhpNKKFTRTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAV 1065
Cdd:cd05935   291 GYWNRPEETEESFI-EIK---GRRFFRTGDLGyMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E---VCV 363


                  ....*.
gi 937914749 1066 VGIPEE 1071
Cdd:cd05935   364 ISVPDE 369
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 602-1144 2.17e-30

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: 126.64  E-value: 2.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  602 NRRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLiHLP-GLEFIDAFFGCIRAGVIPVPVlppdpmqsggqallkveni 680
Cdd:cd05934     2 RRWTYAELLRESARIAAALAALG---IRPGDRVAL-MLDnCPEFLFAWFALAKLGAVLVPI------------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  681 skmcNAVAILSTSSYHaavragyiknivtlakrVQKCSAQWpdipwihtdswiknyrrssdsfnsdtvLFTkpqpsDLCF 760
Cdd:cd05934    59 ----NTALRGDELAYI-----------------IDHSGAQL---------------------------VVV-----DPAS 85

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  761 LQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVL---FSPMIFirn 837
Cdd:cd05934    86 ILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLlprFSASRF--- 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  838 pllWLQtINDYHGT--HSAGpnfafeLVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQkTVRRFIEltqPFGLsegVLAPG 915
Cdd:cd05934   163 ---WSD-VRRYGATvtNYLG------AMLSYLLAQPPSPDDRAHRLRAAYGAPNPPE-LHEEFEE---RFGV---RLLEG 225

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  916 YGLAENCVYVTCAFGECKPVFidwqgrvCCGYVEQDDTdtlIRIVDPDslTEHQEDGVEGEIWI-SSPSSGV--GYWGNS 992
Cdd:cd05934   226 YGMTETIVGVIGPRDEPRRPG-------SIGRPAPGYE---VRIVDDD--GQELPAGEPGELVIrGLRGWGFfkGYYNMP 293

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  993 EMSqrtffnqLKNHPNKKFtRTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEE 1071
Cdd:cd05934   294 EAT-------AEAMRNGWF-HTGDLGyRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVRE---AAVVAVPDE 362

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749 1072 VlaqkgisipdSSDQVGLVVIaeVREGKAVSKEVVnnikARVVEEHgvaVASVKLikPRTIC------KTTSGKIRRFE 1144
Cdd:cd05934   363 V----------GEDEVKAVVV--LRPGETLDPEEL----FAFCEGQ---LAYFKV--PRYIRfvddlpKTPTEKVAKAQ 420
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 603-1142 3.92e-30

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 127.71  E-value: 3.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIhLPG-LEFIDAFFGCIRAGVIPVPVLP---PDPM-----QSGGQA 673
Cdd:PRK07656   30 RLTYAELNARVRRAAAALAALG---IGKGDRVAIW-APNsPHWVIAALGALKAGAVVVPLNTrytADEAayilaRGDAKA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  674 LLkveniskmcnAVAILSTSSYHAAVRAGYIKNIVTlakrvqkCSAQWPDIPWIHTDSWIKNYRRSSDSFNSDTVlftkp 753
Cdd:PRK07656  106 LF----------VLGLFLGVDYSATTRLPALEHVVI-------CETEEDDPHTEKMKTFTDFLAAGDPAERAPEV----- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  754 QPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKR--YRSTSKTVLVswLPQYHDMGLIGGLFTALVSGGTsVLFSP 831
Cdd:PRK07656  164 DPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYlgLTEGDRYLAA--NPFFHVFGYKAGVNAPLMRGAT-ILPLP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  832 mIFirNPLLWLQTINDYHGTHSAGP----NFAfelvirrLEAEKNKVYDLSSMVFLMI--AAEPVRqkTVRRFielTQPF 905
Cdd:PRK07656  241 -VF--DPDEVFRLIETERITVLPGPptmyNSL-------LQHPDRSAEDLSSLRLAVTgaASMPVA--LLERF---ESEL 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  906 GLSegVLAPGYGLAENCVYVT-CAFGECKPVFIDWQGRVCCGyVEqddtdtlIRIVDPdsLTEHQEDGVEGEIWISSPSS 984
Cdd:PRK07656  306 GVD--IVLTGYGLSEASGVTTfNRLDDDRKTVAGTIGTAIAG-VE-------NKIVNE--LGEEVPVGEVGELLVRGPNV 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  985 GVGYWGNSEMSQRTffnqLKN----HpnkkftrTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTV---ESSSE 1056
Cdd:PRK07656  374 MKGYYDDPEATAAA----IDAdgwlH-------TGDLGRlDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLyehPAVAE 442

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1057 VlrpgccAVVGIPEEvlaqkgisipdssdqvglvviaevREGKAVSKEVVNNIKARVVEEHGVAVASVKLIK---PRTIC 1133
Cdd:PRK07656  443 A------AVIGVPDE------------------------RLGEVGKAYVVLKPGAELTEEELIAYCREHLAKykvPRSIE 492

                         570
                  ....*....|....*
gi 937914749 1134 ------KTTSGKIRR 1142
Cdd:PRK07656  493 fldelpKNATGKVLK 507
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
605-1144 2.90e-29

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 125.63  E-value: 2.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTkpvIKPGDRVLLiHLPGL-EFIDAFFGCIRAGVIPVPVLPpdpmQSGGQALLKVENiskM 683
Cdd:PRK06087   51 TYSALDHAASRLANWLLAKG---IEPGDRVAF-QLPGWcEFTIIYLACLKVGAVSVPLLP----SWREAELVWVLN---K 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  684 CNAVAILSTSSYHaavRAGYIKNIVTLAKR---------VQKCSAQWPDIPWIHTdswIKNYRRSSDSFNSDTvlftkpq 754
Cdd:PRK06087  120 CQAKMFFAPTLFK---QTRPVDLILPLQNQlpqlqqivgVDKLAPATSSLSLSQI---IADYEPLTTAITTHG------- 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 pSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSpmIF 834
Cdd:PRK06087  187 -DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD--IF 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 irNPLLWLQTINDYHGTHSAGPN-FAFELvIRRLEAEKnkvYDLSSMVFLMIAAEPVRQKTVRRfielTQPFGLsegVLA 913
Cdd:PRK06087  264 --TPDACLALLEQQRCTCMLGATpFIYDL-LNLLEKQP---ADLSALRFFLCGGTTIPKKVARE----CQQRGI---KLL 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  914 PGYGLAENCVYVTCAFGECKPVFIDWQGRVCCGyVEqddtdtlIRIVDpdsltEHQED---GVEGEIWISSPSSGVGYWG 990
Cdd:PRK06087  331 SVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAG-VE-------IKVVD-----EARKTlppGCEGEEASRGPNVFMGYLD 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  991 NSEMSQRTFfnqlknhPNKKFTRTGDLGRT-IDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVlrpGCCAVVGIP 1069
Cdd:PRK06087  398 EPELTARAL-------DEEGWYYSGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKI---HDACVVAMP 467

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937914749 1070 EEVLAQKGISIPDSSDQVGLVVIAEVRE---GKAVSKevvnnikaRVVEEHGVAVASVklikPRtickTTSGKIRRFE 1144
Cdd:PRK06087  468 DERLGERSCAYVVLKAPHHSLTLEEVVAffsRKRVAK--------YKYPEHIVVIDKL----PR----TASGKIQKFL 529
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 1493-1892 2.14e-28

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 124.09  E-value: 2.14e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1493 IWSVDFVKWWAlnkAQALAAKMLAVHLKGTIFLNYWFKMQGARIGSSVVIDTV--DITDpsLLTVADGAVLAEGALVQGH 1570
Cdd:TIGR02353   75 IWGSTYLRFWT---VKRLVDAAPTVLLSGSPLYSLYLRALGAKIGKGVDIGSLppVCTD--LLTIGAGTIVRKEVMLLGY 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1571 EVCNEVLSFRPIWIGCEASIGPYAVLQKGTVVEDGAVVPPLQKTGAGKSTRRTSR--TSVSIKKEAAKANMILEHLV-SI 1647
Cdd:TIGR02353  150 RAERGRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIPDGERwhGSPAQKTGADYRKVQPARPYtVR 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1648 YAVGILGALSgaIVYTLYTHLSGKAASPLhfsfaciAGAFhWLPAAITAYAVIvqetptsALSFALFTAFADLSYGVILS 1727
Cdd:TIGR02353  230 RRLYVAGALF--VVFVLLPPLAFLFAIPV-------AITF-DEIDWTLGPDMV-------GFILALVLTFVALAGFIAYT 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1728 ILTSITSRAL---AAKPGTK--QNGIASLIHRRITISAHVRFAKMLSG-TEAFCVYLRLLGAKIGRHCSIRAINpVANPE 1801
Cdd:TIGR02353  293 VLLLAAVRLLlnlVLKPGRYyvHSGFYYQAWTVQQLMDNSRVLLFPLYaSSYIPHWYRALGAKIGKVAEISSAQ-HEVPD 371

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1802 LISVGDGVHLGDFCNIVPGFYSKGGFTSAEIKVQENTVVGSGSLLLPGCVLQENVILGALSVAPENAVLRRGGVYVGS-- 1879
Cdd:TIGR02353  372 LTDIGEETFIADGLLMGNARLSGGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGSpp 451

                          410
                   ....*....|....
gi 937914749  1880 -QSPAMVKNTLLDE 1892
Cdd:TIGR02353  452 fELPRRVNRDDELE 465
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 603-1076 2.46e-28

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: 121.67  E-value: 2.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLiHLP-GLEFIDAFFGCIRAGVIPVPVLPpdpmqsgGQALLKVENIS 681
Cdd:cd05920    40 RLTYRELDRRADRLAAGLRGLG---IRPGDRVVV-QLPnVAEFVVLFFALLRLGAVPVLALP-------SHRRSELSAFC 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  682 KMCNAVAILSTSSY----HAAvragyiknivtLAKRVQKCSAqwpdipwihtdswiknyrrssdsfnsdtvlftkpqpsD 757
Cdd:cd05920   109 AHAEAVAYIVPDRHagfdHRA-----------LARELAESIP-------------------------------------E 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  758 LCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIG-GLFTALVSGGTSVLFSPMifir 836
Cdd:cd05920   141 VALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpGVLGTLLAGGRVVLAPDP---- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  837 NPLLWLQTINDYHGTHSAgpnFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIE-----LTQPFGLSEGV 911
Cdd:cd05920   217 SPDAAFPLIEREGVTVTA---LVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPvlgctLQQVFGMAEGL 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  912 LApgyglaencvYVtcAFGECKPVFIDWQGRVCCGYVEqddtdtlIRIVDPDSLTehQEDGVEGEIWISSPSSGVGYWGN 991
Cdd:cd05920   294 LN----------YT--RLDDPDEVIIHTQGRPMSPDDE-------IRVVDEEGNP--VPPGEEGELLTRGPYTIRGYYRA 352

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  992 SEMSQRTFFNQlknhpnkKFTRTGDL-GRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPE 1070
Cdd:cd05920   353 PEHNARAFTPD-------GFYRTGDLvRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHD---AAVVAMPD 422


                  ....*.
gi 937914749 1071 EVLAQK 1076
Cdd:cd05920   423 ELLGER 428
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 605-1143 1.08e-27

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-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. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 119.47  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQkLLTSTKpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPpdpmqsggqallkveniskmc 684
Cdd:cd05914     9 TYKDLADNIAKFAL-LLKING--VGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILA--------------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 navailstsSYHAAVragyIKNIVTlakrvqkcsaqwpdipwihtdswiknyrrssdsfNSDTVLFTKPQPSDLCFLQFT 764
Cdd:cd05914    65 ---------EFTADE----VHHILN----------------------------------HSEAKAIFVSDEDDVALINYT 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  765 SGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMifiRNPLLWLQT 844
Cdd:cd05914    98 SGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKI---PSAKIIALA 174

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  845 IndYHGTHSAGPNFAFELVIRRLEAEKNKVyDLSSMVFLMIAAEPVRQKTVRRFIELTQPFG--LSEGVLApGYGLAENC 922
Cdd:cd05914   175 F--AQVTPTLGVPVPLVIEKIFKMDIIPKL-TLKKFKFKLAKKINNRKIRKLAFKKVHEAFGgnIKEFVIG-GAKINPDV 250

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  923 --------VYVTCAFG--ECKPV--FIDWqGRVCCGYVEQDDTDTLIRIVDPDSLTEhqedgvEGEIWISSPSSGVGYWG 990
Cdd:cd05914   251 eeflrtigFPYTIGYGmtETAPIisYSPP-NRIRLGSAGKVIDGVEVRIDSPDPATG------EGEIIVRGPNVMKGYYK 323

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  991 NSEMSQRTFfnqlknHPNKKFtRTGDLGrTID--GNLFITGRIKDLIIV-AGRNIYSADVEKTVESSSEVLRpgccAVVG 1067
Cdd:cd05914   324 NPEATAEAF------DKDGWF-HTGDLG-KIDaeGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLE----SLVV 391

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749 1068 IPEEVLAQKGISIPDSSDQVGLVVIAEVregKAVSKEVVNNIKARVVEEHgvAVASVKLIKpRTICKTTSGKIRRF 1143
Cdd:cd05914   392 VQEKKLVALAYIDPDFLDVKALKQRNII---DAIKWEVRDKVNQKVPNYK--KISKVKIVK-EEFEKTPKGKIKRF 461
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 602-1059 1.94e-27

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. 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: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 118.18  E-value: 1.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  602 NRRTYQELHGNASYIAQKLLtstKPVIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPV---LPPDPMQsggqallkve 678
Cdd:cd17653    21 GSLTYGELDAASNALANRLL---QLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLdakLPSARIQ---------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  679 niskmcnavAILSTSsyhaavRAGYIknivtlakrvqkcsaqwpdipwIHTDSwiknyrrssdsfnsdtvlftkpqPSDL 758
Cdd:cd17653    88 ---------AILRTS------GATLL----------------------LTTDS-----------------------PDDL 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  759 CFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRST-SKTVLvswlpQYHDMGL---IGGLFTALVSGGTSVLFSPMif 834
Cdd:cd17653   108 AYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGpGSRVA-----QVLSIAFdacIGEIFSTLCNGGTLVLADPS-- 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 irNPllWLQTINDYHGTHSAgPNFafelvirrLEAEKNKVYDLSSMVFLmiAAEPVRQKTVRRFieltqpfglSEGV-LA 913
Cdd:cd17653   181 --DP--FAHVARTVDALMST-PSI--------LSTLSPQDFPNLKTIFL--GGEAVPPSLLDRW---------SPGRrLY 236

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  914 PGYGLAEnCVyVTCAFGECKPvfidwQGRVCCGYVEQDDTdtlIRIVDPDslTEHQEDGVEGEIWISSPSSGVGYWGNSE 993
Cdd:cd17653   237 NAYGPTE-CT-ISSTMTELLP-----GQPVTIGKPIPNST---CYILDAD--LQPVPEGVVGEICISGVQVARGYLGNPA 304

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937914749  994 MSQRTFFNQlKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLR 1059
Cdd:cd17653   305 LTASKFVPD-PFWPGSRMYRTGDYGRwTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVT 370
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
605-1105 3.77e-27

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


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 119.43  E-value: 3.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPV---LPPDPMQ-----SGGQALLk 676
Cdd:COG1022    42 TWAEFAERVRALAAGLLALG---VKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIyptSSAEEVAyilndSGAKVLF- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  677 VENiSKMCNAVAilstssyHAAVRAGYIKNIVTLAKRVQkcsaqwPDIPWIHT-DSWIknyRRSSDSFNSDTV--LFTKP 753
Cdd:COG1022   118 VED-QEQLDKLL-------EVRDELPSLRHIVVLDPRGL------RDDPRLLSlDELL---ALGREVADPAELeaRRAAV 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  754 QPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFtaLVSGGTSVLFS--- 830
Cdd:COG1022   181 KPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYY--ALAAGATVAFAesp 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  831 -----------PMIFIRNPLLW---LQTINDyhGTHSAGP------NFAFELVIRRLEAE------------KNKVYDLs 878
Cdd:COG1022   259 dtlaedlrevkPTFMLAVPRVWekvYAGIQA--KAEEAGGlkrklfRWALAVGRRYARARlagkspslllrlKHALADK- 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  879 sMVFlmiaaEPVRQKT---VRRFI--------ELTQPF-GLseGV-LAPGYGLAENCVYVTC-AFGECKP--VfidwqGR 942
Cdd:COG1022   336 -LVF-----SKLREALggrLRFAVsggaalgpELARFFrAL--GIpVLEGYGLTETSPVITVnRPGDNRIgtV-----GP 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  943 VCCGyVEqddtdtlIRIVDpdsltehqedgvEGEIWISSPssGV--GYWGNSEMSQRTF-----FnqlknhpnkkftRTG 1015
Cdd:COG1022   403 PLPG-VE-------VKIAE------------DGEILVRGP--NVmkGYYKNPEATAEAFdadgwL------------HTG 448

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1016 DLGR-TIDGNLFITGRIKDLIIVA-GRNIYSADVEKTVESS---SEVL-----RPGCCAVVGIPEEVL----AQKGISIP 1081
Cdd:COG1022   449 DIGElDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASpliEQAVvvgdgRPFLAALIVPDFEALgewaEENGLPYT 528

                         570       580
                  ....*....|....*....|....
gi 937914749 1082 DSSDqvgLVVIAEVREgkAVSKEV 1105
Cdd:COG1022   529 SYAE---LAQDPEVRA--LIQEEV 547
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 605-1031 5.58e-26

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: 118.04  E-value: 5.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTkpvIKPGDRVLlIHLP-GLEFIDAFFGCIRAGVIPVPVLPPDPmqsggqallkVENISKM 683
Cdd:COG1020   503 TYAELNARANRLAHHLRALG---VGPGDLVG-VCLErSLEMVVALLAVLKAGAAYVPLDPAYP----------AERLAYM 568

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  684 ---CNAVAILSTSSYHAAVRAgyiknivtlakrvqkcsaqwPDIPWIHTDSwiknyrrSSDSFNSDTVLFTKPQPSDLCF 760
Cdd:COG1020   569 ledAGARLVLTQSALAARLPE--------------------LGVPVLALDA-------LALAAEPATNPPVPVTPDDLAY 621

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  761 LQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGlIGGLFTALVSGGTSVLFSPMIfIRNPLL 840
Cdd:COG1020   622 VIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDAS-VWEIFGALLSGATLVLAPPEA-RRDPAA 699

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  841 WLQTINDYHGTHSagpNF---AFELVIRRLEAeknkvyDLSSMVFLMIAAEPVRQKTVRRFIELtqpfgLSEGVLAPGYG 917
Cdd:COG1020   700 LAELLARHRVTVL---NLtpsLLRALLDAAPE------ALPSLRLVLVGGEALPPELVRRWRAR-----LPGARLVNLYG 765

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  918 LAENCVYVTCAfgECKPVFIDWQ----GRvccgyveqDDTDTLIRIVDpdsltEHQE---DGVEGEIWISSPSSGVGYWG 990
Cdd:COG1020   766 PTETTVDSTYY--EVTPPDADGGsvpiGR--------PIANTRVYVLD-----AHLQpvpVGVPGELYIGGAGLARGYLN 830

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 937914749  991 NSEMSQRTFFNQLKNHPNKKFTRTGDLGR-TIDGNLFITGRI 1031
Cdd:COG1020   831 RPELTAERFVADPFGFPGARLYRTGDLARwLPDGNLEFLGRA 872
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 598-1144 1.25e-25

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 114.48  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  598 GKLMNRRTYQELHGN-ASYIAQKllTStkpvIKPGDRVLlIHLPG-LEFIDAFFGCIRAGVIPV---PVLPPDPMQ---- 668
Cdd:PRK05677   47 GKTLTYGELYKLSGAfAAWLQQH--TD----LKPGDRIA-VQLPNvLQYPVAVFGAMRAGLIVVntnPLYTAREMEhqfn 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  669 -SGGQALLKVENISKMCNAVaILSTSSYHAAVRA-----GYIKNIVTLA--KRVQKCSAQWpDIPWIH--TDSWIKNYRR 738
Cdd:PRK05677  120 dSGAKALVCLANMAHLAEKV-LPKTGVKHVIVTEvadmlPPLKRLLINAvvKHVKKMVPAY-HLPQAVkfNDALAKGAGQ 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  739 SSDSFNsdtvlftkPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHN---VKTMKKRYRSTSKTVLVSWLPQYHDMGLIGG 815
Cdd:PRK05677  198 PVTEAN--------PQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGSNLNEGCEILIAPLPLYHIYAFTFH 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  816 LFTALVSGGTSVLfspmifIRNPL---LWLQTINDYHGTHSAGPNFAFELVIRRleaEKNKVYDLSSMVFLMIAAEPVRQ 892
Cdd:PRK05677  270 CMAMMLIGNHNIL------ISNPRdlpAMVKELGKWKFSGFVGLNTLFVALCNN---EAFRKLDFSALKLTLSGGMALQL 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  893 KTVRRFIELTQpFGLSEGvlapgYGLAENCVYVTcafgeckpvfIDWQGRVCCGYVEQDDTDTLIRIVDPDSltEHQEDG 972
Cdd:PRK05677  341 ATAERWKEVTG-CAICEG-----YGMTETSPVVS----------VNPSQAIQVGTIGIPVPSTLCKVIDDDG--NELPLG 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  973 VEGEIWISSPSSGVGYWGNSEMSQRTFfnqlknhPNKKFTRTGDLGrTI--DGNLFITGRIKDLIIVAGRNIYSADVEKT 1050
Cdd:PRK05677  403 EVGELCVKGPQVMKGYWQRPEATDEIL-------DSDGWLKTGDIA-LIqeDGYMRIVDRKKDMILVSGFNVYPNELEDV 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1051 VESSSEVLRpgcCAVVGIPEEvlaqkgisipDSSDQVGLVVIaeVREGKAVSKE-VVNNIKARVveehgVAVASVKLIKP 1129
Cdd:PRK05677  475 LAALPGVLQ---CAAIGVPDE----------KSGEAIKVFVV--VKPGETLTKEqVMEHMRANL-----TGYKVPKAVEF 534

                         570
                  ....*....|....*.
gi 937914749 1130 RTICKTTS-GKIRRFE 1144
Cdd:PRK05677  535 RDELPTTNvGKILRRE 550
catalase_like cd08150
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ...
 1924-2225 2.84e-25

Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity.


Pssm-ID: 163706  Cd Length: 283  Bit Score: 108.03  E-value: 2.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1924 RYFHRIGVSGRGVLRMYEEIPSFPRHKIFASGKSFPVIVRHSNSLSADDDARlDARGAAVRI-LSDNDGeapLLDLTLKS 2002
Cdd:cd08150     3 RGQHFQGTCAFGTFEVLADLKERLRVGLFAEGKVYPAYIRFSNGAGIDDTKP-DIRGFAIKFtGVADAG---TLDFVLNN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 2003 GKAFYARTIADFATWL------VCGLPARE---EQVKRSPH-IRDAVWGSLRSTDSYTVLHYYSNICRLLRFDDGREMYA 2072
Cdd:cd08150    79 TPVFFIRNTSDYEDFVaefarsARGEPPLDfiaWYVEKRPEdLPNLLGARSQVPDSYAAARYFSQVTFAFINGAGKYRVV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 2073 KFKLRPADPDVPEDSGKVVPRGilppetgaiprdeddtrpllflaDDFRRR------VGSPdgVRYVFQLQLREvPTDAA 2146
Cdd:cd08150   159 RSKDNPVDGIPSLEDHELEARP-----------------------PDYLREelterlQRGP--VVYDFRIQLND-DTDAT 212

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749 2147 ARDvalDCTRPWDEaEFPYIDVGEVSIGRNLPTEETEKLEFNPFLRCPEVDVIPATScaqsaSIDHGRSLVYEICQRLR 2225
Cdd:cd08150   213 TID---NPTILWPT-EHPVEAVAKITIPPPTFTAAQEAFAFNPFTPWHGLLETNDLG-----PILEVRRRVYTSSQGLR 282
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 605-1097 1.49e-24

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: 109.69  E-value: 1.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTKpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPpdpmqsggqallkveniskmc 684
Cdd:cd05941    13 TYADLVARAARLANRLLALGK--DLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNP--------------------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 navailstsSYHAAVRAGYIknivtlakrvqkcsaqwpdipwihTDSwiknyrrssdsfnsdtvlftkpQPS---DLCFL 761
Cdd:cd05941    70 ---------SYPLAELEYVI------------------------TDS----------------------EPSlvlDPALI 94

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  762 QFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVL---FSPMIfiRNP 838
Cdd:cd05941    95 LYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFlpkFDPKE--VAI 172

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  839 LLWLQTIN-------------DYHGTHSAGPNFAFELVIRRLEaeknkvydlssmvfLMI---AAEPVrqKTVRRFIELT 902
Cdd:cd05941   173 SRLMPSITvfmgvptiytrllQYYEAHFTDPQFARAAAAERLR--------------LMVsgsAALPV--PTLEEWEAIT 236

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  903 qpfGLsegVLAPGYGLAENCVYVTCAF-GECKPvfidwqgrvccGYVEQDDTDTLIRIVDPDSLTEHQEDGVeGEIWISS 981
Cdd:cd05941   237 ---GH---TLLERYGMTEIGMALSNPLdGERRP-----------GTVGMPLPGVQARIVDEETGEPLPRGEV-GEIQVRG 298

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  982 PSSGVGYWGNSEMSQRTFfnqlknhPNKKFTRTGDLGRT-IDGNLFITGRIKDLII-VAGRNIYSADVEKTVESSSEVLR 1059
Cdd:cd05941   299 PSVFKEYWNKPEATKEEF-------TDDGWFKTGDLGVVdEDGYYWILGRSSVDIIkSGGYKVSALEIERVLLAHPGVSE 371

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 937914749 1060 pgcCAVVGIPEEVLAQKGISIPDSSDQVGLVVIAEVRE 1097
Cdd:cd05941   372 ---CAVIGVPDPDWGERVVAVVVLRAGAAALSLEELKE 406
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 593-1140 1.91e-24

acetate-CoA ligase; This family 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: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 111.13  E-value: 1.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  593 WINEEGKLMNRRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLlIHLPGL-EFIDAFFGCIRAGVIPVPVLppdpmqsGG 671
Cdd:cd17634    74 YEGDDTSQSRTISYRELHREVCRFAGTLLDLG---VKKGDRVA-IYMPMIpEAAVAMLACARIGAVHSVIF-------GG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  672 QALLKVENISKMCNAVAILSTSSYHAAVRAGYIKNIV-------------TLAKRVQKCSAQWPDIPWIHTDSWIKnyrR 738
Cdd:cd17634   143 FAPEAVAGRIIDSSSRLLITADGGVRAGRSVPLKKNVddalnpnvtsvehVIVLKRTGSDIDWQEGRDLWWRDLIA---K 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  739 SSDSFNSDTVlftkpQPSDLCFLQFTSGSTGDAKGVMITHEG-LIHNVKTMKKRYrSTSKTVLVSWlpqYHDMGLIGG-- 815
Cdd:cd17634   220 ASPEHQPEAM-----NAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVF-DYGPGDIYWC---TADVGWVTGhs 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  816 --LFTALVSGGTSVLFSPMIFIRNPLLWLQTINDYHGTHSagpnFAFELVIRRLEAEKNKV---YDLSSMVFLMIAAEPV 890
Cdd:cd17634   291 ylLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNIL----YTAPTAIRALMAAGDDAiegTDRSSLRILGSVGEPI 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  891 RQKTVRRFIELTQPFG-----------LSEGVLAPGYGLAEncVYVTCAFgecKPVFidwqgrvccGYVEQddtdtlirI 959
Cdd:cd17634   367 NPEAYEWYWKKIGKEKcpvvdtwwqteTGGFMITPLPGAIE--LKAGSAT---RPVF---------GVQPA--------V 424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  960 VDPDSLTehQEDGVEGEIWISSPSSG--VGYWGNSEMSQRTFFNQLKNhpnkkFTRTGDLGRT-IDGNLFITGRIKDLII 1036
Cdd:cd17634   425 VDNEGHP--QPGGTEGNLVITDPWPGqtRTLFGDHERFEQTYFSTFKG-----MYFSGDGARRdEDGYYWITGRSDDVIN 497

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1037 VAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEVlaqKGISIpdssdqVGLVVIaevREGKAVSKEVVNNIKARVVEE 1116
Cdd:cd17634   498 VAGHRLGTAEIESVLVAHPKVAE---AAVVGIPHAI---KGQAP------YAYVVL---NHGVEPSPELYAELRNWVRKE 562

                         570       580
                  ....*....|....*....|....
gi 937914749 1117 HGVAVASVKLIKPRTICKTTSGKI 1140
Cdd:cd17634   563 IGPLATPDVVHWVDSLPKTRSGKI 586
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 605-1070 5.68e-24

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 107.53  E-value: 5.68e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   605 TYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVipvPVLPPDPMQSGGQALLKVENIskmc 684
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQG---IRSGSRVALVGQNSIEMVLLLHACLLLGA---EIAMLNTRLTENERTNQLEDL---- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   685 NAVAILSTSSYHAavragyiKNIVTLakrvqkcsaqwpdipwihtdswikNYRRSSDSFNSDTVLFTKPQPSDLCFLQFT 764
Cdd:TIGR01923   71 DVQLLLTDSLLEE-------KDFQAD------------------------SLDRIEAAGRYETSLSASFNMDQIATLMFT 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   765 SGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLiGGLFTALVSGGTSVLFSPMIFIrnpllwLQT 844
Cdd:TIGR01923  120 SGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFNQL------LEM 192

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   845 INDYHGTH-SAGPNfafelVIRRLEAEKNKVYDLSSmvfLMIAAEPVRQKTVRRFIELTQPFGLsegvlapGYGLAENCV 923
Cdd:TIGR01923  193 IANERVTHiSLVPT-----QLNRLLDEGGHNENLRK---ILLGGSAIPAPLIEEAQQYGLPIYL-------SYGMTETCS 257

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   924 YVTCAFGECKPVFIDwQGRVCcGYVEqddtdtlIRIVDPDsLTEHqedgveGEIWISSPSSGVGYWGNSEMsQRTFFNQl 1003
Cdd:TIGR01923  258 QVTTATPEMLHARPD-VGRPL-AGRE-------IKIKVDN-KEGH------GEIMVKGANLMKGYLYQGEL-TPAFEQQ- 319

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937914749  1004 knhpnkKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPE 1070
Cdd:TIGR01923  320 ------GWFNTGDIGElDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQE---AVVVPKPD 378
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
628-1072 9.06e-24

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


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 108.60  E-value: 9.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  628 IKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLP---PDPMQ-----SGGQALLKVENISKMCNAVaILSTSSYHAAV 699
Cdd:PRK08974   71 LKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPlytPRELEhqlndSGAKAIVIVSNFAHTLEKV-VFKTPVKHVIL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  700 -RAG----------------YIKNIVTLAKRVQKCSAQwpdipwihtDSWIKNYRRSsdsfnsdtvlFTKPQ--PSDLCF 760
Cdd:PRK08974  150 tRMGdqlstakgtlvnfvvkYIKRLVPKYHLPDAISFR---------SALHKGRRMQ----------YVKPElvPEDLAF 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  761 LQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRS---TSKTVLVSWLPQYHDMGLIGG--LFTALvsGGTSVLfspmifI 835
Cdd:PRK08974  211 LQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPllhPGKELVVTALPLYHIFALTVNclLFIEL--GGQNLL------I 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  836 RNPL---LWLQTINDYHGTHSAGPNFAFELVirrLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFglsegvL 912
Cdd:PRK08974  283 TNPRdipGFVKELKKYPFTAITGVNTLFNAL---LNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQY------L 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  913 APGYGLAencvyvtcafgECKPVFidwqgrVCCGYVEQDDT--------DTLIRIVDPDSltEHQEDGVEGEIWISSPSS 984
Cdd:PRK08974  354 LEGYGLT-----------ECSPLV------SVNPYDLDYYSgsiglpvpSTEIKLVDDDG--NEVPPGEPGELWVKGPQV 414

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  985 GVGYWGNSEMSQrtffNQLKNhpnkKFTRTGDLGrTID--GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgc 1062
Cdd:PRK08974  415 MLGYWQRPEATD----EVIKD----GWLATGDIA-VMDeeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLE--- 482

                         490
                  ....*....|
gi 937914749 1063 CAVVGIPEEV 1072
Cdd:PRK08974  483 VAAVGVPSEV 492
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 605-1144 3.22e-23

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: 105.24  E-value: 3.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTKPvikPGDRVLLIHLPGLEFIDAFFGCIRAGVIPV---PVLPPdpmqsggqallkvenis 681
Cdd:cd05919    12 TYGQLHDGANRLGSALRNLGVS---SGDRVLLLMLDSPELVQLFLGCLARGAIAVvinPLLHP----------------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  682 kmcnavailstssyhaavragyiknivtlakrvqkcsaqwPDIPWIHTDSWIKNYRRSSDsfnsdtvlftkpqpsDLCFL 761
Cdd:cd05919    72 ----------------------------------------DDYAYIARDCEARLVVTSAD---------------DIAYL 96

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  762 QFTSGSTGDAKGVMITHEGLIHNVKTMKKRY-RSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMifiRNPLL 840
Cdd:cd05919    97 LYSSGTTGPPKGVMHAHRDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGW---PTAER 173

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  841 WLQTINDYHGTHSAG-PN-FAFELVIRRLEAEknkvyDLSSMVFLMIAAEPVRQKTVRRFIEltqpFGLSEgvLAPGYGL 918
Cdd:cd05919   174 VLATLARFRPTVLYGvPTfYANLLDSCAGSPD-----ALRSLRLCVSAGEALPRGLGERWME----HFGGP--ILDGIGA 242

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  919 AENC-VYVTCAFGECKPvfiDWQGRVCCGYVeqddtdtlIRIVDPDSLTehQEDGVEGEIWISSPSSGVGYWGNSEMSQR 997
Cdd:cd05919   243 TEVGhIFLSNRPGAWRL---GSTGRPVPGYE--------IRLVDEEGHT--IPPGEEGDLLVRGPSAAVGYWNNPEKSRA 309

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  998 TFfnqlknhpNKKFTRTGDL-GRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVesssevlrpgcCAVVGIPEEVLaqk 1076
Cdd:cd05919   310 TF--------NGGWYRTGDKfCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLI-----------IQHPAVAEAAV--- 367

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 937914749 1077 gISIPDSSDQVGLVVIAEVREGKAVSKEVVNNIKARVVEEhgvaVASVKLikPRTIC------KTTSGKIRRFE 1144
Cdd:cd05919   368 -VAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLER----LSAHKV--PRRIAfvdelpRTATGKLQRFK 434
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 605-1071 9.15e-23

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; 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 TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 104.66  E-value: 9.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLltsTKPVIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVlppDPmqsgGQALLKVENISKMC 684
Cdd:cd12114    14 TYGELAERARRVAGAL---KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV---DI----DQPAARREAILADA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 NAVAILSTSSYHAAVRAGYIKNIVTLAkrvqkcsaqwPDIPWihtdswiknyrrssdsfnsDTVLFTKPQPSDLCFLQFT 764
Cdd:cd12114    84 GARLVLTDGPDAQLDVAVFDVLILDLD----------ALAAP-------------------APPPPVDVAPDDLAYVIFT 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  765 SGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGlIGGLFTALVSGGTSVLFSPMIfIRNPLLWLQT 844
Cdd:cd12114   135 SGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLS-VYDIFGALSAGATLVLPDEAR-RRDPAHWAEL 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  845 INDYHGTHSagpNFA---FELVIRRLEAEkNKVYDLSSMVFL---MIAAE-PVRQKTVR---RFIELTqpfGLSEG---- 910
Cdd:cd12114   213 IERHGVTLW---NSVpalLEMLLDVLEAA-QALLPSLRLVLLsgdWIPLDlPARLRALApdaRLISLG---GATEAsiws 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  911 VLAP-------------GYGLAENCVYVtcafgeckpvfIDWQGRVCcgyveqddtdtlirivdPDsltehqedGVEGEI 977
Cdd:cd12114   286 IYHPidevppdwrsipyGRPLANQRYRV-----------LDPRGRDC-----------------PD--------WVPGEL 329

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  978 WISSPSSGVGYWGNSEMSQRTFFnqlkNHPN-KKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSS 1055
Cdd:cd12114   330 WIGGRGVALGYLGDPELTAARFV----THPDgERLYRTGDLGRyRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHP 405

                         490
                  ....*....|....*.
gi 937914749 1056 EVLRpGCCAVVGIPEE 1071
Cdd:cd12114   406 GVAR-AVVVVLGDPGG 420
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 603-1069 1.19e-22

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. 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: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 103.87  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTKPvikPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPMQsggqallKVENISK 682
Cdd:cd05945    16 TLTYRELKERADALAAALASLGLD---AGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAE-------RIREILD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  683 MCNAVAILSTssyhaavragyiknivtlakrvqkcsaqwpdipwihtdswiknyrrssdsfnsdtvlftkpqPSDLCFLQ 762
Cdd:cd05945    86 AAKPALLIAD--------------------------------------------------------------GDDNAYII 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  763 FTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLiGGLFTALVSGGTSVLFSPMIfIRNPLLWL 842
Cdd:cd05945   104 FTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSV-MDLYPALASGATLVPVPRDA-TADPKQLF 181

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  843 QTINDY-----HGThsagPNFAfELVIRRLEAEKNKVYDLSSMVFlmiAAEPVRQKTVRRFIEltqpfglsegvLAPG-- 915
Cdd:cd05945   182 RFLAEHgitvwVST----PSFA-AMCLLSPTFTPESLPSLRHFLF---CGEVLPHKTARALQQ-----------RFPDar 242

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  916 ----YGLAENCVYVTcaFGECKPVFIDWQGRVCCGYVEqddTDTLIRIVDPDslTEHQEDGVEGEIWISSPSSGVGYWGN 991
Cdd:cd05945   243 iyntYGPTEATVAVT--YIEVTPEVLDGYDRLPIGYAK---PGAKLVILDED--GRPVPPGEKGELVISGPSVSKGYLNN 315

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749  992 SEMSQRTFFnqlkNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVlrpGCCAVVGIP 1069
Cdd:cd05945   316 PEKTAAAFF----PDEGQRAYRTGDLVRlEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGV---KEAVVVPKY 387
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
628-1104 2.21e-22

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 104.20  E-value: 2.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  628 IKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPmqsggqallkvenISKMCnavailstssyhaaVRAGYIKNI 707
Cdd:PRK05852   65 LLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALP-------------IAEQR--------------VRSQAAGAR 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  708 VTLAKRVQKCSAQWPDIPWihtdsWIKNYRRSSDSFNSDTVLF------TKPQP---------SDLCFLQFTSGSTGDAK 772
Cdd:PRK05852  118 VVLIDADGPHDRAEPTTRW-----WPLTVNVGGDSGPSGGTLSvhldaaTEPTPatstpeglrPDDAMIMFTGGTTGLPK 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  773 GVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVL-----FSPMIFirnpllWlQTIND 847
Cdd:PRK05852  193 MVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLpargrFSAHTF------W-DDIKA 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  848 YHGT-HSAGPnfAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRrfieltqpfGLSEGVLAPgyglaencvyVT 926
Cdd:PRK05852  266 VGATwYTAVP--TIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQ---------ALQTEFAAP----------VV 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  927 CAFG------ECKPVFIDWQGR-----VCCGYVEQDdTDTLIRIVDPDSLtEHQEDGVeGEIWISSPSSGVGYWGNSEMS 995
Cdd:PRK05852  325 CAFGmteathQVTTTQIEGIGQtenpvVSTGLVGRS-TGAQIRIVGSDGL-PLPAGAV-GEVWLRGTTVVRGYLGDPTIT 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  996 QRTFfnqlknhpNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEVLA 1074
Cdd:PRK05852  402 AANF--------TDGWLRTGDLGSlSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVME---AAVFGVPDQLYG 470

                         490       500       510
                  ....*....|....*....|....*....|
gi 937914749 1075 QkgisipdssdQVGLVVIAevREGKAVSKE 1104
Cdd:PRK05852  471 E----------AVAAVIVP--RESAPPTAE 488
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 628-1071 2.83e-22

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 103.95  E-value: 2.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  628 IKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLP---PDPMQ-----SGGQALLKVENISKMCNAVaILSTSSYHAAV 699
Cdd:PRK07059   70 LAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPlytPRELEhqlkdSGAEAIVVLENFATTVQQV-LAKTAVKHVVV 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  700 RA--------GYIKNIVTlaKRVQKCSAQWpDIPwihtdswiknyrrSSDSFNsdTVL-------FTKP--QPSDLCFLQ 762
Cdd:PRK07059  149 ASmgdllgfkGHIVNFVV--RRVKKMVPAW-SLP-------------GHVRFN--DALaegarqtFKPVklGPDDVAFLQ 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  763 FTSGSTGDAKGVMITHEGLIHNVKTMK-------KRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLfspmifI 835
Cdd:PRK07059  211 YTGGTTGVSKGATLLHRNIVANVLQMEawlqpafEKKPRPDQLNFVCALPLYHIFALTVCGLLGMRTGGRNIL------I 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  836 RNPL---LWLQTINDYHGTHSAGPNFAFELVIRRLEAEKnkvYDLSSMVFL----MIAAEPVrqktVRRFIELTQPFgls 908
Cdd:PRK07059  285 PNPRdipGFIKELKKYQVHIFPAVNTLYNALLNNPDFDK---LDFSKLIVAngggMAVQRPV----AERWLEMTGCP--- 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  909 egvLAPGYGLAENCVYVTcafgeCKPVFID-WQGrvCCGyVEQDDTDTLIRIVDPDSLTEhqedGVEGEIWISSPSSGVG 987
Cdd:PRK07059  355 ---ITEGYGLSETSPVAT-----CNPVDATeFSG--TIG-LPLPSTEVSIRDDDGNDLPL----GEPGEICIRGPQVMAG 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  988 YWGNSE-----MSQRTFFnqlknhpnkkftRTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpg 1061
Cdd:PRK07059  420 YWNRPDetakvMTADGFF------------RTGDVGvMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLE-- 485

                         490
                  ....*....|
gi 937914749 1062 cCAVVGIPEE 1071
Cdd:PRK07059  486 -VAAVGVPDE 494
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 592-1154 3.15e-22

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 103.59  E-value: 3.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  592 TWINEEGKLMNRRTYQELHGNASYIAQKLLtstKPVIKPGDrVLLIHLP-GLEFIDAFFGCIRAGVIPVPVLPpdpmqsg 670
Cdd:PRK13295   44 TAVRLGTGAPRRFTYRELAALVDRVAVGLA---RLGVGRGD-VVSCQLPnWWEFTVLYLACSRIGAVLNPLMP------- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  671 gqaLLKVENISKMCN----AVAILSTSSY---HAAvragyiknivtLAKRVQkcsAQWPDIPWIHT------DSWIKNY- 736
Cdd:PRK13295  113 ---IFRERELSFMLKhaesKVLVVPKTFRgfdHAA-----------MARRLR---PELPALRHVVVvggdgaDSFEALLi 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  737 --RRSSDSFNSDTVLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIG 814
Cdd:PRK13295  176 tpAWEQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMY 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  815 GLFTALVSGGTSVLFSpmifIRNPLLWLQTINDyHG---THSAGPnFAFELVirrlEAEKNKVYDLSSMVFLMIAAEPVR 891
Cdd:PRK13295  256 GLMMPVMLGATAVLQD----IWDPARAAELIRT-EGvtfTMASTP-FLTDLT----RAVKESGRPVSSLRTFLCAGAPIP 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  892 QKTVRRfieLTQPFGLSegvLAPGYGLAENCVYVTCAFGECKPVFIDWQGRVCCGyVEqddtdtlIRIVDPDSLTEHQed 971
Cdd:PRK13295  326 GALVER---ARAALGAK---IVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPG-VE-------VRVVDADGAPLPA-- 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  972 GVEGEIWISSPSSGVGYWGNSemsqrtffnQLKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKT 1050
Cdd:PRK13295  390 GQIGRLQVRGCSNFGGYLKRP---------QLNGTDADGWFDTGDLARiDADGYIRISGRSKDVIIRGGENIPVVEIEAL 460

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1051 VESSSEVLRpgcCAVVGIPEEVLAQKGisipdssdqVGLVVIaevREGKAVSKEVVnnikARVVEEHGVAVASV--KLIK 1128
Cdd:PRK13295  461 LYRHPAIAQ---VAIVAYPDERLGERA---------CAFVVP---RPGQSLDFEEM----VEFLKAQKVAKQYIpeRLVV 521

                         570       580
                  ....*....|....*....|....*.
gi 937914749 1129 PRTICKTTSGKIRRFECMRQFVDNTL 1154
Cdd:PRK13295  522 RDALPRTPSGKIQKFRLREMLRGEDA 547
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
605-1071 2.68e-21

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 100.32  E-value: 2.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTKpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPV---LPPDPMQSGgqalLKVENIS 681
Cdd:PRK06839   29 TYKQLHEYVSKVAAYLIYELN--VKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLnirLTENELIFQ----LKDSGTT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  682 KMCnavailSTSSYHAAvrAGYIKNIVTLAKRVqkcsaqwpdipwihtdsWIKNYRRSSDSFNSDtvlFTKPQPSDLCFL 761
Cdd:PRK06839  103 VLF------VEKTFQNM--ALSMQKVSYVQRVI-----------------SITSLKEIEDRKIDN---FVEKNESASFII 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  762 QFTSGSTGDAKGVMITHEGL----IHNVKTMKkryrSTSKTVLVSWLPQYHDMGLigGLFT--ALVSGGTSVLfsPMIFi 835
Cdd:PRK06839  155 CYTSGTTGKPKGAVLTQENMfwnaLNNTFAID----LTMHDRSIVLLPLFHIGGI--GLFAfpTLFAGGVIIV--PRKF- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  836 rNPLLWLQTINDYHGTHSAGPNFAFElviRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGlsegvlaPG 915
Cdd:PRK06839  226 -EPTKALSMIEKHKVTVVMGVPTIHQ---ALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFG-------QG 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  916 YGLAENCVYVTCAFGEckpvfiDWQGRVccGYVEQDDTDTLIRIVDPDslTEHQEDGVEGEIWISSPSSGVGYWGNSEMS 995
Cdd:PRK06839  295 FGMTETSPTVFMLSEE------DARRKV--GSIGKPVLFCDYELIDEN--KNKVEVGEVGELLIRGPNVMKEYWNRPDAT 364

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937914749  996 QRTFFNqlknhpnkKFTRTGDLGRTI-DGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEE 1071
Cdd:PRK06839  365 EETIQD--------GWLCTGDLARVDeDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYE---VAVVGRQHV 430
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 603-1143 2.75e-21

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 100.60  E-value: 2.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVlppDPMQSGGQallkVENISK 682
Cdd:PRK06155   46 RWTYAEAARAAAAAAHALAAAG---VKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI---NTALRGPQ----LEHILR 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  683 MCNAVAIlstssyhaAVRAGYIKNIVTLAKRVQKCSAQWPdIPWIHTDSWIKNYRRSSDSFNSDTVLFTKPQPSDLCFLQ 762
Cdd:PRK06155  116 NSGARLL--------VVEAALLAALEAADPGDLPLPAVWL-LDAPASVSVPAGWSTAPLPPLDAPAPAAAVQPGDTAAIL 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  763 FTSGSTGDAKGVMITHEGL----IHNVKTMKKRYRStsktVLVSWLPQYHDMGLiGGLFTALVSGGTSVLfspmifirnp 838
Cdd:PRK06155  187 YTSGTTGPSKGVCCPHAQFywwgRNSAEDLEIGADD----VLYTTLPLFHTNAL-NAFFQALLAGATYVL---------- 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  839 llwlqtindyhgthsaGPNFA---FELVIRRLEAekNKVYDLSSMVFLMIAAEPV---RQKTVRRFI------ELTQPFG 906
Cdd:PRK06155  252 ----------------EPRFSasgFWPAVRRHGA--TVTYLLGAMVSILLSQPAResdRAHRVRVALgpgvpaALHAAFR 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  907 LSEGV-LAPGYGLAENCVYVTCAFGECKPvfiDWQGRVCCGYVeqddtdtlIRIVDpdsltEHQE---DGVEGEIWISSP 982
Cdd:PRK06155  314 ERFGVdLLDGYGSTETNFVIAVTHGSQRP---GSMGRLAPGFE--------ARVVD-----EHDQelpDGEPGELLLRAD 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  983 SSGV---GYWGnseMSQRTF--FNQLKNHpnkkftrTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSE 1056
Cdd:PRK06155  378 EPFAfatGYFG---MPEKTVeaWRNLWFH-------TGDRVvRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPA 447

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1057 VLRpgcCAVVGIPEEvLAQkgisipdssDQVGLVVIaeVREGKAVS-KEVVNNIKARvveehgVAVASVklikPRTIC-- 1133
Cdd:PRK06155  448 VAA---AAVFPVPSE-LGE---------DEVMAAVV--LRDGTALEpVALVRHCEPR------LAYFAV----PRYVEfv 502

                         570
                  ....*....|....
gi 937914749 1134 ----KTTSGKIRRF 1143
Cdd:PRK06155  503 aalpKTENGKVQKF 516
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 754-1140 2.90e-21

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 100.10  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  754 QPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGtSVLFSPmi 833
Cdd:cd05909   145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGI-KVVFHP-- 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  834 firNPLLWLQ---TINDYHGTHSAG-PNFaFELVIRRLEAeknkvYDLSSMVFLMIAAEPVRQKTVRRFIELtqpFGLse 909
Cdd:cd05909   222 ---NPLDYKKipeLIYDKKATILLGtPTF-LRGYARAAHP-----EDFSSLRLVVAGAEKLKDTLRQEFQEK---FGI-- 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  910 gVLAPGYGLAENCVYVTCAfgecKPVFIDWQGRVcCGYVEQDDtdtlIRIVDPDSLTEHQEdGVEGEIWISSPSSGVGYW 989
Cdd:cd05909   288 -RILEGYGTTECSPVISVN----TPQSPNKEGTV-GRPLPGME----VKIVSVETHEEVPI-GEGGLLLVRGPNVMLGYL 356

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  990 GNSEMSQRTFfnqlknhpNKKFTRTGDLGRtIDGN--LFITGRIKDLIIVAGRNIYSADVEktvESSSEVLRP-GCCAVV 1066
Cdd:cd05909   357 NEPELTSFAF--------GDGWYDTGDIGK-IDGEgfLTITGRLSRFAKIAGEMVSLEAIE---DILSEILPEdNEVAVV 424

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1067 GIPEEvlaQKGisipdssDQVGLVVIaevreGKAVSKEVVNNIkarvVEEHGVAvasvKLIKPRTICKTT------SGKI 1140
Cdd:cd05909   425 SVPDG---RKG-------EKIVLLTT-----TTDTDPSSLNDI----LKNAGIS----NLAKPSYIHQVEeipllgTGKP 481
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 605-1144 3.75e-21

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 100.28  E-value: 3.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTKpvIKPGDRVLlIHLPG-LEFIDAFFGCIRAGVIPV---PVLPPDPMQ-----SGGQALL 675
Cdd:PRK12492   51 SYAELERHSAAFAAYLQQHTD--LVPGDRIA-VQMPNvLQYPIAVFGALRAGLIVVntnPLYTAREMRhqfkdSGARALV 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  676 KVENISKMCNAVAILSTSSYHAAVRAGYIKN------IVTLAKRVQKCSaqwPDIPWIHTDSWIKNYRRSSDsfnsdtvL 749
Cdd:PRK12492  128 YLNMFGKLVQEVLPDTGIEYLIEAKMGDLLPaakgwlVNTVVDKVKKMV---PAYHLPQAVPFKQALRQGRG-------L 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  750 FTKPQP---SDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRST----------SKTVLVSWLPQYHDMGLIGGL 816
Cdd:PRK12492  198 SLKPVPvglDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLgpdgqplmkeGQEVMIAPLPLYHIYAFTANC 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  817 FTALVSGGTSVLfspmifIRNPLL---WLQTINDYHGTHSAGPNFAFELVI-----RRLEAEKNKVYDLSSMVFLMIAAE 888
Cdd:PRK12492  278 MCMMVSGNHNVL------ITNPRDipgFIKELGKWRFSALLGLNTLFVALMdhpgfKDLDFSALKLTNSGGTALVKATAE 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  889 PVRQKTVRRFIEltqpfglsegvlapGYGLAENC-VYVTCAFGEckpvfidwQGRVccGYVEQDDTDTLIRIVDPDSLte 967
Cdd:PRK12492  352 RWEQLTGCTIVE--------------GYGLTETSpVASTNPYGE--------LARL--GTVGIPVPGTALKVIDDDGN-- 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  968 HQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFfnqlknhPNKKFTRTGDLGrTIDGNLF--ITGRIKDLIIVAGRNIYSA 1045
Cdd:PRK12492  406 ELPLGERGELCIKGPQVMKGYWQQPEATAEAL-------DAEGWFKTGDIA-VIDPDGFvrIVDRKKDLIIVSGFNVYPN 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1046 DVEKTVESSSEVlrpGCCAVVGIPEEvlaqkgisipDSSDQVGLVVIA-----EVREGKAVSKEvvnNIKARVVEEHGVA 1120
Cdd:PRK12492  478 EIEDVVMAHPKV---ANCAAIGVPDE----------RSGEAVKLFVVArdpglSVEELKAYCKE---NFTGYKVPKHIVL 541

                         570       580
                  ....*....|....*....|....
gi 937914749 1121 VASVKLikprtickTTSGKIRRFE 1144
Cdd:PRK12492  542 RDSLPM--------TPVGKILRRE 557
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 605-1048 6.85e-21

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. 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: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 98.94  E-value: 6.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPMQsggqallKVENISKMC 684
Cdd:cd17655    24 TYRELNERANQLARTLREKG---VGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEE-------RIQYILEDS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 NAVAILSTSsyHAAVRAGYIKNIVTLAKRvqkcsaqwpDIpwihtdswiknYRRSSDSFNSDTvlftkpQPSDLCFLQFT 764
Cdd:cd17655    94 GADILLTQS--HLQPPIAFIGLIDLLDED---------TI-----------YHEESENLEPVS------KSDDLAYVIYT 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  765 SGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGlIGGLFTALVSGGTSVLfSPMIFIRNPLLWLQT 844
Cdd:cd17655   146 SGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDAS-VTEIFASLLSGNTLYI-VRKETVLDGQALTQY 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  845 INDYHGTHSAGPNFAFELVirrleaEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELtqpFGLSEGVLApGYGLAENCVy 924
Cdd:cd17655   224 IRQNRITIIDLTPAHLKLL------DAADDSEGLSLKHLIVGGEALSTELAKKIIEL---FGTNPTITN-AYGPTETTV- 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  925 vtcafgeCKPVFIdwqgrvccgYVEQDDTDTLIRIVDP---------DSLTEHQEDGVEGEIWISSPSSGVGYWGNSEMS 995
Cdd:cd17655   293 -------DASIYQ---------YEPETDQQVSVPIGKPlgntriyilDQYGRPQPVGVAGELYIGGEGVARGYLNRPELT 356

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 937914749  996 QRTFFnqlkNHP---NKKFTRTGDLGRTI-DGNLFITGRIKDLIIVAGRNIYSADVE 1048
Cdd:cd17655   357 AEKFV----DDPfvpGERMYRTGDLARWLpDGNIEFLGRIDHQVKIRGYRIELGEIE 409
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 754-1066 8.34e-21

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); 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 of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. 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: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 98.38  E-value: 8.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  754 QPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKT-VL--------VSwlpqyhdmglIGGLFTALVSGG 824
Cdd:cd05918   104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESrVLqfasytfdVS----------ILEIFTTLAAGG 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  825 TsvLFSPMIFIR-NPLLwlQTINDYhgthsaGPNFAFeL---VIRRLEAEknkvyDLSSMVFLMIAAEPVRQKTVRRFie 900
Cdd:cd05918   174 C--LCIPSEEDRlNDLA--GFINRL------RVTWAF-LtpsVARLLDPE-----DVPSLRTLVLGGEALTQSDVDTW-- 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  901 ltqpfglSEGV-LAPGYGLAENCVYVTCafgecKPVFIDWQGRvCCGYVeqddTDTLIRIVDPDSLTEHQEDGVEGEIWI 979
Cdd:cd05918   236 -------ADRVrLINAYGPAECTIAATV-----SPVVPSTDPR-NIGRP----LGATCWVVDPDNHDRLVPIGAVGELLI 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  980 SSPSSGVGYWGNSEMSQRTFFN------QLKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVE 1052
Cdd:cd05918   299 EGPILARGYLNDPEKTAAAFIEdpawlkQEGSGRGRRLYRTGDLVRyNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLR 378

                         330
                  ....*....|....
gi 937914749 1053 SSSEVLRPGCCAVV 1066
Cdd:cd05918   379 QSLPGAKEVVVEVV 392
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 630-1142 8.61e-21

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: 98.28  E-value: 8.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  630 PGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPdpmqsggqallkveniskmCNAVAILSTSSYHAAVRAGYIKNIV- 708
Cdd:cd05922    17 RGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVP-------------------LNPTLKESVLRYLVADAGGRIVLADa 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  709 TLAKRVQKCSAQWPD-IPWIHTDSWiKNYRRSSDSFnsdtvlftKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKT 787
Cdd:cd05922    78 GAADRLRDALPASPDpGTVLDADGI-RAARASAPAH--------EVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  788 MKKRYRSTSKTVLVSWLPQYHDMGLiGGLFTALVSGGTSVLFSPMIFIRNplLWlQTINDYHGTHSAGPNFAFELvIRRL 867
Cdd:cd05922   149 IAEYLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVLDDA--FW-EDLREHGATGLAGVPSTYAM-LTRL 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  868 EAEKNKvydLSSMVFLMIAAEPVRQKTVRRFIEltqpfglsegvLAPG------YGLAENCVYVTCAFGEC---KPvfid 938
Cdd:cd05922   224 GFDPAK---LPSLRYLTQAGGRLPQETIARLRE-----------LLPGaqvyvmYGQTEATRRMTYLPPERileKP---- 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  939 wqGRVCCGYVEqddtdTLIRIVDPDSLTEHqeDGVEGEIWISSPSSGVGYWGNS--EMSQRTFFNQLknhpnkkftRTGD 1016
Cdd:cd05922   286 --GSIGLAIPG-----GEFEILDDDGTPTP--PGEPGEIVHRGPNVMKGYWNDPpyRRKEGRGGGVL---------HTGD 347

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1017 LG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVlrpGCCAVVGIPeevlaqkgisiPDSSDQVGLVVIAEV 1095
Cdd:cd05922   348 LArRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI---IEAAAVGLP-----------DPLGEKLALFVTAPD 413

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 937914749 1096 R-EGKAVSKEVvnnikARVVEEHGVAVASVKLikpRTICKTTSGKIRR 1142
Cdd:cd05922   414 KiDPKDVLRSL-----AERLPPYKVPATVRVV---DELPLTASGKVDY 453
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 603-1148 2.08e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 97.92  E-value: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPMQSGGQALLKVEniSK 682
Cdd:PRK12583   45 RYTWRQLADAVDRLARGLLALG---VQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSG--VR 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  683 MCNAVAILSTSSYHAAVrAGYIKNIVtLAKRVQKCSAQWPDIPWI---------HTDSWIKNYRRSSDSfnSDTVLFTKP 753
Cdd:PRK12583  120 WVICADAFKTSDYHAML-QELLPGLA-EGQPGALACERLPELRGVvslapapppGFLAWHELQARGETV--SREALAERQ 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  754 Q---PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLfs 830
Cdd:PRK12583  196 AsldRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVY-- 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  831 PMIFIrNPLLWLQTINDYHGTHSAGPNFAFelvIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIEltqpfglseg 910
Cdd:PRK12583  274 PNEAF-DPLATLQAVEEERCTALYGVPTMF---IAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMD---------- 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  911 vlapgyglAENCVYVTCAFG--ECKPVFI------DWQGRVCCgyVEQDDTDTLIRIVDPDSLTEHQedGVEGEIWISSP 982
Cdd:PRK12583  340 --------EMHMAEVQIAYGmtETSPVSLqttaadDLERRVET--VGRTQPHLEVKVVDPDGATVPR--GEIGELCTRGY 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  983 SSGVGYWGNSEMSQRTFFNQLKNHpnkkftrTGDLGrTID--GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRp 1060
Cdd:PRK12583  408 SVMKGYWNNPEATAESIDEDGWMH-------TGDLA-TMDeqGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVAD- 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1061 gcCAVVGIPEEVLAQKgisipdssdqvgLVVIAEVREGKAVSKEVVNNI-KARvveehgvaVASVKLikPRTI------C 1133
Cdd:PRK12583  479 --VQVFGVPDEKYGEE------------IVAWVRLHPGHAASEEELREFcKAR--------IAHFKV--PRYFrfvdefP 534

                         570
                  ....*....|....*
gi 937914749 1134 KTTSGKIRRFEcMRQ 1148
Cdd:PRK12583  535 MTVTGKVQKFR-MRE 548
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 756-1142 2.16e-20

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 95.02  E-value: 2.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  756 SDLCFLQFTSGSTGDAKGVMITHEGLI-HNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLfTALVSGGTSVLFSPMIF 834
Cdd:cd17635     1 EDPLAVIFTSGTTGEPKAVLLANKTFFaVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWIL-TCLIHGGLCVTGGENTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 IRNPLLWLQTiNDYHGTHSAgPNFAFELVIRRleaeKNKVYDLSSMVFLMIAAEPVRQKTVrRFIELtqpFGLSEGVLAp 914
Cdd:cd17635    80 YKSLFKILTT-NAVTTTCLV-PTLLSKLVSEL----KSANATVPSLRLIGYGGSRAIAADV-RFIEA---TGLTNTAQV- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  915 gYGLAENcvyvtcafgeckpvfidwqGRVCCGYVEQDDTD----------TLIRIVDPDSLtEHQEDGvEGEIWISSPSS 984
Cdd:cd17635   149 -YGLSET-------------------GTALCLPTDDDSIEinavgrpypgVDVYLAATDGI-AGPSAS-FGTIWIKSPAN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  985 GVGYWGNSEMSQRTFFNQlknhpnkkFTRTGDLGRTI-DGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcC 1063
Cdd:cd17635   207 MLGYWNNPERTAEVLIDG--------WVNTGDLGERReDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQE---C 275

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749 1064 AVVGIPEEVLaqkgisipdssdqvGLVVIAEVREGKAVSKEVVNNIKARVVEEHGVAVASVKLIKPRTICKTTSGKIRR 1142
Cdd:cd17635   276 ACYEISDEEF--------------GELVGLAVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 757-1100 9.04e-20

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 92.95  E-value: 9.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  757 DLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKK--RYRSTSKTVLVSwlPQYHDMGLIGGLFTALVSGGTSVlfsPMIf 834
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADcaDLTEDDRYLIIN--PFFHTFGYKAGIVACLLTGATVV---PVA- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 IRNPLLWLQTINDYHGTHSAGPNFAFELVirrLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIEltqpfGLSEGVLAP 914
Cdd:cd17638    75 VFDVDAILEAIERERITVLPGPPTLFQSL---LDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRS-----ELGFETVLT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  915 GYGLAENCVYVTCAFGECKPVFIDWQGRVCCGyveqddtdTLIRIVDPdsltehqedgveGEIWISSPSSGVGYWGNSEM 994
Cdd:cd17638   147 AYGLTEAGVATMCRPGDDAETVATTCGRACPG--------FEVRIADD------------GEVLVRGYNVMQGYLDDPEA 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  995 SQRTFfnqlknhPNKKFTRTGDLGrTID--GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEV 1072
Cdd:cd17638   207 TAEAI-------DADGWLHTGDVG-ELDerGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQ---VAVIGVPDER 275

                         330       340       350
                  ....*....|....*....|....*....|.
gi 937914749 1073 LAQKGISIPDSSDQVGLV---VIAEVREGKA 1100
Cdd:cd17638   276 MGEVGKAFVVARPGVTLTeedVIAWCRERLA 306
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 749-1077 3.77e-19

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 95.38  E-value: 3.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  749 LFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGgtsvl 828
Cdd:PRK08633  775 YGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEG----- 849

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  829 fSPMIFIRNPLLWL---QTINDYHGTHSAG-PNFaFELVIRRLEAEKNkvyDLSSMVFLMIAAEPVRQKTVRRFIEltqP 904
Cdd:PRK08633  850 -IKVVYHPDPTDALgiaKLVAKHRATILLGtPTF-LRLYLRNKKLHPL---MFASLRLVVAGAEKLKPEVADAFEE---K 921

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  905 FGLSegvLAPGYGLAENCVYVTCafgECKPVFIDwqgrvccGYVEQDDTD----------TLIRIVDPDSLTEhQEDGVE 974
Cdd:PRK08633  922 FGIR---ILEGYGATETSPVASV---NLPDVLAA-------DFKRQTGSKegsvgmplpgVAVRIVDPETFEE-LPPGED 987

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  975 GEIWISSPSSGVGYWGNSEMSQRTffnqLKNHPNKKFTRTGDLGRtID--GNLFITGRIKDLIIVAGRNIYSADVEktvE 1052
Cdd:PRK08633  988 GLILIGGPQVMKGYLGDPEKTAEV----IKDIDGIGWYVTGDKGH-LDedGFLTITDRYSRFAKIGGEMVPLGAVE---E 1059

                         330       340
                  ....*....|....*....|....*..
gi 937914749 1053 SSSEVL--RPGCCAVVGIPEEvlaQKG 1077
Cdd:PRK08633 1060 ELAKALggEEVVFAVTAVPDE---KKG 1083
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 603-1151 6.66e-19

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 93.07  E-value: 6.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVlppdpmqsggQALLKVENIS- 681
Cdd:PRK08316   36 SWTYAELDAAVNRVAAALLDLG---LKKGDRVAALGHNSDAYALLWLACARAGAVHVPV----------NFMLTGEELAy 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  682 --KMCNAVAILSTSSYHAAVRAGYIKNIVTLAKRVQKCSAQWPDIPWIHTDSWIKNYrrssdsfnSDTVLFTKPQPSDLC 759
Cdd:PRK08316  103 ilDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAG--------SVAEPDVELADDDLA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  760 FLQFTSGSTGDAKGVMITHEGLIHNvktmkkrYRST-------SKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLF-SP 831
Cdd:PRK08316  175 QILYTSGTESLPKGAMLTHRALIAE-------YVSCivagdmsADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILdAP 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  832 mifirNPLLWLQTINdyhgTHSAGPNFAFELV----IRRLEAEKnkvYDLSSMVFLMIAA----EPVRQKTVRRF--IEL 901
Cdd:PRK08316  248 -----DPELILRTIE----AERITSFFAPPTVwislLRHPDFDT---RDLSSLRKGYYGAsimpVEVLKELRERLpgLRF 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  902 TQPFGLSE-----GVLAPGYGLAencvyvtcAFGEC-KPVFidwqgrvccgYVEQddtdtliRIVDPDslteHQE--DGV 973
Cdd:PRK08316  316 YNCYGQTEiaplaTVLGPEEHLR--------RPGSAgRPVL----------NVET-------RVVDDD----GNDvaPGE 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  974 EGEIWISSPSSGVGYWGNSEMSQRTF----FnqlknhpnkkftRTGDLGrTID--GNLFITGRIKDLIIVAGRNIYSADV 1047
Cdd:PRK08316  367 VGEIVHRSPQLMLGYWDDPEKTAEAFrggwF------------HSGDLG-VMDeeGYITVVDRKKDMIKTGGENVASREV 433

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1048 EKTV---ESSSEVlrpgccAVVGIPEEvlaqKGIsipdssDQVGLVVIaeVREGKAVS-KEVVNNIKARvveehgvaVAS 1123
Cdd:PRK08316  434 EEALythPAVAEV------AVIGLPDP----KWI------EAVTAVVV--PKAGATVTeDELIAHCRAR--------LAG 487

                         570       580       590
                  ....*....|....*....|....*....|....
gi 937914749 1124 VKLikPRTIC------KTTSGKIRRFECMRQFVD 1151
Cdd:PRK08316  488 FKV--PKRVIfvdelpRNPSGKILKRELRERYAG 519
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 756-1144 8.10e-19

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 91.63  E-value: 8.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  756 SDLCFLQFTSGSTGDAKGVMITHeglihnvktmkkRYRSTSKTVLVSWLP-QYHDM-----------GLIGGLFTALVSG 823
Cdd:cd05972    81 EDPALIYFTSGTTGLPKGVLHTH------------SYPLGHIPTAAYWLGlRPDDIhwniadpgwakGAWSSFFGPWLLG 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  824 GTSVLFSPMIFirNPLLWLQTINDYHGTHSAGPNFAFelviRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIEltq 903
Cdd:cd05972   149 ATVFVYEGPRF--DAERILELLERYGVTSFCGPPTAY----RMLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRA--- 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  904 PFGLSegvLAPGYGLAENCVYV-TCAFGECKPVFIdwqGRVCCGYVeqddtdtlIRIVDPDSltEHQEDGVEGEIWISSP 982
Cdd:cd05972   220 ATGLP---IRDGYGQTETGLTVgNFPDMPVKPGSM---GRPTPGYD--------VAIIDDDG--RELPPGEEGDIAIKLP 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  983 SSG--VGYWGNSEMSQRTFfnqlknhpNKKFTRTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLR 1059
Cdd:cd05972   284 PPGlfLGYVGDPEKTEASI--------RGDYYLTGDRAyRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAE 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1060 pgcCAVVGIPEEVLAQkgisipdssdqvglVVIAEV--REGKAVSKEVVNNIKARVVEEHGVAVASVKLIKPRTICKTTS 1137
Cdd:cd05972   356 ---AAVVGSPDPVRGE--------------VVKAFVvlTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTIS 418


                  ....*..
gi 937914749 1138 GKIRRFE 1144
Cdd:cd05972   419 GKIRRVE 425
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 586-1144 1.09e-18

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). 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 family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 92.56  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  586 EKNVIyTWINEEGklmNRR--TYQELhgnASYIAQKLLTSTKPVIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPvlp 663
Cdd:cd05970    32 DKLAL-VWCDDAG---EERifTFAEL---ADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP--- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  664 pdpmqsgGQALLKVENISKMCNavailstssyhaavRAGyIKNIVTLA-----KRVQKCSAQWPDIP---WIH---TDSW 732
Cdd:cd05970   102 -------ATHQLTAKDIVYRIE--------------SAD-IKMIVAIAednipEEIEKAAPECPSKPklvWVGdpvPEGW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  733 IkNYRRSSDSFNSDtvlFTKPQPS------DLCFLQFTSGSTGDAKgvMITHE-----GLI------HNVKTMKKRYrST 795
Cdd:cd05970   160 I-DFRKLIKNASPD---FERPTANsypcgeDILLVYFSSGTTGMPK--MVEHDftyplGHIvtakywQNVREGGLHL-TV 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  796 SKTvlvSWlpqyhDMGLIGGLFTALVSGGTSVLFSPMIFIrnPLLWLQTINDYHGTHSAGPNFAFELVIRrleaEKNKVY 875
Cdd:cd05970   233 ADT---GW-----GKAVWGKIYGQWIAGAAVFVYDYDKFD--PKALLEKLSKYGVTTFCAPPTIYRFLIR----EDLSRY 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  876 DLSSMVFLMIAAEPVRQKTVRRFIELTqpfGLSegvLAPGYGLAENCVYV-TCAFGECKPVFIdwqGRVCCGYVeqddtd 954
Cdd:cd05970   299 DLSSLRYCTTAGEALNPEVFNTFKEKT---GIK---LMEGFGQTETTLTIaTFPWMEPKPGSM---GKPAPGYE------ 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  955 tlIRIVDPDSltEHQEDGVEGEIWISSpSSGV------GYWGNSEMSQRTFFNqlknhpnkKFTRTGDLG-RTIDGNLFI 1027
Cdd:cd05970   364 --IDLIDREG--RSCEAGEEGEIVIRT-SKGKpvglfgGYYKDAEKTAEVWHD--------GYYHTGDAAwMDEDGYLWF 430

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1028 TGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEVLAQkgisipdsSDQVGLVVIAEVREGKAVSKEVVN 1107
Cdd:cd05970   431 VGRTDDLIKSSGYRIGPFEVESALIQHPAVLE---CAVTGVPDPIRGQ--------VVKATIVLAKGYEPSEELKKELQD 499

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*
gi 937914749 1108 NIK--------ARVVEehgvAVASVklikPRTIckttSGKIRRFE 1144
Cdd:cd05970   500 HVKkvtapykyPRIVE----FVDEL----PKTI----SGKIRRVE 532
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
605-1144 1.65e-18

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 91.86  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTKpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLP---PDPMQ-----SGGQALLK 676
Cdd:PRK08751   52 TYREADQLVEQFAAYLLGELQ--LKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPlytPRELKhqlidSGASVLVV 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  677 VENISKMCNAVaILSTSSYHAAVRA-----GYIKNIVT--LAKRVQKCsaqwpdIPWIHTDSWIKnYRRSSDSFNSDTVL 749
Cdd:PRK08751  130 IDNFGTTVQQV-IADTPVKQVITTGlgdmlGFPKAALVnfVVKYVKKL------VPEYRINGAIR-FREALALGRKHSMP 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  750 FTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSK-----TVLVSWLPQYHDMGLIG-GLFTALVSG 823
Cdd:PRK08751  202 TLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegcEVVITALPLYHIFALTAnGLVFMKIGG 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  824 GTSVLFSPmifiRNPLLWLQTINDYHGTHSAGPNFAFELVIRRLEAEKnkvYDLSSMVFLMIAAEPVRQKTVRRFIELTq 903
Cdd:PRK08751  282 CNHLISNP----RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQ---IDFSSLKMTLGGGMAVQRSVAERWKQVT- 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  904 pfGLSegvLAPGYGLAENcvyvtcAFGEC-KPV-FIDWQGR---------VCCgyveQDDTDTLIRIvdpdsltehqedG 972
Cdd:PRK08751  354 --GLT---LVEAYGLTET------SPAACiNPLtLKEYNGSiglpipstdACI----KDDAGTVLAI------------G 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  973 VEGEIWISSPSSGVGYWGNSEMSQRTFfnqlknhPNKKFTRTGDLGRTID-GNLFITGRIKDLIIVAGRNIYSADVEKTV 1051
Cdd:PRK08751  407 EIGELCIKGPQVMKGYWKRPEETAKVM-------DADGWLHTGDIARMDEqGFVYIVDRKKDMILVSGFNVYPNEIEDVI 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1052 ESSSEVLRpgcCAVVGIPEEvlaqkgisipdSSDQVGLVVIaevregkaVSKEvvNNIKARVVEEHgvAVASVKLIK-PR 1130
Cdd:PRK08751  480 AMMPGVLE---VAAVGVPDE-----------KSGEIVKVVI--------VKKD--PALTAEDVKAH--ARANLTGYKqPR 533

                         570       580
                  ....*....|....*....|
gi 937914749 1131 TI------CKTTSGKIRRFE 1144
Cdd:PRK08751  534 IIefrkelPKTNVGKILRRE 553
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 605-1143 3.35e-18

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 90.23  E-value: 3.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTstKPVIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPpdpmqsggqaLLKVENISKmc 684
Cdd:cd05958    12 TYRDLLALANRIANVLVG--ELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP----------LLRPKELAY-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 navaILStssyhaavragyiKNIVTLAKRVQKCSAqwpdipwihtdswiknyrrssdsfnSDtvlftkpqpsDLCFLQFT 764
Cdd:cd05958    78 ----ILD-------------KARITVALCAHALTA-------------------------SD----------DICILAFT 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  765 SGSTGDAKGVMITHEGLIHNVKTMKKR-YRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPmifiRNPLLWLQ 843
Cdd:cd05958   106 SGTTGAPKATMHFHRDPLASADRYAVNvLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE----ATPDLLLS 181

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  844 TINDYHGTHSAGPNFAFELVIRRLEAEKNkvyDLSSMVFLMIAAEPVRQKTVRRFIELTqpfglseGV-LAPGYGLAENC 922
Cdd:cd05958   182 AIARYKPTVLFTAPTAYRAMLAHPDAAGP---DLSSLRKCVSAGEALPAALHRAWKEAT-------GIpIIDGIGSTEMF 251

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  923 -VYVTCAFGECKPvfiDWQGRVCCGYVeqddtdtlIRIVDPDSLTehQEDGVEGEIWISSPSsgvGYWGNSEMSQRTFFN 1001
Cdd:cd05958   252 hIFISARPGDARP---GATGKPVPGYE--------AKVVDDEGNP--VPDGTIGRLAVRGPT---GCRYLADKRQRTYVQ 315

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1002 QLKNHpnkkftrTGDL-GRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEvlaqKGISI 1080
Cdd:cd05958   316 GGWNI-------TGDTySRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAE---CAVVGHPDE----SRGVV 381

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749 1081 PDSSdqvgLVVIAEVREGKAVSKEVVNNIKARvveehgvaVASVKliKPRTIC------KTTSGKIRRF 1143
Cdd:cd05958   382 VKAF----VVLRPGVIPGPVLARELQDHAKAH--------IAPYK--YPRAIEfvtelpRTATGKLQRF 436
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 586-1071 6.30e-18

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation 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. The 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. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 90.00  E-value: 6.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  586 EKNVIYTWINEEGklmNRRTYQELHGNASYIAQKLltsTKPVIKPGDRVLLIHLPGLEFIDAFFGCIRAGVI--PV-PVL 662
Cdd:cd12119    11 DREIVSRTHEGEV---HRYTYAEVAERARRLANAL---RRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlhTInPRL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  663 PPdpmqsggqallkvENISKMCNavailstssyHAAVRAGYIKNivTLAKRVQKCSAQWP------------------DI 724
Cdd:cd12119    85 FP-------------EQIAYIIN----------HAEDRVVFVDR--DFLPLLEAIAPRLPtvehvvvmtddaampepaGV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  725 PWIHTDSWIknyrrSSDSFNSDTVLFTKPQPSDLCFlqfTSGSTGDAKGVMITHEGLI-HNVKTMKK--RYRSTSKTVLV 801
Cdd:cd12119   140 GVLAYEELL-----AAESPEYDWPDFDENTAAAICY---TSGTTGNPKGVVYSHRSLVlHAMAALLTdgLGLSESDVVLP 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  802 SwLPQYHDMGLigGL-FTALVSGGTSVLFSPMIfirNPLLWLQTINDYHGTHSAGPNFAFELVIRRLEAEKnkvYDLSSM 880
Cdd:cd12119   212 V-VPMFHVNAW--GLpYAAAMVGAKLVLPGPYL---DPASLAELIEREGVTFAAGVPTVWQGLLDHLEANG---RDLSSL 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  881 VFLMIAAEPVRQKTVRRFIELTQPfglsegVLApGYGLAENCVYVTCAF------GECKPVFIDW---QGRVCCGyVEqd 951
Cdd:cd12119   283 RRVVIGGSAVPRSLIEAFEERGVR------VIH-AWGMTETSPLGTVARppsehsNLSEDEQLALrakQGRPVPG-VE-- 352

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  952 dtdtlIRIVDPDSlTEHQEDGVE-GEIWISSPSSGVGYWGNSEMSQRTFFNqlknhpnkKFTRTGDLGrTID--GNLFIT 1028
Cdd:cd12119   353 -----LRIVDDDG-RELPWDGKAvGELQVRGPWVTKSYYKNDEESEALTED--------GWLRTGDVA-TIDedGYLTIT 417

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 937914749 1029 GRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEE 1071
Cdd:cd12119   418 DRSKDVIKSGGEWISSVELENAIMAHPAVAE---AAVIGVPHP 457
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 755-1070 7.08e-18

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: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 87.92  E-value: 7.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMIF 834
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 iRNPLL----WlQTINDYHGTH-SAGPNFAFELVIRRLEAeknkvyDLSSMVFLMIAAEPVRQKTVRRFIELTqpfGLSe 909
Cdd:cd05944    81 -RNPGLfdnfW-KLVERYRITSlSTVPTVYAALLQVPVNA------DISSLRFAMSGAAPLPVELRARFEDAT---GLP- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  910 gvLAPGYGLAENCVYVTCAF--GECKPvfidwqgrvccGYVEQDDTDTLIRIVDPDSLTEHQED---GVEGEIWISSPSS 984
Cdd:cd05944   149 --VVEGYGLTEATCLVAVNPpdGPKRP-----------GSVGLRLPYARVRIKVLDGVGRLLRDcapDEVGEICVAGPGV 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  985 GVGYWgNSEMSQRTFFNQLknhpnkkFTRTGDLGRT-IDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVlrpGCC 1063
Cdd:cd05944   216 FGGYL-YTEGNKNAFVADG-------WLNTGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAV---AFA 284


                  ....*..
gi 937914749 1064 AVVGIPE 1070
Cdd:cd05944   285 GAVGQPD 291
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 738-1054 9.05e-18

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. 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. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 88.96  E-value: 9.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  738 RSSDSfnsdTVLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLF 817
Cdd:cd17640    74 NHSES----VALVVENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYF 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  818 taLVSGGTSVLFSPMIFIRNPllwLQTINdyhgthsagPNFaFELVIRRLEAEKNKVYDLSSmvflmiAAEPVRQKTVRR 897
Cdd:cd17640   150 --IFACGCSQAYTSIRTLKDD---LKRVK---------PHY-IVSVPRLWESLYSGIQKQVS------KSSPIKQFLFLF 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  898 FIELTQ-PFGLS-EGVLAP---------------GYGLAENCVYVTC---------AFGECKPvfidwqgrvccgyveqd 951
Cdd:cd17640   209 FLSGGIfKFGISgGGALPPhvdtffeaigievlnGYGLTETSPVVSArrlkcnvrgSVGRPLP----------------- 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  952 dtDTLIRIVDPDSlTEHQEDGVEGEIWISSPSSGVGYWGNSE-----MSQRTFFNqlknhpnkkftrTGDLGR-TIDGNL 1025
Cdd:cd17640   272 --GTEIKIVDPEG-NVVLPPGEKGIVWVRGPQVMKGYYKNPEatskvLDSDGWFN------------TGDLGWlTCGGEL 336

                         330       340       350
                  ....*....|....*....|....*....|
gi 937914749 1026 FITGRIKDLIIVA-GRNIYSADVEKTVESS 1054
Cdd:cd17640   337 VLTGRAKDTIVLSnGENVEPQPIEEALMRS 366
PRK07529 PRK07529
AMP-binding domain protein; Validated
 745-1069 1.75e-17

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 89.24  E-value: 1.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  745 SDTVLF--TKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVS 822
Cdd:PRK07529  200 PGDRLFsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLAR 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  823 GGTSVLFSPMIFiRNPLL----WlQTINDYHGTH-SAGPNFAFELVIRRLEAeknkvYDLSSMVFLMIAAEPVRQKTVRR 897
Cdd:PRK07529  280 GAHVVLATPQGY-RGPGVianfW-KIVERYRINFlSGVPTVYAALLQVPVDG-----HDISSLRYALCGAAPLPVEVFRR 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  898 FIELTqpfglseGV-LAPGYGLAENCVYVTCAF--GECKPvfidwqgrvccGYVEQDDTDTLIRIV--DPD--SLTEHQE 970
Cdd:PRK07529  353 FEAAT-------GVrIVEGYGLTEATCVSSVNPpdGERRI-----------GSVGLRLPYQRVRVVilDDAgrYLRDCAV 414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  971 DGVeGEIWISSPSSGVGYWgNSEMSQRTFFNQlknhpnkKFTRTGDLGRT-IDGNLFITGRIKDLIIVAGRNIYSADVEK 1049
Cdd:PRK07529  415 DEV-GVLCIAGPNVFSGYL-EAAHNKGLWLED-------GWLNTGDLGRIdADGYFWLTGRAKDLIIRGGHNIDPAAIEE 485

                         330       340
                  ....*....|....*....|
gi 937914749 1050 TVESSSEVlrpGCCAVVGIP 1069
Cdd:PRK07529  486 ALLRHPAV---ALAAAVGRP 502
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 754-1112 2.02e-17

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 88.39  E-value: 2.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  754 QPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGgtsvlfSPMI 833
Cdd:PRK07514  154 GADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAG------ASMI 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  834 FIrnpllwlqtindyhgthsagPNFAFELVIR----------------RLEAEKNKVYDLSSMVFLMIA-AEPVRQKTVR 896
Cdd:PRK07514  228 FL--------------------PKFDPDAVLAlmpratvmmgvptfytRLLQEPRLTREAAAHMRLFISgSAPLLAETHR 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  897 RFIELTqpfglsegvlapG------YGLAENCVYVTCAF-GECKPvfidwqGRVccGY----VEqddtdtlIRIVDPDSL 965
Cdd:PRK07514  288 EFQERT------------GhailerYGMTETNMNTSNPYdGERRA------GTV--GFplpgVS-------LRVTDPETG 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  966 TEHQEDGVeGEIWISSPSSGVGYWGNSEMSQRTFfnqlknHPNKKFtRTGDLGRtID--GNLFITGRIKDLIIVAGRNIY 1043
Cdd:PRK07514  341 AELPPGEI-GMIEVKGPNVFKGYWRMPEKTAEEF------RADGFF-ITGDLGK-IDerGYVHIVGRGKDLIISGGYNVY 411

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1044 SADVEKTVESSSEVLRPgccAVVGIPEevlaqkgisiPDSSDQVGLVVIAevREGKAVS-KEVVNNIKAR 1112
Cdd:PRK07514  412 PKEVEGEIDELPGVVES---AVIGVPH----------PDFGEGVTAVVVP--KPGAALDeAAILAALKGR 466
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 745-1142 4.90e-17

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 87.34  E-value: 4.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  745 SDTVLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRS--TSKTVLVSWLPQYHDMGLIGGLFTALVS 822
Cdd:PLN02330  173 GDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPemIGQVVTLGLIPFFHIYGITGICCATLRN 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  823 GGTSVL---FSPMIFIrNPLLwlqtindyhgTHSAG-----PNFAFELVirrleaeKNKV---YDLSSMVF--LMIAAEP 889
Cdd:PLN02330  253 KGKVVVmsrFELRTFL-NALI----------TQEVSfapivPPIILNLV-------KNPIveeFDLSKLKLqaIMTAAAP 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  890 VRQKTVRRF------IELTQPFGLSE--------GVLAPGYGLAEncvyvtcafgeckpvfidwqgRVCCGYVEqddTDT 955
Cdd:PLN02330  315 LAPELLTAFeakfpgVQVQEAYGLTEhscitlthGDPEKGHGIAK---------------------KNSVGFIL---PNL 370

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  956 LIRIVDPD---SLTEHqedgVEGEIWISSPSSGVGYWGNSEMSQRTFFNQLKNHpnkkftrTGDLGRTI-DGNLFITGRI 1031
Cdd:PLN02330  371 EVKFIDPDtgrSLPKN----TPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLH-------TGDIGYIDdDGDIFIVDRI 439

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1032 KDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEVLAQkgisIPdssdqVGLVVIAevREGKAVSKEVVNNIKA 1111
Cdd:PLN02330  440 KELIKYKGFQVAPAELEAILLTHPSVED---AAVVPLPDEEAGE----IP-----AACVVIN--PKAKESEEDILNFVAA 505

                         410       420       430
                  ....*....|....*....|....*....|.
gi 937914749 1112 RVVeeHGVAVASVKLIKprTICKTTSGKIRR 1142
Cdd:PLN02330  506 NVA--HYKKVRVVQFVD--SIPKSLSGKIMR 532
PRK08315 PRK08315
AMP-binding domain protein; Validated
 754-1148 7.82e-17

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 86.79  E-value: 7.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  754 QPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPmI 833
Cdd:PRK08315  197 DPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGATMVYPGE-G 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  834 FirNPLLWLQTIND-----YHG---------THsagPNFAfelvirrleaeknkVYDLSSMVFLMIAAEPVRQKTVRRFI 899
Cdd:PRK08315  276 F--DPLATLAAVEEerctaLYGvptmfiaelDH---PDFA--------------RFDLSSLRTGIMAGSPCPIEVMKRVI 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  900 ELtqpFGLSEgvlapgyglaencvyVTCAFG--ECKPVFIdwQGRVccgyveqDD-----TDTL--------IRIVDPDS 964
Cdd:PRK08315  337 DK---MHMSE---------------VTIAYGmtETSPVST--QTRT-------DDplekrVTTVgralphleVKIVDPET 389

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  965 lTEHQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFFNQlknhpnkKFTRTGDLGrTID--GNLFITGRIKDLIIVAGRNI 1042
Cdd:PRK08315  390 -GETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDAD-------GWMHTGDLA-VMDeeGYVNIVGRIKDMIIRGGENI 460

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1043 YSADVEK---TVESSSEVlrpgccAVVGIP-----EEVLAqkgisipdssdqvglVVIaeVREGKAVSKEvvnNIKA--- 1111
Cdd:PRK08315  461 YPREIEEflyTHPKIQDV------QVVGVPdekygEEVCA---------------WII--LRPGATLTEE---DVRDfcr 514

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 937914749 1112 ------------RVVEEHgvavasvklikPRTIckttSGKIRRFEcMRQ 1148
Cdd:PRK08315  515 gkiahykipryiRFVDEF-----------PMTV----TGKIQKFK-MRE 547
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 761-1144 8.44e-17

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation 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. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 86.20  E-value: 8.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  761 LQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLiGGLFTALVSGGTSVlfspmiFIRN--- 837
Cdd:cd12118   138 LNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGW-CFPWTVAAVGGTNV------CLRKvda 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  838 PLLWlQTINDYHGTHSAGPNFAFELVIRRLEAEKNKvydLSSMVFLMIAAEP----VRQKTVRRFIELTQPFGLSEgvla 913
Cdd:cd12118   211 KAIY-DLIEKHKVTHFCGAPTVLNMLANAPPSDARP---LPHRVHVMTAGAPppaaVLAKMEELGFDVTHVYGLTE---- 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  914 pGYGLAENCVYvtcafgecKPvfiDWQG-----------RVCCGYVEQDDtdtlIRIVDPDSLTEHQEDGVE-GEIWISS 981
Cdd:cd12118   283 -TYGPATVCAW--------KP---EWDElpteerarlkaRQGVRYVGLEE----VDVLDPETMKPVPRDGKTiGEIVFRG 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  982 PSSGVGYWGNSEMSQRTF----FnqlknhpnkkftRTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSE 1056
Cdd:cd12118   347 NIVMKGYLKNPEATAEAFrggwF------------HSGDLAvIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPA 414

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1057 VLRpgcCAVVGIPEEVLaqkgisipdssdqvGLVVIA--EVREGKAVSKEVVnnIKarVVEEHgvaVASVKLikPRTIC- 1133
Cdd:cd12118   415 VLE---AAVVARPDEKW--------------GEVPCAfvELKEGAKVTEEEI--IA--FCREH---LAGFMV--PKTVVf 468

                         410
                  ....*....|....*
gi 937914749 1134 ----KTTSGKIRRFE 1144
Cdd:cd12118   469 gelpKTSTGKIQKFV 483
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 756-1142 8.69e-17

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 86.63  E-value: 8.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  756 SDLCFLQFTSGSTGDAKGVMITHEGLIHN-VKTMKKRYRSTS-KTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFS--- 830
Cdd:PRK06710  206 NDLALLQYTGGTTGFPKGVMLTHKNLVSNtLMGVQWLYNCKEgEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPkfd 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  831 -PMIFirnpllwlQTINDYHGTHSAGpnfAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQpfglse 909
Cdd:PRK06710  286 mKMVF--------EAIKKHKVTLFPG---APTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTG------ 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  910 GVLAPGYGLAENCVYVTCAFgeckpvfiDWQGRVcCGYVEQDDTDTLIRIVDPDSlTEHQEDGVEGEIWISSPSSGVGYW 989
Cdd:PRK06710  349 GKLVEGYGLTESSPVTHSNF--------LWEKRV-PGSIGVPWPDTEAMIMSLET-GEALPPGEIGEIVVKGPQIMKGYW 418

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  990 GNSEMSQRTFfnqlknhpNKKFTRTGDLGRTI-DGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGI 1068
Cdd:PRK06710  419 NKPEETAAVL--------QDGWLHTGDVGYMDeDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQE---VVTIGV 487

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937914749 1069 PEevlaqkgisiPDSSDQVGLVVIaeVREGKAVSKEVVNNIKARVVEEHGVAvasvKLIKPRT-ICKTTSGKIRR 1142
Cdd:PRK06710  488 PD----------PYRGETVKAFVV--LKEGTECSEEELNQFARKYLAAYKVP----KVYEFRDeLPKTTVGKILR 546
PLN02246 PLN02246
4-coumarate--CoA ligase
 605-1142 9.21e-17

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 86.19  E-value: 9.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLltsTKPVIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPpdpmqsggqallkveniskMC 684
Cdd:PLN02246   52 TYADVELLSRRVAAGL---HKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANP-------------------FY 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 NAVAIlstssyHAAVRAGYIKNIVTLAKRVQKCS--AQWPDIPWIHTDSWIKNYRRSSDSFNSDTVLFTKP--QPSDLCF 760
Cdd:PLN02246  110 TPAEI------AKQAKASGAKLIITQSCYVDKLKglAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVeiSPDDVVA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  761 LQFTSGSTGDAKGVMITHEGLIHNVKTM----KKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPmiFIR 836
Cdd:PLN02246  184 LPYSSGTTGLPKGVMLTHKGLVTSVAQQvdgeNPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPK--FEI 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  837 NPLLWLqtINDYHGThsAGPnFAFELVirrLEAEKNKV---YDLSSMVFLMIAAEPVRQktvrrfiELTQPFG--LSEGV 911
Cdd:PLN02246  262 GALLEL--IQRHKVT--IAP-FVPPIV---LAIAKSPVvekYDLSSIRMVLSGAAPLGK-------ELEDAFRakLPNAV 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  912 LAPGYGLAE-NCVYVTC-AFGecKPVFIDWQGrvCCGYVEQddtDTLIRIVDPD---SLTEHQedgvEGEIWISSPSSGV 986
Cdd:PLN02246  327 LGQGYGMTEaGPVLAMClAFA--KEPFPVKSG--SCGTVVR---NAELKIVDPEtgaSLPRNQ----PGEICIRGPQIMK 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  987 GYWGNSEMSQRTFfnqlknhPNKKFTRTGDLGrTIDGN--LFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCA 1064
Cdd:PLN02246  396 GYLNDPEATANTI-------DKDGWLHTGDIG-YIDDDdeLFIVDRLKELIKYKGFQVAPAELEALLISHPSIAD---AA 464

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1065 VVGIPEEVLAQkgisIPdssdqVGLVV------IAEVREGKAVSKEVVNNIKARvveehgvavasvKLIKPRTICKTTSG 1138
Cdd:PLN02246  465 VVPMKDEVAGE----VP-----VAFVVrsngseITEDEIKQFVAKQVVFYKRIH------------KVFFVDSIPKAPSG 523


                  ....
gi 937914749 1139 KIRR 1142
Cdd:PLN02246  524 KILR 527
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 744-1144 1.75e-16

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 84.79  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  744 NSDTVLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQyhDMGLIGGLFTALVS- 822
Cdd:cd05971    76 NSGASALVTDGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPA--DWAWIGGLLDVLLPs 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  823 ---GGTSVLFSPMIFirNPLLWLQTINDYHGTHSAGPNFAfeLVIRRLEAEKNKVYDLSsMVFLMIAAEPVRQKTV---- 895
Cdd:cd05971   154 lyfGVPVLAHRMTKF--DPKAALDLMSRYGVTTAFLPPTA--LKMMRQQGEQLKHAQVK-LRAIATGGESLGEELLgwar 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  896 RRF-IELTQPFGLSEGVLAPGyglaeNCVyvtcAFGECKPVFIdwqGRVCCGYVeqddtdtlIRIVDPDSltEHQEDGVE 974
Cdd:cd05971   229 EQFgVEVNEFYGQTECNLVIG-----NCS----ALFPIKPGSM---GKPIPGHR--------VAIVDDNG--TPLPPGEV 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  975 GEIWISSPSSG--VGYWGNSEMSQRTFfnqlknhpNKKFTRTGDLGRT-IDGNLFITGRIKDLIIVAGRNIYSADVEKTV 1051
Cdd:cd05971   287 GEIAVELPDPVafLGYWNNPSATEKKM--------AGDWLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEECL 358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1052 ESSSEVLRpgcCAVVGIPEEVlaqkgisipdSSDQV-GLVVIAEVREG-KAVSKEVVNNIKARV-VEEHGVAVASVKLIk 1128
Cdd:cd05971   359 LKHPAVLM---AAVVGIPDPI----------RGEIVkAFVVLNPGETPsDALAREIQELVKTRLaAHEYPREIEFVNEL- 424

                         410
                  ....*....|....*.
gi 937914749 1129 PRtickTTSGKIRRFE 1144
Cdd:cd05971   425 PR----TATGKIRRRE 436
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 759-1132 2.12e-16

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. 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: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 83.12  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  759 CFLQFTSGSTGDAKGVMITHEGLI-HNVKTMKKRyRSTSKTVLVSWLPQYHdMGLIGGLFTALVSGGTSVlfspmiFIR- 836
Cdd:cd17636     3 VLAIYTAAFSGRPNGALLSHQALLaQALVLAVLQ-AIDEGTVFLNSGPLFH-IGTLMFTLATFHAGGTNV------FVRr 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  837 -NPLLWLQTINDYHGTHSagpnFAFELVIRRL-EAEKNKVYDLSSMVFLMIAAEPVRQKTVrrfieLTQPFGLSEGvlap 914
Cdd:cd17636    75 vDAEEVLELIEAERCTHA----FLLPPTIDQIvELNADGLYDLSSLRSSPAAPEWNDMATV-----DTSPWGRKPG---- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  915 GYGLAENCVYVTCAfgeckpvfidWQGRVCCGYVEQDDTDTLIRIVDPDSltehQE--DGVEGEIWISSPSSGVGYWGNS 992
Cdd:cd17636   142 GYGQTEVMGLATFA----------ALGGGAIGGAGRPSPLVQVRILDEDG----REvpDGEVGEIVARGPTVMAGYWNRP 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  993 EMSQRTFFNqlknhpnkKFTRTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEE 1071
Cdd:cd17636   208 EVNARRTRG--------GWHHTNDLGrREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVAD---AAVIGVPDP 276

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937914749 1072 VLAQkgisipdssdQVGLVVIaeVREGKAVSK-EVVNNIKARvveehgvaVASVKliKPRTI 1132
Cdd:cd17636   277 RWAQ----------SVKAIVV--LKPGASVTEaELIEHCRAR--------IASYK--KPKSV 316
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 754-1048 2.79e-16

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. 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: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 84.06  E-value: 2.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  754 QPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLfSPMI 833
Cdd:cd17650    91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVI-CPDE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  834 FIRNPLLWLQTINDYHGThsagpnfAFELV---IRRL--EAEKNKVyDLSSMVFLMIAAEPVrqkTVRRFIELTQPFGLS 908
Cdd:cd17650   170 VKLDPAALYDLILKSRIT-------LMESTpalIRPVmaYVYRNGL-DLSAMRLLIVGSDGC---KAQDFKTLAARFGQG 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  909 EgVLAPGYGLAENCV----YVTCAFGECKPVFIDwqgrvccgyVEQDDTDTLIRIVDPDslTEHQEDGVEGEIWISSPSS 984
Cdd:cd17650   239 M-RIINSYGVTEATIdstyYEEGRDPLGDSANVP---------IGRPLPNTAMYVLDER--LQPQPVGVAGELYIGGAGV 306

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937914749  985 GVGYWGNSEMSQRTFFnQLKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVE 1048
Cdd:cd17650   307 ARGYLNRPELTAERFV-ENPFAPGERMYRTGDLARwRADGNVELLGRVDHQVKIRGFRIELGEIE 370
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 750-1142 5.37e-16

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 83.70  E-value: 5.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  750 FTKPQPSD-LCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTsVL 828
Cdd:PRK09088  128 DTPSIPPErVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGS-IL 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  829 FSPMIFIRNPLLWLQTInDYHGTHSAG-PNFAfelviRRLEAEKNkvYD---LSSMVFLMIAAEPVRQKTVRRFIELTQP 904
Cdd:PRK09088  207 VSNGFEPKRTLGRLGDP-ALGITHYFCvPQMA-----QAFRAQPG--FDaaaLRHLTALFTGGAPHAAEDILGWLDDGIP 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  905 ----FGLSE-GVLapgYGLAENCVYVTC---AFGECKPVFidwQGRVccgyVEQDDTDTlirivdpdsltehqEDGVEGE 976
Cdd:PRK09088  279 mvdgFGMSEaGTV---FGMSVDCDVIRAkagAAGIPTPTV---QTRV----VDDQGNDC--------------PAGVPGE 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  977 IWISSPSSGVGYWGNSEMSQRTFFNQlknhpnkKFTRTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSS 1055
Cdd:PRK09088  335 LLLRGPNLSPGYWRRPQATARAFTGD-------GWFRTGDIArRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHP 407

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1056 EVLRpgcCAVVGIPEevlAQKGisipdssdQVGLVVIAeVREGKAVS-KEVVNNIKARV----VEEHGVAVASVklikPR 1130
Cdd:PRK09088  408 GIRE---CAVVGMAD---AQWG--------EVGYLAIV-PADGAPLDlERIRSHLSTRLakykVPKHLRLVDAL----PR 468

                         410
                  ....*....|..
gi 937914749 1131 tickTTSGKIRR 1142
Cdd:PRK09088  469 ----TASGKLQK 476
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 747-1035 8.92e-16

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-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. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to 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. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 83.03  E-value: 8.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  747 TVLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRS--TSKTVLVSWLPQYHDM------------GL 812
Cdd:cd17639    79 SAIFTDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPEllGPDDRYLAYLPLAHIFelaaenvclyrgGT 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  813 IG-----GLFTALVSG--GTSVLFSPMIFIRNPLLW-------LQTINdyhgthSAGP------NFAFELVIRRLEAEKN 872
Cdd:cd17639   159 IGygsprTLTDKSKRGckGDLTEFKPTLMVGVPAIWdtirkgvLAKLN------PMGGlkrtlfWTAYQSKLKALKEGPG 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  873 KVYdLSSMVFlmiaaEPVRQKT---VRRFI-------ELTQPFgLSEgVLAP---GYGLAEncvyvTCAFGeCKPVFIDW 939
Cdd:cd17639   233 TPL-LDELVF-----KKVRAALggrLRYMLsggaplsADTQEF-LNI-VLCPviqGYGLTE-----TCAGG-TVQDPGDL 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  940 Q-GRV----CCGYveqddtdtlIRIVDPDSLtEHQEDGVE--GEIWISSPSSGVGYWGNSEMSQRTFFNQlknhpnkKFT 1012
Cdd:cd17639   299 EtGRVgpplPCCE---------IKLVDWEEG-GYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGD-------GWF 361

                         330       340
                  ....*....|....*....|....
gi 937914749 1013 RTGDLGR-TIDGNLFITGRIKDLI 1035
Cdd:cd17639   362 HTGDIGEfHPDGTLKIIDRKKDLV 385
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 605-1075 1.29e-15

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: 82.34  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIhLP-GLEFIDAFFGCIRAGVIPVPVLPPDPMQsggqallKVENISKM 683
Cdd:cd12116    14 SYAELDERANRLAARLRARG---VGPGDRVAVY-LPrSARLVAAMLAVLKAGAAYVPLDPDYPAD-------RLRYILED 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  684 CNAVAILSTSsyhaAVRAGYIKNIVTLAKRVqkcsaqwPDIPwihtdswiknyrrssdsfNSDTVLFTKPQPSDLCFLQF 763
Cdd:cd12116    83 AEPALVLTDD----ALPDRLPAGLPVLLLAL-------AAAA------------------AAPAAPRTPVSPDDLAYVIY 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  764 TSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIgGLFTALVSGGTSVLFSPMIfIRNPLLWLQ 843
Cdd:cd12116   134 TSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLL-ELLLPLLAGARVVIAPRET-QRDPEALAR 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  844 TINDYHGTH-SAGPNFAFELVIRRLEAEKNkvydlssmVFLMIAAEPVrqktvrrfieltqPFGLSEGVLAPG------Y 916
Cdd:cd12116   212 LIEAHSITVmQATPATWRMLLDAGWQGRAG--------LTALCGGEAL-------------PPDLAARLLSRVgslwnlY 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  917 GLAENCVYVTCAF--GECKPVFIdwqGRVCCG---YVeqddTDTLIRIVDPdsltehqedGVEGEIWISSPSSGVGYWGN 991
Cdd:cd12116   271 GPTETTIWSTAARvtAAAGPIPI---GRPLANtqvYV----LDAALRPVPP---------GVPGELYIGGDGVAQGYLGR 334

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  992 SEMSQRTFFNQLKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPE 1070
Cdd:cd12116   335 PALTAERFVPDPFAGPGSRLYRTGDLVRrRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQ---AAVVVRED 411


                  ....*
gi 937914749 1071 EVLAQ 1075
Cdd:cd12116   412 GGDRR 416
y4iL_like cd08152
Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ...
 1934-2190 1.47e-15

Catalase-like heme-binding proteins similar to the uncharacterized y4iL; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to Rhizobium sp. NGR234 y4iL, of mostly bacterial origin.


Pssm-ID: 163708  Cd Length: 305  Bit Score: 80.00  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1934 RGVLRMYEEIPSFPRHKIFASGKSFPVIVRHSNSLSADDDARL-DARGAAVRILsDNDGE-------APLLDLTLKSGKA 2005
Cdd:cd08152    16 KAEFTVLDDLPPELAQGLFAEPGTYPAVIRFSNAPGDILDDSVpDPRGMAIKVL-GVPGEkllpeedATTQDFVLVNHPV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 2006 FYARTIADFA--TWLVCGLPAREEQVKR-----SPHIRDAV--------WGSLRSTDSYTVLH--YYSniCRLLRFDDGr 2068
Cdd:cd08152    95 FFARDAKDYLalLKLLARTTSLPDGAKAalsapLRGALRVLeaaggespTLKLGGHPPAHPLGetYWS--QAPYRFGDY- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 2069 emYAKFKLRPADPDVPEdsgkvvprgiLPPETGAIPRDEDDTRPLlfLADDFRRRvgspdGVRYVFQLQLRevpTDAAAR 2148
Cdd:cd08152   172 --VAKYSVVPASPALPA----------LTGKELDLTDDPDALREA--LADFLAEN-----DAEFEFRIQLC---TDLEKM 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 937914749 2149 DVAlDCTRPWDEAEFPYIDVGEVSIGR-NLPTEET-----EKLEFNPF 2190
Cdd:cd08152   230 PIE-DASVEWPEALSPFVPVATITIPPqDFDSPARqrafdDNLSFNPW 276
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 630-1095 1.54e-15

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-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. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 82.13  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  630 PGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPMQSGGQALLKVEniSKMCnAVAILSTSSYHAAVRAGYIKNIVT 709
Cdd:cd05932    30 PGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSE--SKAL-FVGKLDDWKAMAPGVPEGLISISL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  710 LAKRVQKCSAQWPDIpwihtdswIKNYRRSSDSfnsdtvlfTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMK 789
Cdd:cd05932   107 PPPSAANCQYQWDDL--------IAQHPPLEER--------PTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGI 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  790 KRYRSTSKTVLVSWLPQYH-------DMG-LIGGLFTALV-SGGTSV----LFSPMIFIRNPLLWLQTindYHGTHSAGP 856
Cdd:cd05932   171 EHIGTEENDRMLSYLPLAHvtervfvEGGsLYGGVLVAFAeSLDTFVedvqRARPTLFFSVPRLWTKF---QQGVQDKIP 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  857 NFAFEL-----VIRRLEaeKNKVYD---LSSMVFLMIAAEPVRQKtvrrFIELTQPFGLSegvLAPGYGLAENCVYVTCa 928
Cdd:cd05932   248 QQKLNLllkipVVNSLV--KRKVLKglgLDQCRLAGCGSAPVPPA----LLEWYRSLGLN---ILEAYGMTENFAYSHL- 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  929 fgeCKPvfidwqGRVCCGYVEQDDTDTLIRIVDpdsltehqedgvEGEIWISSPSSGVGYWGNSEMSQRTFfnqlknhPN 1008
Cdd:cd05932   318 ---NYP------GRDKIGTVGNAGPGVEVRISE------------DGEILVRSPALMMGYYKDPEATAEAF-------TA 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1009 KKFTRTGDLGRT-IDGNLFITGRIKDLIIVA-GRNIYSADVEKTVESSSEVlrPGCCaVVGipeevlaqKGISIPdssdq 1086
Cdd:cd05932   370 DGFLRTGDKGELdADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRV--EMVC-VIG--------SGLPAP----- 433


                  ....*....
gi 937914749 1087 VGLVVIAEV 1095
Cdd:cd05932   434 LALVVLSEE 442
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
105-172 1.88e-15

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 72.95  E-value: 1.88e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937914749   105 IVGAGPSGLSAAYALAKLGYRnVTLFEKCHTVSGMCESIDIEGRIYDLGGQVIAANSAPVITHLAEEL 172
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSYRVPGYVFDYGAHIFHGSDEPNVRDLLDEL 67
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
100-343 1.94e-15

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 81.51  E-value: 1.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  100 DTRIGIVGAGPSGLSAAYALAKLGYRnVTLFE-------KCHTVSGmcesiDIEGRIYDLGGQVIAANSaPVITHLAEEL 172
Cdd:COG1231     7 GKDVVIVGAGLAGLAAARELRKAGLD-VTVLEardrvggRVWTLRF-----GDDGLYAELGAMRIPPSH-TNLLALAREL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  173 G-SDFEEMDTHKLSLIDSQTGNIRDLEVAEDYVSMVSLTLKLQDEANKSGRAGLHALSGLASDPTHEFLKQNGINSMPKS 251
Cdd:COG1231    80 GlPLEPFPNENGNALLYLGGKRVRAGEIAADLRGVAELLAKLLRALAAALDPWAHPAAELDRESLAEWLRRNGASPSARR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  252 VAYGYTASGYG-------FVQDMPYAFIQEFtrtsmAGKIRRFKHGYMSMWERLSKSLPFEVFCDTQVLNVKRNscGANV 324
Cdd:COG1231   160 LLGLLGAGEYGadpdelsLLDLLRYAASAGG-----GAQQFRIVGGMDQLPRALAAELGDRIRLGAPVTRIRQD--GDGV 232

                         250
                  ....*....|....*....
gi 937914749  325 TIKNNNGEkqVLEFDKIIL 343
Cdd:COG1231   233 TVTTDDGG--TVRADAVIV 249
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 628-1071 2.04e-15

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 82.01  E-value: 2.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  628 IKPGDRVLlIHLPGL-EFIDAFFGCIRAGVIPVPVLPpdpmQSGGQALLKVENISKMCNAVAILSTSSYHAAVRAGY-IK 705
Cdd:PRK06178   80 VGAGDRVA-VFLPNCpQFHIVFFGILKLGAVHVPVSP----LFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETsLR 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  706 NIVTLAkrvqkCSAQWPDIPWIHTDSWIKNYRRSS----DSFNS-DTVLFTKPQPS----DLCFLQFTSGSTGDAKGVMI 776
Cdd:PRK06178  155 HVIVTS-----LADVLPAEPTLPLPDSLRAPRLAAagaiDLLPAlRACTAPVPLPPpaldALAALNYTGGTTGMPKGCEH 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  777 THEgliHNVKTMKKRY----RSTSKTVLVSWLPQY----HDMGLIGGLFtalvSGGTSVLFSpmifiR-NPLLWLQTIND 847
Cdd:PRK06178  230 TQR---DMVYTAAAAYavavVGGEDSVFLSFLPEFwiagENFGLLFPLF----SGATLVLLA-----RwDAVAFMAAVER 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  848 YHGTHSAGP-NFAFELvirrLEAEKNKVYDLSSMVFLMiAAEPVRQKTV---RRFIELTQpfglseGVLAPG-YGLAEN- 921
Cdd:PRK06178  298 YRVTRTVMLvDNAVEL----MDHPRFAEYDLSSLRQVR-VVSFVKKLNPdyrQRWRALTG------SVLAEAaWGMTETh 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  922 -CVYVTCAFGE------CKPVFIdwqGRVCCGyveqddtdTLIRIVDPDSlTEHQEDGVEGEIWISSPSSGVGYWGNSEM 994
Cdd:PRK06178  367 tCDTFTAGFQDddfdllSQPVFV---GLPVPG--------TEFKICDFET-GELLPLGAEGEIVVRTPSLLKGYWNKPEA 434

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749  995 SQRTFFNqlknhpnkKFTRTGDLGrTID--GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEE 1071
Cdd:PRK06178  435 TAEALRD--------GWLHTGDIG-KIDeqGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLG---SAVVGRPDP 501
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 752-1147 2.13e-15

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 81.24  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  752 KPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHdmglIGGLFTAL--VSGGTSVLF 829
Cdd:cd05912    73 DVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFH----ISGLSILMrsVIYGMTVYL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  830 SPMIfirNPLLWLQTINDYHGTH-SAGPNfafelVIRRLEAEKNKVYDLSSMVFLM---IAAEPVRQKTVRRFIELTQPF 905
Cdd:cd05912   149 VDKF---DAEQVLHLINSGKVTIiSVVPT-----MLQRLLEILGEGYPNNLRCILLgggPAPKPLLEQCKEKGIPVYQSY 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  906 GLSEG-----VLAPGYGLAEncvyvTCAFGecKPVFidwqgrvccgyveqddtDTLIRIVDPDsltehQEDGVEGEIWIS 980
Cdd:cd05912   221 GMTETcsqivTLSPEDALNK-----IGSAG--KPLF-----------------PVELKIEDDG-----QPPYEVGEILLK 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  981 SPSSGVGYWGNSEMSQRTFFNqlknhpnkKFTRTGDLGRtID--GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVL 1058
Cdd:cd05912   272 GPNVTKGYLNRPDATEESFEN--------GWFKTGDIGY-LDeeGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIK 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1059 RpgcCAVVGIPEevlaqkgisipdssDQVGLVVIAEVREGKAVSKEVVNNIkarvVEEHgvaVASVKLikPRTIC----- 1133
Cdd:cd05912   343 E---AGVVGIPD--------------DKWGQVPVAFVVSERPISEEELIAY----CSEK---LAKYKV--PKKIYfvdel 396

                         410
                  ....*....|....*
gi 937914749 1134 -KTTSGKIRRFECMR 1147
Cdd:cd05912   397 pRTASGKLLRHELKQ 411
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 761-1075 2.73e-15

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 81.27  E-value: 2.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  761 LQFTSGSTGDAKGVMITHEG-LIHNVKTMKKRYRS--TSKTVLVSWLPQYHDMGLIGgLFTALVSGGTSVL---FSPMIF 834
Cdd:cd05929   130 MLYSGGTTGRPKGIKRGLPGgPPDNDTLMAAALGFgpGADSVYLSPAPLYHAAPFRW-SMTALFMGGTLVLmekFDPEEF 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 irnpllwLQTINDYHGTHSagpNFAFELVIRRL---EAEKNKvYDLSSM--VFLMIAAEPVRQKtvRRFIELTQPfglse 909
Cdd:cd05929   209 -------LRLIERYRVTFA---QFVPTMFVRLLklpEAVRNA-YDLSSLkrVIHAAAPCPPWVK--EQWIDWGGP----- 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  910 gVLAPGYGLAEnCVYVTCAFGEckpvfiDWQ------GRVCCGYVeqddtdtliRIVDPDSltEHQEDGVEGEIWISsPS 983
Cdd:cd05929   271 -IIWEYYGGTE-GQGLTIINGE------EWLthpgsvGRAVLGKV---------HILDEDG--NEVPPGEIGEVYFA-NG 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  984 SGVGYwgnsemsqrtffnqlKNHPNKK--------FTRTGDLGRT-IDGNLFITGRIKDLIIVAGRNIYSADVEKTVESS 1054
Cdd:cd05929   331 PGFEY---------------TNDPEKTaaarneggWSTLGDVGYLdEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAH 395

                         330       340
                  ....*....|....*....|.
gi 937914749 1055 SEVLRpgcCAVVGIPEEVLAQ 1075
Cdd:cd05929   396 PKVLD---AAVVGVPDEELGQ 413
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 101-173 3.19e-15

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 80.65  E-value: 3.19e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937914749  101 TRIGIVGAGPSGLSAAYALAKLGYRnVTLFEKCHTVSGMCESIDIEGRIYDLGGQVIAANSaPVITHLAEELG 173
Cdd:COG1232     2 KRVAVIGGGIAGLTAAYRLAKAGHE-VTVLEASDRVGGLIRTVEVDGFRIDRGPHSFLTRD-PEVLELLRELG 72
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 1492-1625 6.31e-15

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 80.95  E-value: 6.31e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1492 SIWSVDFvkW-----WALnkAQALAAKMLAVHLKGTIFLNYWFKMQGARIGSSVVIDTVDITDPSLLTVADGAVLAEGAL 1566
Cdd:TIGR02353  555 PLWSPFV--WlhelhWKL--YESVAVPNFLRPFRGTPFLPAILRLLGVKIGRGVYIDGTDLTERDLVTIGDDSTLNEGSV 630

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749  1567 VQGHEVCNEVLSFRPIWIGCEASIGPYAVLQKGTVVEDGAVVPPLQKTGAGKSTRRTSR 1625
Cdd:TIGR02353  631 IQTHLFEDRVMKSDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKGEEVPAHTR 689
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 2279-2489 7.94e-15

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 80.57  E-value: 7.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  2279 LWATLCQPLLQTLVPYSVLGLVIFLPLR--GLLAVAAATRFPLYWLLPAF-WAASGVAAMATCAAAKWALVGsRVDGDTV 2355
Cdd:TIGR02353  476 RLARKNVENLRIILPFLLVQWAMLFALVvlDLQALDDYTEWGAVALLAALiLMAVGVGAFLILVERKWLVFG-RLKPQEH 554

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  2356 HIWSPAVFL-DTVWQAVRAATAEYFAELTPGSAPFAAWMRVMGASVspGDGVYVDsmGALLnPE--MVRLERGAAVGRDA 2432
Cdd:TIGR02353  555 PLWSPFVWLhELHWKLYESVAVPNFLRPFRGTPFLPAILRLLGVKI--GRGVYID--GTDL-TErdLVTIGDDSTLNEGS 629

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 937914749  2433 LLFGHVYEGEAGKVKFgaVSVGEDGFVGSRAVAMPSVTVDDGGCLAALGLAMKGETV 2489
Cdd:TIGR02353  630 VIQTHLFEDRVMKSDT--VTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKGEEV 684
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 757-1076 1.35e-14

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 77.37  E-value: 1.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  757 DLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHdmglIGGLFTA---LVSGGTSVLFSpmi 833
Cdd:cd17630     1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYH----VGGLAILvrsLLAGAELVLLE--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  834 fiRNPLLwLQTINDYHGTHSAgpnfafeLV---IRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPfglseg 910
Cdd:cd17630    74 --RNQAL-AEDLAPPGVTHVS-------LVptqLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIP------ 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  911 vLAPGYGLAE--NCVYVTCAFGECKPVFidwqGRVCcGYVEqddtdtlIRIVDPdsltehqedgveGEIWISSPSSGVGY 988
Cdd:cd17630   138 -LYTTYGMTEtaSQVATKRPDGFGRGGV----GVLL-PGRE-------LRIVED------------GEIWVGGASLAMGY 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  989 WGNSEMSQRtffnqlknhPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVG 1067
Cdd:cd17630   193 LRGQLVPEF---------NEDGWFTTKDLGElHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRD---AFVVG 260


                  ....*....
gi 937914749 1068 IPEEVLAQK 1076
Cdd:cd17630   261 VPDEELGQR 269
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 593-1142 1.60e-14

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 79.46  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  593 WINEEGKlMNRRTYQELHGNASYIAQKLltsTKPVIKPGDRVLlIHLP-GLEFIDAFFGCIRAGVIPVPVLppdpmqSG- 670
Cdd:cd05968    82 WEGEDGT-SRTLTYGELLYEVKRLANGL---RALGVGKGDRVG-IYLPmIPEIVPAFLAVARIGGIVVPIF------SGf 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  671 --GQALLKVENiskmCNAVAILSTSSYhaaVRAGyikNIVTLAKRVQKCSAQWPDIPWI----HT---DSWIK-NYRRSS 740
Cdd:cd05968   151 gkEAAATRLQD----AEAKALITADGF---TRRG---REVNLKEEADKACAQCPTVEKVvvvrHLgndFTPAKgRDLSYD 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  741 DSFNSDTVLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLihNVKTMKKRYR--STSKTVLVSWLPqyhDMGLIGG--- 815
Cdd:cd05968   221 EEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGF--PLKAAQDMYFqfDLKPGDLLTWFT---DLGWMMGpwl 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  816 LFTALVSGGTSVLF--SPMiFIRNPLLWlQTINDYHGTH-SAGPNfafelVIRRLEA---EKNKVYDLSSMVFLMIAAEP 889
Cdd:cd05968   296 IFGGLILGATMVLYdgAPD-HPKADRLW-RMVEDHEITHlGLSPT-----LIRALKPrgdAPVNAHDLSSLRVLGSTGEP 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  890 VRQKTVRRFIELTqpfglsegvlapgygLAENCVYVTCAFGeckpvfIDWQGRVCCGYveqddtdtLIRIVDPDSL---- 965
Cdd:cd05968   369 WNPEPWNWLFETV---------------GKGRNPIINYSGG------TEISGGILGNV--------LIKPIKPSSFngpv 419

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  966 -----TEHQEDG-----VEGEIWISSPSSGV--GYWGNSEMSQRTFFNQLKNhpnkkFTRTGDLGRT-IDGNLFITGRIK 1032
Cdd:cd05968   420 pgmkaDVLDESGkparpEVGELVLLAPWPGMtrGFWRDEDRYLETYWSRFDN-----VWVHGDFAYYdEEGYFYILGRSD 494

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1033 DLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEVlaqKGISIpdssdqVGLVVIaevREGKAVSKEVVNNIKAR 1112
Cdd:cd05968   495 DTINVAGKRVGPAEIESVLNAHPAVLE---SAAIGVPHPV---KGEAI------VCFVVL---KPGVTPTEALAEELMER 559

                         570       580       590
                  ....*....|....*....|....*....|....*.
gi 937914749 1113 VVEEHGvavasvKLIKPRTIC------KTTSGKIRR 1142
Cdd:cd05968   560 VADELG------KPLSPERILfvkdlpKTRNAKVMR 589
PRK05857 PRK05857
fatty acid--CoA ligase;
606-1142 2.16e-14

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 78.90  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  606 YQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPV---LPPdpmqsggqalLKVENISK 682
Cdd:PRK05857   44 YRELVAEVGGLAADLRAQS---VSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAdgnLPI----------AAIERFCQ 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  683 MCNAVAILstssyhaavragyiknivtLAKRVQKCSAQWPDIPWIHTDSWIKNYRRSSDSFNSDTVLFTKPQPS----DL 758
Cdd:PRK05857  111 ITDPAAAL-------------------VAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADqgseDP 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  759 CFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRS----TSKTVLVSWLPQYHdmglIGGLF---TALVSGGTSVLFSp 831
Cdd:PRK05857  172 LAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEGLNwvtwVVGETTYSPLPATH----IGGLWwilTCLMHGGLCVTGG- 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  832 mifiRNPLLWLQTINDyhgtHSAGPNFAFELVIRRLEAE-KNKVYDLSSMVFLMIAAEPVRQKTVRrFIELTqpfglseG 910
Cdd:PRK05857  247 ----ENTTSLLEILTT----NAVATTCLVPTLLSKLVSElKSANATVPSLRLVGYGGSRAIAADVR-FIEAT-------G 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  911 V-LAPGYGLAEncvyvTCAFGECKPVFIDWQGRVCCGYVEQDDTDTLIRIVDPDSLTEHQEDGVE----GEIWISSPSSG 985
Cdd:PRK05857  311 VrTAQVYGLSE-----TGCTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGPsasfGTLWIKSPANM 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  986 VGYWGNSEMSQRTFFNQLKNhpnkkftrTGDL-GRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRPGCca 1064
Cdd:PRK05857  386 LGYWNNPERTAEVLIDGWVN--------TGDLlERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAAC-- 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1065 vvgipeevlaqkgISIPDS--SDQVGLVVIAEVREGKAVSKEVVNNIKARVVEEHGVAVASVKLIKPRTICKTTSGKIRR 1142
Cdd:PRK05857  456 -------------YEIPDEefGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMR 522
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 755-1070 2.74e-14

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 78.39  E-value: 2.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHdmglIGGL----FTALVSGGTsvlfs 830
Cdd:PRK06145  148 PTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYH----VGAFdlpgIAVLWVGGT----- 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  831 pMIFIRN--PLLWLQTINDYHGThsaGPNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELtqpfgLS 908
Cdd:PRK06145  219 -LRIHREfdPEAVLAAIERHRLT---CAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRV-----FT 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  909 EGVLAPGYGLAENCVYVTCAFGECKPVFIDWQGRVCcGYVEqddtdtlIRIVDPDSLTehQEDGVEGEIWISSPSSGVGY 988
Cdd:PRK06145  290 RARYIDAYGLTETCSGDTLMEAGREIEKIGSTGRAL-AHVE-------IRIADGAGRW--LPPNMKGEICMRGPKVTKGY 359

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  989 WGNSEMSQRTFFNQlknhpnkkFTRTGDLGRTID-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVG 1067
Cdd:PRK06145  360 WKDPEKTAEAFYGD--------WFRSGDVGYLDEeGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAE---AAVIG 428


                  ...
gi 937914749 1068 IPE 1070
Cdd:PRK06145  429 VHD 431
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
603-1031 4.69e-14

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 77.63  E-value: 4.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTKPVIKPgdrvlLIHLPGLEF--IDAFFGCIRAG--VIPVPV-LPPDpmqsggqALLKV 677
Cdd:PRK04813   27 KLTYGQLKEDSDALAAFIDSLKLPDKSP-----IIVFGHMSPemLATFLGAVKAGhaYIPVDVsSPAE-------RIEMI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  678 ENISKmcnAVAILSTSSyhAAVRAGYIKnIVTLAKrVQKCSAQWPDIPwihTDSWIKNyrrsSDSFnsdtvlftkpqpsd 757
Cdd:PRK04813   95 IEVAK---PSLIIATEE--LPLEILGIP-VITLDE-LKDIFATGNPYD---FDHAVKG----DDNY-------------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  758 lcFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGgLFTALVSGGTSVLFSPMIfIRN 837
Cdd:PRK04813  147 --YIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMD-LYPTLASGGTLVALPKDM-TAN 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  838 PLLWLQTINDYH-GTHSAGPNFA-FELVIRRLEAEKnkvydLSSMVFLMIAAE--PVR--QKTVRRFieltqPfglsEGV 911
Cdd:PRK04813  223 FKQLFETLPQLPiNVWVSTPSFAdMCLLDPSFNEEH-----LPNLTHFLFCGEelPHKtaKKLLERF-----P----SAT 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  912 LAPGYGLAENCVYVTCAfgECKPVFIDWQGRVCCGYVeQDDTDTLIrivdPDSLTEHQEDGVEGEIWISSPSSGVGYWGN 991
Cdd:PRK04813  289 IYNTYGPTEATVAVTSI--EITDEMLDQYKRLPIGYA-KPDSPLLI----IDEEGTKLPDGEQGEIVISGPSVSKGYLNN 361

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 937914749  992 SEMSQRTFFnQLKNHPnkkFTRTGDLGRTIDGNLFITGRI 1031
Cdd:PRK04813  362 PEKTAEAFF-TFDGQP---AYHTGDAGYLEDGLLFYQGRI 397
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 603-1071 6.54e-14

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: 77.16  E-value: 6.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPdpmqsggqalLKVENIS- 681
Cdd:cd05923    28 RLTYSELRARIEAVAARLHARG---LRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR----------LKAAELAe 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  682 -----KMCNAVAilstssyhaAVRAGYIKNIVTLAKRVQKCSAQwPDIpwihtdswiknyrRSSDSFnSDTVLFTKPQPS 756
Cdd:cd05923    95 liergEMTAAVI---------AVDAQVMDAIFQSGVRVLALSDL-VGL-------------GEPESA-GPLIEDPPREPE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  757 DLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKR--YRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVL---FSP 831
Cdd:cd05923   151 QPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQagLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVveeFDP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  832 MifirNPLLWLQT--INDYHG--THsagpnfaFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFI--ELTQPF 905
Cdd:cd05923   231 A----DALKLIEQerVTSLFAtpTH-------LDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLpgEKVNIY 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  906 GLSE-------------GVLAPGYglaencvyvtcaFGECKPVFIDwqgrvccgyveqddtdtlirivdpDSLTEHQEDG 972
Cdd:cd05923   300 GTTEamnslymrdartgTEMRPGF------------FSEVRIVRIG------------------------GSPDEALANG 343

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  973 VEGEIWISSPSSG--VGYWGNSEMSqrtffnqLKNHPNKKFtRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEK 1049
Cdd:cd05923   344 EEGELIVAAAADAafTGYLNQPEAT-------AKKLQDGWY-RTGDVGYvDPSGDVRILGRVDDMIISGGENIHPSEIER 415

                         490       500
                  ....*....|....*....|..
gi 937914749 1050 TVESSSEVLRpgcCAVVGIPEE 1071
Cdd:cd05923   416 VLSRHPGVTE---VVVIGVADE 434
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 758-1152 8.24e-14

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 77.36  E-value: 8.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  758 LCFLqFTSGSTGDAKGVMITHEGliHNVK---TMKKRYRSTSKTVLvsWLPQyhDMGLIGG----LFTALVSGGTSVLF- 829
Cdd:cd05967   233 LYIL-YTSGTTGKPKGVVRDNGG--HAVAlnwSMRNIYGIKPGDVW--WAAS--DVGWVVGhsyiVYGPLLHGATTVLYe 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  830 -----SPmifirNPLLWLQTINDYHGTH--SAgPNfAFElVIRR--LEAEKNKVYDLSSMVFLMIAAEPVRQKTVRrFIE 900
Cdd:cd05967   306 gkpvgTP-----DPGAFWRVIEKYQVNAlfTA-PT-AIR-AIRKedPDGKYIKKYDLSSLRTLFLAGERLDPPTLE-WAE 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  901 LTqpfgLSEGVL------APGYGLAENCVYVtcafgECKPVFIDWQGRVCCGYVeqddtdtlIRIVDPDSltEHQEDGVE 974
Cdd:cd05967   377 NT----LGVPVIdhwwqtETGWPITANPVGL-----EPLPIKAGSPGKPVPGYQ--------VQVLDEDG--EPVGPNEL 437

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  975 GEIWIS---SPSSGVGYWGNSEMSQRTFFNQLKNhpnkkFTRTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKT 1050
Cdd:cd05967   438 GNIVIKlplPPGCLLTLWKNDERFKKLYLSKFPG-----YYDTGDAGyKDEDGYLFIMGRTDDVINVAGHRLSTGEMEES 512

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1051 VESSSEVLRpgcCAVVGIPEEVlaqKGiSIPdssdqVGLVVIAEvrEGKAVSKEVVNNIKARVVEEHGvAVASVKL-IKP 1129
Cdd:cd05967   513 VLSHPAVAE---CAVVGVRDEL---KG-QVP-----LGLVVLKE--GVKITAEELEKELVALVREQIG-PVAAFRLvIFV 577

                         410       420
                  ....*....|....*....|...
gi 937914749 1130 RTICKTTSGKIRRfECMRQFVDN 1152
Cdd:cd05967   578 KRLPKTRSGKILR-RTLRKIADG 599
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 764-1142 1.62e-13

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. 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: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 74.23  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  764 TSGSTGDAKGVMITHEGLIH-NVKTMKKrYRSTSKTVLVSWLPQYHDMGLiGGLFTALVSGGTSVLFSPMifirNPLLWL 842
Cdd:cd17637     8 TAAVAGRPRGAVLSHGNLIAaNLQLIHA-MGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKF----DPAEAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  843 QTINDYHGTHSagpnFAFELVIRRL--EAEKNKVyDLSSM--VFLMIAAEpvrqkTVRRFIELTQpfglseGVLAPGYGL 918
Cdd:cd17637    82 ELIEEEKVTLM----GSFPPILSNLldAAEKSGV-DLSSLrhVLGLDAPE-----TIQRFEETTG------ATFWSLYGQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  919 AENCVYVTCAFGECKPvfidwqgrvccGYVEQDDTDTLIRIVDPDSltEHQEDGVEGEIWISSPSSGVGYWGNSEMSQRT 998
Cdd:cd17637   146 TETSGLVTLSPYRERP-----------GSAGRPGPLVRVRIVDDND--RPVPAGETGEIVVRGPLVFQGYWNLPELTAYT 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  999 FFNqlknhpnkKFTRTGDLGR-TIDGNLFITGRI--KDLIIVAGRNIYSADVEKTVESssevlRPGCCAVVgipeeVlaq 1075
Cdd:cd17637   213 FRN--------GWHHTGDLGRfDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILE-----HPAIAEVC-----V--- 271

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 937914749 1076 kgISIPDSSDQVGLVVIAEVREGKAV-SKEVVNNIKARvveehgvaVASVKliKPR------TICKTTSGKIRR 1142
Cdd:cd17637   272 --IGVPDPKWGEGIKAVCVLKPGATLtADELIEFVGSR--------IARYK--KPRyvvfveALPKTADGSIDR 333
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 959-1142 1.73e-13

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 76.06  E-value: 1.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  959 IVDPDslTEHQEDGVEGEIWISSPSSGV--GYWGNSEMSQRTFFnqlKNHPNKKFTrtGDlG--RTIDGNLFITGRIKDL 1034
Cdd:cd05966   423 ILDEE--GNEVEGEVEGYLVIKRPWPGMarTIYGDHERYEDTYF---SKFPGYYFT--GD-GarRDEDGYYWITGRVDDV 494

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1035 IIVAGRNIYSADVEktvesSSEVLRPGC--CAVVGIPEEVlaqKGISIpdssdqVGLVViaeVREGKAVSKEVVNNIKAR 1112
Cdd:cd05966   495 INVSGHRLGTAEVE-----SALVAHPAVaeAAVVGRPHDI---KGEAI------YAFVT---LKDGEEPSDELRKELRKH 557

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 937914749 1113 VVEEHGvAVASVKLIK-----PrticKTTSGKI-RR 1142
Cdd:cd05966   558 VRKEIG-PIATPDKIQfvpglP----KTRSGKImRR 588
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 1502-1863 2.12e-13

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 75.94  E-value: 2.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1502 WALNKAQAL--AAKMLAVHLKGTIFLNYWFKMQGARIGSSVVIDTVDITDPSLLTVADGAVLAEGALVQGHEVCNEVLSF 1579
Cdd:TIGR02353  320 YQAWTVQQLmdNSRVLLFPLYASSYIPHWYRALGAKIGKVAEISSAQHEVPDLTDIGEETFIADGLLMGNARLSGGWFRL 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1580 RPIWIGCEASIGPYAVLQKGTVVEDGAVVPPLQKTGA-GKSTRRTS-----------RTSVSIKKEAAK---------AN 1638
Cdd:TIGR02353  400 GRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKdGKVREGVGwlgsppfelprRVNRDDELEALTfepdprrrlAR 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1639 MILEHLVSIyavgiLGALSGAIVYTLYTHLSGKAASPLHFSFACIagafhWLPAAITAYAVIVqetptsaLSFALFTAFA 1718
Cdd:TIGR02353  480 KNVENLRII-----LPFLLVQWAMLFALVVLDLQALDDYTEWGAV-----ALLAALILMAVGV-------GAFLILVERK 542

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1719 DLSYGVILSILTSITSRALaakpgtkqngiasLIHRRIT----ISAHVRFAKMLSGTEAFCVYLRLLGAKIGRHCSIRAI 1794
Cdd:TIGR02353  543 WLVFGRLKPQEHPLWSPFV-------------WLHELHWklyeSVAVPNFLRPFRGTPFLPAILRLLGVKIGRGVYIDGT 609

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749  1795 NpVANPELISVGDGVHLGDFCNIVPGFYSKGGFTSAEIKVQENTVVGSGSLLLPGCVLQENVILGALSV 1863
Cdd:TIGR02353  610 D-LTERDLVTIGDDSTLNEGSVIQTHLFEDRVMKSDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSL 677
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 755-1071 2.57e-13

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 75.41  E-value: 2.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHdmglIGGLFTA--LVSGGTSVL---F 829
Cdd:PRK06188  167 PPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSH----AGGAFFLptLLRGGTVIVlakF 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  830 SPMIFIRnpllwlqTINDYhgthsaGPNFAF---ELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPfg 906
Cdd:PRK06188  243 DPAEVLR-------AIEEQ------RITATFlvpTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGP-- 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  907 lsegVLAPGYGLAEnCVYVTCAFGECKPVFIDWQGRVCCGYVEQDDTdtlIRIVDPDSLTEHQedGVEGEIWISSPSSGV 986
Cdd:PRK06188  308 ----IFAQYYGQTE-APMVITYLRKRDHDPDDPKRLTSCGRPTPGLR---VALLDEDGREVAQ--GEVGEICVRGPLVMD 377

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  987 GYWGNSEMSQRTFFNqlknhpnkKFTRTGDLGRT-IDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVlrpGCCAV 1065
Cdd:PRK06188  378 GYWNRPEETAEAFRD--------GWLHTGDVAREdEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAV---AQVAV 446


                  ....*.
gi 937914749 1066 VGIPEE 1071
Cdd:PRK06188  447 IGVPDE 452
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 748-1076 2.63e-13

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. 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: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 74.78  E-value: 2.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  748 VLFTkpQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGlIGGLFTALVSGGTSV 827
Cdd:cd17644   100 VLLT--QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVA-AEEIYVTLLSGATLV 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  828 LfSPMIFIRNPLLWLQTINDYHGT-HSAGPNFAFELVirrLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFg 906
Cdd:cd17644   177 L-RPEEMRSSLEDFVQYIQQWQLTvLSLPPAYWHLLV---LELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNF- 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  907 lseGVLAPGYGLAENCVYVTCafgeCKPVFIDWQG--RVCCGyveQDDTDTLIRIVDPDSLTehQEDGVEGEIWISSPSS 984
Cdd:cd17644   252 ---IQLINVYGPTEATIAATV----CRLTQLTERNitSVPIG---RPIANTQVYILDENLQP--VPVGVPGELHIGGVGL 319

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  985 GVGYWGNSEMSQRTFFNQLKNH-PNKKFTRTGDLGRTI-DGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgc 1062
Cdd:cd17644   320 ARGYLNRPELTAEKFISHPFNSsESERLYKTGDLARYLpDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKT--- 396

                         330
                  ....*....|....
gi 937914749 1063 cAVVGIPEEVLAQK 1076
Cdd:cd17644   397 -AVVIVREDQPGNK 409
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 605-1048 5.32e-13

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: 73.88  E-value: 5.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPmqsggqallkveniskmc 684
Cdd:cd17643    14 TYGELDARANRLARTLRAEG---VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYP------------------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 navailstssyhaavragyiknivtlAKRVQkcsaqwpdipWIHTDSWIKnyrrssdsfnsdtVLFTkpQPSDLCFLQFT 764
Cdd:cd17643    73 --------------------------VERIA----------FILADSGPS-------------LLLT--DPDDLAYVIYT 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  765 SGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVlvsWLpQYHDMGL---IGGLFTALVSGGTSVLFSPMIfIRNPLLW 841
Cdd:cd17643   102 SGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDV---WT-LFHSYAFdfsVWEIWGALLHGGRLVVVPYEV-ARSPEDF 176

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  842 LQTINDYHGT-HSAGPNfAFELVIRRLEAEKNKVYDLSSMVFlmiAAEPVRQKTVRRFIeltQPFGLSEGVLAPGYGLAE 920
Cdd:cd17643   177 ARLLRDEGVTvLNQTPS-AFYQLVEAADRDGRDPLALRYVIF---GGEALEAAMLRPWA---GRFGLDRPQLVNMYGITE 249

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  921 NCVYVTcaFGECKPVFIDWQGRVCCGyveQDDTDTLIRIVDPDSLTehQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFF 1000
Cdd:cd17643   250 TTVHVT--FRPLDAADLPAAAASPIG---RPLPGLRVYVLDADGRP--VPPGVVGELYVSGAGVARGYLGRPELTAERFV 322

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 937914749 1001 NQLKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVE 1048
Cdd:cd17643   323 ANPFGGPGSRMYRTGDLARrLPDGELEYLGRADEQVKIRGFRIELGEIE 371
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 757-1155 5.77e-13

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 74.11  E-value: 5.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  757 DLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKK----RYR-STSKTVLVSWLPQYHDMGLigGLF-TALVSGGTSVLF- 829
Cdd:PLN02574  199 DVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfeasQYEyPGSDNVYLAALPMFHIYGL--SLFvVGLLSLGSTIVVm 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  830 -----SPMIfirnpllwlQTINDYHGTHsagpnfaFELVIRRLEAEKNKVYDLSSMVF-----LMIAAEPVRQKTVRRFI 899
Cdd:PLN02574  277 rrfdaSDMV---------KVIDRFKVTH-------FPVVPPILMALTKKAKGVCGEVLkslkqVSCGAAPLSGKFIQDFV 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  900 ELtqpfgLSEGVLAPGYGLAENCVYVTCAFGECKpvfidWQGRVCCGYVEqddTDTLIRIVDPDSlTEHQEDGVEGEIWI 979
Cdd:PLN02574  341 QT-----LPHVDFIQGYGMTESTAVGTRGFNTEK-----LSKYSSVGLLA---PNMQAKVVDWST-GCLLPPGNCGELWI 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  980 SSPSSGVGYWGNSEMSQRTFFNQlknhpnkKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVL 1058
Cdd:PLN02574  407 QGPGVMKGYLNNPKATQSTIDKD-------GWLRTGDIAYfDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEII 479

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1059 RpgcCAVVGIPEEVLAQkgisIPdssdqVGLVViaeVREGKAVSKE-VVNNIKARVVEEHGVAvasvKLIKPRTICKTTS 1137
Cdd:PLN02574  480 D---AAVTAVPDKECGE----IP-----VAFVV---RRQGSTLSQEaVINYVAKQVAPYKKVR----KVVFVQSIPKSPA 540

                         410
                  ....*....|....*...
gi 937914749 1138 GKIRRFECMRQFVDNTLS 1155
Cdd:PLN02574  541 GKILRRELKRSLTNSVSS 558
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
 754-1051 6.62e-13

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) 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. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It 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. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 74.32  E-value: 6.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  754 QPSDLCFLQFTSGSTGDAKGVMITHEGL----IHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTsVLF 829
Cdd:cd05933   148 KPNQCCTLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQ-VYF 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  830 S-----------------PMIFIRNPLLW-----------------------------LQTINDYHGTHSAGPNF---AF 860
Cdd:cd05933   227 AqpdalkgtlvktlrevrPTAFMGVPRVWekiqekmkavgaksgtlkrkiaswakgvgLETNLKLMGGESPSPLFyrlAK 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  861 ELVIRRLEAEknkvYDLSSMVFLMIAAEPVRQKTVRRFIELTQPfglsegvLAPGYGLAEN------CVYVTCAFGECkp 934
Cdd:cd05933   307 KLVFKKVRKA----LGLDRCQKFFTGAAPISRETLEFFLSLNIP-------IMELYGMSETsgphtiSNPQAYRLLSC-- 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  935 vfidwqGRVCCGyveqddtdTLIRIVDPDSltehqeDGVeGEIWISSPSSGVGYWGNSEMSQRTffnqLKNHpnkKFTRT 1014
Cdd:cd05933   374 ------GKALPG--------CKTKIHNPDA------DGI-GEICFWGRHVFMGYLNMEDKTEEA----IDED---GWLHS 425

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 937914749 1015 GDLGRT-IDGNLFITGRIKDLIIVA-GRNIYSADVEKTV 1051
Cdd:cd05933   426 GDLGKLdEDGFLYITGRIKELIITAgGENVPPVPIEDAV 464
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 603-1048 8.63e-13

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. 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: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 73.53  E-value: 8.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPMQsggqallKVENISK 682
Cdd:cd17651    20 RLTYAELDRRANRLAHRLRARG---VGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE-------RLAFMLA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  683 MCNAVAILSTSsyHAAVRAGYIKNIVTLAKRvqkcsAQWPDIPwihtdswiknyrrssdsfnsDTVLFTKPQPSDLCFLQ 762
Cdd:cd17651    90 DAGPVLVLTHP--ALAGELAVELVAVTLLDQ-----PGAAAGA--------------------DAEPDPALDADDLAYVI 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  763 FTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLiGGLFTALVSGGTSVLFSPMifIRNP---- 838
Cdd:cd17651   143 YTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSV-QEIFSTLCAGATLVLPPEE--VRTDppal 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  839 LLWLQTindyHG-THSAGPNFAFELVirrLEAEKNKVYDLSSMVFLMIAAEPVR-QKTVRRFIElTQPFGLsegvLAPGY 916
Cdd:cd17651   220 AAWLDE----QRiSRVFLPTVALRAL---AEHGRPLGVRLAALRYLLTGGEQLVlTEDLREFCA-GLPGLR----LHNHY 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  917 GLAENCVyVTC--------AFGECKPVfidwqGRVCCGyveqddtdTLIRIVDpdsltEHQE---DGVEGEIWISSPSSG 985
Cdd:cd17651   288 GPTETHV-VTAlslpgdpaAWPAPPPI-----GRPIDN--------TRVYVLD-----AALRpvpPGVPGELYIGGAGLA 348

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937914749  986 VGYWGNSEMSQRTF----FNqlknhPNKKFTRTGDLGRTI-DGNLFITGRIKDLIIVAGRNIYSADVE 1048
Cdd:cd17651   349 RGYLNRPELTAERFvpdpFV-----PGARMYRTGDLARWLpDGELEFLGRADDQVKIRGFRIELGEIE 411
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 749-1142 1.21e-12

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 72.53  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  749 LFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMK--------KRYRSTSKTVLVSwlpqyhdmGLIGGLFTAL 820
Cdd:cd05969    82 LYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKyvldlhpdDIYWCTADPGWVT--------GTVYGIWAPW 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  821 VSGGTSVLFSPMIfirNPLLWLQTINDYHGT--HSAGPNFAfelVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRF 898
Cdd:cd05969   154 LNGVTNVVYEGRF---DAESWYGIIERVKVTvwYTAPTAIR---MLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWG 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  899 IELtqpFGLSegvLAPGYGLAENCVYVTCAFgECKPVFIDWQGRVCCGYVEQddtdtlirIVDPDSltEHQEDGVEGEIW 978
Cdd:cd05969   228 MEV---FGVP---IHDTWWQTETGSIMIANY-PCMPIKPGSMGKPLPGVKAA--------VVDENG--NELPPGTKGILA 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  979 ISS--PSSGVGYWGNSEMSQRTFfnqlknhPNKKFTrTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSS 1055
Cdd:cd05969   291 LKPgwPSMFRGIWNDEERYKNSF-------IDGWYL-TGDLAyRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHP 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1056 EVLRPGccaVVGIPEEVLaqkgisipdssdqvGLVVIAEV--REGKAVSKEVVNNIKARVVEEHGVAVAsvklikPRTI- 1132
Cdd:cd05969   363 AVAEAG---VIGKPDPLR--------------GEIIKAFIslKEGFEPSDELKEEIINFVRQKLGAHVA------PREIe 419

                         410
                  ....*....|....*
gi 937914749 1133 -----CKTTSGKIRR 1142
Cdd:cd05969   420 fvdnlPKTRSGKIMR 434
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 603-1068 1.58e-12

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: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 72.49  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPMQSGGQALLKVEnisk 682
Cdd:cd05910     2 RLSFRELDERSDRIAQGLTAYG---IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAE---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  683 mcnavailstssyhaavragyiknivtlakrvqkcsaqwPDipwihtdswiknyrrssdsfnsdtVLFTKPQPSDLCFLQ 762
Cdd:cd05910    75 ---------------------------------------PD------------------------AFIGIPKADEPAAIL 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  763 FTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYhdmgligGLFTALVsGGTSVLfSPMIFIR----NP 838
Cdd:cd05910    92 FTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGPAL-GLTSVI-PDMDPTRparaDP 162

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  839 LLWLQTINDYHGTHSAGPNFAFELVIRRLEAEKNKvydLSSMVFLMIAAEPVRQKTVRRFIELtqpfgLSEG--VLAPgY 916
Cdd:cd05910   163 QKLVGAIRQYGVSIVFGSPALLERVARYCAQHGIT---LPSLRRVLSAGAPVPIALAARLRKM-----LSDEaeILTP-Y 233

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  917 GLAEnCVYVTC-----AFGECKPVFIDWQGrVCCGYVEQDDTDTLIRIVDPD----SLTEHQEDGVEGEIWISSPSSGVG 987
Cdd:cd05910   234 GATE-ALPVSSigsreLLATTTAATSGGAG-TCVGRPIPGVRVRIIEIDDEPiaewDDTLELPRGEIGEITVTGPTVTPT 311

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  988 YWGNSemsQRTFFNQLKNHPNKKFTRTGDLGRTID-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVV 1066
Cdd:cd05910   312 YVNRP---VATALAKIDDNSEGFWHRMGDLGYLDDeGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRR---SALV 385


                  ..
gi 937914749 1067 GI 1068
Cdd:cd05910   386 GV 387
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 605-1113 2.65e-12

insect luciferase, similar to plant 4-coumarate: CoA ligases; 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: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 72.17  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLltsTKPVIKPGDRVLLIHLPGLEFIDAFFGC--IRAGVIPVPVLPPDpmqsggQALLKVENISK 682
Cdd:cd17642    46 SYAEYLEMSVRLAEAL---KKYGLKQNDRIAVCSENSLQFFLPVIAGlfIGVGVAPTNDIYNE------RELDHSLNISK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  683 ----MCNAVAILSTSSYHAAVRagYIKNIVTLAKRVQKCSAQwPDIPWI--HTDSWIKNYRRSSDSFNSDTvlftkpqps 756
Cdd:cd17642   117 ptivFCSKKGLQKVLNVQKKLK--IIKTIIILDSKEDYKGYQ-CLYTFItqNLPPGFNEYDFKPPSFDRDE--------- 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  757 DLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKR---YRSTSKTVLVSWLPQYHDMGLIGGLFTALVsgGTSVLFSPMI 833
Cdd:cd17642   185 QVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPifgNQIIPDTAILTVIPFHHGFGMFTTLGYLIC--GFRVVLMYKF 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  834 firNPLLWLQTINDYHGTHS--AGPNFAF----ELVirrleaekNKvYDLSSMVFLMIAAEPVRQKT---VRRFIELtqP 904
Cdd:cd17642   263 ---EEELFLRSLQDYKVQSAllVPTLFAFfaksTLV--------DK-YDLSNLHEIASGGAPLSKEVgeaVAKRFKL--P 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  905 FglsegvLAPGYGLAEN--CVYVTCAfGECKPVFIdwqGRVCCGYVeqddtdtlIRIVDPD---SLTEHQedgvEGEIWI 979
Cdd:cd17642   329 G------IRQGYGLTETtsAILITPE-GDDKPGAV---GKVVPFFY--------AKVVDLDtgkTLGPNE----RGELCV 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  980 SSPSSGVGYWGNSEMSQrTFFNQlknhpnKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVL 1058
Cdd:cd17642   387 KGPMIMKGYVNNPEATK-ALIDK------DGWLHSGDIAYyDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIF 459

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749 1059 RPGccaVVGIPEevlaqkgisiPDSSDQVGLVVIAEvrEGKAVS-KEVVNNIKARV 1113
Cdd:cd17642   460 DAG---VAGIPD----------EDAGELPAAVVVLE--AGKTMTeKEVMDYVASQV 500
PRK13382 PRK13382
bile acid CoA ligase;
753-1076 2.85e-12

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 72.10  E-value: 2.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  753 PQPSDLCFLqfTSGSTGDAKGVMITHEGLIHNVKTMKKR--YRSTSKTVLVSwlPQYHDMGLIGGLFTALVSggtsvlfS 830
Cdd:PRK13382  195 GRKGRVILL--TSGTTGTPKGARRSGPGGIGTLKAILDRtpWRAEEPTVIVA--PMFHAWGFSQLVLAASLA-------C 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  831 PMIFIR--NPLLWLQTINDYHGTHSAGPNFAFELvIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIEltqPFGls 908
Cdd:PRK13382  264 TIVTRRrfDPEATLDLIDRHRATGLAVVPVMFDR-IMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMD---QFG-- 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  909 eGVLAPGYGLAENCVYVTCAFGECKPVfIDWQGRVCCGyveqddtdTLIRIVDPDslteHQE--DGVEGEIWISSPSSGV 986
Cdd:PRK13382  338 -DVIYNNYNATEAGMIATATPADLRAA-PDTAGRPAEG--------TEIRILDQD----FREvpTGEVGTIFVRNDTQFD 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  987 GYwgnSEMSQRTFfnqlknhpNKKFTRTGDLGRTID-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAV 1065
Cdd:PRK13382  404 GY---TSGSTKDF--------HDGFMASGDVGYLDEnGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAE---AAV 469

                         330
                  ....*....|.
gi 937914749 1066 VGIPEEVLAQK 1076
Cdd:PRK13382  470 IGVDDEQYGQR 480
PRK09274 PRK09274
peptide synthase; Provisional
 603-1107 3.78e-12

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 71.47  E-value: 3.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVlppDPmqsGgqalLKVENIsK 682
Cdd:PRK09274   41 ELSFAELDARSDAIAHGLNAAG---IGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV---DP---G----MGIKNL-K 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  683 MCnavaiLSTSSYHAAV---RAgyiknivTLAKRVQKcsaqWPDiPWIHTdsWIKNYRR------SSDSFNSDTVL---- 749
Cdd:PRK09274  107 QC-----LAEAQPDAFIgipKA-------HLARRLFG----WGK-PSVRR--LVTVGGRllwggtTLATLLRDGAAapfp 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  750 FTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLvswLPQYHDMGLIGglfTALvsGGTSVLf 829
Cdd:PRK09274  168 MADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEID---LPTFPLFALFG---PAL--GMTSVI- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  830 SPMIFIR----NPLLWLQTINDYHGTHSAGpNFAfelVIRRL-EAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELtqp 904
Cdd:PRK09274  239 PDMDPTRpatvDPAKLFAAIERYGVTNLFG-SPA---LLERLgRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAM--- 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  905 fgLSEG--VLAPgYGlaencvyVTcafgECKPV---------FIDWQ-----GRVCCGYVEQDDTDTLIRIVDpDSLTEH 968
Cdd:PRK09274  312 --LPPDaeILTP-YG-------AT----EALPIssiesreilFATRAatdngAGICVGRPVDGVEVRIIAISD-APIPEW 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  969 QED-----GVEGEIWISSPSSGVGYWGNSEM--------SQRTFFnqlknHpnkkftRTGDLGRtID--GNLFITGRIKD 1033
Cdd:PRK09274  377 DDAlrlatGEIGEIVVAGPMVTRSYYNRPEAtrlakipdGQGDVW-----H------RMGDLGY-LDaqGRLWFCGRKAH 444

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 937914749 1034 LIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEevlaqKGISIPdssdqvglVVIAEVREGKAVSKEVVN 1107
Cdd:PRK09274  445 RVETAGGTLYTIPCERIFNTHPGVKR---SALVGVGV-----PGAQRP--------VLCVELEPGVACSKSALY 502
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 754-1048 3.86e-12

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 71.13  E-value: 3.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  754 QPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKT-VLvswlpQYHDMGLIGG---LFTALVSGGTSVLF 829
Cdd:cd17652    91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSrVL-----QFASPSFDASvweLLMALLAGATLVLA 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  830 SPMIFIRNPLLwLQTINDYHGTHSAGPNFAfelvIRRLEAEknkvyDLSSMVFLMIAAEPVRQKTVRRFieltqpfglse 909
Cdd:cd17652   166 PAEELLPGEPL-ADLLREHRITHVTLPPAA----LAALPPD-----DLPDLRTLVVAGEACPAELVDRW----------- 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  910 gvlAPG------YGLAENCVYVTCAfgECK------PVFIDWQGRVCcgYVeqddTDTLIRIVDPdsltehqedGVEGEI 977
Cdd:cd17652   225 ---APGrrminaYGPTETTVCATMA--GPLpgggvpPIGRPVPGTRV--YV----LDARLRPVPP---------GVPGEL 284

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937914749  978 WISSPSSGVGYWGNSEMSQRTFFNQLKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVE 1048
Cdd:cd17652   285 YIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARwRADGQLEFLGRADDQVKIRGFRIELGEVE 356
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 603-1071 4.00e-12

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 71.27  E-value: 4.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPV---LPPDPM-----QSGGQAL 674
Cdd:PRK12406   11 RRSFDELAQRAARAAGGLAALG---VRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVnwhFKPEEIayileDSGARVL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  675 LKVENI-----SKMCNAVAILSTSSyHAAVRAGYiknivtlakRVQKCSAQWP--DIPWihtDSWIKNYRRSSDSfnsdt 747
Cdd:PRK12406   88 IAHADLlhglaSALPAGVTVLSVPT-PPEIAAAY---------RISPALLTPPagAIDW---EGWLAQQEPYDGP----- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  748 vlfTKPQPSDLCFlqfTSGSTGDAKGVM---ITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFtALVSGG 824
Cdd:PRK12406  150 ---PVPQPQSMIY---TSGTTGHPKGVRraaPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSAPNAYGLR-AGRLGG 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  825 TSVL---FSPMIFirnpllwLQTINDYHGTHSAGPNFAFelvIR--RLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFI 899
Cdd:PRK12406  223 VLVLqprFDPEEL-------LQLIERHRITHMHMVPTMF---IRllKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMI 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  900 ELTQPfglsegVLAPGYGLAENCVYVTCAFGEC--KPVFIdwqGRVCCGyveqddtdTLIRIVDPDSltEHQEDGVEGEI 977
Cdd:PRK12406  293 EWWGP------VIYEYYGSTESGAVTFATSEDAlsHPGTV---GKAAPG--------AELRFVDEDG--RPLPQGEIGEI 353

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  978 WISSPssgvgywgnsEMSQRTFfnqlKNHPNKK-------FTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEK 1049
Cdd:PRK12406  354 YSRIA----------GNPDFTY----HNKPEKRaeidrggFITSGDVGYlDADGYLFLCDRKRDMVISGGVNIYPAEIEA 419

                         490       500
                  ....*....|....*....|..
gi 937914749 1050 TVESSSEVlrpGCCAVVGIPEE 1071
Cdd:PRK12406  420 VLHAVPGV---HDCAVFGIPDA 438
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 605-1048 4.09e-12

Peptide Synthetase; 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: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 71.15  E-value: 4.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTkpvIKPGDRVLlIHLP-GLEFIDAFFGCIRAGVIPVPVLPPDPMQsggqallKVENISKM 683
Cdd:cd17646    25 TYRELDERANRLAHLLRARG---VGPEDRVA-VLLPrSADLVVALLAVLKAGAAYLPLDPGYPAD-------RLAYMLAD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  684 CNAVAILSTSSYHAAVRAGyiknivtlAKRVQKCSAQWPDIPwihtdswiknyrrssdsfnsDTVLFTKPQPSDLCFLQF 763
Cdd:cd17646    94 AGPAVVLTTADLAARLPAG--------GDVALLGDEALAAPP--------------------ATPPLVPPRPDNLAYVIY 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  764 TSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGlIGGLFTALVSGGTSVLFSPMIFiRNPLLWLQ 843
Cdd:cd17646   146 TSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVS-VWELFWPLVAGARLVVARPGGH-RDPAYLAA 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  844 TINDYHGThsagpnfAFELVIRRLEA--EKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTqpfglsEGVLAPGYGLAEN 921
Cdd:cd17646   224 LIREHGVT-------TCHFVPSMLRVflAEPAAGSCASLRRVFCSGEALPPELAARFLALP------GAELHNLYGPTEA 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  922 CVYVTcaFGECKPVfiDWQGRVCCGYveqDDTDTLIRIVDPDslTEHQEDGVEGEIWISSPSSGVGYWGNSEMSQRTF-- 999
Cdd:cd17646   291 AIDVT--HWPVRGP--AETPSVPIGR---PVPNTRLYVLDDA--LRPVPVGVPGELYLGGVQLARGYLGRPALTAERFvp 361

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 937914749 1000 --FNqlknhPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVE 1048
Cdd:cd17646   362 dpFG-----PGSRMYRTGDLARwRPDGALEFLGRSDDQVKIRGFRVEPGEIE 408
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 628-1104 2.05e-11

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 69.30  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  628 IKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPV---LPPDPM-----QSGGQALLkveniskmCNAvailSTSSYHAAV 699
Cdd:PRK07470   54 VRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTnfrQTPDEVaylaeASGARAMI--------CHA----DFPEHAAAV 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  700 RAG--YIKNIVTLAKrvqkcSAQWPDIPWI---HTDSWIKNYRRSSDsfnsdtvlftkpqpsDLCFLQFTSGSTGDAKGV 774
Cdd:PRK07470  122 RAAspDLTHVVAIGG-----ARAGLDYEALvarHLGARVANAAVDHD---------------DPCWFFFTSGTTGRPKAA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  775 MITHEGLI-----HNVKTMKKryrSTSKTVLVSWLPQYHDMGlIGGLfTALVSGGTSVL-----FSPmifirnPLLWlQT 844
Cdd:PRK07470  182 VLTHGQMAfvitnHLADLMPG---TTEQDASLVVAPLSHGAG-IHQL-CQVARGAATVLlpserFDP------AEVW-AL 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  845 INDYHGThsagpNFAFELVIRRLEAEKNKV--YDLSSMVFLMIAAEPV---RQKTVRRFI--ELTQPFGLSE-----GVL 912
Cdd:PRK07470  250 VERHRVT-----NLFTVPTILKMLVEHPAVdrYDHSSLRYVIYAGAPMyraDQKRALAKLgkVLVQYFGLGEvtgniTVL 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  913 APGYGLAENcvyvtcafgeckpvfiDWQGRV-CCGYveqDDTDTLIRIVDpdslTEHQE--DGVEGEIWISSPSSGVGYW 989
Cdd:PRK07470  325 PPALHDAED----------------GPDARIgTCGF---ERTGMEVQIQD----DEGRElpPGETGEICVIGPAVFAGYY 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  990 GNSEMSQRTFFNqlknhpnkKFTRTGDLGRT-IDGNLFITGRIKDLIIVAGRNIYSADVEK---TVESSSEVlrpgccAV 1065
Cdd:PRK07470  382 NNPEANAKAFRD--------GWFRTGDLGHLdARGFLYITGRASDMYISGGSNVYPREIEEkllTHPAVSEV------AV 447

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 937914749 1066 VGIPEEVLAQKGISipdssdqvglVVIAevREGKAVSKE 1104
Cdd:PRK07470  448 LGVPDPVWGEVGVA----------VCVA--RDGAPVDEA 474
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 605-1057 2.65e-11

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); 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 adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 68.77  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLtstKPVIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPmqsggqallkVENISKMC 684
Cdd:cd12117    24 TYAELNERANRLARRLR---AAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP----------AERLAFML 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 ---NAVAILSTSSYHAAVRAGyiknivtlakrvqkCSAQWPDIPWihtdswiknyrRSSDSFNSDTVLftkpQPSDLCFL 761
Cdd:cd12117    91 adaGAKVLLTDRSLAGRAGGL--------------EVAVVIDEAL-----------DAGPAGNPAVPV----SPDDLAYV 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  762 QFTSGSTGDAKGVMITHEGLIHNVKtmKKRYRS-TSKTVLVSWLPQYHDMGLIgGLFTALVSGGTSVLFSPmifirNPLL 840
Cdd:cd12117   142 MYTSGSTGRPKGVAVTHRGVVRLVK--NTNYVTlGPDDRVLQTSPLAFDASTF-EIWGALLNGARLVLAPK-----GTLL 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  841 WLQTINDYHGTHsaGPNFAF-------ELVIRRLEAeknkvydLSSMVFLMIAAEPVRQKTVRRFIEltqpfGLSEGVLA 913
Cdd:cd12117   214 DPDALGALIAEE--GVTVLWltaalfnQLADEDPEC-------FAGLRELLTGGEVVSPPHVRRVLA-----ACPGLRLV 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  914 PGYGLAENCVYVTCAfgeckpvfidwqgRVCCGYVEQDD-------TDTLIRIVDPDSLTehQEDGVEGEIWISSPSSGV 986
Cdd:cd12117   280 NGYGPTENTTFTTSH-------------VVTELDEVAGSipigrpiANTRVYVLDEDGRP--VPPGVPGELYVGGDGLAL 344

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937914749  987 GYWGNSEMSQRtFFNQLKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEV 1057
Cdd:cd12117   345 GYLNRPALTAE-RFVADPFGPGERLYRTGDLARwLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGV 415
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 755-1148 3.23e-11

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 68.67  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIhnVKTMKK----RYrsTSKTVLVSWLPQYHdmglIGGLFTA---LVSGGTSV 827
Cdd:PLN02860  171 PDDAVLICFTSGTTGRPKGVTISHSALI--VQSLAKiaivGY--GEDDVYLHTAPLCH----IGGLSSAlamLMVGACHV 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  828 LFspmifirnpllwlqtindyhgthsagPNFAFELVirrLEAEKNkvYDLSSMVFL--MIA--AEPVRQK-------TVR 896
Cdd:PLN02860  243 LL--------------------------PKFDAKAA---LQAIKQ--HNVTSMITVpaMMAdlISLTRKSmtwkvfpSVR 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  897 RFieLTQPFGLSEGVLA------------PGYGLAENCVYVT----------------CAFGECKPVFIDWQGRVCCG-- 946
Cdd:PLN02860  292 KI--LNGGGSLSSRLLPdakklfpnaklfSAYGMTEACSSLTfmtlhdptlespkqtlQTVNQTKSSSVHQPQGVCVGkp 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  947 --YVEqddtdtlIRIVDPDSLTEhqedgveGEIWISSPSSGVGYWGNSEMSQrtffnqlKNHPNKKFTRTGDLGrTID-- 1022
Cdd:PLN02860  370 apHVE-------LKIGLDESSRV-------GRILTRGPHVMLGYWGQNSETA-------SVLSNDGWLDTGDIG-WIDka 427

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1023 GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEVLAQKgisipdssdqvglvVIAEVR--EG-K 1099
Cdd:PLN02860  428 GNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVAS---VVVVGVPDSRLTEM--------------VVACVRlrDGwI 490

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937914749 1100 AVSKEVVNNIKARVV---------EEHGVAVASV-KLI----KPRTIckTTSGKIRRFECMRQ 1148
Cdd:PLN02860  491 WSDNEKENAKKNLTLssetlrhhcREKNLSRFKIpKLFvqwrKPFPL--TTTGKIRRDEVRRE 551
PRK12467 PRK12467
peptide synthase; Provisional
 755-1154 6.11e-11

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 68.65  E-value: 6.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGlIGGLFTALVSGGTSVLFSPmif 834
Cdd:PRK12467  655 PDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLG-VTELFGALASGATLHLLPP--- 730

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 irnpllwlqtindyhGTHSAGPNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEGV-LA 913
Cdd:PRK12467  731 ---------------DCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRaLG 795

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  914 PG------YGLAENCVYVTcaFGECKPVFIDWQGrvccGYVEQDDTDTLIRIVDPDslTEHQEDGVEGEIWISSPSSGVG 987
Cdd:PRK12467  796 PGarlinhYGPTETTVGVS--TYELSDEERDFGN----VPIGQPLANLGLYILDHY--LNPVPVGVVGELYIGGAGLARG 867

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  988 YWGNSEMSQRTFFNQLKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgccAVv 1066
Cdd:PRK12467  868 YHRRPALTAERFVPDPFGADGGRLYRTGDLARyRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVRE----AV- 942

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1067 gipeeVLAQKGISipdSSDQVGLVV---IAEVREGKAVSKEVVNNIKARV----VEEHGVAVASVKLikprtickTTSGK 1139
Cdd:PRK12467  943 -----VLAQPGDA---GLQLVAYLVpaaVADGAEHQATRDELKAQLRQVLpdymVPAHLLLLDSLPL--------TPNGK 1006

                         410
                  ....*....|....*
gi 937914749 1140 IRRfECMRQFVDNTL 1154
Cdd:PRK12467 1007 LDR-KALPKPDASAV 1020
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 755-1143 6.71e-11

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. 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: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 67.39  E-value: 6.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDmGLIGGLFTALVSGGTSVLfspmif 834
Cdd:cd17649    93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFD-GAHEQLLPPLICGACVVL------ 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 iRNPLLW-----LQTINDYHGTHSAG--PNFAFELViRRLEAEKNKVYdlSSMVFLMIAAEPVRQKTVRRF----IELTQ 903
Cdd:cd17649   166 -RPDELWasadeLAEMVRELGVTVLDlpPAYLQQLA-EEADRTGDGRP--PSLRLYIFGGEALSPELLRRWlkapVRLFN 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  904 PFGLSEGVLAPgygLAENCVYVTCAFGECKPVfidwqGRVCCGYVeqddtdtlIRIVDPDsLTEhQEDGVEGEIWISSPS 983
Cdd:cd17649   242 AYGPTEATVTP---LVWKCEAGAARAGASMPI-----GRPLGGRS--------AYILDAD-LNP-VPVGVTGELYIGGEG 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  984 SGVGYWGNSEMSQRTFFNQLKNHPNKKFTRTGDLGRTI-DGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgc 1062
Cdd:cd17649   304 LARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRdDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVRE--- 380

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1063 cAVvgipeeVLAQKGisipDSSDQ-VGLVVIAEVREGKAVSKEVVNNIKARV----VEEHGVAVASVKLikprtickTTS 1137
Cdd:cd17649   381 -AA------VVALDG----AGGKQlVAYVVLRAAAAQPELRAQLRTALRASLpdymVPAHLVFLARLPL--------TPN 441


                  ....*.
gi 937914749 1138 GKIRRF 1143
Cdd:cd17649   442 GKLDRK 447
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 757-1080 7.40e-11

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which 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: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 65.89  E-value: 7.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  757 DLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFtALVSGGTSVLFSPMifir 836
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAIS-ALYLGGTFIGQRKF---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  837 NPLLWLQTINDYHGTHSAGPNFAFELVIRRLEAEKNKVYDLSSMVFLmiaaEPVRQKTVRRF---IELTQPFGLSEgvla 913
Cdd:cd17633    76 NPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSIFSSGQKL----FESTKKKLKNIfpkANLIEFYGTSE---- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  914 pgyglaenCVYVTCAF-GECKPVfiDWQGRVCCGyVEqddtdtlIRIVDpdsltehQEDGVEGEIWISSPSSGVGYWGNS 992
Cdd:cd17633   148 --------LSFITYNFnQESRPP--NSVGRPFPN-VE-------IEIRN-------ADGGEIGKIFVKSEMVFSGYVRGG 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  993 EMSqrtffnqlknhpNKKFTRTGDLGRT-IDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRPGccaVVGIPEE 1071
Cdd:cd17633   203 FSN------------PDGWMSVGDIGYVdEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAI---VVGIPDA 267


                  ....*....
gi 937914749 1072 VLAQKGISI 1080
Cdd:cd17633   268 RFGEIAVAL 276
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 605-1082 8.70e-11

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 66.81  E-value: 8.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPMQSggqallkveniskmc 684
Cdd:cd17645    25 TYKQLNEKANQLARHLRGKG---VKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER--------------- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 navailstssyhaavragyiknivtlakrvqkcsaqwpdIPWIHTDSWIKnyrrssdsfnsdtVLFTkpQPSDLCFLQFT 764
Cdd:cd17645    87 ---------------------------------------IAYMLADSSAK-------------ILLT--NPDDLAYVIYT 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  765 SGSTGDAKGVMITHEGLIhNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLFSPMIfirnpLLWLQT 844
Cdd:cd17645   113 SGSTGLPKGVMIEHHNLV-NLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSER-----RLDLDA 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  845 INDYHGTHSAGPNFAFELVirrleAEKNKVYDLSSMVFLMIAAEpvrqkTVRRFIEltQPFGLSEgvlapGYGLAENCVY 924
Cdd:cd17645   187 LNDYFNQEGITISFLPTGA-----AEQFMQLDNQSLRVLLTGGD-----KLKKIER--KGYKLVN-----NYGPTENTVV 249

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  925 VTcAFGECKPvfidwQGRVCCGyveQDDTDTLIRIVDPDslTEHQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFFNQlK 1004
Cdd:cd17645   250 AT-SFEIDKP-----YANIPIG---KPIDNTRVYILDEA--LQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVH-P 317

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1005 NHPNKKFTRTGDLGRTI-DGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVL------------RPGCCAVVGIPEE 1071
Cdd:cd17645   318 FVPGERMYRTGDLAKFLpDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIElaavlakedadgRKYLVAYVTAPEE 397

                         490
                  ....*....|....*.
gi 937914749 1072 VLAQK-----GISIPD 1082
Cdd:cd17645   398 IPHEElrewlKNDLPD 413
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 761-1144 1.09e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 66.89  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  761 LQFTSGSTGDAKGVMITHEGL----IHNVKT--MKKR--YRSTsktvlvswLPQYHdmgLIGGLF--TALVSGGTSVlfs 830
Cdd:PRK08162  187 LNYTSGTTGNPKGVVYHHRGAylnaLSNILAwgMPKHpvYLWT--------LPMFH---CNGWCFpwTVAARAGTNV--- 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  831 pmiFIR--NPLLWLQTINDYHGTHSAGPNFAFELVIRRLEAEKNKvydLSSMVFLMIAAEP----VRQKTVRRFIELTQP 904
Cdd:PRK08162  253 ---CLRkvDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAG---IDHPVHAMVAGAAppaaVIAKMEEIGFDLTHV 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  905 FGLSEGvlapgYGLAencvyVTCAFGEckpvfiDW-----------QGRVCCGYVEQDDtdtlIRIVDPDSLTEHQEDGV 973
Cdd:PRK08162  327 YGLTET-----YGPA-----TVCAWQP------EWdalplderaqlKARQGVRYPLQEG----VTVLDPDTMQPVPADGE 386

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  974 E-GEIWISSPSSGVGYWGNSEMSQRTF----FnqlknHpnkkftrTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADV 1047
Cdd:PRK08162  387 TiGEIMFRGNIVMKGYLKNPKATEEAFaggwF-----H-------TGDLAvLHPDGYIKIKDRSKDIIISGGENISSIEV 454

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1048 EKTVESSSEVLrpgCCAVVGIPEEvlaqkgisipdssdQVGLVVIA--EVREGKAVSK-EVVNNIKARVveehgvavASV 1124
Cdd:PRK08162  455 EDVLYRHPAVL---VAAVVAKPDP--------------KWGEVPCAfvELKDGASATEeEIIAHCREHL--------AGF 509

                         410       420
                  ....*....|....*....|....*
gi 937914749 1125 KLikPRTIC-----KTTSGKIRRFE 1144
Cdd:PRK08162  510 KV--PKAVVfgelpKTSTGKIQKFV 532
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 605-1051 1.24e-10

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. 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: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 66.34  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLltSTKPVIKpgDRVLLIHLP-GLEFIDAFFGCIRAGVIPVPVLPPDPMQsggqallkvENISKM 683
Cdd:cd17656    15 TYRELNERSNQLARFL--REKGVKK--DSIVAIMMErSAEMIVGILGILKAGGAFVPIDPEYPEE---------RRIYIM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  684 CNAVAILSTSSYHAAVRAGYIKNIVTLakrvqkcsaQWPDIPwiHTDSWIKNYRRSSDsfnsdtvlftkpqpsDLCFLQF 763
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLSFNKSTILL---------EDPSIS--QEDTSNIDYINNSD---------------DLLYIIY 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  764 TSGSTGDAKGVMITHEGLIHNVK-TMKKRYRSTSKTVL----VSWLPQYHDmgliggLFTALVSGGTsvlfspMIFIRNP 838
Cdd:cd17656   136 TSGTTGKPKGVQLEHKNMVNLLHfEREKTNINFSDKVLqfatCSFDVCYQE------IFSTLLSGGT------LYIIREE 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  839 L-LWLQTINDYHGTHSAGPNFAFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTvRRFIELTQPFGLSegvLAPGYG 917
Cdd:cd17656   204 TkRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGEQLVIT-NEFKEMLHEHNVH---LHNHYG 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  918 LAENCVYVTCAFGECKPvfidWQGRVCCGyveQDDTDTLIRIVDpdSLTEHQEDGVEGEIWISSPSSGVGYWGNSEMSQR 997
Cdd:cd17656   280 PSETHVVTTYTINPEAE----IPELPPIG---KPISNTWIYILD--QEQQLQPQGIVGELYISGASVARGYLNRQELTAE 350

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749  998 TFF-NQLKnhPNKKFTRTGDLGRTI-DGNLFITGRIKDLIIVAGRNIYSADVEKTV 1051
Cdd:cd17656   351 KFFpDPFD--PNERMYRTGDLARYLpDGNIEFLGRADHQVKIRGYRIELGEIEAQL 404
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 576-1144 1.86e-10

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 65.95  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  576 LQYWGTHKVTEK---NVIYTWINEEGKLMnRRTYQELhGNASYIAQKLLTSTKPvIKPGDRVLLIhLPGL-EFIDAFFGC 651
Cdd:cd05928    12 LDQWADKEKAGKrppNPALWWVNGKGDEV-KWSFREL-GSLSRKAANVLSGACG-LQRGDRVAVI-LPRVpEWWLVNVAC 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  652 IRAGVIPVPvlppdpmqsgGQALLKVENIskmcnaVAILSTSsyhaavRAGYIKNIVTLAKRVQKCSAQWPDI------- 724
Cdd:cd05928    88 IRTGLVFIP----------GTIQLTAKDI------LYRLQAS------KAKCIVTSDELAPEVDSVASECPSLktkllvs 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  725 --PWihtDSWI---KNYRRSSDSFNSdtvlfTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKtMKKRYRSTSKTV 799
Cdd:cd05928   146 ekSR---DGWLnfkELLNEASTEHHC-----VETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLK-VNGRYWLDLTAS 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  800 LVSWlpQYHDMG----LIGGLFTALVSGGTSVLFSPMIFirNPLLWLQTINDYHGTHSAGPNFAFelviRRLEAEKNKVY 875
Cdd:cd05928   217 DIMW--NTSDTGwiksAWSSLFEPWIQGACVFVHHLPRF--DPLVILKTLSSYPITTFCGAPTVY----RMLVQQDLSSY 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  876 DLSSMVFLMIAAEPVRQKTVRRFIELTqpfGLSegvLAPGYGLAEncVYVTCAFG---ECKPVFIdwqGRVCCGYVEQ-- 950
Cdd:cd05928   289 KFPSLQHCVTGGEPLNPEVLEKWKAQT---GLD---IYEGYGQTE--TGLICANFkgmKIKPGSM---GKASPPYDVQii 357

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  951 DDTDTlirIVDPdsltehqedGVEGEIWIS-SPSSGVGywgnsemsqrtFFNQLKNHPNK-------KFTRTGDLGRT-I 1021
Cdd:cd05928   358 DDNGN---VLPP---------GTEGDIGIRvKPIRPFG-----------LFSGYVDNPEKtaatirgDFYLTGDRGIMdE 414

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1022 DGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRPgccAVVGIPEEVLaqkgisipdssdqvGLVVIAEV------ 1095
Cdd:cd05928   415 DGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVES---AVVSSPDPIR--------------GEVVKAFVvlapqf 477

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 937914749 1096 --REGKAVSKEVVNNIKArvveehgvAVASVKLikPRTI------CKTTSGKIRRFE 1144
Cdd:cd05928   478 lsHDPEQLTKELQQHVKS--------VTAPYKY--PRKVefvqelPKTVTGKIQRNE 524
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 594-1071 3.06e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 65.33  E-value: 3.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  594 INEEGKLmnrrTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGViPVPVLPPDpmqSGGQA 673
Cdd:PRK07788   69 IDERGTL----TYAELDEQSNALARGLLALG---VRAGDGVAVLARNHRGFVLALYAAGKVGA-RIILLNTG---FSGPQ 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  674 LLKVeniSKMCNAVAILSTSSYHAAVRA-----GYIKNIVTLAKRVQKCSAQWPDIpwihtDSWIKNyrrssdsfNSDTV 748
Cdd:PRK07788  138 LAEV---AAREGVKALVYDDEFTDLLSAlppdlGRLRAWGGNPDDDEPSGSTDETL-----DDLIAG--------SSTAP 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  749 LFTKPQPSDLCFLqfTSGSTGDAKGVMITHEGLIHNVKTMKKR--YRSTSKTVLVSwlPQYHDMGL-IGGLFTALvsGGT 825
Cdd:PRK07788  202 LPKPPKPGGIVIL--TSGTTGTPKGAPRPEPSPLAPLAGLLSRvpFRAGETTLLPA--PMFHATGWaHLTLAMAL--GST 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  826 SVLfsPMIFirNPLLWLQTINDYHGTH-SAGPNFAFELVirRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELtqp 904
Cdd:PRK07788  276 VVL--RRRF--DPEATLEDIAKHKATAlVVVPVMLSRIL--DLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEA--- 346

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  905 FGlseGVLAPGYGLAEnCVYVTCAFGEckpvfiDWQ------GRVCCGyveqddtdTLIRIVDPDslteHQE--DGVEGE 976
Cdd:PRK07788  347 FG---PVLYNLYGSTE-VAFATIATPE------DLAeapgtvGRPPKG--------VTVKILDEN----GNEvpRGVVGR 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  977 IWISSPSSGVGYWGNsemsqrtffnqlkNHPNKK--FTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVES 1053
Cdd:PRK07788  405 IFVGNGFPFEGYTDG-------------RDKQIIdgLLSSGDVGYfDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAG 471

                         490
                  ....*....|....*...
gi 937914749 1054 SSEVLRpgcCAVVGIPEE 1071
Cdd:PRK07788  472 HPDVVE---AAVIGVDDE 486
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 747-1130 4.61e-10

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 64.76  E-value: 4.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  747 TVLFTKPQPSDLCFLQFT-SGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLiGGLFTALVSGGT 825
Cdd:PRK06164  171 AAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF-STLLGALAGGAP 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  826 SVLFSPMIFIRNpllwLQTINDYHGTHSAGPNFAFelviRRLEAEKNKVYDLSSMVFLMIAA-EPvrqktvrRFIELTqP 904
Cdd:PRK06164  250 LVCEPVFDAART----ARALRRHRVTHTFGNDEML----RRILDTAGERADFPSARLFGFASfAP-------ALGELA-A 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  905 FGLSEGVLAPG-YGLAEncvyvTCAFGECKPVFIDWQGRVCCGYVEQDDTDTlIRIVDPDSlTEHQEDGVEGEIWISSPS 983
Cdd:PRK06164  314 LARARGVPLTGlYGSSE-----VQALVALQPATDPVSVRIEGGGRPASPEAR-VRARDPQD-GALLPDGESGEIEIRAPS 386

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  984 SGVGYWGNSEMSQRTFfnqlknhPNKKFTRTGDLGRTI-DGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVlrpGC 1062
Cdd:PRK06164  387 LMRGYLDNPDATARAL-------TDDGYFRTGDLGYTRgDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGV---AA 456

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1063 CAVVGIPEE--------VLAQKGISiPDSSDqvglvVIAEVREGKAVSKevvnnIKARV--VEEHGVAVA--SVKLIKPR 1130
Cdd:PRK06164  457 AQVVGATRDgktvpvafVIPTDGAS-PDEAG-----LMAACREALAGFK-----VPARVqvVEAFPVTESanGAKIQKHR 525
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 2283-2490 1.02e-09

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 64.00  E-value: 1.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  2283 LCQpLLQTLVPYSVLGLVIFLPLRGLLAVAAATRFPLYWLLPA--FWAASGVAAMATCAAAKWALVGSrvdgdtvhiWSP 2360
Cdd:TIGR02353    1 VCQ-TLQLIPIVTLSGLQWLAPLLGYNWLYEALDDVSWLYLRAvaLVFAVPVGRLGFAIAAKWLLVGR---------WKP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  2361 AVFldTVWQAV--RAATAEYFAELTP-----GSAPFAAWMRVMGASVspGDGVYVDSMGALLNpEMVRLERGAAVGRDAL 2433
Cdd:TIGR02353   71 GTY--PIWGSTylRFWTVKRLVDAAPtvllsGSPLYSLYLRALGAKI--GKGVDIGSLPPVCT-DLLTIGAGTIVRKEVM 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 937914749  2434 LFGhvYEGEAGKVKFGAVSVGEDGFVGSRAVAMPSVTVDDGGCLAALGLAMKGETVK 2490
Cdd:TIGR02353  146 LLG--YRAERGRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIP 200
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 77-139 1.11e-09

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 63.23  E-value: 1.11e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749   77 IGEMdpKRSIDDQFSK----LHPSLPVDT--RIGIVGAGPSGLSAAYALAKLGYRnVTLFEKCHTVSGM 139
Cdd:COG0493    94 IGAL--ERFIADKAFEegwvKPPPPAPRTgkKVAVVGSGPAGLAAAYQLARAGHE-VTVFEALDKPGGL 159
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1748-1894 1.20e-09

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 58.73  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1748 IASLIHRRITISAHVRFAKMlsgteafcVYLRLLGAKIGRHCSIRAINPVANPELISVGDGVHLGDFCNIVPGFY----- 1822
Cdd:COG0110     1 MKLLLLFGARIGDGVVIGPG--------VRIYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHpiddp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749 1823 SKGGFTSAEIKVQENTVVGSGSLLLPGCVLQENVILGALSVA----PENAvlrrggVYVGsqSPAMVKNTLLDEDE 1894
Cdd:COG0110    73 ATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVtkdvPPYA------IVAG--NPARVIRKRDEEER 140
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 756-1143 1.27e-09

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 62.92  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  756 SDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLvsWlpQYHDMGLIGGLFTALVS----GGTSVL--- 828
Cdd:cd05973    88 SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF--W--NAADPGWAYGLYYAITGplalGHPTILleg 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  829 -FSPmifirnPLLWlQTINDYHGTHSAGPNFAFELVIRR-LEAE---KNKVYDLSSmvflmiAAEPVRQKTVRRFieltq 903
Cdd:cd05973   164 gFSV------ESTW-RVIERLGVTNLAGSPTAYRLLMAAgAEVParpKGRLRRVSS------AGEPLTPEVIRWF----- 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  904 pfGLSEGVLA-PGYGLAENCVYVTCAFGECKPVFIDWQGRVCCGY---VEQDDTDTLIrivdpdsltehqeDGVEGEIWI 979
Cdd:cd05973   226 --DAALGVPIhDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWrvaVLDDDGDELG-------------PGEPGRLAI 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  980 SSPSSGV----GYWGNSEMSqrtffnqlknhPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESS 1054
Cdd:cd05973   291 DIANSPLmwfrGYQLPDTPA-----------IDGGYYLTGDTVEfDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEH 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1055 SEVLRpgcCAVVGIPEevlaqkgisiPDSSDQV-GLVVIAEVREG-KAVSKEVVNNIKARvVEEHGvavasvkliKPRTI 1132
Cdd:cd05973   360 PAVAE---AAVIGVPD----------PERTEVVkAFVVLRGGHEGtPALADELQLHVKKR-LSAHA---------YPRTI 416

                         410
                  ....*....|....*..
gi 937914749 1133 ------CKTTSGKIRRF 1143
Cdd:cd05973   417 hfvdelPKTPSGKIQRF 433
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 603-1106 1.51e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 63.37  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPV---LPPDpmqsggqallKVEN 679
Cdd:PRK07798   28 RLTYAELEERANRLAHYLIAQG---LGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnyrYVED----------ELRY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  680 ISKMCNAVAILstssYHAavragyiknivTLAKRVQKCSaqwPDIPWIHT-----DSWIKNYRRSSDSFN------SDTV 748
Cdd:PRK07798   95 LLDDSDAVALV----YER-----------EFAPRVAEVL---PRLPKLRTlvvveDGSGNDLLPGAVDYEdalaagSPER 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  749 LFTKPQPSDLCFLqFTSGSTGDAKGVMITHEGL---------------IHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLI 813
Cdd:PRK07798  157 DFGERSPDDLYLL-YTGGTTGMPKGVMWRQEDIfrvllggrdfatgepIEDEEELAKRAAAGPGMRRFPAPPLMHGAGQW 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  814 GGlFTALVSGGTSVLFSPMIFirNPLLWLQTInDYHGTHS---AGPNFAFELvIRRLEAEKNkvYDLSSMVFLMIAAEPV 890
Cdd:PRK07798  236 AA-FAALFSGQTVVLLPDVRF--DADEVWRTI-EREKVNVitiVGDAMARPL-LDALEARGP--YDLSSLFAIASGGALF 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  891 RQKTVRRFIELtqpfgLSEGVLAPGYGLAE--NCVYVTCAFGECK---PVF-IDWQGRVCcgyveqdDTDTliRIVDPDS 964
Cdd:PRK07798  309 SPSVKEALLEL-----LPNVVLTDSIGSSEtgFGGSGTVAKGAVHtggPRFtIGPRTVVL-------DEDG--NPVEPGS 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  965 ltehqedGVEGeiWIS-SPSSGVGYWGNSEMSQRTFfnqlKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNI 1042
Cdd:PRK07798  375 -------GEIG--WIArRGHIPLGYYKDPEKTAETF----PTIDGVRYAIPGDRARvEADGTITLLGRGSVCINTGGEKV 441

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937914749 1043 YSADVEktvesssEVLR--PGC--CAVVGIPEEVLAQkgisipdssdQVGLVViaEVREGKAVSKEVV 1106
Cdd:PRK07798  442 FPEEVE-------EALKahPDVadALVVGVPDERWGQ----------EVVAVV--QLREGARPDLAEL 490
PRK12467 PRK12467
peptide synthase; Provisional
 605-1048 1.78e-09

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 64.03  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPMqsggqallkvENISKMC 684
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALG---VGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPR----------ERLAYMI 1667

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 --NAVAILSTSSyHAAVRAGYIKNIVTLAKrvqkcsaqwpDIPwihtDSWIKNYrrssdsfnSDTVLFTKPQPSDLCFLQ 762
Cdd:PRK12467 1668 edSGIELLLTQS-HLQARLPLPDGLRSLVL----------DQE----DDWLEGY--------SDSNPAVNLAPQNLAYVI 1724

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  763 FTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGlIGGLFTALVSGGTSVLFSPMIFiRNPLLWL 842
Cdd:PRK12467 1725 YTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVS-VWELFWPLINGARLVIAPPGAH-RDPEQLI 1802

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  843 QTINDYHGTHSAGPNFAFELVIRRLEAEKNKvydlSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSEgvlapGYGLAENC 922
Cdd:PRK12467 1803 QLIERQQVTTLHFVPSMLQQLLQMDEQVEHP----LSLRRVVCGGEALEVEALRPWLERLPDTGLFN-----LYGPTETA 1873

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  923 VYVTcaFGECKPVfiDWQGRVCCGY-VEQDDTDTLIRivdpDSLTEHQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFFN 1001
Cdd:PRK12467 1874 VDVT--HWTCRRK--DLEGRDSVPIgQPIANLSTYIL----DASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVA 1945

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 937914749 1002 QLKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVE 1048
Cdd:PRK12467 1946 DPFGTVGSRLYRTGDLARyRADGVIEYLGRIDHQVKIRGFRIELGEIE 1993
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 742-1063 1.83e-09

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. 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: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 62.49  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  742 SFNSDTVLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIgGLFTALV 821
Cdd:cd17654   104 SFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVV-EIFLSLS 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  822 SGGTsVLFSPMIFIRNPLLwLQTINDYHgtHSAGPNFAFELVIRRLEAEKNKVYDLS---SMVFLMIAAEPVRQKTV--- 895
Cdd:cd17654   183 SGAT-LLIVPTSVKVLPSK-LADILFKR--HRITVLQATPTLFRRFGSQSIKSTVLSatsSLRVLALGGEPFPSLVIlss 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  896 RRFIEL-TQPFGLsegvlapgYGLAENCVYVTcaFGECKPVFIDWQGrvcCGYVEqddtDTLIRIVDPDSLTEHQEDGVE 974
Cdd:cd17654   259 WRGKGNrTRIFNI--------YGITEVSCWAL--AYKVPEEDSPVQL---GSPLL----GTVIEVRDQNGSEGTGQVFLG 321

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  975 GeiwisspssgvgywgnseMSQRTFFNQLKNHPNKKFTRTGDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESS 1054
Cdd:cd17654   322 G------------------LNRVCILDDEVTVPKGTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESC 383


                  ....*....
gi 937914749 1055 SEVLrpGCC 1063
Cdd:cd17654   384 LGVE--SCA 390
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
957-1142 1.85e-09

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 62.67  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  957 IRIVDPdslTEHQEDGVEGEIWISSPSSGVGYWGNSEMSQRTFFNQ-LKnhpnkkftrTGDLGRT-IDGNLFITGRIKDL 1034
Cdd:PRK03640  318 LKIEKD---GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGwFK---------TGDIGYLdEEGFLYVLDRRSDL 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1035 IIVAGRNIYSADVEKTVESSSEVLRPGccaVVGIPEEvlaqkgisipdssdQVGLVVIAEVREGKAVSKEVVNNIkarvV 1114
Cdd:PRK03640  386 IISGGENIYPAEIEEVLLSHPGVAEAG---VVGVPDD--------------KWGQVPVAFVVKSGEVTEEELRHF----C 444

                         170       180       190
                  ....*....|....*....|....*....|..
gi 937914749 1115 EEHgvaVASVKLIKPRTIC----KTTSGKIRR 1142
Cdd:PRK03640  445 EEK---LAKYKVPKRFYFVeelpRNASGKLLR 473
PLN02654 PLN02654
acetate-CoA ligase
 586-1142 1.93e-09

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 62.99  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  586 EKNVIYTWINEEGKLMnRRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLlIHLPGL-EFIDAFFGCIRAGVIPVPVLPP 664
Cdd:PLN02654  104 DKIAIYWEGNEPGFDA-SLTYSELLDRVCQLANYLKDVG---VKKGDAVV-IYLPMLmELPIAMLACARIGAVHSVVFAG 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  665 DPMQSGGQALLKveniskmCNAVAILSTSSYHAAVRAGYIKNIV--TLAKRVQ-------------KCSAQWPDIPWIH- 728
Cdd:PLN02654  179 FSAESLAQRIVD-------CKPKVVITCNAVKRGPKTINLKDIVdaALDESAKngvsvgicltyenQLAMKREDTKWQEg 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  729 TDSW----IKNYRRSSDSFNSDTvlftkpqpSDLCFLQFTSGSTGDAKGVMITHEG-LIHNVKTMKkrYRSTSKTVLVSW 803
Cdd:PLN02654  252 RDVWwqdvVPNYPTKCEVEWVDA--------EDPLFLLYTSGSTGKPKGVLHTTGGyMVYTATTFK--YAFDYKPTDVYW 321

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  804 LPQyhDMGLIGG----LFTALVSGGTSVLFSPMIFIRNPLLWLQTINDYHGT-HSAGPNFAFELVirRLEAEKNKVYDLS 878
Cdd:PLN02654  322 CTA--DCGWITGhsyvTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTiFYTAPTLVRSLM--RDGDEYVTRHSRK 397

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  879 SMVFLMIAAEPVRQKTVRRFIELTqpfGLSEGVLAPGYGLAENCVYV---------------TCAFGECKPVFIDWQGRV 943
Cdd:PLN02654  398 SLRVLGSVGEPINPSAWRWFFNVV---GDSRCPISDTWWQTETGGFMitplpgawpqkpgsaTFPFFGVQPVIVDEKGKE 474

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  944 ----CCGYVEqddtdtlirivdpdsltehqedgvegeIWISSPSSGVGYWGNSEMSQRTFFNqlknhPNKKFTRTGD-LG 1018
Cdd:PLN02654  475 iegeCSGYLC---------------------------VKKSWPGAFRTLYGDHERYETTYFK-----PFAGYYFSGDgCS 522

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1019 RTIDGNLFITGRIKDLIIVAGRNIYSADVEktvesSSEVLRPGC--CAVVGIPEEVLAQkgisipdssdqvGLVVIAEVR 1096
Cdd:PLN02654  523 RDKDGYYWLTGRVDDVINVSGHRIGTAEVE-----SALVSHPQCaeAAVVGIEHEVKGQ------------GIYAFVTLV 585

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 937914749 1097 EGKAVSKEVVNNIKARVVEEHGVAVASVKLIKPRTICKTTSGKIRR 1142
Cdd:PLN02654  586 EGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMR 631
PRK07233 PRK07233
hypothetical protein; Provisional
 102-173 2.56e-09

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 62.21  E-value: 2.56e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749  102 RIGIVGAGPSGLSAAYALAKLGYRnVTLFEKCHTVSGMCESIDIEG----RIYdlggQVIAANSAPVItHLAEELG 173
Cdd:PRK07233    1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAASFEFGGlpieRFY----HHIFKSDEALL-ELLDELG 70
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 750-808 4.28e-09

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-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. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to 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.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 61.85  E-value: 4.28e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937914749  750 FTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNV----KTMKKRYRSTSKTVLVSWLPQYH 808
Cdd:cd05927   108 PPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLAH 170
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 959-1143 1.01e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 60.54  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  959 IVDPDSltEHQEDGVEGEIWISSPSSGV--GYWGNSEMSQRTFFNQlknHPNKKFTrtGDlG--RTIDGNLFITGRIKDL 1034
Cdd:PRK00174  437 VVDEEG--NPLEGGEGGNLVIKDPWPGMmrTIYGDHERFVKTYFST---FKGMYFT--GD-GarRDEDGYYWITGRVDDV 508

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1035 IIVAGRNIYSADVEktvesSSEVLRPGC--CAVVGIPEEVlaqKGISIpdssdqVGLVVIaevREGKAVSKEVVNNIKAR 1112
Cdd:PRK00174  509 LNVSGHRLGTAEIE-----SALVAHPKVaeAAVVGRPDDI---KGQGI------YAFVTL---KGGEEPSDELRKELRNW 571

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 937914749 1113 VVEEHGvAVASVKLIK-----PrticKTTSGKI-RRF 1143
Cdd:PRK00174  572 VRKEIG-PIAKPDVIQfapglP----KTRSGKImRRI 603
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 754-1142 1.09e-08

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; 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 saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 60.02  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  754 QPSDLCFLQFTSGSTGDAKGVMITHegliHNVKTMKKRYRST-SKTVLVSWL---PQYHDMGlIGGLFTALVSGGTSVLF 829
Cdd:cd12115   103 DPDDLAYVIYTSGSTGRPKGVAIEH----RNAAAFLQWAAAAfSAEELAGVLastSICFDLS-VFELFGPLATGGKVVLA 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  830 -SPMIFIRNP-LLWLQTINDYhgthsagPNFAFELVirrleaEKNKVYDLSSMVFLmiAAEPVRQKTVRRFIELTQP--- 904
Cdd:cd12115   178 dNVLALPDLPaAAEVTLINTV-------PSAAAELL------RHDALPASVRVVNL--AGEPLPRDLVQRLYARLQVerv 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  905 FGLsegvlapgYGLAENCVYVTCAF---GECKPVFIdwqGRVCCGyveqddtdTLIRIVDpDSLTEhQEDGVEGEIWISS 981
Cdd:cd12115   243 VNL--------YGPSEDTTYSTVAPvppGASGEVSI---GRPLAN--------TQAYVLD-RALQP-VPLGVPGELYIGG 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  982 PSSGVGYWGNSEMSQRTFfnqLKN--HPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVL 1058
Cdd:cd12115   302 AGVARGYLGRPGLTAERF---LPDpfGPGARLYRTGDLVRwRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVR 378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1059 RpgccAVVGIPEEVLAQKGIsipdssdqVGLVViaevreGKAVSKEVVNNIKAR---VVEEHGVAVASVKLikpRTICKT 1135
Cdd:cd12115   379 E----AVVVAIGDAAGERRL--------VAYIV------AEPGAAGLVEDLRRHlgtRLPAYMVPSRFVRL---DALPLT 437


                  ....*..
gi 937914749 1136 TSGKIRR 1142
Cdd:cd12115   438 PNGKIDR 444
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 604-1074 1.14e-08

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 60.30  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  604 RTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPV---LPPDpmqsggqallKVENI 680
Cdd:PRK08276   12 VTYGELEARSNRLAHGLRALG---LREGDVVAILLENNPEFFEVYWAARRSGLYYTPInwhLTAA----------EIAYI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  681 SKMCNAVAILStssyHAAVRAGYIKNIVTLAKRVQKCSAQWPDIP-WIHTDSWIKNYrrssdsfnSDTVLftkPQPSDLC 759
Cdd:PRK08276   79 VDDSGAKVLIV----SAALADTAAELAAELPAGVPLLLVVAGPVPgFRSYEEALAAQ--------PDTPI---ADETAGA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  760 FLQFTSGSTGDAKGVMIT------HEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLfTALVSGGTSVL---FS 830
Cdd:PRK08276  144 DMLYSSGTTGRPKGIKRPlpgldpDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGM-SALALGGTVVVmekFD 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  831 PMIFirnpllwLQTINDYHGTHSagpnfafELV----IRRL---EAEKNKvYDLSSMVFLMIAAEPVRQKTVRRFIELTQ 903
Cdd:PRK08276  223 AEEA-------LALIERYRVTHS-------QLVptmfVRMLklpEEVRAR-YDVSSLRVAIHAAAPCPVEVKRAMIDWWG 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  904 PfglsegVLAPGYGLAENCVyVTCAFGEckpvfiDWQGRVccGYVEQDdTDTLIRIVDPDSltEHQEDGVEGEIWISSPS 983
Cdd:PRK08276  288 P------IIHEYYASSEGGG-VTVITSE------DWLAHP--GSVGKA-VLGEVRILDEDG--NELPPGEIGTVYFEMDG 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  984 SGVGYWGNSEMSQRTFfnqlknHPNKKFTrTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVessseVLRPGC 1062
Cdd:PRK08276  350 YPFEYHNDPEKTAAAR------NPHGWVT-VGDVGYlDEDGYLYLTDRKSDMIISGGVNIYPQEIENLL-----VTHPKV 417

                         490
                  ....*....|....*....
gi 937914749 1063 --CAVVGIP-----EEVLA 1074
Cdd:PRK08276  418 adVAVFGVPdeemgERVKA 436
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 1782-1903 1.48e-08

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 55.88  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1782 GAKIGRHCSIRA-INPvanpelISVGDGVHLGDFCNI--VPGFyskggftSAEI---------------KVQENTVVGSG 1843
Cdd:cd04645    23 GSSVWFGAVLRGdVNP------IRIGERTNIQDGSVLhvDPGY-------PTIIgdnvtvghgavlhgcTIGDNCLIGMG 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937914749 1844 SLLLPGCVLQENVILGALSVAPENAVLRRGGVYVGsqSPAMVKNTLLDED-ERIEEMDQAY 1903
Cdd:cd04645    90 AIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAG--SPAKVVRELTDEEiAELRESAEHY 148
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 605-1071 1.66e-08

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 59.79  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLltsTKPVIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPV----LPPDpmqsggqallkVENI 680
Cdd:PRK07786   44 TWRELDDRVAALAGAL---SRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVnfrlTPPE-----------IAFL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  681 SKMCNAVAILSTSSYhaAVRAGYIKNIVTLAKRVQKCSAQwpdipwihTDSWIKNYrrsSDSFNSDTvlfTKPQPSDL-- 758
Cdd:PRK07786  110 VSDCGAHVVVTEAAL--APVATAVRDIVPLLSTVVVAGGS--------SDDSVLGY---EDLLAEAG---PAHAPVDIpn 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  759 ---CFLQFTSGSTGDAKGVMITHEGLIHNVKTMKK--RYRSTSKTVLVSwLPQYHDMGLiGGLFTALVSGGTSVLFspmi 833
Cdd:PRK07786  174 dspALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRtnGADINSDVGFVG-VPLFHIAGI-GSMLPGLLLGAPTVIY---- 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  834 firnpllwlqtindyhgthsagPNFAFE--LVIRRLEAEKnkvydlSSMVFLMiaaePVRQKTVRRfIELTQPFGLSEGV 911
Cdd:PRK07786  248 ----------------------PLGAFDpgQLLDVLEAEK------VTGIFLV----PAQWQAVCA-EQQARPRDLALRV 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  912 LAPGYGLAENCV-----------YVTCAFG--ECKPVFIDWQGRVCC---GYVEQDDTDTLIRIVDpdsltEHQED---G 972
Cdd:PRK07786  295 LSWGAAPASDTLlrqmaatfpeaQILAAFGqtEMSPVTCMLLGEDAIrklGSVGKVIPTVAARVVD-----ENMNDvpvG 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  973 VEGEIWISSPSSGVGYWGNSEMSQRTFfnqlknhpNKKFTRTGDLGRT-IDGNLFITGRIKDLIIVAGRNIYSADVEKTV 1051
Cdd:PRK07786  370 EVGEIVYRAPTLMSGYWNNPEATAEAF--------AGGWFHSGDLVRQdEEGYVWVVDRKKDMIISGGENIYCAEVENVL 441

                         490       500
                  ....*....|....*....|
gi 937914749 1052 ESSSEVLRpgcCAVVGIPEE 1071
Cdd:PRK07786  442 ASHPDIVE---VAVIGRADE 458
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 755-1071 2.02e-08

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 59.44  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGL-IGGLFTALVsgGTSVLFSpmi 833
Cdd:PRK06334  182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFnSCTLFPLLS--GVPVVFA--- 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  834 fiRNPLL---WLQTINDYHGTHSAGPNFAFELVirrLEAEKNKVYDLSSMVFLMIAAEpVRQKTVRRFIELTQPfglsEG 910
Cdd:PRK06334  257 --YNPLYpkkIVEMIDEAKVTFLGSTPVFFDYI---LKTAKKQESCLPSLRFVVIGGD-AFKDSLYQEALKTFP----HI 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  911 VLAPGYGLAencvyvtcafgECKPVF----IDWQGRVCCGYVEQDDTDTLIrivdpdsltehqedgVEGEIWISSPSSGV 986
Cdd:PRK06334  327 QLRQGYGTT-----------ECSPVItintVNSPKHESCVGMPIRGMDVLI---------------VSEETKVPVSSGET 380

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  987 GY---WGNSemsqrTFFNQLKNHPNKKFTR--------TGDLGrTID--GNLFITGRIKDLIIVAGRNIysadvekTVES 1053
Cdd:PRK06334  381 GLvltRGTS-----LFSGYLGEDFGQGFVElggetwyvTGDLG-YVDrhGELFLKGRLSRFVKIGAEMV-------SLEA 447

                         330
                  ....*....|....*...
gi 937914749 1054 SSEVLRPGCcavvGIPEE 1071
Cdd:PRK06334  448 LESILMEGF----GQNAA 461
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 722-1087 2.30e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 59.31  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  722 PDIPWIHTDSwiKNYRRSSDSFNSDTVLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYR-STSKTVL 800
Cdd:PRK07867  120 PGVRVINVDS--PAWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGlGPDDVCY 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  801 VSwLPQYHDMGLIGGLFTALVSGGTSVL---FSPMIFirnpllwLQTINDYHGTHS--AGPNFAFELvirrleAEKNKVY 875
Cdd:PRK07867  198 VS-MPLFHSNAVMAGWAVALAAGASIALrrkFSASGF-------LPDVRRYGATYAnyVGKPLSYVL------ATPERPD 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  876 DLSS---MVFLMIAAEPVRQKTVRRF-IELTQPFGLSEGVLA--------PGyglaencvyvtcAFGeckPVFIDwqgrv 943
Cdd:PRK07867  264 DADNplrIVYGNEGAPGDIARFARRFgCVVVDGFGSTEGGVAitrtpdtpPG------------ALG---PLPPG----- 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  944 ccgyveqddtdtlIRIVDPDSLTE-----HQEDGVE------GEIW-ISSPSSGVGYWGNSEMSQRtffnQLKN---Hpn 1008
Cdd:PRK07867  324 -------------VAIVDPDTGTEcppaeDADGRLLnadeaiGELVnTAGPGGFEGYYNDPEADAE----RMRGgvyW-- 384

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1009 kkftrTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEevlaqkgisiPDSSDQV 1087
Cdd:PRK07867  385 -----SGDLAyRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATE---VAVYAVPD----------PVVGDQV 446
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
752-832 2.77e-08

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 59.34  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  752 KPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVLF-S 830
Cdd:PRK08043  361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYpS 440


                  ..
gi 937914749  831 PM 832
Cdd:PRK08043  441 PL 442
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 744-1078 3.18e-08

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 58.96  E-value: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  744 NSDTVLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQ---YHDMGLIgglftAL 820
Cdd:PLN02736  209 RSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLahiYERVNQI-----VM 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  821 VSGGTSVLF---------------SPMIFIRNPLLWLQTINDYHGT-HSAGP------NFAFELVIRRLEAEK------- 871
Cdd:PLN02736  284 LHYGVAVGFyqgdnlklmddlaalRPTIFCSVPRLYNRIYDGITNAvKESGGlkerlfNAAYNAKKQALENGKnpspmwd 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  872 ----NKVYD-LSSMVFLMIA-AEPVRQKtVRRFIELTqpFGlseGVLAPGYGLAE-NCVYVTCAfgeckpvfidwQGRVC 944
Cdd:PLN02736  364 rlvfNKIKAkLGGRVRFMSSgASPLSPD-VMEFLRIC--FG---GRVLEGYGMTEtSCVISGMD-----------EGDNL 426

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  945 CGYVEQDDTDTLIRIVD-PD-SLTEHQEDGVEGEIWISSPSSGVGYWgNSEMSQRTFFNqlknhpNKKFTRTGDLGRTI- 1021
Cdd:PLN02736  427 SGHVGSPNPACEVKLVDvPEmNYTSEDQPYPRGEICVRGPIIFKGYY-KDEVQTREVID------EDGWLHTGDIGLWLp 499

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937914749 1022 DGNLFITGRIKDLIIVA-GRNIYSADVEKTVESSSEV---------LRPGCCAVVGIPEEVL----AQKGI 1078
Cdd:PLN02736  500 GGRLKIIDRKKNIFKLAqGEYIAPEKIENVYAKCKFVaqcfvygdsLNSSLVAVVVVDPEVLkawaASEGI 570
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 754-1142 3.75e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 58.75  E-value: 3.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  754 QPSDLCFLQFTSGSTGDAKGVMITHEGLI-HNVktmkkryrsTSKTVL------VSWLPQyhDMGLIGG----LFTALVS 822
Cdd:PRK04319  203 DREDGAILHYTSGSTGKPKGVLHVHNAMLqHYQ---------TGKYVLdlheddVYWCTA--DPGWVTGtsygIFAPWLN 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  823 GGTSVL----FSPmifirnpLLWLQTINDYHGT--HSAgPNfAFELVIRrLEAEKNKVYDLSSMVFLMIAAEPVRQKTVR 896
Cdd:PRK04319  272 GATNVIdggrFSP-------ERWYRILEDYKVTvwYTA-PT-AIRMLMG-AGDDLVKKYDLSSLRHILSVGEPLNPEVVR 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  897 rfieltqpfglsegvlapgYGLAencvyvtcAFGecKPVFiD--WQ----GRVCCGYVEQDdtdtlIR------------ 958
Cdd:PRK04319  342 -------------------WGMK--------VFG--LPIH-DnwWMtetgGIMIANYPAMD-----IKpgsmgkplpgie 386

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  959 --IVDpdslteHQEDG----VEGEIWISS--PSSGVGYWGNSEMSQRTFFNQLknhpnkkfTRTGDLG-RTIDGNLFITG 1029
Cdd:PRK04319  387 aaIVD------DQGNElppnRMGNLAIKKgwPSMMRGIWNNPEKYESYFAGDW--------YVSGDSAyMDEDGYFWFQG 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1030 RIKDLIIVAGRNIYSADVE-KTVE--SSSEVlrpgccAVVGIPEEVlaqkgisipdssdqVGLVVIAEV--REGKAVSKE 1104
Cdd:PRK04319  453 RVDDVIKTSGERVGPFEVEsKLMEhpAVAEA------GVIGKPDPV--------------RGEIIKAFValRPGYEPSEE 512

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 937914749 1105 VVNNIKARVVEEHGVAVAsvklikPRTIC------KTTSGKIRR 1142
Cdd:PRK04319  513 LKEEIRGFVKKGLGAHAA------PREIEfkdklpKTRSGKIMR 550
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 1784-1885 4.04e-08

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 53.23  E-value: 4.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1784 KIGRHCSIRAINPVANPELISVGDGVHLGDFCNIV--------PGFYSKGGFTSAEIKVQENTVVGSGSLLLPGCVLQEN 1855
Cdd:cd04647     3 SIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYdhnhdiddPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDG 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 937914749 1856 VILGALSVA----PENAvlrrggVYVGsqSPAMV 1885
Cdd:cd04647    83 AVVGAGSVVtkdvPPNS------IVAG--NPAKV 108
PRK07208 PRK07208
hypothetical protein; Provisional
 105-154 4.60e-08

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 58.36  E-value: 4.60e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 937914749  105 IVGAGPSGLSAAYALAKLGYrNVTLFEKCHTVSGMCESIDIEGRIYDLGG 154
Cdd:PRK07208    9 IIGAGPAGLTAAYELLKRGY-PVTVLEADPVVGGISRTVTYKGNRFDIGG 57
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1205-1279 4.62e-08

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 52.16  E-value: 4.62e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749 1205 NEITEFLTQIVSEHTGISKDKISLTDSL-PSYGFDSIAVVRAAQKLSDFLGVPVGAIDIFTASCISELASFLENLV 1279
Cdd:COG0236     4 EELEERLAEIIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 761-1069 5.27e-08

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 58.49  E-value: 5.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  761 LQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTAlVSGGTSVLfspMIFIRNPLL 840
Cdd:PLN03102  191 LNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTA-ARGGTSVC---MRHVTAPEI 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  841 WlQTINDYHGTHSAGPNFAFELVirrLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRfielTQPFGLSegvLAPGYGLAE 920
Cdd:PLN03102  267 Y-KNIEMHNVTHMCCVPTVFNIL---LKGNSLDLSPRSGPVHVLTGGSPPPAALVKK----VQRLGFQ---VMHAYGLTE 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  921 ncvyvtcAFGeckPV-FIDWQ---------------GRVCCGYVEQDDTDtlirIVDPDSLTEHQEDG-VEGEIWISSPS 983
Cdd:PLN03102  336 -------ATG---PVlFCEWQdewnrlpenqqmelkARQGVSILGLADVD----VKNKETQESVPRDGkTMGEIVIKGSS 401

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  984 SGVGYWGNSEMSQRTFFNQLKNhpnkkftrTGDLGRT-IDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgc 1062
Cdd:PLN03102  402 IMKGYLKNPKATSEAFKHGWLN--------TGDVGVIhPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLE--- 470


                  ....*..
gi 937914749 1063 CAVVGIP 1069
Cdd:PLN03102  471 TAVVAMP 477
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 1710-1883 6.26e-08

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 55.19  E-value: 6.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1710 SFALFTAFADLSYGVILSILTSITSRALAAKPGTKQNGIASLIHRRITISahvRFAKMLSGTE--AFCVYLRllGAKIGR 1787
Cdd:TIGR03570   48 GDEDLLRYPPDEVDLVVAIGDNKLRRRLVEKLKAKGYRFATLIHPSAIVS---PSASIGEGTVimAGAVINP--DVRIGD 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  1788 HCSiraINPVAnpeliSVGDGVHLGDFCNIVPgfyskGGFTSAEIKVQENTVVGSGSLLLPGCVLQENVILGALSVapen 1867
Cdd:TIGR03570  123 NVI---INTGA-----IVEHDCVIGDFVHIAP-----GVTLSGGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAV---- 185

                          170
                   ....*....|....*....
gi 937914749  1868 aVLR---RGGVYVGsqSPA 1883
Cdd:TIGR03570  186 -VTKdipDGGVVVG--VPA 201
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1300-1371 6.84e-08

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 51.78  E-value: 6.84e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937914749 1300 IIEFLTKIVSDQTGIPKDKISPMDSL-PSYGFDSIAVVQAAQKLSDFLGVPVGAIDIFTAGCISELATFLENL 1371
Cdd:COG0236     6 LEERLAEIIAEVLGVDPEEITPDDSFfEDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1209-1270 1.06e-07

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 50.64  E-value: 1.06e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937914749  1209 EFLTQIVSEHTGISKDKISLTDSLPSYGFDSIAVVRAAQKLSDFLGVPVGAIDIFTASCISE 1270
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 931-1141 1.14e-07

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 56.94  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  931 ECKPVFIDWQGRVCCGYVEQDDTDTLIRIVDPDSLTEHQEDG--VEGEIWISS------PSSGVG--YWGNSEMSQRTFF 1000
Cdd:PRK13390  285 DVKHAMIDWLGPIVYEYYSSTEAHGMTFIDSPDWLAHPGSVGrsVLGDLHICDddgnelPAGRIGtvYFERDRLPFRYLN 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1001 NQLK----NHPNKKF-TRTGDLGRTID-GNLFITGRIKDLIIVAGRNIYSADVEKTVessseVLRPGC--CAVVGIPEev 1072
Cdd:PRK13390  365 DPEKtaaaQHPAHPFwTTVGDLGSVDEdGYLYLADRKSFMIISGGVNIYPQETENAL-----TMHPAVhdVAVIGVPD-- 437

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 937914749 1073 laqkgisiPDSSDQVGLVV--IAEVREGKAVSKEVVNNIKARVVeeHGVAVASVKLIK--PRT-ICKTTSGKIR 1141
Cdd:PRK13390  438 --------PEMGEQVKAVIqlVEGIRGSDELARELIDYTRSRIA--HYKAPRSVEFVDelPRTpTGKLVKGLLR 501
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1302-1363 1.15e-07

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 50.64  E-value: 1.15e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937914749  1302 EFLTKIVSDQTGIPKDKISPMDSLPSYGFDSIAVVQAAQKLSDFLGVPVGAIDIFTAGCISE 1363
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 102-138 1.86e-07

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 56.34  E-value: 1.86e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 937914749  102 RIGIVGAGPSGLSAAYALAKLGYRnVTLFEKCHTVSG 138
Cdd:PRK11749  142 KVAVIGAGPAGLTAAHRLARKGYD-VTIFEARDKAGG 177
PRK12316 PRK12316
peptide synthase; Provisional
 755-1142 2.84e-07

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 56.50  E-value: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDmGLIGGLFTALVSGGTsvlfspmIF 834
Cdd:PRK12316 4693 PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFD-GSHEGLYHPLINGAS-------VV 4764

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 IRNPLLWL-----QTINDYHGTHSAGPNFAFELVIRRLEAEKNkvydLSSMVFLMIAAEPVRQKTVRRFIELTQPFGLSE 909
Cdd:PRK12316 4765 IRDDSLWDperlyAEIHEHRVTVLVFPPVYLQQLAEHAERDGE----PPSLRVYCFGGEAVAQASYDLAWRALKPVYLFN 4840

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  910 gvlapGYGLAENCVYVTC----AFGECKPVFIDWqGRVCCGyveqddtdTLIRIVDpDSLtEHQEDGVEGEIWISSPSSG 985
Cdd:PRK12316 4841 -----GYGPTETTVTVLLwkarDGDACGAAYMPI-GTPLGN--------RSGYVLD-GQL-NPLPVGVAGELYLGGEGVA 4904

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  986 VGYWGNSEMSQRTFFNQLKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgccA 1064
Cdd:PRK12316 4905 RGYLERPALTAERFVPDPFGAPGGRLYRTGDLARyRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE----A 4980

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1065 VvgipeeVLAQKGisiPDSSDQVGLVVIAEVR--EGKAVSKEVVNNIKARV--------VEEHGVAVASVKLikprtick 1134
Cdd:PRK12316 4981 V------VIAQEG---AVGKQLVGYVVPQDPAlaDADEAQAELRDELKAALrerlpeymVPAHLVFLARMPL-------- 5043


                  ....*...
gi 937914749 1135 TTSGKIRR 1142
Cdd:PRK12316 5044 TPNGKLDR 5051
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 100-153 3.82e-07

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 55.24  E-value: 3.82e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 937914749  100 DTRIGIVGAGPSGLSAAYALAKLGYRnVTLFEKCHTVSGMCESIDIEGRIYDLG 153
Cdd:COG1233     3 MYDVVVIGAGIGGLAAAALLARAGYR-VTVLEKNDTPGGRARTFERPGFRFDVG 55
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
102-343 4.97e-07

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 54.74  E-value: 4.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  102 RIGIVGAGPSGLSAAYALAKlgYRNVTLFEK-------CHTVsgmceSIDIEGRIY--DLGGQVIaaNSA--PVITHLAE 170
Cdd:COG2907     5 RIAVIGSGISGLTAAWLLSR--RHDVTLFEAndrlgghTHTV-----DVDLDGRTVpvDTGFIVF--NERtyPNLTALFA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  171 ELGSDFEEMDT---------------HKLSLIDSQTGNIRDLEvaedYVSMVSLTLKLqdeaNKSGRAglHALSGLASDP 235
Cdd:COG2907    76 ELGVPTQPSDMsfsvsldgggleyagSNLNGLFAQRRNLLRPR----FWRMLRDILRF----NREAPA--LLEAGSDDDL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  236 T-HEFLKQNginsmpksvaygytasGYG--FVQD--MPyafiqeftrtsMAG--------KIRRFK----------HGYM 292
Cdd:COG2907   146 TlGEFLDRN----------------GYSeaFRDHylLP-----------MGAaiwscppdDMLDFParffvrffhnHGLL 198

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937914749  293 S-----MW-----------ERLSKSLPFEVFCDTQVLNVKRNSCGanVTIKNNNGEKQvlEFDKIIL 343
Cdd:COG2907   199 SvtdrpQWrtvkggsreyvRRLTAGLKDRIRLNTPVRSVRRDADG--VEVRTADGEEE--RFDHVVF 261
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 842-1144 5.39e-07

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 54.77  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  842 LQTINDY-----HGThsagPNFAFELvIRRLEAEKNKVYDLS--SMVFlmiAAEPVRQKTVRRF-----IELTQPFGLSE 909
Cdd:COG1541   168 LRLMQDFgptvlVGT----PSYLLYL-AEVAEEEGIDPRDLSlkKGIF---GGEPWSEEMRKEIeerwgIKAYDIYGLTE 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  910 GvlapGYGLAencvyvtcafGEC--KPVFIDWQGRVccgYVEqddtdtlirIVDPDSLtEHQEDGVEGEIWISSpssgvg 987
Cdd:COG1541   240 V----GPGVA----------YECeaQDGLHIWEDHF---LVE---------IIDPETG-EPVPEGEEGELVVTT------ 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  988 ywgnsemsqrtffnqlknhpnkkFT---------RTGDL----------GRT---IDGnlfITGRIKDLIIVAGRNIYSA 1045
Cdd:COG1541   287 -----------------------LTkeampliryRTGDLtrllpepcpcGRThprIGR---ILGRADDMLIIRGVNVFPS 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1046 DVEktvesssEVLRpgccAVVGIPEEVLAQkgISIPDSSDQvgLVVIAEVREGKAvSKEVVNNIKARVVEEHGVAVAsVK 1125
Cdd:COG1541   341 QIE-------EVLL----RIPEVGPEYQIV--VDREGGLDE--LTVRVELAPGAS-LEALAEAIAAALKAVLGLRAE-VE 403

                         330
                  ....*....|....*....
gi 937914749 1126 LIKPRTICKTTsGKIRRFE 1144
Cdd:COG1541   404 LVEPGSLPRSE-GKAKRVI 421
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
958-1080 8.74e-07

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 54.40  E-value: 8.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  958 RIVDPDSLTEhQEDGVEGEIWISSPSSGVGYW----GNSEMSQRTFFNQLKNHPNKKFT-----RTGDLGR-TIDGNLFI 1027
Cdd:PRK05620  370 RIVNDGQVME-STDRNEGEIQVRGNWVTASYYhsptEEGGGAASTFRGEDVEDANDRFTadgwlRTGDVGSvTRDGFLTI 448

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 937914749 1028 TGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVGIPEEVLAQKGISI 1080
Cdd:PRK05620  449 HDRARDVIRSGGEWIYSAQLENYIMAAPEVVE---CAVIGYPDDKWGERPLAV 498
PRK12316 PRK12316
peptide synthase; Provisional
 603-1048 1.11e-06

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 54.58  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  603 RRTYQELHGNASYIAQKLLTSTkpvIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPMQSggQALLkVENisk 682
Cdd:PRK12316  536 TLDYAELNRRANRLAHALIERG---VGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAER--LAYM-LED--- 606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  683 mcNAVAILSTSSYhaavragyIKNIVTLAKRVQKCSAQWPDipwihtdSWIKNYrrssdsfnSDTVLFTKPQPSDLCFLQ 762
Cdd:PRK12316  607 --SGVQLLLSQSH--------LGRKLPLAAGVQVLDLDRPA-------AWLEGY--------SEENPGTELNPENLAYVI 661

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  763 FTSGSTGDAKGVMITHEGLIHNVKTMKKRY-RSTSKTVLVSwLPQYHDMGlIGGLFTALVSGGTSVLFSPMIFiRNPLLW 841
Cdd:PRK12316  662 YTSGSTGKPKGAGNRHRALSNRLCWMQQAYgLGVGDTVLQK-TPFSFDVS-VWEFFWPLMSGARLVVAAPGDH-RDPAKL 738

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  842 LQTINdyhgTHSAGpnfAFELVIRRLEA--EKNKVYDLSSMVFLMIAAEPVRQKTVRRFIELtqpfgLSEGVLAPGYGLA 919
Cdd:PRK12316  739 VELIN----REGVD---TLHFVPSMLQAflQDEDVASCTSLRRIVCSGEALPADAQEQVFAK-----LPQAGLYNLYGPT 806

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  920 ENCVYVTC-----AFGECKPVfidwqGRVCCGyveqddtdTLIRIVDPDslTEHQEDGVEGEIWISSPSSGVGYWGNSEM 994
Cdd:PRK12316  807 EAAIDVTHwtcveEGGDSVPI-----GRPIAN--------LACYILDAN--LEPVPVGVLGELYLAGRGLARGYHGRPGL 871

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  995 SQRTFFnqlknhPN-----KKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVE 1048
Cdd:PRK12316  872 TAERFV------PSpfvagERMYRTGDLARyRADGVIEYAGRIDHQVKLRGLRIELGEIE 925
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 1748-1879 1.61e-06

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 50.95  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1748 IASLIHRRITISAHVRFAKmlsGTE--AFCVylrlLG--AKIGRHCSIraiNPVAnpeliSVGDGVHLGDFCNIVPgfys 1823
Cdd:cd03360    83 FATLIHPSAVVSPSAVIGE---GCVimAGAV----INpdARIGDNVII---NTGA-----VIGHDCVIGDFVHIAP---- 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749 1824 kGGFTSAEIKVQENTVVGSGSLLLPGCVLQENVILGALSVapenaVLRR---GGVYVGS 1879
Cdd:cd03360   144 -GVVLSGGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAV-----VTKDvpdGSVVVGN 196
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 605-825 1.79e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 53.51  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTSTKPvikPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVLPPDPMQSGGQALLKveNISKMC 684
Cdd:PRK12582   82 TYGEAKRAVDALAQALLDLGLD---PGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHAKLK--HLFDLV 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 NAVAILSTssyHAAVRAGYIKNIVTLAKRVQKCSAQWPDIPWIHTDSWIKN-----YRRSSDSFNSDTVlfTKpqpsdlc 759
Cdd:PRK12582  157 KPRVVFAQ---SGAPFARALAALDLLDVTVVHVTGPGEGIASIAFADLAATpptaaVAAAIAAITPDTV--AK------- 224

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749  760 fLQFTSGSTGDAKGVMITHEGLIHNVKTMKK---RYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGT 825
Cdd:PRK12582  225 -YLFTSGSTGMPKAVINTQRMMCANIAMQEQlrpREPDPPPPVSLDWMPWNHTMGGNANFNGLLWGGGT 292
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
748-920 1.81e-06

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 53.82  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  748 VLFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSV 827
Cdd:PRK06814  785 VYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVF 864

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  828 LF-SP--------MIFIRNPLLWLQT---INDYhgTHSAGPnfafelvirrleaeknkvYDLSSMVFLMIAAEPVRQKTV 895
Cdd:PRK06814  865 LYpSPlhyriipeLIYDTNATILFGTdtfLNGY--ARYAHP------------------YDFRSLRYVFAGAEKVKEETR 924

                         170       180
                  ....*....|....*....|....*
gi 937914749  896 RRFIEltqPFGLSegvLAPGYGLAE 920
Cdd:PRK06814  925 QTWME---KFGIR---ILEGYGVTE 943
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1785-1901 1.89e-06

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 50.41  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1785 IGRHCSI------RA-INPvanpelISVGDGVHLGDFCNI--VPGFyskggftSAEI---------------KVQENTVV 1840
Cdd:COG0663    31 IGEDVSVwpgavlRGdVGP------IRIGEGSNIQDGVVLhvDPGY-------PLTIgddvtighgailhgcTIGDNVLI 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937914749 1841 GSGSLLLPGCVLQENVILGALSVAPENAVLRRGGVYVGsqSPAMVKNTLldEDERIEEMDQ 1901
Cdd:COG0663    98 GMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVG--SPAKVVREL--TEEEIAFLRE 154
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 94-139 2.04e-06

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 52.96  E-value: 2.04e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 937914749   94 HPSLPVDT--RIGIVGAGPSGLSAAYALAKLGYRnVTLFEKCHTVSGM 139
Cdd:PRK12771  129 FPAPAPDTgkRVAVIGGGPAGLSAAYHLRRMGHA-VTIFEAGPKLGGM 175
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 760-1142 2.43e-06

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 52.82  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  760 FLQFTSGSTGDAKGVMITHEGlihNVKTMKKRYRSTSKTVLVSWLPQYHDMGLI---GGLFTALVSGGTSVLFSPMIFIR 836
Cdd:PTZ00237  258 YILYTSGTTGNSKAVVRSNGP---HLVGLKYYWRSIIEKDIPTVVFSHSSIGWVsfhGFLYGSLSLGNTFVMFEGGIIKN 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  837 NPL---LWlQTINDYHGTHSagpnFAFELVIRRL-----EAEK-NKVYDLSSMVFLMIAAEPVRQkTVRRFIE------L 901
Cdd:PTZ00237  335 KHIeddLW-NTIEKHKVTHT----LTLPKTIRYLiktdpEATIiRSKYDLSNLKEIWCGGEVIEE-SIPEYIEnklkikS 408

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  902 TQPFGLSEGVLAPGYGL-AENCVYVTCAFgecKPVFIdwqgrvccgyveqddtdtlirivDPDSLTehqEDGVE------ 974
Cdd:PTZ00237  409 SRGYGQTEIGITYLYCYgHINIPYNATGV---PSIFI-----------------------KPSILS---EDGKElnvnei 459

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  975 GEIWIS---SPSSGVGYWGNSEMSQRtFFNQLKNHPNkkftrTGDLGrTIDGNLF--ITGRIKDLIIVAGRNIYSADVEK 1049
Cdd:PTZ00237  460 GEVAFKlpmPPSFATTFYKNDEKFKQ-LFSKFPGYYN-----SGDLG-FKDENGYytIVSRSDDQIKISGNKVQLNTIET 532

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1050 TVESSSEVLRpgCCAVvgipeevlaqkGISIPDSSDQ-VGLVVIAEVREGKAVS----KEVVNNIKARVVEEHgvAVASV 1124
Cdd:PTZ00237  533 SILKHPLVLE--CCSI-----------GIYDPDCYNVpIGLLVLKQDQSNQSIDlnklKNEINNIITQDIESL--AVLRK 597

                         410
                  ....*....|....*...
gi 937914749 1125 KLIKPRtICKTTSGKIRR 1142
Cdd:PTZ00237  598 IIIVNQ-LPKTKTGKIPR 614
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 605-1076 2.82e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 52.30  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTStkpvikpgDRVLLIHLPGLEFIDAFFGCIRAGVIPVPVlPPD--PMQ-------SGGQALL 675
Cdd:PRK07787   27 SRSDLAGAATAVAERVAGA--------RRVAVLATPTLATVLAVVGALIAGVPVVPV-PPDsgVAErrhiladSGAQAWL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  676 kveniskmcnavailstssyhAAVRAGYiknivtlakrvqkcsAQWPDIPW-IHTDSWiknyrrssdsfnsdtVLFTKPQ 754
Cdd:PRK07787   98 ---------------------GPAPDDP---------------AGLPHVPVrLHARSW---------------HRYPEPD 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSV---LFSP 831
Cdd:PRK07787  127 PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVhtgRPTP 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  832 mifirnpllwlqtiNDYHGTHSAGPN--FAFELVIRRLEAEKNKVYDLSSMVFLM--IAAEPV------RQKTVRRFIEL 901
Cdd:PRK07787  207 --------------EAYAQALSEGGTlyFGVPTVWSRIAADPEAARALRGARLLVsgSAALPVpvfdrlAALTGHRPVER 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  902 tqpfglsegvlapgYGLAENCVYV-TCAFGECKPvfiDWQGRVCCGyVEqddtdtlIRIVDpDSLTEHQEDGVE-GEIWI 979
Cdd:PRK07787  273 --------------YGMTETLITLsTRADGERRP---GWVGLPLAG-VE-------TRLVD-EDGGPVPHDGETvGELQV 326

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  980 SSPSSGVGYWGNSEMSQRTFfnqlknHPNKKFtRTGDLG-RTIDGNLFITGRIK-DLIIVAGRNIYSADVEKTVESSSEV 1057
Cdd:PRK07787  327 RGPTLFDGYLNRPDATAAAF------TADGWF-RTGDVAvVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGV 399

                         490
                  ....*....|....*....
gi 937914749 1058 LRpgcCAVVGIPEEVLAQK 1076
Cdd:PRK07787  400 RE---AAVVGVPDDDLGQR 415
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 755-1098 3.45e-06

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 52.34  E-value: 3.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVL---FSP 831
Cdd:PRK13388  149 AMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALpakFSA 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  832 MIFirnpllwLQTINDYHGTHsagpnfaFELVIRRL-----EAEKNKVYDLSSMV-FLMIAAEPVRQKTVRRFieltqpf 905
Cdd:PRK13388  229 SGF-------LDDVRRYGATY-------FNYVGKPLayilaTPERPDDADNPLRVaFGNEASPRDIAEFSRRF------- 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  906 glseGV-LAPGYGLAENCVYVTCAFGeCKPVFIdwqGRVCCGyveqddtdtlIRIVDPDSLTE-------------HQED 971
Cdd:PRK13388  288 ----GCqVEDGYGSSEGAVIVVREPG-TPPGSI---GRGAPG----------VAIYNPETLTEcavarfdahgallNADE 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  972 GVeGEIwISSPSSG--VGYWGNSEMSQRTFFNqlknhpnkKFTRTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVE 1048
Cdd:PRK13388  350 AI-GEL-VNTAGAGffEGYYNNPEATAERMRH--------GMYWSGDLAyRDADGWIYFAGRTADWMRVDGENLSAAPIE 419

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 937914749 1049 KTVESSSEVLRpgcCAVVGIPEEVlaqkgisipdSSDQVGLVViaEVREG 1098
Cdd:PRK13388  420 RILLRHPAINR---VAVYAVPDER----------VGDQVMAAL--VLRDG 454
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 753-1104 3.48e-06

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: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 52.00  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  753 PQPSDLcFLQFTSGSTGDAKGVMITHE----------GLIHNVKTMKKRY-RSTSKTVLVSWL---PQYHDMGLIGGlfT 818
Cdd:cd05924     1 RSADDL-YILYTGGTTGMPKGVMWRQEdifrmlmggaDFGTGEFTPSEDAhKAAAAAAGTVMFpapPLMHGTGSWTA--F 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  819 ALVSGGTSVLFSPMIFirNPLLWLQTINDyHGTHSA---GPNFAFELvirrLEA-EKNKVYDLSSMVFLMIAAEPVRQKT 894
Cdd:cd05924    78 GGLLGGQTVVLPDDRF--DPEEVWRTIEK-HKVTSMtivGDAMARPL----IDAlRDAGPYDLSSLFAISSGGALLSPEV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  895 VRRFIE------LTQPFGLSEGVlAPGYGlaencvyVTCAFGECKPVFIDWQGRVCcgyVEQDDTdtliRIVDPDSlteh 968
Cdd:cd05924   151 KQGLLElvpnitLVDAFGSSETG-FTGSG-------HSAGSGPETGPFTRANPDTV---VLDDDG----RVVPPGS---- 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  969 qedGVEGeiWISspSSG---VGYWGNSEMSQRTFFNQlknhPNKKFTRTGDLGRTI-DGNLFITGRIKDLIIVAGRNIYS 1044
Cdd:cd05924   212 ---GGVG--WIA--RRGhipLGYYGDEAKTAETFPEV----DGVRYAVPGDRATVEaDGTVTLLGRGSVCINTGGEKVFP 280

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1045 ADVEKTVESSSEVLRpgcCAVVGIPEEVLAQKgisipdssdqvgLVVIAEVREGKAVSKE 1104
Cdd:cd05924   281 EEVEEALKSHPAVYD---VLVVGRPDERWGQE------------VVAVVQLREGAGVDLE 325
PRK13984 PRK13984
putative oxidoreductase; Provisional
 83-131 3.67e-06

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 52.46  E-value: 3.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749   83 KRSIDDQ-----FSKL--HPSLPVDTRIGIVGAGPSGLSAAYALAKLGYRnVTLFE 131
Cdd:PRK13984  259 KRYIVDNvpvekYSEIldDEPEKKNKKVAIVGSGPAGLSAAYFLATMGYE-VTVYE 313
PRK12316 PRK12316
peptide synthase; Provisional
 755-1048 6.09e-06

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 52.27  E-value: 6.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDmGLIGGLFTALVSGGTsvlfspmIF 834
Cdd:PRK12316 2145 GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFD-GAHEQWFHPLLNGAR-------VL 2216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 IRNPLLWL--QTINDY--HG-THSAGPNFAFELVIRRLEAEKNKVydlsSMVFLMIAAEPVRQKTVRRFIELTQPFGLSE 909
Cdd:PRK12316 2217 IRDDELWDpeQLYDEMerHGvTILDFPPVYLQQLAEHAERDGRPP----AVRVYCFGGEAVPAASLRLAWEALRPVYLFN 2292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  910 gvlapGYGLAENCvyVTCAFGECKPVfidwqgrVCCGYVEQ------DDTDTLIRIVDPDSLTEhqedGVEGEIWISSPS 983
Cdd:PRK12316 2293 -----GYGPTEAV--VTPLLWKCRPQ-------DPCGAAYVpigralGNRRAYILDADLNLLAP----GMAGELYLGGEG 2354

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749  984 SGVGYWGNSEMSQRTFFNQLKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVE 1048
Cdd:PRK12316 2355 LARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARyRADGVVEYLGRIDHQVKIRGFRIELGEIE 2420
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 100-132 6.48e-06

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 50.71  E-value: 6.48e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 937914749  100 DTRIGIVGAGPSGLSAAYALAKLGYRnVTLFEK 132
Cdd:COG0654     3 RTDVLIVGGGPAGLALALALARAGIR-VTVVER 34
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
 605-830 7.57e-06

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 51.14  E-value: 7.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLLTStkPVIKPGDRVLLIHLPGLEFIDAFFGCIRAGViPVPVLPP----DPMQ-----SGGQALL 675
Cdd:cd05938     7 TYRDVDRRSNQAARALLAH--AGLRPGDTVALLLGNEPAFLWIWLGLAKLGC-PVAFLNTnirsKSLLhcfrcCGAKVLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  676 -------KVENI----SKMCNAVAILSTSSYHAavragyikNIVTLAKRVQKCSAQWPDIPWihtdswiknyrRSSDSFN 744
Cdd:cd05938    84 vapelqeAVEEVlpalRADGVSVWYLSHTSNTE--------GVISLLDKVDAASDEPVPASL-----------RAHVTIK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  745 SdTVLFTkpqpsdlcflqFTSGSTGDAKGVMITHEGLIHnvktMKKRYRS---TSKTVLVSWLPQYHDMGLIGGLFTALV 821
Cdd:cd05938   145 S-PALYI-----------YTSGTTGLPKAARISHLRVLQ----CSGFLSLcgvTADDVIYITLPLYHSSGFLLGIGGCIE 208

                         250
                  ....*....|..
gi 937914749  822 SGGTSVL---FS 830
Cdd:cd05938   209 LGATCVLkpkFS 220
PLN02614 PLN02614
long-chain acyl-CoA synthetase
 754-808 7.90e-06

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 51.17  E-value: 7.90e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937914749  754 QPSDLCFLQFTSGSTGDAKGVMITHE-------GLIHNVKTMKKRYrsTSKTVLVSWLPQYH 808
Cdd:PLN02614  221 KKSDICTIMYTSGTTGDPKGVMISNEsivtliaGVIRLLKSANAAL--TVKDVYLSYLPLAH 280
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 111-393 8.20e-06

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 50.95  E-value: 8.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   111 SGLSAAYALAKLGyRNVTLFEKCHTVSGMCESIDIEGRIYDLGGQVIaANSAPVITHLAEELG--SDFEEMDTHKLSLID 188
Cdd:pfam01593    2 AGLAAARELLRAG-HDVTVLEARDRVGGRIRTVRDDGFLIELGAMWF-HGAQPPLLALLKELGleDRLVLPDPAPFYTVL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   189 SQTGNI---------RDLEVAEDYVSMVSLTLKLQDEANKSGRAGLHALsGLASDPTHEFLKQNGINSMPKSVAYGYTAS 259
Cdd:pfam01593   80 FAGGRRypgdfrrvpAGWEGLLEFGRLLSIPEKLRLGLAALASDALDEF-DLDDFSLAESLLFLGRRGPGDVEVWDRLID 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   260 GYGFvQDMPY----------------AFIQEFTRTSMAGKIRRFKHGYMSMWERLSKSLP-FEVFCDTQVLNVKRNSCGA 322
Cdd:pfam01593  159 PELF-AALPFasgafagdpselsaglALPLLWALLGEGGSLLLPRGGLGALPDALAAQLLgGDVRLNTRVRSIDREGDGV 237

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749   323 NVTIKnnNGEkqVLEFDKIILSgavafknsktyrsssltdgesevVELNNLERELFS------KVQTID--YYTTVVKI 393
Cdd:pfam01593  238 TVTLT--DGE--VIEADAVIVT-----------------------VPLGVLKRILFTpplppeKARAIRnlGYGPVNKV 289
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
 753-808 1.45e-05

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 50.58  E-value: 1.45e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937914749  753 PQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTM-----KKRYRSTSKTVLVSWLPQYH 808
Cdd:PLN02430  217 PKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlfmeQFEDKMTHDDVYLSFLPLAH 277
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 755-1097 1.54e-05

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-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. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 50.11  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTsvlfspMIF 834
Cdd:cd17641   157 GEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFI------VNF 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 IRNPLLWLQTINDyhgthsAGPNFAF-----------ELVIRRLEAE--KNKVYDLSSMVFLMIAAEPVRQKTVRRFIEL 901
Cdd:cd17641   231 PEEPETMMEDLRE------IGPTFVLlpprvwegiaaDVRARMMDATpfKRFMFELGMKLGLRALDRGKRGRPVSLWLRL 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  902 TQPFG--LSEGVLAPGYGLAENCVYVT--CAFGeckP-VF------------IDWQGRVCCGYVEQDDTDtliriVDPDS 964
Cdd:cd17641   305 ASWLAdaLLFRPLRDRLGFSRLRSAATggAALG---PdTFrffhaigvplkqLYGQTELAGAYTVHRDGD-----VDPDT 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  965 L------TEHQEDGVeGEIWISSPSSGVGYWGNSEMSQRTFFNQlknhpnkKFTRTGDLGR-TIDGNLFITGRIKDLIIV 1037
Cdd:cd17641   377 VgvpfpgTEVRIDEV-GEILVRSPGVFVGYYKNPEATAEDFDED-------GWLHTGDAGYfKENGHLVVIDRAKDVGTT 448

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937914749 1038 AGRNIYSAD-VEKTVESSSEVL--------RPGCCAVVGIPEEVLA----QKGISIPDSSD-----QVGLVVIAEVRE 1097
Cdd:cd17641   449 SDGTRFSPQfIENKLKFSPYIAeavvlgagRPYLTAFICIDYAIVGkwaeQRGIAFTTYTDlasrpEVYELIRKEVEK 526
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 101-169 1.54e-05

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 50.02  E-value: 1.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749  101 TRIGIVGAGPSGLSAAYALAKLGYRnVTLFEKcHTVSGMCESidiegriYDLGGQVIAANsAPVITHLA 169
Cdd:PRK12409    2 SHIAVIGAGITGVTTAYALAQRGYQ-VTVFDR-HRYAAMETS-------FANGGQLSASN-AEVWNHWA 60
PLN02479 PLN02479
acetate-CoA ligase
 761-1071 2.89e-05

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 49.46  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  761 LQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHdmgLIGGLFTALVSG--GTSVLF----SPMIF 834
Cdd:PLN02479  200 LGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFH---CNGWCFTWTLAAlcGTNICLrqvtAKAIY 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 irnpllwlQTINDYHGTHSAGPNFAFELVIRRLEAEKnkVYDLSSMVFLMIA-AEP---VRQKTVRRFIELTQPFGLSEG 910
Cdd:PLN02479  277 --------SAIANYGVTHFCAAPVVLNTIVNAPKSET--ILPLPRVVHVMTAgAAPppsVLFAMSEKGFRVTHTYGLSET 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  911 vlapgYGLAENCVYvtcafgecKPvfiDW-------QGRVCC----GYVEQDDTDtlirIVDPDSLTEHQEDGVE-GEIW 978
Cdd:PLN02479  347 -----YGPSTVCAW--------KP---EWdslppeeQARLNArqgvRYIGLEGLD----VVDTKTMKPVPADGKTmGEIV 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  979 ISSPSSGVGYWGNSEMSQRTFFNqlknhpnkKFTRTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEV 1057
Cdd:PLN02479  407 MRGNMVMKGYLKNPKANEEAFAN--------GWFHSGDLGvKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAV 478

                         330
                  ....*....|....
gi 937914749 1058 LRpgcCAVVGIPEE 1071
Cdd:PLN02479  479 LE---ASVVARPDE 489
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
2394-2474 3.21e-05

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 46.02  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 2394 RVMGASVSPGDGVYVDSMGALLNPEMVRLERGAAVGRDALLF--GHVYEG-EAGKVKFGAVSVGEDGFVGSRAVAMPSVT 2470
Cdd:COG0110    22 RIYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILtgNHPIDDpATFPLRTGPVTIGDDVWIGAGATILPGVT 101


                  ....
gi 937914749 2471 VDDG 2474
Cdd:COG0110   102 IGDG 105
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
 975-1071 3.49e-05

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 48.84  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  975 GEIWISSPSSGVGYWGNSEMSQRTFFnqlknhpnkkftrTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVES 1053
Cdd:PRK07445  302 GNITIQAQSLALGYYPQILDSQGIFE-------------TDDLGYlDAQGYLHILGRNSQKIITGGENVYPAEVEAAILA 368

                          90
                  ....*....|....*...
gi 937914749 1054 SSEVLRpgcCAVVGIPEE 1071
Cdd:PRK07445  369 TGLVQD---VCVLGLPDP 383
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 92-138 4.59e-05

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 48.97  E-value: 4.59e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 937914749   92 KLHPSLPV-----DTRIGIVGAGPSGLSAAYALAKLGYrNVTLFEKCHTVSG 138
Cdd:PRK12778  418 SGNISVPEvaeknGKKVAVIGSGPAGLSFAGDLAKRGY-DVTVFEALHEIGG 468
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 753-1035 4.69e-05

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 48.96  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  753 PQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVK-TMKKRYRSTSKTVLVSWLPQYHDMGLIG-----------GLFTAL 820
Cdd:PLN02387  247 PSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAgVMTVVPKLGKNDVYLAYLPLAHILELAAesvmaavgaaiGYGSPL 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  821 ------------VSGGTSVLfSPMIFIRNPLLW-------LQTINDYHGTHSAGPNFAFElviRRLEA-----------E 870
Cdd:PLN02387  327 tltdtsnkikkgTKGDASAL-KPTLMTAVPAILdrvrdgvRKKVDAKGGLAKKLFDIAYK---RRLAAiegswfgawglE 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  871 K--------NKVYDL--SSMVFLMIAAEPVRQKTvRRFIELTqpFGLSEGvlaPGYGLAEncvyvTCAFGeckpVFIDWQ 940
Cdd:PLN02387  403 KllwdalvfKKIRAVlgGRIRFMLSGGAPLSGDT-QRFINIC--LGAPIG---QGYGLTE-----TCAGA----TFSEWD 467

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  941 ----GRVC----CGYVEqddtdtlirivdpdsLTEHQEDGV--------EGEIWISSPSSGVGYWGNSEMSQRTFfnqlk 1004
Cdd:PLN02387  468 dtsvGRVGpplpCCYVK---------------LVSWEEGGYlisdkpmpRGEIVIGGPSVTLGYFKNQEKTDEVY----- 527

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 937914749 1005 nHPNKKFTR---TGDLGR-TIDGNLFITGRIKDLI 1035
Cdd:PLN02387  528 -KVDERGMRwfyTGDIGQfHPDGCLEIIDRKKDIV 561
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
753-1066 5.34e-05

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 48.89  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  753 PQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGlIGGLFTALVSGGTSVLFSPM 832
Cdd:PRK10252  595 SQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVS-VWEFFWPFIAGAKLVMAEPE 673

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  833 IFiRNPlLWLQTINDYHG---TH---SAGPNFAFELVIRRLEAEknkvydLSSM--VFLMIAAEPVRQktVRRFIELTQp 904
Cdd:PRK10252  674 AH-RDP-LAMQQFFAEYGvttTHfvpSMLAAFVASLTPEGARQS------CASLrqVFCSGEALPADL--CREWQQLTG- 742

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  905 fglsegvlAP---GYGLAENCVYVTC--AFGECK------PVFID---WQGRVccgYVeqddTDTLIRIVDPdsltehqe 970
Cdd:PRK10252  743 --------APlhnLYGPTEAAVDVSWypAFGEELaavrgsSVPIGypvWNTGL---RI----LDARMRPVPP-------- 799

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  971 dGVEGEIWISSPSSGVGYWGNSEMSQRTF----FNqlknhPNKKFTRTGDLGRTI-DGNLFITGRIKDLIIVAGRNIYSA 1045
Cdd:PRK10252  800 -GVAGDLYLTGIQLAQGYLGRPDLTASRFiadpFA-----PGERMYRTGDVARWLdDGAVEYLGRSDDQLKIRGQRIELG 873

                         330       340
                  ....*....|....*....|.
gi 937914749 1046 DVEKTVESSSEVLRPGCCAVV 1066
Cdd:PRK10252  874 EIDRAMQALPDVEQAVTHACV 894
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 757-830 5.52e-05

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 48.12  E-value: 5.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937914749  757 DLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVL---FS 830
Cdd:cd05940    82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIrkkFS 158
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 95-132 7.43e-05

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 47.85  E-value: 7.43e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 937914749   95 PSLPVDTRIGIVGAGPSGLSAAYALAKLGYRnVTLFEK 132
Cdd:PRK12810  138 PVKRTGKKVAVVGSGPAGLAAADQLARAGHK-VTVFER 174
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1523-1617 1.08e-04

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 44.48  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1523 IFLNYWFKMQGARIGSSVVIDT-VDITDPSLLTVADGAVLAEGALV--QGHEVCN---EVLSFRPIWIGCEASIGPYAVL 1596
Cdd:COG0110    17 IGPGVRIYGGNITIGDNVYIGPgVTIDDPGGITIGDNVLIGPGVTIltGNHPIDDpatFPLRTGPVTIGDDVWIGAGATI 96

                          90       100
                  ....*....|....*....|.
gi 937914749 1597 QKGTVVEDGAVVpplqktGAG 1617
Cdd:COG0110    97 LPGVTIGDGAVV------GAG 111
PRK12316 PRK12316
peptide synthase; Provisional
 755-1082 1.27e-04

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 47.64  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTVLVSWLPQYHDmGLIGGLFTALVSGGTSVLfspmif 834
Cdd:PRK12316 3195 PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFD-VFVEELFWPLMSGARVVL------ 3267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  835 iRNPLLWLQTINDYHGTHSAGPNF-AFELVIRRLEAEKNKVYDLSSMVFLMIAAEPVRQKTVRRFieltqpfgLSEGVLA 913
Cdd:PRK12316 3268 -AGPEDWRDPALLVELINSEGVDVlHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQV--------FAGLPLY 3338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  914 PGYGLAENCVYVT---CAFGECKPVFIdwqGRVCCGyveqddtdTLIRIVDPDSLTEHQedGVEGEIWISSPSSGVGYWG 990
Cdd:PRK12316 3339 NLYGPTEATITVThwqCVEEGKDAVPI---GRPIAN--------RACYILDGSLEPVPV--GALGELYLGGEGLARGYHN 3405

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  991 NSEMSQRTFFNQlKNHPNKKFTRTGDLGR-TIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRPGCCAVVG-- 1067
Cdd:PRK12316 3406 RPGLTAERFVPD-PFVPGERLYRTGDLARyRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGrq 3484

                         330       340
                  ....*....|....*....|....*...
gi 937914749 1068 -------------IPEEVLAQKGISIPD 1082
Cdd:PRK12316 3485 lvayvvpedeagdLREALKAHLKASLPE 3512
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 1012-1076 1.30e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 47.30  E-value: 1.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937914749 1012 TRTGDLGRTID-GNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRPgccAVVGIPEEVLAQK 1076
Cdd:PRK13383  398 TSTGDMGYLDNaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADN---AVIGVPDERFGHR 460
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
 605-826 1.32e-04

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 47.45  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  605 TYQELHGNASYIAQKLltSTKPVIKPGDRVLLIHLPGLEFIDAFFGCIRAGVIPVPvlppdpMQSGGQAllkveniSKMC 684
Cdd:cd17632    69 TYAELWERVGAVAAAH--DPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVP------LQAGASA-------AQLA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  685 NAVA-----ILSTSSYH--AAVRA----GYIKNIVTLAKRvqkcsaqwPDIPwIHTDSWIKNYRRSSDSFNSDTVL---- 749
Cdd:cd17632   134 PILAeteprLLAVSAEHldLAVEAvlegGTPPRLVVFDHR--------PEVD-AHRAALESARERLAAVGIPVTTLtlia 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  750 ------------FTKPQPSDLCFLQFTSGSTGDAKGVMITHegliHNVKTMKKRYRST-----SKTVLVSWLPQYHDMGL 812
Cdd:cd17632   205 vrgrdlppaplfRPEPDDDPLALLIYTSGSTGTPKGAMYTE----RLVATFWLKVSSIqdirpPASITLNFMPMSHIAGR 280

                         250
                  ....*....|....
gi 937914749  813 IgGLFTALVSGGTS 826
Cdd:cd17632   281 I-SLYGTLARGGTA 293
PRK12831 PRK12831
putative oxidoreductase; Provisional
 102-138 1.64e-04

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 46.93  E-value: 1.64e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 937914749  102 RIGIVGAGPSGLSAAYALAKLGYrNVTLFEKCHTVSG 138
Cdd:PRK12831  142 KVAVIGSGPAGLTCAGDLAKMGY-DVTIFEALHEPGG 177
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 757-830 1.67e-04

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 46.79  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  757 DLCFLQFTSGSTGDAKGVMITHegliHNVKTMKKRY----RSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGTSVL---F 829
Cdd:PRK08279  200 DTAFYIYTSGTTGLPKAAVMSH----MRWLKAMGGFggllRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALrrkF 275


                  .
gi 937914749  830 S 830
Cdd:PRK08279  276 S 276
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 102-139 1.74e-04

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 47.03  E-value: 1.74e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 937914749  102 RIGIVGAGPSGLSAAYALAKLGYRnVTLFEKCHTVSGM 139
Cdd:PRK12814  195 KVAIIGAGPAGLTAAYYLLRKGHD-VTIFDANEQAGGM 231
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
 752-922 1.83e-04

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 46.76  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  752 KPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRSTSKTV-----LVSWLPQYHDMGLIGGlfTALVSGGTS 826
Cdd:PLN02861  216 PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVAteedsYFSYLPLAHVYDQVIE--TYCISKGAS 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  827 VLF---------------SPMIFIRNPLLW-------LQTINDYHGTHSAGPNFAFELVIRRLE-----AEKNKVYD--- 876
Cdd:PLN02861  294 IGFwqgdirylmedvqalKPTIFCGVPRVYdriytgiMQKISSGGMLRKKLFDFAYNYKLGNLRkglkqEEASPRLDrlv 373

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 937914749  877 -------LSSMVFLMIAAEPVRQKTVRRFIELTqpfglSEGVLAPGYGLAENC 922
Cdd:PLN02861  374 fdkikegLGGRVRLLLSGAAPLPRHVEEFLRVT-----SCSVLSQGYGLTESC 421
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 972-1155 1.86e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 46.70  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  972 GVEGEIWISSPSSGVGYWGNSEMSQRTffnqlknhPNKKFTRTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKT 1050
Cdd:PRK07638  331 GEIGTVYVKSPQFFMGYIIGGVLAREL--------NADGWMTVRDVGyEDEEGFIYIVGREKNMILFGGINIFPEEIESV 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1051 VESSSEVLRpgcCAVVGIPEEVLAQKGISIPdssdqvglvviaevrEGKAVSKEvvnnIKARVVEEhgvaVASVKLIKP- 1129
Cdd:PRK07638  403 LHEHPAVDE---IVVIGVPDSYWGEKPVAII---------------KGSATKQQ----LKSFCLQR----LSSFKIPKEw 456

                         170       180
                  ....*....|....*....|....*....
gi 937914749 1130 ---RTICKTTSGKIRRFEcMRQFVDNTLS 1155
Cdd:PRK07638  457 hfvDEIPYTNSGKIARME-AKSWIENQEK 484
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
102-132 1.95e-04

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 46.64  E-value: 1.95e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 937914749  102 RIGIVGAGPSGLSAAYALAKLGYRnVTLFEK 132
Cdd:COG2509    32 DVVIVGAGPAGLFAALELAEAGLK-PLVLER 61
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 101-131 3.53e-04

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 45.62  E-value: 3.53e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 937914749  101 TRIGIVGAGPSGLSAAYALAKLGYRnVTLFE 131
Cdd:COG3349     4 PRVVVVGGGLAGLAAAVELAEAGFR-VTLLE 33
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 101-170 3.78e-04

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 45.60  E-value: 3.78e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937914749   101 TRIGIVGAGPSGLSAAYALAKLGYR---NVTLFEKCHTVSGMCESIDIEGRIYDLGGQVIAANSAPVITHLAE 170
Cdd:TIGR00562    3 KHVVIIGGGISGLCAAYYLEKEIPElpvELTLVEASDRVGGKIQTVKEDGYLIERGPDSFLERKKSAPDLVKD 75
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 1300-1369 4.40e-04

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 44.74  E-value: 4.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1300 IIEFLTKIVSDQTGIPKDKISPMDSLPSYGFDSIAVVQAAQKLSDfLGVPVGAIDIFTAGCISELATFLE 1369
Cdd:COG3433   220 TEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRK-AGLDVSFADLAEHPTLAAWWALLA 288
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
99-132 4.43e-04

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 45.28  E-value: 4.43e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 937914749   99 VDTRIGIVGAGPSGLSAAYALAKLGYRnVTLFEK 132
Cdd:COG0665     1 ATADVVVIGGGIAGLSTAYHLARRGLD-VTVLER 33
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 1783-1870 4.49e-04

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 43.94  E-value: 4.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1783 AKIGRHCSIRAinpvanpeLISVGDGVHLGDFCNIVPGFYskggftsaeikVQENTVVGSGSLLLPGCVLQENVILGALS 1862
Cdd:cd03352     2 AKIGENVSIGP--------NAVIGEGVVIGDGVVIGPGVV-----------IGDGVVIGDDCVIHPNVTIYEGCIIGDRV 62


                  ....*...
gi 937914749 1863 VAPENAVL 1870
Cdd:cd03352    63 IIHSGAVI 70
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 102-192 4.95e-04

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 45.22  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  102 RIGIVGAGPSGLSAAYALAKLGYR-NVTLFEKCHTVSGMCESIDIEGRIYDLGgqviaANS----APVITHLAEELG-SD 175
Cdd:PRK11883    2 KVAIIGGGITGLSAAYRLHKKGPDaDITLLEASDRLGGKIQTVRKDGFPIELG-----PESflarKPSAPALVKELGlED 76

                          90
                  ....*....|....*..
gi 937914749  176 feemdthklSLIDSQTG 192
Cdd:PRK11883   77 ---------ELVANTTG 84
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 1783-1863 5.43e-04

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 40.70  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1783 AKIGRHCSIrainpvanPELISVGDGVHLGDFCNIVPG--FYSKGGFTSA-EIKVQENTVVGSGSLLLPGCVLQENVILG 1859
Cdd:cd00208     1 VFIGEGVKI--------HPKAVIRGPVVIGDNVNIGPGavIGAATGPNEKnPTIIGDNVEIGANAVIHGGVKIGDNAVIG 72


                  ....
gi 937914749 1860 ALSV 1863
Cdd:cd00208    73 AGAV 76
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 1204-1276 5.68e-04

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 44.36  E-value: 5.68e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937914749 1204 SNEITEFLTQIVSEHTGISKDKISLTDSLPSYGFDSIAVVRAAQKLSDfLGVPVGAIDIFTASCISELASFLE 1276
Cdd:COG3433   217 TALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRK-AGLDVSFADLAEHPTLAAWWALLA 288
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 749-825 6.99e-04

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 44.73  E-value: 6.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749  749 LFTKPQPSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRY--RSTSKTVLVSWLPQYHDMGLIGGLFTALVSGGT 825
Cdd:cd05921   158 AFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYpfFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGT 236
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 755-1066 8.18e-04

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 44.31  E-value: 8.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  755 PSDLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRY---RSTSKTVLVswLPQYHDMGLIGGLFTALVSGGT------ 825
Cdd:cd17648    93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYfgrDNGDEAVLF--FSNYVFDFFVEQMTLALLNGQKlvvppd 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  826 SVLFSPMIFIRnpllwlqTINDYHGTH-SAGPNfafelVIRRleaeknkvYDLSSMVFL--MIAAEpvRQKTVRRFIELT 902
Cdd:cd17648   171 EMRFDPDRFYA-------YINREKVTYlSGTPS-----VLQQ--------YDLARLPHLkrVDAAG--EEFTAPVFEKLR 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  903 QPFGlseGVLAPGYGLAENCVYVTCAFGECKPVFIDWQGRVCCG---YVEQDDTDTLirivdpdsltehqEDGVEGEIWI 979
Cdd:cd17648   229 SRFA---GLIINAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNtkcYVLNDAMKRV-------------PVGAVGELYL 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  980 SSPSSGVGYWGNSEMSQRTFF-------NQLKNHPNKKFTRTGDLGRTI-DGNLFITGRiKDL-IIVAGRNIYSADVEKT 1050
Cdd:cd17648   293 GGDGVARGYLNRPELTAERFLpnpfqteQERARGRNARLYKTGDLVRWLpSGELEYLGR-NDFqVKIRGQRIEPGEVEAA 371

                         330
                  ....*....|....*.
gi 937914749 1051 VESSSEVLRpgcCAVV 1066
Cdd:cd17648   372 LASYPGVRE---CAVV 384
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 102-177 8.68e-04

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 43.93  E-value: 8.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749   102 RIGIVGAGPSGLSAAYALAKLGYRnVTLFEKCHTV--------SGMCESIDIEGRIYDLGGqvIAANSAPVITHLAEELG 173
Cdd:pfam01266    1 DVVVIGGGIVGLSTAYELARRGLS-VTLLERGDDPgsgasgrnAGLIHPGLRYLEPSELAR--LALEALDLWEELEEELG 77


                   ....
gi 937914749   174 SDFE 177
Cdd:pfam01266   78 IDCG 81
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 95-132 1.03e-03

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 44.08  E-value: 1.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 937914749   95 PSLPVDTRIGIVGAGPSGLSAAYALAKLGyRNVTLFEK 132
Cdd:COG2072     1 TAATEHVDVVVIGAGQAGLAAAYHLRRAG-IDFVVLEK 37
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
 1013-1144 1.08e-03

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 44.15  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1013 RTGDL----------GRT---IDGnlfITGRIKDLIIVAGRNIYSADVEktvesssEVLR--PGCcavvgIPEevlAQKG 1077
Cdd:cd05913   294 RTRDItrllpgpcpcGRThrrIDR---ITGRSDDMLIIRGVNVFPSQIE-------DVLLkiPGL-----GPH---YQLI 355

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 937914749 1078 ISIPDSSDQvgLVVIAEVREG-------KAVSKEVVNNIKARVveehGVAVAsVKLIKPRTIcKTTSGKIRRFE 1144
Cdd:cd05913   356 LTRQEHLDE--LTIKVEVRPEadddeklEALKQRLERHIKSVL----GVTVE-VELVEPGSL-PRSEGKAKRVI 421
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
100-132 1.18e-03

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 44.17  E-value: 1.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 937914749  100 DTRIGIVGAGPSGLSAAYALAKLGYRN--VTLFEK 132
Cdd:COG4529     5 RKRIAIIGGGASGTALAIHLLRRAPEPlrITLFEP 39
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
108-132 1.52e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 43.03  E-value: 1.52e-03
                          10        20
                  ....*....|....*....|....*
gi 937914749  108 AGPSGLSAAYALAKLGYRnVTLFEK 132
Cdd:COG0644     1 AGPAGSAAARRLARAGLS-VLLLEK 24
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 1833-1905 1.85e-03

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 41.40  E-value: 1.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 937914749 1833 KVQENTVVGSGSLLLPGCVLQENVILGALSVAPENAVLRRGGVYVGsqSPAMVKNTLLDED-ERIEEMDQAYKK 1905
Cdd:cd04650    80 KVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLG--VPAKVVRKLTEEEiEWIKKNAEEYVE 151
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1206-1275 1.87e-03

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 39.54  E-value: 1.87e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937914749   1206 EITEFLTQIVSEHTGI-SKDKISLTDSLPSYGFDSIAVVRAAQKLSDFLGVPVGAIDIFTASCISELASFL 1275
Cdd:smart00823   12 LLLDLVREQVAAVLGHaAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
PLN02576 PLN02576
protoporphyrinogen oxidase
 100-161 1.88e-03

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 43.46  E-value: 1.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937914749  100 DTRIGIVGAGPSGLSAAYALAKLGYRNVTLFEKCHTVSGMCESIDIEGRIYDLGgqviaANS 161
Cdd:PLN02576   12 SKDVAVVGAGVSGLAAAYALASKHGVNVLVTEARDRVGGNITSVSEDGFIWEEG-----PNS 68
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 973-1057 2.34e-03

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 42.94  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  973 VEGEIWISSPSSGVGYWGNSEMsqRTFFNQlknhpNKKF-TRtgDLGRTIDGNLFITGRIKDLIIVAGRNIYSADVEKTV 1051
Cdd:PRK09029  303 VDGEIWLRGASLALGYWRQGQL--VPLVND-----EGWFaTR--DRGEWQNGELTILGRLDNLFFSGGEGIQPEEIERVI 373


                  ....*.
gi 937914749 1052 ESSSEV 1057
Cdd:PRK09029  374 NQHPLV 379
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1299-1368 2.56e-03

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 39.16  E-value: 2.56e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937914749   1299 VIIEFLTKIVSDQTGIPKDKISPMD-SLPSYGFDSIAVVQAAQKLSDFLGVPVGAIDIFTAGCISELATFL 1368
Cdd:smart00823   12 LLLDLVREQVAAVLGHAAAEAIDPDrPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
 760-825 2.90e-03

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 42.94  E-value: 2.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937914749  760 FLqFTSGSTGDAKGVMITHEGLIHNVKTMKKRYR--STSKTVLVSWLPQYHDMGLIGGLFTALVSGGT 825
Cdd:PRK08180  214 FL-FTSGSTGLPKAVINTHRMLCANQQMLAQTFPflAEEPPVLVDWLPWNHTFGGNHNLGIVLYNGGT 280
PRK10502 PRK10502
putative acyl transferase; Provisional
 1775-1888 3.01e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 41.09  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1775 CVYLRLLGAKIGRHCSIRAINPVANPELISVGD--------------GVHLGDFCNIVPGFY--------SKGGF--TSA 1830
Cdd:PRK10502   44 AFLLRLFGAKIGKGVVIRPSVRITYPWKLTIGDyawigddvwlynlgEITIGAHCVISQKSYlctgshdySDPHFdlNTA 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 937914749 1831 EIKVQENTVVGSGSLLLPGCVLQENVILGALSVAPENavLRRGGVYVGsqSPAMVKNT 1888
Cdd:PRK10502  124 PIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKS--LPANTICRG--NPAVPIRP 177
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 105-132 3.09e-03

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 42.31  E-value: 3.09e-03
                           10        20
                   ....*....|....*....|....*...
gi 937914749   105 IVGAGPSGLSAAYALAKLGYRnVTLFEK 132
Cdd:TIGR02032    5 VVGAGPAGASAAYRLADKGLR-VLLLEK 31
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 1782-1860 4.17e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 41.93  E-value: 4.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 937914749 1782 GAKIGRHCSIRAinpvanpeLISVGDGVHLGDFCNIVPGFYskggftsaeikVQENTVVGSGSLLLPGCVLQENVILGA 1860
Cdd:COG1044   108 SAKIGEGVSIGP--------FAVIGAGVVIGDGVVIGPGVV-----------IGDGVVIGDDCVLHPNVTIYERCVIGD 167
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
 103-158 5.32e-03

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 42.13  E-value: 5.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937914749  103 IGIVGAGPSGLSAAYALAKLGYrNVTLFEKCHTVSGMC-----------ESI-DIEGRIYDLGGQVIA 158
Cdd:PRK12779  309 IAVVGSGPSGLINAYLLAVEGF-PVTVFEAFHDLGGVLrygipefrlpnQLIdDVVEKIKLLGGRFVK 375
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 95-132 6.03e-03

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 41.51  E-value: 6.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 937914749   95 PSLPVDTRIGIVGAGPSGLSAAYALAKLGYrNVTLFEK 132
Cdd:PRK12770   13 KPPPTGKKVAIIGAGPAGLAAAGYLACLGY-EVHVYDK 49
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 102-131 6.39e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 37.57  E-value: 6.39e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 937914749   102 RIGIVGAGPSGLSAAYALAKLGYRnVTLFE 131
Cdd:pfam00070    1 RVVVVGGGYIGLELAGALARLGSK-VTVVE 29
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 1783-1859 6.83e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.28  E-value: 6.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937914749 1783 AKIGRHCSIRAiNPVanpelisVGDGVHLGDFCNIVPGFYskggftsaeikVQENTVVGSGSLLLPGCVLQENVILG 1859
Cdd:PRK00892  113 AKIGEGVSIGP-NAV-------IGAGVVIGDGVVIGAGAV-----------IGDGVKIGADCRLHANVTIYHAVRIG 170
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 757-813 7.46e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 41.50  E-value: 7.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 937914749  757 DLCFLQFTSGSTGDAKGVMITHEGLIHNVKTMKKRYRS-----TSKTVLVSWLPQYHDMGLI 813
Cdd:PTZ00216  265 DLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDligppEEDETYCSYLPLAHIMEFG 326
PRK06753 PRK06753
hypothetical protein; Provisional
 102-137 8.77e-03

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 40.83  E-value: 8.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 937914749  102 RIGIVGAGPSGLSAAYALAKLGYrNVTLFEKCHTVS 137
Cdd:PRK06753    2 KIAIIGAGIGGLTAAALLQEQGH-EVKVFEKNESVK 36
prpE PRK10524
propionyl-CoA synthetase; Provisional
 989-1142 9.33e-03

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 41.09  E-value: 9.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749  989 WGNSEMSQRTFFNqlknHPNKKFTRTGDLG-RTIDGNLFITGRIKDLIIVAGRNIYSADVEKTVESSSEVLRpgcCAVVG 1067
Cdd:PRK10524  456 WGDDDRFVKTYWS----LFGRQVYSTFDWGiRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAE---VAVVG 528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937914749 1068 IPEEVLAQKGIS--IPDSSDqvglvVIAEVREGKAVSKEVVnnikaRVVEEHGVAVAsvkliKPRTIC------KTTSGK 1139
Cdd:PRK10524  529 VKDALKGQVAVAfvVPKDSD-----SLADREARLALEKEIM-----ALVDSQLGAVA-----RPARVWfvsalpKTRSGK 593


                  ...
gi 937914749 1140 IRR 1142
Cdd:PRK10524  594 LLR 596
 
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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